|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-527 |
0e+00 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 1039.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 1 MTQPLLRIDNLSIAFSKQDETRTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLLPSPPVSYPQGDILFHDRSLLH 80
Cdd:PRK15134 1 MTQPLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVVYPSGDIRFHGESLLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 81 ADEQTLRGIRGNKIAMIFQEPMVSLNPLHSLEKQLYEVLSLHRGMRKEAARGEILDCLERTGIRNAAKRLNDFPHQLSGG 160
Cdd:PRK15134 81 ASEQTLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTDYPHQLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 161 ERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGRCVEQNA 240
Cdd:PRK15134 161 ERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 241 ASTLLSAPQHPYTQRLLNSEPSGDPVPLDADSTPLLRVEDLSVSFPIRKGILRRIVDRNPVLKNIRFSLRPGESLGLVGE 320
Cdd:PRK15134 241 AATLFSAPTHPYTQKLLNSEPSGDPVPLPEPASPLLDVEQLQVAFPIRKGILKRTVDHNVVVKNISFTLRPGETLGLVGE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 321 SGSGKSTTGLALLRLIASQGEILFDGMPLHRWNRRQMLPVRPRMQVVFQDPNSSLNPRLSVLQIVEEGLRVHQPGLSAQQ 400
Cdd:PRK15134 321 SGSGKSTTGLALLRLINSQGEIWFDGQPLHNLNRRQLLPVRHRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHQPTLSAAQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 401 REQEVMRVMVEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYI 480
Cdd:PRK15134 401 REQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYL 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1278835479 481 FISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSAPTQRYTRQLLS 527
Cdd:PRK15134 481 FISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQLLA 527
|
|
| 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: 958.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 1 MTQPLLRIDNLSIAFSKQDETRTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLLPSPPvSYPQGDILFHDRSLLH 80
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPA-AHPSGSILFDGQDLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 81 ADEQTLRGIRGNKIAMIFQEPMVSLNPLHSLEKQLYEVLSLHRGMRKEAARGEILDCLERTGIRNAAKRLNDFPHQLSGG 160
Cdd:COG4172 81 LSERELRRIRGNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPERRLDAYPHQLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 161 ERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGRCVEQNA 240
Cdd:COG4172 161 QRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 241 ASTLLSAPQHPYTQRLLNSEPSGDPVPLDADSTPLLRVEDLSVSFPIRKGILRRIVDRNPVLKNIRFSLRPGESLGLVGE 320
Cdd:COG4172 241 TAELFAAPQHPYTRKLLAAEPRGDPRPVPPDAPPLLEARDLKVWFPIKRGLFRRTVGHVKAVDGVSLTLRRGETLGLVGE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 321 SGSGKSTTGLALLRLIASQGEILFDGMPLHRWNRRQMLPVRPRMQVVFQDPNSSLNPRLSVLQIVEEGLRVHQPGLSAQQ 400
Cdd:COG4172 321 SGSGKSTLGLALLRLIPSEGEIRFDGQDLDGLSRRALRPLRRRMQVVFQDPFGSLSPRMTVGQIIAEGLRVHGPGLSAAE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 401 REQEVMRVMVEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYI 480
Cdd:COG4172 401 RRARVAEALEEVGLDPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYL 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1278835479 481 FISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSAPTQRYTRQLLSS 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: 613.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 3 QPLLRIDNLSIAFSKQDetRTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLLPSPpvSYPQGDILFHDRSLLHAD 82
Cdd:COG1123 2 TPLLEVRDLSVRYPGGD--VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHG--GRISGEVLLDGRDLLELS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 83 EQtlrgIRGNKIAMIFQEPMVSLNPLhSLEKQLYEVLSLhRGMRKEAARGEILDCLERTGIrnaAKRLNDFPHQLSGGER 162
Cdd:COG1123 78 EA----LRGRRIGMVFQDPMTQLNPV-TVGDQIAEALEN-LGLSRAEARARVLELLEAVGL---ERRLDRYPHQLSGGQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 163 QRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGRCVEQNAAS 242
Cdd:COG1123 149 QRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 243 TLLSAPQHPYTQRLLNSePSGDPVPLDADSTPLLRVEDLSVSFPIRKGilrrivDRNPVLKNIRFSLRPGESLGLVGESG 322
Cdd:COG1123 229 EILAAPQALAAVPRLGA-ARGRAAPAAAAAEPLLEVRNLSKRYPVRGK------GGVRAVDDVSLTLRRGETLGLVGESG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 323 SGKSTTGLALLRLI-ASQGEILFDGMPLHRWNRRQMLPVRPRMQVVFQDPNSSLNPRLSVLQIVEEGLRVHQpGLSAQQR 401
Cdd:COG1123 302 SGKSTLARLLLGLLrPTSGSILFDGKDLTKLSRRSLRELRRRVQMVFQDPYSSLNPRMTVGDIIAEPLRLHG-LLSRAER 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 402 EQEVMRVMVEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIF 481
Cdd:COG1123 381 RERVAELLERVGLPPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLF 460
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1278835479 482 ISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSAPTQRYTRQLLSS 528
Cdd:COG1123 461 ISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQHPYTRALLAA 507
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-528 |
8.32e-156 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 458.17 E-value: 8.32e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 2 TQPLLRIDNLSIAFSKQDETRTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLLPSPPVSYPQGDILFHDRS--LL 79
Cdd:PRK10261 9 ARDVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSrqVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 80 HADEQT---LRGIRGNKIAMIFQEPMVSLNPLHSLEKQLYEVLSLHRGMRKEAARGEILDCLERTGIRNAAKRLNDFPHQ 156
Cdd:PRK10261 89 ELSEQSaaqMRHVRGADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYPHQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGRCV 236
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 237 EQNAASTLLSAPQHPYTQRLLNSEP-----SGDPVPLD---------------------ADSTPLLRVEDLSVSFPIRKG 290
Cdd:PRK10261 249 ETGSVEQIFHAPQHPYTRALLAAVPqlgamKGLDYPRRfplislehpakqeppieqdtvVDGEPILQVRNLVTRFPLRSG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 291 ILRRIVDRNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIASQ-GEILFDGMPLHRWNRRQMLPVRPRMQVVFQ 369
Cdd:PRK10261 329 LLNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQgGEIIFNGQRIDTLSPGKLQALRRDIQFIFQ 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 370 DPNSSLNPRLSVLQIVEEGLRVHQ--PGLSAQQReqeVMRVMVEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPELI 447
Cdd:PRK10261 409 DPYASLDPRQTVGDSIMEPLRVHGllPGKAAAAR---VAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVI 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 448 ILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSAPTQRYTRQLLS 527
Cdd:PRK10261 486 IADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMA 565
|
.
gi 1278835479 528 S 528
Cdd:PRK10261 566 A 566
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-265 |
7.00e-132 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 385.95 E-value: 7.00e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 5 LLRIDNLSIAFSKQDETRTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLLPSPPVSypQGDILFHDRSLLHADEQ 84
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGIT--SGEILFDGEDLLKLSEK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 85 TLRGIRGNKIAMIFQEPMVSLNPLHSLEKQLYEVLSLHRGMRKEAARGEILDCLERTGIRNAAKRLNDFPHQLSGGERQR 164
Cdd:COG0444 79 ELRKIRGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRLDRYPHELSGGMRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 165 VMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGRCVEQNAASTL 244
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEEL 238
|
250 260
....*....|....*....|.
gi 1278835479 245 LSAPQHPYTQRLLNSEPSGDP 265
Cdd:COG0444 239 FENPRHPYTRALLSSIPRLDP 259
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
270-528 |
1.62e-116 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 347.10 E-value: 1.62e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 270 ADSTPLLRVEDLSVSFPIRKGILRRivdRNPVLK---NIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEILFD 345
Cdd:COG4608 2 AMAEPLLEVRDLKKHFPVRGGLFGR---TVGVVKavdGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEePTSGEILFD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 346 GMPLHRWNRRQMLPVRPRMQVVFQDPNSSLNPRLSVLQIVEEGLRVHQPGlSAQQREQEVMRVMVEVGLDPETRHRYPAE 425
Cdd:COG4608 79 GQDITGLSGRELRPLRRRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLA-SKAERRERVAELLELVGLRPEHADRYPHE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 426 FSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVV 505
Cdd:COG4608 158 FSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIV 237
|
250 260
....*....|....*....|...
gi 1278835479 506 EQGECQRVFSAPTQRYTRQLLSS 528
Cdd:COG4608 238 EIAPRDELYARPLHPYTQALLSA 260
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
275-528 |
2.11e-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: 325.85 E-value: 2.11e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 275 LLRVEDLSVSFPIRKGILRrivdrnpVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIA----SQGEILFDGMPLH 350
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVK-------AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgiTSGEILFDGEDLL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 351 RWNRRQMLPVRPR-MQVVFQDPNSSLNPRLSVLQIVEEGLRVHQpGLSAQQREQEVMRVMVEVGL-DPETR-HRYPAEFS 427
Cdd:COG0444 74 KLSEKELRKIRGReIQMIFQDPMTSLNPVMTVGDQIAEPLRIHG-GLSKAEARERAIELLERVGLpDPERRlDRYPHELS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 428 GGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQ 507
Cdd:COG0444 153 GGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEE 232
|
250 260
....*....|....*....|.
gi 1278835479 508 GECQRVFSAPTQRYTRQLLSS 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 |
3.60e-107 |
|
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: 319.45 E-value: 3.60e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 275 LLRVEDLSVSFPIRKGilrrivdRNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIA-SQGEILFDGMPLHRWN 353
Cdd:cd03257 1 LLEVKNLSVSFPTGGG-------SVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKpTSGSIIFDGKDLLKLS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 354 RRQMLPVRPRMQVVFQDPNSSLNPRLSVLQIVEEGLRVHQPGLSAQQREQEVMRVMVEVGLDPETRHRYPAEFSGGQRQR 433
Cdd:cd03257 74 RRLRKIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1278835479 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 |
6.37e-103 |
|
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: 308.67 E-value: 6.37e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 5 LLRIDNLSIAFSKQDETRTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLLPspPVSypqGDILFHDRSLLHADEQ 84
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLK--PTS---GSIIFDGKDLLKLSRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 85 TLRgIRGNKIAMIFQEPMVSLNPLHSLEKQLYEVLSLHRGMRKEAARGEILdCLERTGIRNAAKRLNDFPHQLSGGERQR 164
Cdd:cd03257 76 LRK-IRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAV-LLLLVGVGLPEEVLNRYPHELSGGQRQR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1278835479 165 VMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGRCVEQN 239
Cdd:cd03257 154 VAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
275-528 |
2.58e-98 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 297.48 E-value: 2.58e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 275 LLRVEDLSVSFPIRKgilrrivDRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPL 349
Cdd:COG1124 1 MLEVRNLSVSYGQGG-------RRVPVLKDVSLEVAPGESFGLVGESGSGKST----LLRALAglerpWSGEVTFDGRPV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 350 HRWNRRQMlpvRPRMQVVFQDPNSSLNPRLSVLQIVEEGLRVHqpGLsaQQREQEVMRVMVEVGLDPETRHRYPAEFSGG 429
Cdd:COG1124 70 TRRRRKAF---RRRVQMVFQDPYASLHPRHTVDRILAEPLRIH--GL--PDREERIAELLEQVGLPPSFLDRYPHQLSGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 430 QRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGE 509
Cdd:COG1124 143 QRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELT 222
|
250
....*....|....*....
gi 1278835479 510 CQRVFSAPTQRYTRQLLSS 528
Cdd:COG1124 223 VADLLAGPKHPYTRELLAA 241
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-265 |
8.80e-94 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 294.89 E-value: 8.80e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 1 MTQPLLRIDNLSIAF-SKQDETRTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLLPspPVSypqGDILFHDRSLL 79
Cdd:COG1123 256 AAEPLLEVRNLSKRYpVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLR--PTS---GSILFDGKDLT 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 80 HADEQTLRGIRGnKIAMIFQEPMVSLNPLHSLEKQLYEVLSLHRGMRKEAARGEILDCLERTGIRnaAKRLNDFPHQLSG 159
Cdd:COG1123 331 KLSRRSLRELRR-RVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLP--PDLADRYPHELSG 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 160 GERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGRCVEQN 239
Cdd:COG1123 408 GQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDG 487
|
250 260
....*....|....*....|....*.
gi 1278835479 240 AASTLLSAPQHPYTQRLLNSEPSGDP 265
Cdd:COG1123 488 PTEEVFANPQHPYTRALLAAVPSLDP 513
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-276 |
2.04e-92 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 285.47 E-value: 2.04e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 1 MTQPLLRIDNLSIAFSKQDETRTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLLPSPPVSypQGDILFHDRSLLH 80
Cdd:PRK09473 8 QADALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRI--GGSATFNGREILN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 81 ADEQTLRGIRGNKIAMIFQEPMVSLNPLHSLEKQLYEVLSLHRGMRKEAARGEILDCLERTGIRNAAKRLNDFPHQLSGG 160
Cdd:PRK09473 86 LPEKELNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMKMYPHEFSGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 161 ERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGRCVEQNA 240
Cdd:PRK09473 166 MRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGN 245
|
250 260 270
....*....|....*....|....*....|....*.
gi 1278835479 241 ASTLLSAPQHPYTQRLLNSEPSgdpvpLDADSTPLL 276
Cdd:PRK09473 246 ARDVFYQPSHPYSIGLLNAVPR-----LDAEGESLL 276
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-265 |
9.91e-86 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 268.14 E-value: 9.91e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 1 MTQPLLRIDNLSI-------AFSKQDETRTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLLPspPVSypqGDILF 73
Cdd:COG4608 3 MAEPLLEVRDLKKhfpvrggLFGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEE--PTS---GEILF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 74 HDRSLLHADEQTLRGIRgNKIAMIFQEPMVSLNPLHSLEKQLYEVLSLHRGMRKEAARGEILDCLERTGIRnaAKRLNDF 153
Cdd:COG4608 78 DGQDITGLSGRELRPLR-RRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLR--PEHADRY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 154 PHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNG 233
Cdd:COG4608 155 PHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLG 234
|
250 260 270
....*....|....*....|....*....|..
gi 1278835479 234 RCVEQNAASTLLSAPQHPYTQRLLNSEPSGDP 265
Cdd:COG4608 235 KIVEIAPRDELYARPLHPYTQALLSAVPVPDP 266
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-264 |
1.80e-83 |
|
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: 268.86 E-value: 1.80e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 4 PLLRIDNLSIAF-------SKQDETRTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLLPSppvsypQGDILFHDR 76
Cdd:COG4172 274 PLLEARDLKVWFpikrglfRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPS------EGEIRFDGQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 77 SLLHADEQTLRGIRgNKIAMIFQEPMVSLNPLHSLEKQLYEVLSLHR-GMRKEAARGEILDCLERTGIRNAAkrLNDFPH 155
Cdd:COG4172 348 DLDGLSRRALRPLR-RRMQVVFQDPFGSLSPRMTVGQIIAEGLRVHGpGLSAAERRARVAEALEEVGLDPAA--RHRYPH 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGRC 235
Cdd:COG4172 425 EFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKV 504
|
250 260
....*....|....*....|....*....
gi 1278835479 236 VEQNAASTLLSAPQHPYTQRLLNSEPSGD 264
Cdd:COG4172 505 VEQGPTEQVFDAPQHPYTRALLAAAPLLE 533
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
273-528 |
2.47e-83 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 259.38 E-value: 2.47e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 273 TPLLRVEDLSVSFPIRKGILRRivDRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGM 347
Cdd:COG4167 2 SALLEVRNLSKTFKYRTGLFRR--QQFEAVKPVSFTLEAGQTLAIIGENGSGKST----LAKMLAgiiepTSGEILINGH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 348 PLHRWNRRQmlpvRP---RMqvVFQDPNSSLNPRLSVLQIVEEGLRVHQpGLSAQQREQEVMRVMVEVGLDPETRHRYPA 424
Cdd:COG4167 76 KLEYGDYKY----RCkhiRM--IFQDPNTSLNPRLNIGQILEEPLRLNT-DLTAEEREERIFATLRLVGLLPEHANFYPH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 425 EFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEV 504
Cdd:COG4167 149 MLSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEV 228
|
250 260
....*....|....*....|....
gi 1278835479 505 VEQGECQRVFSAPTQRYTRQLLSS 528
Cdd:COG4167 229 VEYGKTAEVFANPQHEVTKRLIES 252
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-259 |
1.34e-81 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 254.34 E-value: 1.34e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 5 LLRIDNLSIAFSKQDETRTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLLP--SPPVSypqGDILFHDRSLLHAD 82
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKS----TLLRALAglERPWS---GEVTFDGRPVTRRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 83 EQTLRGirgnKIAMIFQEPMVSLNPLHSLEKQLYEVLSLHRGMRKEAargEILDCLERTGIRNAAkrLNDFPHQLSGGER 162
Cdd:COG1124 74 RKAFRR----RVQMVFQDPYASLHPRHTVDRILAEPLRIHGLPDREE---RIAELLEQVGLPPSF--LDRYPHQLSGGQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 163 QRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGRCVEQNAAS 242
Cdd:COG1124 145 QRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVA 224
|
250
....*....|....*..
gi 1278835479 243 TLLSAPQHPYTQRLLNS 259
Cdd:COG1124 225 DLLAGPKHPYTRELLAA 241
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
270-528 |
1.71e-78 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 249.62 E-value: 1.71e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 270 ADSTPLLRVEDLSVSFPIR--------KGILRRIVDrnpvlkNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQG 340
Cdd:PRK15079 3 EGKKVLLEVADLKVHFDIKdgkqwfwqPPKTLKAVD------GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVkATDG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 341 EILFDGMPLHRWNRRQMLPVRPRMQVVFQDPNSSLNPRLSVLQIVEEGLRVHQPGLSAQQREQEVMRVMVEVGLDPETRH 420
Cdd:PRK15079 77 EVAWLGKDLLGMKDDEWRAVRSDIQMIFQDPLASLNPRMTIGEIIAEPLRTYHPKLSRQEVKDRVKAMMLKVGLLPNLIN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 421 RYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLR 500
Cdd:PRK15079 157 RYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMY 236
|
250 260
....*....|....*....|....*...
gi 1278835479 501 QGEVVEQGECQRVFSAPTQRYTRQLLSS 528
Cdd:PRK15079 237 LGHAVELGTYDEVYHNPLHPYTKALMSA 264
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
271-528 |
2.07e-78 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 249.11 E-value: 2.07e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 271 DSTPLLRVEDLSVSFPIRKGILR--RIVDrnpVLKNIRFSLRPGESLGLVGESGSGKSTTGlALLRLI--ASQGEILFDG 346
Cdd:PRK11308 1 SQQPLLQAIDLKKHYPVKRGLFKpeRLVK---ALDGVSFTLERGKTLAVVGESGCGKSTLA-RLLTMIetPTGGELYYQG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 347 MPLHRWNRRQMLPVRPRMQVVFQDPNSSLNPRLSVLQIVEEGLRVHQPgLSAQQREQEVMRVMVEVGLDPETRHRYPAEF 426
Cdd:PRK11308 77 QDLLKADPEAQKLLRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINTS-LSAAERREKALAMMAKVGLRPEHYDRYPHMF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 427 SGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVE 506
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVE 235
|
250 260
....*....|....*....|..
gi 1278835479 507 QGECQRVFSAPTQRYTRQLLSS 528
Cdd:PRK11308 236 KGTKEQIFNNPRHPYTQALLSA 257
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
5-261 |
1.60e-76 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 244.27 E-value: 1.60e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 5 LLRIDNLSIAFSKQDETRTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLLPSP-PVSYPQgdILFHDRSLLHADE 83
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPgRVMAEK--LEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 84 QTLRGIRGNKIAMIFQEPMVSLNPLHSLEKQLYEVLSLHRGMRKEAARGEILDCLERTGIRNAAKRLNDFPHQLSGGERQ 163
Cdd:PRK11022 81 KERRNLVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLDVYPHQLSGGMSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 164 RVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGRCVEQNAAST 243
Cdd:PRK11022 161 RVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHD 240
|
250
....*....|....*...
gi 1278835479 244 LLSAPQHPYTQRLLNSEP 261
Cdd:PRK11022 241 IFRAPRHPYTQALLRALP 258
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-265 |
6.69e-67 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 219.07 E-value: 6.69e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 1 MTQPLLRIDNL------SIAFSKQDETRTVVSDLTLQIQRGETLALVGESGSGKSVSAlsilRLLP--SPPVSypqGDIL 72
Cdd:PRK11308 1 SQQPLLQAIDLkkhypvKRGLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLA----RLLTmiETPTG---GELY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 73 FHDRSLLHADEQTLRGIRgNKIAMIFQEPMVSLNPLHSLEKQLYEVLSLHRGMRKEAARGEILDCLERTGIR-NAAKRln 151
Cdd:PRK11308 74 YQGQDLLKADPEAQKLLR-QKIQIVFQNPYGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLRpEHYDR-- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 152 dFPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQ 231
Cdd:PRK11308 151 -YPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMY 229
|
250 260 270
....*....|....*....|....*....|....
gi 1278835479 232 NGRCVEQNAASTLLSAPQHPYTQRLLNSEPSGDP 265
Cdd:PRK11308 230 LGRCVEKGTKEQIFNNPRHPYTQALLSATPRLNP 263
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
269-528 |
2.75e-65 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 214.97 E-value: 2.75e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 269 DADSTPLLRVEDLSVSFPIRKGILRRIVDRNpvlknirFSLRPGESLGLVGESGSGKSTTGLALLRLIASQGEI----LF 344
Cdd:PRK09473 6 QQQADALLDVKDLRVTFSTPDGDVTAVNDLN-------FSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIggsaTF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 345 DGMPLHRWNRRQMLPVRP-RMQVVFQDPNSSLNPRLSVLQIVEEGLRVHQpGLSAQQREQEVMRVMVEVGLdPETRHR-- 421
Cdd:PRK09473 79 NGREILNLPEKELNKLRAeQISMIFQDPMTSLNPYMRVGEQLMEVLMLHK-GMSKAEAFEESVRMLDAVKM-PEARKRmk 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 422 -YPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLR 500
Cdd:PRK09473 157 mYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMY 236
|
250 260
....*....|....*....|....*...
gi 1278835479 501 QGEVVEQGECQRVFSAPTQRYTRQLLSS 528
Cdd:PRK09473 237 AGRTMEYGNARDVFYQPSHPYSIGLLNA 264
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
4-267 |
1.28e-61 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 205.52 E-value: 1.28e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 4 PLLRIDNLSIAFSKQDETRTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLL-PSPPVSypqGDIL-FHDRSLLHA 81
Cdd:COG4170 2 PLLDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITkDNWHVT---ADRFrWNGIDLLKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 82 DEQTLRGIRGNKIAMIFQEPMVSLNPLHSLEKQLYEVL--SLHRGM---RKEAARGEILDCLERTGIRNAAKRLNDFPHQ 156
Cdd:COG4170 79 SPRERRKIIGREIAMIFQEPSSCLDPSAKIGDQLIEAIpsWTFKGKwwqRFKWRKKRAIELLHRVGIKDHKDIMNSYPHE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGRCV 236
Cdd:COG4170 159 LTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTV 238
|
250 260 270
....*....|....*....|....*....|..
gi 1278835479 237 EQNAASTLLSAPQHPYTQRLLNSEPS-GDPVP 267
Cdd:COG4170 239 ESGPTEQILKSPHHPYTKALLRSMPDfRQPLP 270
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
271-508 |
4.37e-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: 200.98 E-value: 4.37e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 271 DSTPLLRVEDLSVSFpirkgilrrivDRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFD 345
Cdd:COG1127 1 MSEPMIEVRNLTKSF-----------GDRVVLDGVSLDVPRGEILAIIGGSGSGKSV----LLKLIIgllrpDSGEILVD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 346 GMPLHRWNRRQMLPVRPRMQVVFQDP---NSslnprLSVLQIVEEGLRVHqPGLSAQQREQEVMRVMVEVGLdPETRHRY 422
Cdd:COG1127 66 GQDITGLSEKELYELRRRIGMLFQGGalfDS-----LTVFENVAFPLREH-TDLSEAEIRELVLEKLELVGL-PGAADKM 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 423 PAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQG 502
Cdd:COG1127 139 PSELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADG 218
|
....*.
gi 1278835479 503 EVVEQG 508
Cdd:COG1127 219 KIIAEG 224
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
275-507 |
4.48e-61 |
|
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: 201.96 E-value: 4.48e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 275 LLRVEDLSVSFpiRKGILRRIVDRNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIA-SQGEILFDGMPLHRWN 353
Cdd:TIGR02769 2 LLEVRDVTHTY--RTGGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKpAQGTVSFRGQDLYQLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 354 RRQMLPVRPRMQVVFQDPNSSLNPRLSVLQIVEEGLRvHQPGLSAQQREQEVMRVMVEVGLDPETRHRYPAEFSGGQRQR 433
Cdd:TIGR02769 80 RKQRRAFRRDVQLVFQDSPSAVNPRMTVRQIIGEPLR-HLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1278835479 434 IAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQ 507
Cdd:TIGR02769 159 INIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEE 232
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
273-520 |
2.89e-59 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 197.22 E-value: 2.89e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 273 TPLLRVEDLSVSFpiRKGILRRIVDRNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIA-SQGEILFDGMPLHR 351
Cdd:PRK10419 1 MTLLNVSGLSHHY--AHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESpSQGNVSWRGEPLAK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 352 WNRRQMLPVRPRMQVVFQDPNSSLNPRLSVLQIVEEGLRvHQPGLSAQQREQEVMRVMVEVGLDPETRHRYPAEFSGGQR 431
Cdd:PRK10419 79 LNRAQRKAFRRDIQMVFQDSISAVNPRKTVREIIREPLR-HLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 432 QRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQ---G 508
Cdd:PRK10419 158 QRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETqpvG 237
|
250
....*....|..
gi 1278835479 509 ECQRvFSAPTQR 520
Cdd:PRK10419 238 DKLT-FSSPAGR 248
|
|
| PhnK |
COG4107 |
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and ... |
3-259 |
5.99e-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: 5.99e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 3 QPLLRIDNLSIAFSKQDETRTVVSDLTLQIQRGETLALVGESGSGKS--VSALSiLRLLPSppvsypQGDILFHDR---- 76
Cdd:COG4107 6 QPLLSVRGLSKRYGPGCGTVVACRDVSFDLYPGEVLGIVGESGSGKStlLKCLY-FDLAPT------SGSVYYRDRdggp 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 77 -SLLHADEQTLRGIRGNKIAMIFQEPMVSLNPLHSLEKQLYEVLsLHRGMRK-EAARGEILDCLERTGIrnAAKRLNDFP 154
Cdd:COG4107 79 rDLFALSEAERRRLRRTDWGMVYQNPRDGLRMDVSAGGNIAERL-MAAGERHyGDIRARALEWLERVEI--PLERIDDLP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 155 HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGR 234
Cdd:COG4107 156 RTFSGGMQQRVQIARALVTNPRLLFLDEPTTGLDVSVQARLLDLIRRLQRELGLSMIVVTHDLGVIRLLADRTMVMKNGR 235
|
250 260
....*....|....*....|....*
gi 1278835479 235 CVEQNAASTLLSAPQHPYTQRLLNS 259
Cdd:COG4107 236 VVESGLTDQVLEDPQHPYTQLLVSS 260
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
272-529 |
6.93e-59 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 203.78 E-value: 6.93e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 272 STPLLRVEDLSVSFPiRKGILRRIVDrnpvlkNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIAS------QGEILFD 345
Cdd:PRK15134 2 TQPLLAIENLSVAFR-QQQTVRTVVN------DVSLQIEAGETLALVGESGSGKSVTALSILRLLPSppvvypSGDIRFH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 346 GMPLHRWNRRQMLPVR-PRMQVVFQDPNSSLNPRLSVLQIVEEGLRVHQpGLSAQQREQEVMRVMVEVGL-DPETR-HRY 422
Cdd:PRK15134 75 GESLLHASEQTLRGVRgNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHR-GMRREAARGEILNCLDRVGIrQAAKRlTDY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 423 PAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQG 502
Cdd:PRK15134 154 PHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNG 233
|
250 260
....*....|....*....|....*..
gi 1278835479 503 EVVEQGECQRVFSAPTQRYTRQLLSSD 529
Cdd:PRK15134 234 RCVEQNRAATLFSAPTHPYTQKLLNSE 260
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
276-517 |
1.19e-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: 194.09 E-value: 1.19e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 276 LRVEDLSVSFPirkgilrrivDRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLH 350
Cdd:COG1122 1 IELENLSFSYP----------GGTPALDDVSLSIEKGEFVAIIGPNGSGKST----LLRLLNgllkpTSGEVLVDGKDIT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 351 RWNRRQmlpVRPRMQVVFQDPNSSLnprlsVLQIVEE----GLRvhQPGLSAQQREQEVMRVMVEVGLDpETRHRYPAEF 426
Cdd:COG1122 67 KKNLRE---LRRKVGLVFQNPDDQL-----FAPTVEEdvafGPE--NLGLPREEIRERVEEALELVGLE-HLADRPPHEL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 427 SGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRQGEVVE 506
Cdd:COG1122 136 SGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGK-TVIIVTHDLDLVAELADRVIVLDDGRIVA 214
|
250
....*....|.
gi 1278835479 507 QGECQRVFSAP 517
Cdd:COG1122 215 DGTPREVFSDY 225
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
3-265 |
1.81e-58 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 197.24 E-value: 1.81e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 3 QPLLRIDNLSIAFSKQD---------ETRTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLLPSPpvsypQGDILF 73
Cdd:PRK15079 6 KVLLEVADLKVHFDIKDgkqwfwqppKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKAT-----DGEVAW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 74 HDRSLLHADEQTLRGIRgNKIAMIFQEPMVSLNPLHSLEKQLYEVL-SLHRGMRKEAARGEILDCLERTGIRnaAKRLND 152
Cdd:PRK15079 81 LGKDLLGMKDDEWRAVR-SDIQMIFQDPLASLNPRMTIGEIIAEPLrTYHPKLSRQEVKDRVKAMMLKVGLL--PNLINR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 153 FPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQN 232
Cdd:PRK15079 158 YPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYL 237
|
250 260 270
....*....|....*....|....*....|...
gi 1278835479 233 GRCVEQNAASTLLSAPQHPYTQRLLNSEPSGDP 265
Cdd:PRK15079 238 GHAVELGTYDEVYHNPLHPYTKALMSAVPIPDP 270
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
6-257 |
2.99e-58 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 194.15 E-value: 2.99e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 6 LRIDNLSIAfskqdETRTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLLPsPPVSYPQGDILFHDRSLLHADeqt 85
Cdd:PRK10418 5 IELRNIALQ-----AAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILP-AGVRQTAGRVLLDGKPVAPCA--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 86 lrgIRGNKIAMIFQEPMVSLNPLHSLEKQLYEVLslhRGMRKEAARGEILDCLERTGIRNAAKRLNDFPHQLSGGERQRV 165
Cdd:PRK10418 76 ---LRGRKIATIMQNPRSAFNPLHTMHTHARETC---LALGKPADDATLTAALEAVGLENAARVLKLYPFEMSGGMLQRM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 166 MIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGRCVEQNAASTLL 245
Cdd:PRK10418 150 MIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLF 229
|
250
....*....|..
gi 1278835479 246 SAPQHPYTQRLL 257
Cdd:PRK10418 230 NAPKHAVTRSLV 241
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
275-528 |
2.55e-57 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 191.93 E-value: 2.55e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 275 LLRVEDLSVSFPIRKGILRRivDRNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIA-SQGEILFDGMPLHRWN 353
Cdd:PRK15112 4 LLEVRNLSKTFRYRTGWFRR--QTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEpTSGELLIDDHPLHFGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 354 ---RRQmlpvrpRMQVVFQDPNSSLNPRLSVLQIVEEGLRVHQpGLSAQQREQEVMRVMVEVGLDPETRHRYPAEFSGGQ 430
Cdd:PRK15112 82 ysyRSQ------RIRMIFQDPSTSLNPRQRISQILDFPLRLNT-DLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 431 RQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGEC 510
Cdd:PRK15112 155 KQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGST 234
|
250
....*....|....*...
gi 1278835479 511 QRVFSAPTQRYTRQLLSS 528
Cdd:PRK15112 235 ADVLASPLHELTKRLIAG 252
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
4-259 |
2.59e-57 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 191.97 E-value: 2.59e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 4 PLLRIDNLSIA-------FSKQDetRTVVSDLTLQIQRGETLALVGESGSGKSVSAlsilRLLPS--PPVSypqGDILFH 74
Cdd:COG4167 3 ALLEVRNLSKTfkyrtglFRRQQ--FEAVKPVSFTLEAGQTLAIIGENGSGKSTLA----KMLAGiiEPTS---GEILIN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 75 DRSLLHADEQTlrgiRGNKIAMIFQEPMVSLNPLHSLEKQLYEVLSLHRGMRKEAARGEILDCLERTGIRnaAKRLNDFP 154
Cdd:COG4167 74 GHKLEYGDYKY----RCKHIRMIFQDPNTSLNPRLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGLL--PEHANFYP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 155 HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGR 234
Cdd:COG4167 148 HMLSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGE 227
|
250 260
....*....|....*....|....*
gi 1278835479 235 CVEQNAASTLLSAPQHPYTQRLLNS 259
Cdd:COG4167 228 VVEYGKTAEVFANPQHEVTKRLIES 252
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
276-528 |
3.38e-56 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 191.44 E-value: 3.38e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 276 LRVEDLSVSFPIRKGILRrivdrnpVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEILFDGMPLH 350
Cdd:COG1135 2 IELENLSKTFPTKGGPVT-------ALDDVSLTIEKGEIFGIIGYSGAGKST----LIRCInllerPTSGSVLVDGVDLT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 351 RWNRRQMLPVRPRMQVVFQDPNssLNPRLSVLQIVEEGLRVHqpGLSAQQREQEVMRVMVEVGLDpETRHRYPAEFSGGQ 430
Cdd:COG1135 71 ALSERELRAARRKIGMIFQHFN--LLSSRTVAENVALPLEIA--GVPKAEIRKRVAELLELVGLS-DKADAYPSQLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 431 RQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGEC 510
Cdd:COG1135 146 KQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPV 225
|
250
....*....|....*...
gi 1278835479 511 QRVFSAPTQRYTRQLLSS 528
Cdd:COG1135 226 LDVFANPQSELTRRFLPT 243
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
273-507 |
4.09e-56 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 187.56 E-value: 4.09e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 273 TPLLRVEDLSVSFPIRKGilrrivdRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGM 347
Cdd:COG1136 2 SPLLELRNLTKSYGTGEG-------EVTALRGVSLSIEAGEFVAIVGPSGSGKST----LLNILGgldrpTSGEVLIDGQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 348 PLHRWNRRQMLPVRpRMQV--VFQDPNssLNPRLSVLQIVEEGLRVHqpGLSAQQREQEVMRVMVEVGLDpETRHRYPAE 425
Cdd:COG1136 71 DISSLSERELARLR-RRHIgfVFQFFN--LLPELTALENVALPLLLA--GVSRKERRERARELLERVGLG-DRLDHRPSQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 426 FSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVrALCHQVIVLRQGEVV 505
Cdd:COG1136 145 LSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELA-ARADRVIRLRDGRIV 223
|
..
gi 1278835479 506 EQ 507
Cdd:COG1136 224 SD 225
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
275-517 |
8.53e-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: 181.63 E-value: 8.53e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 275 LLRVEDLSVSFPIRKGILrrivdrnPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEILFDGMPL 349
Cdd:cd03258 1 MIELKNVSKVFGDTGGKV-------TALKDVSLSVPKGEIFGIIGRSGAGKST----LIRCInglerPTSGSVLVDGTDL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 350 HRWNRRQMLPVRPRMQVVFQDPNssLNPRLSVLQIVEEGLRVHqpGLSAQQREQEVMRVMVEVGLDpETRHRYPAEFSGG 429
Cdd:cd03258 70 TLLSGKELRKARRRIGMIFQHFN--LLSSRTVFENVALPLEIA--GVPKAEIEERVLELLELVGLE-DKADAYPAQLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 430 QRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGE 509
Cdd:cd03258 145 QKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGT 224
|
....*...
gi 1278835479 510 CQRVFSAP 517
Cdd:cd03258 225 VEEVFANP 232
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
275-528 |
9.99e-54 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 184.56 E-value: 9.99e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 275 LLRVEDLSVSFPIRKGILRrIVDRnpvlknIRFSLRPGESLGLVGESGSGKSTTGLALLRLIASQGEIL-----FDGMPL 349
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPFR-AVDR------ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVMaekleFNGQDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 350 HRWN---RRQMlpVRPRMQVVFQDPNSSLNPRLSV-LQIVEeGLRVHQPGlSAQQREQEVMRVMVEVGL-DPETR-HRYP 423
Cdd:PRK11022 76 QRISekeRRNL--VGAEVAMIFQDPMTSLNPCYTVgFQIME-AIKVHQGG-NKKTRRQRAIDLLNQVGIpDPASRlDVYP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 424 AEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGE 503
Cdd:PRK11022 152 HQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQ 231
|
250 260
....*....|....*....|....*
gi 1278835479 504 VVEQGECQRVFSAPTQRYTRQLLSS 528
Cdd:PRK11022 232 VVETGKAHDIFRAPRHPYTQALLRA 256
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
276-508 |
1.98e-53 |
|
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: 180.78 E-value: 1.98e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 276 LRVEDLSVSFpirkgilrrivDRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIASQ-----GEILFDGMPLH 350
Cdd:cd03261 1 IELRGLTKSF-----------GGRTVLKGVDLDVRRGEILAIIGPSGSGKST----LLRLIVGLlrpdsGEVLIDGEDIS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 351 RWNRRQMLPVRPRMQVVFQDpnSSLNPRLSVLQIVEEGLRVHQpGLSAQQREQEVMRVMVEVGLdPETRHRYPAEFSGGQ 430
Cdd:cd03261 66 GLSEAELYRLRRRMGMLFQS--GALFDSLTVFENVAFPLREHT-RLSEEEIREIVLEKLEAVGL-RGAEDLYPAELSGGM 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1278835479 431 RQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:cd03261 142 KKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEG 219
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
6-265 |
2.78e-53 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 183.74 E-value: 2.78e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 6 LRIDNLSIAFSKQDETRTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLL-----PSppvsypQGDILFHDRSLLH 80
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKS----TLIRCInllerPT------SGSVLVDGVDLTA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 81 ADEQTLRGIRGnKIAMIFQepmvSLNPLHS----------LEkqlyevlslHRGMRKEAARGEILDCLERTGIrnaAKRL 150
Cdd:COG1135 72 LSERELRAARR-KIGMIFQ----HFNLLSSrtvaenvalpLE---------IAGVPKAEIRKRVAELLELVGL---SDKA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 151 NDFPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVM 230
Cdd:COG1135 135 DAYPSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVL 214
|
250 260 270
....*....|....*....|....*....|....*
gi 1278835479 231 QNGRCVEQNAASTLLSAPQHPYTQRLLNSEPSGDP 265
Cdd:COG1135 215 ENGRIVEQGPVLDVFANPQSELTRRFLPTVLNDEL 249
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
275-527 |
1.03e-51 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 176.34 E-value: 1.03e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 275 LLRVEDLSVSFpirkgilrrivDRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPL 349
Cdd:COG1126 1 MIEIENLHKSF-----------GDLEVLKGISLDVEKGEVVVIIGPSGSGKST----LLRCINlleepDSGTITVDGEDL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 350 HRwNRRQMLPVRPRMQVVFQDPNssLNPRLSVLQIVEEGLRVHQpGLSAQQREQEVMRVMVEVGLdPETRHRYPAEFSGG 429
Cdd:COG1126 66 TD-SKKDINKLRRKVGMVFQQFN--LFPHLTVLENVTLAPIKVK-KMSKAEAEERAMELLERVGL-ADKADAYPAQLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 430 QRQRIAIARALILKPELIILDEPTSSLD-RTVqAQILALLKGLQEKHrLAYIFISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:COG1126 141 QQQRVAIARALAMEPKVMLFDEPTSALDpELV-GEVLDVMRDLAKEG-MTMVVVTHEMGFAREVADRVVFMDGGRIVEEG 218
|
250
....*....|....*....
gi 1278835479 509 ECQRVFSAPTQRYTRQLLS 527
Cdd:COG1126 219 PPEEFFENPQHERTRAFLS 237
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-238 |
1.22e-51 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 175.62 E-value: 1.22e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 3 QPLLRIDNLSIAFSKQDETRTVVSDLTLQIQRGETLALVGESGSGKSvSALSILRLL--PSppvsypQGDILFHDRSLLH 80
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKS-TLLNILGGLdrPT------SGEVLIDGQDISS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 81 ADEQTLRGIRGNKIAMIFQEPmvslnplhslekQLYEVLS---------LHRGMRKEAARGEILDCLERTGIrnaAKRLN 151
Cdd:COG1136 75 LSERELARLRRRHIGFVFQFF------------NLLPELTalenvalplLLAGVSRKERRERARELLERVGL---GDRLD 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 152 DFPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRkLADSVAVMQ 231
Cdd:COG1136 140 HRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAA-RADRVIRLR 218
|
....*..
gi 1278835479 232 NGRCVEQ 238
Cdd:COG1136 219 DGRIVSD 225
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
270-506 |
1.33e-51 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 176.82 E-value: 1.33e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 270 ADSTPLLRVEDLSVSFPIRKGilrrivdRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILF 344
Cdd:COG1116 2 SAAAPALELRGVSKRFPTGGG-------GVTALDDVSLTVAAGEFVALVGPSGCGKST----LLRLIAglekpTSGEVLV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 345 DGMPLHRwnrrqmlpVRPRMQVVFQDPnsSLNPRLSVLQIVEEGLRVHqpGLSAQQREQEVMRVMVEVGLDpETRHRYPA 424
Cdd:COG1116 71 DGKPVTG--------PGPDRGVVFQEP--ALLPWLTVLDNVALGLELR--GVPKAERRERARELLELVGLA-GFEDAYPH 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 425 EFSGGQRQRIAIARALILKPELIILDEPTSSLD----RTVQAQILALLkglqEKHRLAYIFISHDLQ--VvrALCHQVIV 498
Cdd:COG1116 138 QLSGGMRQRVAIARALANDPEVLLMDEPFGALDaltrERLQDELLRLW----QETGKTVLFVTHDVDeaV--FLADRVVV 211
|
250
....*....|
gi 1278835479 499 L--RQGEVVE 506
Cdd:COG1116 212 LsaRPGRIVE 221
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
276-504 |
2.32e-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: 174.60 E-value: 2.32e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 276 LRVEDLSVSFPIRKGilrrivdRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLH 350
Cdd:cd03255 1 IELKNLSKTYGGGGE-------KVQALKGVSLSIEKGEFVAIVGPSGSGKST----LLNILGgldrpTSGEVRVDGTDIS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 351 RWNRRQMLPVRPR-MQVVFQDPNssLNPRLSVLQIVEEGLRVHqpGLSAQQREQEVMRVMVEVGLDpETRHRYPAEFSGG 429
Cdd:cd03255 70 KLSEKELAAFRRRhIGFVFQSFN--LLPDLTALENVELPLLLA--GVPKKERRERAEELLERVGLG-DRLNHYPSELSGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1278835479 430 QRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRaLCHQVIVLRQGEV 504
Cdd:cd03255 145 QQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
275-518 |
2.78e-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: 175.62 E-value: 2.78e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 275 LLRVEDLSVSFpirkgilrrivDRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPL 349
Cdd:COG1120 1 MLEAENLSVGY-----------GGRPVLDDVSLSLPPGEVTALLGPNGSGKST----LLRALAgllkpSSGEVLLDGRDL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 350 HRWNRRQmlpVRPRMQVVFQDPNSSLNprLSVLQIVEEGLRVHQPGLSAQQRE--QEVMRVMVEVGLDpETRHRYPAEFS 427
Cdd:COG1120 66 ASLSRRE---LARRIAYVPQEPPAPFG--LTVRELVALGRYPHLGLFGRPSAEdrEAVEEALERTGLE-HLADRPVDELS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 428 GGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQ 507
Cdd:COG1120 140 GGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQ 219
|
250
....*....|.
gi 1278835479 508 GECQRVFSAPT 518
Cdd:COG1120 220 GPPEEVLTPEL 230
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
4-267 |
7.82e-51 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 176.92 E-value: 7.82e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 4 PLLRIDNLSIAFSKQDETRTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLlPSPPVSYPQGDILFHDRSLLHADE 83
Cdd:PRK15093 2 PLLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV-TKDNWRVTADRMRFDDIDLLRLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 84 QTLRGIRGNKIAMIFQEPMVSLNPLHSLEKQLYEVL--SLHRGM-------RKEAArgeiLDCLERTGIRNAAKRLNDFP 154
Cdd:PRK15093 81 RERRKLVGHNVSMIFQEPQSCLDPSERVGRQLMQNIpgWTYKGRwwqrfgwRKRRA----IELLHRVGIKDHKDAMRSFP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 155 HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGR 234
Cdd:PRK15093 157 YELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQ 236
|
250 260 270
....*....|....*....|....*....|....
gi 1278835479 235 CVEQNAASTLLSAPQHPYTQRLLNSEPS-GDPVP 267
Cdd:PRK15093 237 TVETAPSKELVTTPHHPYTQALIRAIPDfGSAMP 270
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
277-503 |
1.12e-50 |
|
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: 1.12e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 277 RVEDLSVSFPIRKgilrrivdrNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLHR 351
Cdd:cd03225 1 ELKNLSFSYPDGA---------RPALDDISLTIKKGEFVLIVGPNGSGKST----LLRLLNgllgpTSGEVLVDGKDLTK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 352 WNRRQmlpVRPRMQVVFQDPNSSL-NPRlsvlqiVEE----GLRvhQPGLSAQQREQEVMRVMVEVGLDpETRHRYPAEF 426
Cdd:cd03225 68 LSLKE---LRRKVGLVFQNPDDQFfGPT------VEEevafGLE--NLGLPEEEIEERVEEALELVGLE-GLRDRSPFTL 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1278835479 427 SGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRQGE 503
Cdd:cd03225 136 SGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGK-TIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
274-513 |
1.61e-50 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 173.32 E-value: 1.61e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 274 PLLRVEDLSVSFPirkgilrrivDRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMP 348
Cdd:COG3638 1 PMLELRNLSKRYP----------GGTPALDDVSLEIERGEFVALIGPSGAGKST----LLRCLNglvepTSGEILVDGQD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 349 LHRWNRRQMLPVRPRMQVVFQDPNssLNPRLSVLQIVEEGLRVHQPGL-------SAQQReQEVMRVMVEVGLDPETRHR 421
Cdd:COG3638 67 VTALRGRALRRLRRRIGMIFQQFN--LVPRLSVLTNVLAGRLGRTSTWrsllglfPPEDR-ERALEALERVGLADKAYQR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 422 yPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQ 501
Cdd:COG3638 144 -ADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRD 222
|
250
....*....|..
gi 1278835479 502 GEVVEQGECQRV 513
Cdd:COG3638 223 GRVVFDGPPAEL 234
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
276-507 |
5.14e-50 |
|
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: 171.12 E-value: 5.14e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 276 LRVEDLSVSFPIRKGilrrivdRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLH 350
Cdd:cd03293 1 LEVRNVSKTYGGGGG-------AVTALEDISLSVEEGEFVALVGPSGCGKST----LLRIIAglerpTSGEVLVDGEPVT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 351 RwnrrqmlpVRPRMQVVFQDPnsSLNPRLSVLQIVEEGLRVHqpGLSAQQREQEVMRVMVEVGLDpETRHRYPAEFSGGQ 430
Cdd:cd03293 70 G--------PGPDRGYVFQQD--ALLPWLTVLDNVALGLELQ--GVPKAEARERAEELLELVGLS-GFENAYPHQLSGGM 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1278835479 431 RQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVL--RQGEVVEQ 507
Cdd:cd03293 137 RQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVAE 215
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
272-521 |
2.67e-49 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 173.36 E-value: 2.67e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 272 STPLLRVEDLSVSFpirkgilrrivDRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDG 346
Cdd:COG3842 2 AMPALELENVSKRY-----------GDVTALDDVSLSIEPGEFVALLGPSGCGKTT----LLRMIAgfetpDSGRILLDG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 347 mplhrwnrRQMLPVRP---RMQVVFQDPnsSLNPRLSVLQIVEEGLRVHqpGLSAQQREQEVMRVMVEVGLDpETRHRYP 423
Cdd:COG3842 67 --------RDVTGLPPekrNVGMVFQDY--ALFPHLTVAENVAFGLRMR--GVPKAEIRARVAELLELVGLE-GLADRYP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 424 AEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGE 503
Cdd:COG3842 134 HQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGR 213
|
250
....*....|....*...
gi 1278835479 504 VVEQGECQRVFSAPTQRY 521
Cdd:COG3842 214 IEQVGTPEEIYERPATRF 231
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
276-508 |
1.83e-48 |
|
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: 166.93 E-value: 1.83e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 276 LRVEDLSVSFpirkgilrrivDRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLH 350
Cdd:cd03259 1 LELKGLSKTY-----------GSVRALDDLSLTVEPGEFLALLGPSGCGKTT----LLRLIAglerpDSGEILIDGRDVT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 351 RwnrrqmLPVRPR---MqvVFQDPnsSLNPRLSVLQIVEEGLRVHqpGLSAQQREQEVMRVMVEVGLDPEtRHRYPAEFS 427
Cdd:cd03259 66 G------VPPERRnigM--VFQDY--ALFPHLTVAENIAFGLKLR--GVPKAEIRARVRELLELVGLEGL-LNRYPHELS 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 428 GGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQ 507
Cdd:cd03259 133 GGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQV 212
|
.
gi 1278835479 508 G 508
Cdd:cd03259 213 G 213
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-505 |
1.89e-48 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 174.82 E-value: 1.89e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 2 TQPLLRIDNLSIAFSkqdeTRTVVSDLTLQIQRGETLALVGESGSGKS--VSALS-ILrllpsPPVSypqGDILFHDRsl 78
Cdd:COG1129 1 AEPLLEMRGISKSFG----GVKALDGVSLELRPGEVHALLGENGAGKStlMKILSgVY-----QPDS---GEILLDGE-- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 79 lhadEQTLRGIR---GNKIAMIFQEPmvslnplhSLEKQL--YEVLSL-----------HRGMRKEAARgeildCLERTG 142
Cdd:COG1129 67 ----PVRFRSPRdaqAAGIAIIHQEL--------NLVPNLsvAENIFLgreprrgglidWRAMRRRARE-----LLARLG 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 143 IR-NAAKRLNDfphqLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDElNMSLLFITHNLSIVR 221
Cdd:COG1129 130 LDiDPDTPVGD----LSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISHRLDEVF 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 222 KLADSVAVMQNGRCVEQNAASTLlsaPQHPYTQRLLNSEPSGD-PVPLDADSTPLLRVEDLSvsfpirkgilrrivdRNP 300
Cdd:COG1129 205 EIADRVTVLRDGRLVGTGPVAEL---TEDELVRLMVGRELEDLfPKRAAAPGEVVLEVEGLS---------------VGG 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 301 VLKNIRFSLRPGESLGLVGESGSGKSttglALLRLI-----ASQGEILFDGMPLHRWNRRQ-------MLPVRPRMQVVF 368
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRT----ELARALfgadpADSGEIRLDGKPVRIRSPRDairagiaYVPEDRKGEGLV 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 369 QDPNSSLNPRLSVLQiveeglRVHQPGLSAQQREQEVMRVMVE-VGLDPETRHRYPAEFSGGQRQRIAIARALILKPELI 447
Cdd:COG1129 343 LDLSIRENITLASLD------RLSRGGLLDRRRERALAEEYIKrLRIKTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVL 416
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1278835479 448 ILDEPTSSLDRTVQAQILALLKGLQEKhRLAYIFISHDLQVVRALCHQVIVLRQGEVV 505
Cdd:COG1129 417 ILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-518 |
2.02e-48 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 175.38 E-value: 2.02e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 6 LRIDNLSIAFskqdETRTVVSDLTLQIQRGETLALVGESGSGKSVsALSILRLLPS-PPVSypqGDILFH---------- 74
Cdd:TIGR03269 1 IEVKNLTKKF----DGKEVLKNISFTIEEGEVLGILGRSGAGKSV-LMHVLRGMDQyEPTS---GRIIYHvalcekcgyv 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 75 --------------------DRSLLHADEQTLRGIRgNKIAMIFQ-------EPMVSLNPLHSLEKQLYEvlslhrgmrK 127
Cdd:TIGR03269 73 erpskvgepcpvcggtlepeEVDFWNLSDKLRRRIR-KRIAIMLQrtfalygDDTVLDNVLEALEEIGYE---------G 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 128 EAARGEILDCLERTgirNAAKRLNDFPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELN 207
Cdd:TIGR03269 143 KEAVGRAVDLIEMV---QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 208 MSLLFITHNLSIVRKLADSVAVMQNGRCVEQNAASTLLSApqhpYTQRLlnSEPSGDPVPLDADstPLLRVEDLSVSF-P 286
Cdd:TIGR03269 220 ISMVLTSHWPEVIEDLSDKAIWLENGEIKEEGTPDEVVAV----FMEGV--SEVEKECEVEVGE--PIIKVRNVSKRYiS 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 287 IRKGILrRIVDrnpvlkNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEILF-------DGMPLHRWNRRQml 358
Cdd:TIGR03269 292 VDRGVV-KAVD------NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLePTSGEVNVrvgdewvDMTKPGPDGRGR-- 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 359 pVRPRMQVVFQDpnSSLNPRLSVLQIVEEGLRVHQPGLSAQQReqeVMRVMVEVGLDPETR----HRYPAEFSGGQRQRI 434
Cdd:TIGR03269 363 -AKRYIGILHQE--YDLYPHRTVLDNLTEAIGLELPDELARMK---AVITLKMVGFDEEKAeeilDKYPDELSEGERHRV 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 435 AIARALILKPELIILDEPTSSLD----RTVQAQILALLKGLQEkhrlAYIFISHDLQVVRALCHQVIVLRQGEVVEQGEC 510
Cdd:TIGR03269 437 ALAQVLIKEPRIVILDEPTGTMDpitkVDVTHSILKAREEMEQ----TFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDP 512
|
....*...
gi 1278835479 511 QRVFSAPT 518
Cdd:TIGR03269 513 EEIVEELT 520
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-257 |
1.08e-47 |
|
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: 165.54 E-value: 1.08e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 1 MTQPLLRIDNLSIAFskqdETRTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLLpsPPVSypqGDILFHDRSLLH 80
Cdd:COG1127 1 MSEPMIEVRNLTKSF----GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLL--RPDS---GEILVDGQDITG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 81 ADEQTLRGIRgNKIAMIFQEPMV--SLNPLHSLEKQLYEvlslHRGMRKEAARGEILDCLERTGIRNAAKRlndFPHQLS 158
Cdd:COG1127 72 LSEKELYELR-RRIGMLFQGGALfdSLTVFENVAFPLRE----HTDLSEAEIRELVLEKLELVGLPGAADK---MPSELS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 159 GGERQRVMIAMALLTRPELLIADEPTTALD-VTVqAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGRCVE 237
Cdd:COG1127 144 GGMRKRVALARALALDPEILLYDEPTAGLDpITS-AVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIA 222
|
250 260
....*....|....*....|
gi 1278835479 238 QNAASTLLSAPqHPYTQRLL 257
Cdd:COG1127 223 EGTPEELLASD-DPWVRQFL 241
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
276-508 |
2.87e-47 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 164.47 E-value: 2.87e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 276 LRVEDLSVSFpirkgilrrivDRNPVLKNIRFSLRPGESLGLVGESGSGKSTTglalLRLIA-----SQGEILFDGMPLH 350
Cdd:COG1131 1 IEVRGLTKRY-----------GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTT----IRMLLgllrpTSGEVRVLGEDVA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 351 RWNRRqmlpVRPRMQVVFQDPNssLNPRLSVLQIVEEGLRVHqpGLSAQQREQEVMRVMVEVGLDpETRHRYPAEFSGGQ 430
Cdd:COG1131 66 RDPAE----VRRRIGYVPQEPA--LYPDLTVRENLRFFARLY--GLPRKEARERIDELLELFGLT-DAADRKVGTLSGGM 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1278835479 431 RQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLayIFIS-HDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:COG1131 137 KQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKT--VLLStHYLEEAERLCDRVAIIDKGRIVADG 213
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-234 |
4.23e-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: 163.43 E-value: 4.23e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 6 LRIDNLSIAFSKQDETRTVVSDLTLQIQRGETLALVGESGSGKSvSALSILRLLpSPPVSypqGDILFHDRSLLHADEQT 85
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKS-TLLNILGGL-DRPTS---GEVRVDGTDISKLSEKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 86 LRGIRGNKIAMIFQEpmvslnplHSLEKQL--YEVLSL---HRGMRKEAARGEILDCLERTGIrnaAKRLNDFPHQLSGG 160
Cdd:cd03255 76 LAAFRRRHIGFVFQS--------FNLLPDLtaLENVELpllLAGVPKKERRERAEELLERVGL---GDRLNHYPSELSGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1278835479 161 ERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRkLADSVAVMQNGR 234
Cdd:cd03255 145 QQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGK 217
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-265 |
2.53e-46 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 171.19 E-value: 2.53e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 3 QPLLRIDNLSIAFSKQDE-----TRTV--VSDLTLQIQRGETLALVGESGSGKSVSALSILRLLPSPpvsypQGDILFHD 75
Cdd:PRK10261 311 EPILQVRNLVTRFPLRSGllnrvTREVhaVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQ-----GGEIIFNG 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 76 RSLLHADEQTLRGIRGNkIAMIFQEPMVSLNPLHSLEKQLYEVLSLHRGMRKEAARGEILDCLERTGIR-NAAKRlndFP 154
Cdd:PRK10261 386 QRIDTLSPGKLQALRRD-IQFIFQDPYASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLpEHAWR---YP 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 155 HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGR 234
Cdd:PRK10261 462 HEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQ 541
|
250 260 270
....*....|....*....|....*....|.
gi 1278835479 235 CVEQNAASTLLSAPQHPYTQRLLNSEPSGDP 265
Cdd:PRK10261 542 IVEIGPRRAVFENPQHPYTRKLMAAVPVADP 572
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
276-509 |
5.64e-46 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 160.60 E-value: 5.64e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 276 LRVEDLSVSFPirkgilrrivDRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLH 350
Cdd:COG2884 2 IRFENVSKRYP----------GGREALSDVSLEIEKGEFVFLTGPSGAGKST----LLKLLYgeerpTSGQVLVNGQDLS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 351 RWNRRQMLPVRPRMQVVFQDPNssLNPRLSVLQIVEEGLRVHqpGLSAQQREQEVMRVMVEVGLDpETRHRYPAEFSGGQ 430
Cdd:COG2884 68 RLKRREIPYLRRRIGVVFQDFR--LLPDRTVYENVALPLRVT--GKSRKEIRRRVREVLDLVGLS-DKAKALPHELSGGE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 431 RQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLqekHRL--AYIFISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:COG2884 143 QQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEI---NRRgtTVLIATHDLELVDRMPKRVLELEDGRLVRDE 219
|
.
gi 1278835479 509 E 509
Cdd:COG2884 220 A 220
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
271-518 |
6.04e-46 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 161.02 E-value: 6.04e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 271 DSTPLLRVEDLSVSFpirkgilrrivDRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFD 345
Cdd:COG1121 2 MMMPAIELENLTVSY-----------GGRPVLEDVSLTIPPGEFVAIVGPNGAGKST----LLKAILgllppTSGTVRLF 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 346 GMPLHRWNRR-----QMLPVRPRMqvvfqdpnsslnPrLSVLQIVEEGLRVHQP---GLSAQQREQeVMRVMVEVGLDpE 417
Cdd:COG1121 67 GKPPRRARRRigyvpQRAEVDWDF------------P-ITVRDVVLMGRYGRRGlfrRPSRADREA-VDEALERVGLE-D 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 418 TRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQeKHRLAYIFISHDLQVVRALCHQVI 497
Cdd:COG1121 132 LADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELR-REGKTILVVTHDLGAVREYFDRVL 210
|
250 260
....*....|....*....|.
gi 1278835479 498 VLRQGeVVEQGECQRVFSAPT 518
Cdd:COG1121 211 LLNRG-LVAHGPPEEVLTPEN 230
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-249 |
9.30e-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: 160.05 E-value: 9.30e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 5 LLRIDNLSIAFSKQDETRTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLL-----PSppvsypQGDILFHDRSLL 79
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKS----TLIRCInglerPT------SGSVLVDGTDLT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 80 HADEQTLRGIRgNKIAMIFQEpmvsLNPLHSleKQLYEVLSL---HRGMRKEAARGEILDCLERTGIRNAAKRlndFPHQ 156
Cdd:cd03258 71 LLSGKELRKAR-RRIGMIFQH----FNLLSS--RTVFENVALpleIAGVPKAEIEERVLELLELVGLEDKADA---YPAQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGRCV 236
Cdd:cd03258 141 LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVV 220
|
250
....*....|...
gi 1278835479 237 EQNAASTLLSAPQ 249
Cdd:cd03258 221 EEGTVEEVFANPQ 233
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
270-528 |
4.53e-45 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 159.32 E-value: 4.53e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 270 ADSTPLLRVEDLSVSFPIRKGilrrivdrnpvLKNIRFSLRPGESLGLVGESGSGKSTTgLALL--RLIASQGEILFDG- 346
Cdd:PRK11701 1 MMDQPLLSVRGLTKLYGPRKG-----------CRDVSFDLYPGEVLGIVGESGSGKTTL-LNALsaRLAPDAGEVHYRMr 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 347 ----MPLHRWN--RRQMLpVRPRMQVVFQDPNSSLNPRLSVlqiveeGLRVHQPGLSAQQR-----EQEVMRVMVEVGLD 415
Cdd:PRK11701 69 dgqlRDLYALSeaERRRL-LRTEWGFVHQHPRDGLRMQVSA------GGNIGERLMAVGARhygdiRATAGDWLERVEID 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 416 PETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQ 495
Cdd:PRK11701 142 AARIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHR 221
|
250 260 270
....*....|....*....|....*....|...
gi 1278835479 496 VIVLRQGEVVEQGECQRVFSAPTQRYTRQLLSS 528
Cdd:PRK11701 222 LLVMKQGRVVESGLTDQVLDDPQHPYTQLLVSS 254
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-259 |
8.78e-45 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 158.55 E-value: 8.78e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 1 MTQPLLRIDNLSIAFSkqdeTRTVVSDLTLQIQRGETLALVGESGSGKS--VSALSiLRLLPSppvsypQGDILFHDRS- 77
Cdd:PRK11701 2 MDQPLLSVRGLTKLYG----PRKGCRDVSFDLYPGEVLGIVGESGSGKTtlLNALS-ARLAPD------AGEVHYRMRDg 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 78 ----LLHADEQTLRGIRGNKIAMIFQEPMVSLNPLHS----LEKQLYEVLSLHRGMRKEAArgeiLDCLERTGIrnAAKR 149
Cdd:PRK11701 71 qlrdLYALSEAERRRLLRTEWGFVHQHPRDGLRMQVSaggnIGERLMAVGARHYGDIRATA----GDWLERVEI--DAAR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 150 LNDFPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAV 229
Cdd:PRK11701 145 IDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLV 224
|
250 260 270
....*....|....*....|....*....|
gi 1278835479 230 MQNGRCVEQNAASTLLSAPQHPYTQRLLNS 259
Cdd:PRK11701 225 MKQGRVVESGLTDQVLDDPQHPYTQLLVSS 254
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
276-526 |
9.88e-44 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 158.39 E-value: 9.88e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 276 LRVEDLSVSFPirkgilrrivdRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLH 350
Cdd:COG1118 3 IEVRNISKRFG-----------SFTLLDDVSLEIASGELVALLGPSGSGKTT----LLRIIAgletpDSGRIVLNGRDLF 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 351 RWnrrqmLPVRPRmQV--VFQDPnsSLNPRLSVLQIVEEGLRVHQPglSAQQREQEVMRVMVEVGLDpETRHRYPAEFSG 428
Cdd:COG1118 68 TN-----LPPRER-RVgfVFQHY--ALFPHMTVAENIAFGLRVRPP--SKAEIRARVEELLELVQLE-GLADRYPSQLSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 429 GQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:COG1118 137 GQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVG 216
|
250
....*....|....*...
gi 1278835479 509 ECQRVFSAPTQRYTRQLL 526
Cdd:COG1118 217 TPDEVYDRPATPFVARFL 234
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
297-508 |
1.44e-43 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 164.62 E-value: 1.44e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 297 DRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLHRWNRRQmlpVRPRMQVVFQDP 371
Cdd:COG2274 486 DSPPVLDNISLTIKPGERVAIVGRSGSGKST----LLKLLLglyepTSGRILIDGIDLRQIDPAS---LRRQIGVVLQDV 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 372 ---NSSlnprlsvlqiVEEGLRVHQPGLSaqqrEQEVMRVMVEVGLDPETRHRyP-----------AEFSGGQRQRIAIA 437
Cdd:COG2274 559 flfSGT----------IRENITLGDPDAT----DEEIIEAARLAGLHDFIEAL-PmgydtvvgeggSNLSGGQRQRLAIA 623
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1278835479 438 RALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLayIFISHDLQVVRaLCHQVIVLRQGEVVEQG 508
Cdd:COG2274 624 RALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTV--IIIAHRLSTIR-LADRIIVLDKGRIVEDG 691
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-505 |
5.51e-43 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 159.81 E-value: 5.51e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 1 MTQPLLRIDNLSIAFSkqdetrTVV--SDLTLQIQRGETLALVGESGSGKS--VSalsilrllpsppvsypqgdILFhdr 76
Cdd:COG3845 1 MMPPALELRGITKRFG------GVVanDDVSLTVRPGEIHALLGENGAGKStlMK-------------------ILY--- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 77 SLLHADEQTLRgIRGNK-------------IAMIFQEPMvslnplhslekqLYEVLS------------LHRGMRKEAAR 131
Cdd:COG3845 53 GLYQPDSGEIL-IDGKPvrirsprdaialgIGMVHQHFM------------LVPNLTvaenivlgleptKGGRLDRKAAR 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 132 GEILDCLERTGIR-NAAKRLndfpHQLSGGERQRVMIAMALLTRPELLIADEPTTALdvTVQ--AQILTLLRDLRDElNM 208
Cdd:COG3845 120 ARIRELSERYGLDvDPDAKV----EDLSVGEQQRVEILKALYRGARILILDEPTAVL--TPQeaDELFEILRRLAAE-GK 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 209 SLLFITHNLSIVRKLADSVAVMQNGRCV-EQNAASTllsapqhpyTQRLLNSEPSGDPVPLDADSTP------LLRVEDL 281
Cdd:COG3845 193 SIIFITHKLREVMAIADRVTVLRRGKVVgTVDTAET---------SEEELAELMVGREVLLRVEKAPaepgevVLEVENL 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 282 SVsfPIRKGIlrrivdrnPVLKNIRFSLRPGESLGLVGESGSGKSttglALLRLIA-----SQGEILFDGMPLHRWNRRQ 356
Cdd:COG3845 264 SV--RDDRGV--------PALKDVSLEVRAGEILGIAGVAGNGQS----ELAEALAglrppASGSIRLDGEDITGLSPRE 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 357 MLpvrpRMQVVF--QDPNSS-LNPRLSvlqiVEEGL---RVHQPGLS---------AQQREQEVMRVM-VEVGlDPETRH 420
Cdd:COG3845 330 RR----RLGVAYipEDRLGRgLVPDMS----VAENLilgRYRRPPFSrggfldrkaIRAFAEELIEEFdVRTP-GPDTPA 400
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 421 RypaEFSGGQRQRIAIARALILKPELIILDEPTSSLD----RTVQAQILALL-KGlqekhrLAYIFISHDLQVVRALCHQ 495
Cdd:COG3845 401 R---SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDvgaiEFIHQRLLELRdAG------AAVLLISEDLDEILALSDR 471
|
570
....*....|
gi 1278835479 496 VIVLRQGEVV 505
Cdd:COG3845 472 IAVMYEGRIV 481
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
275-509 |
1.27e-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: 152.32 E-value: 1.27e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 275 LLRVEDLSVSFpirkgilrrivDRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPL 349
Cdd:COG4555 1 MIEVENLSKKY-----------GKVPALKDVSFTAKDGEITGLLGPNGAGKTT----LLRMLAgllkpDSGSILIDGEDV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 350 HRWNRRqmlpVRPRMQVVFQDPNssLNPRLSVLQIVEEGLRVHqpGLSAQQREQEVMRVMVEVGLDpETRHRYPAEFSGG 429
Cdd:COG4555 66 RKEPRE----ARRQIGVLPDERG--LYDRLTVRENIRYFAELY--GLFDEELKKRIEELIELLGLE-EFLDRRVGELSTG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 430 QRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRQGEVVEQGE 509
Cdd:COG4555 137 MKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGK-TVLFSSHIMQEVEALCDRVVILHKGKVVAQGS 215
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
6-249 |
1.44e-42 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 151.72 E-value: 1.44e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 6 LRIDNLSiaFSKQDETRtVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLL-----PSppvsypQGDILFHDRSLlh 80
Cdd:COG1122 1 IELENLS--FSYPGGTP-ALDDVSLSIEKGEFVAIIGPNGSGKS----TLLRLLngllkPT------SGEVLVDGKDI-- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 81 aDEQTLRGIRgNKIAMIFQEPmvslnplhslEKQLYE--VLS------LHRGMRKEAARGEILDCLERTGIRNAAKRlnd 152
Cdd:COG1122 66 -TKKNLRELR-RKVGLVFQNP----------DDQLFAptVEEdvafgpENLGLPREEIRERVEEALELVGLEHLADR--- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 153 FPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDElNMSLLFITHNLSIVRKLADSVAVMQN 232
Cdd:COG1122 131 PPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDD 209
|
250
....*....|....*..
gi 1278835479 233 GRCVEQNAASTLLSAPQ 249
Cdd:COG1122 210 GRIVADGTPREVFSDYE 226
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
7-279 |
1.84e-42 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 154.57 E-value: 1.84e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 7 RIDNLSIAFSKQDETRTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLL-----PSppvsypQGDILFHDRSLLHA 81
Cdd:PRK11153 3 ELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKS----TLIRCInllerPT------SGRVLVDGQDLTAL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 82 DEQTLRGIRgNKIAMIFQEpmvsLNPLHSleKQLYEVLSLH---RGMRKEAARGEILDCLERTGIrnAAKRlNDFPHQLS 158
Cdd:PRK11153 73 SEKELRKAR-RQIGMIFQH----FNLLSS--RTVFDNVALPlelAGTPKAEIKARVTELLELVGL--SDKA-DRYPAQLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 159 GGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGRCVEQ 238
Cdd:PRK11153 143 GGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQ 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1278835479 239 NAASTLLSAPQHPYTQRLLNS-EPSGDPVPLDA--------DSTPLLRVE 279
Cdd:PRK11153 223 GTVSEVFSHPKHPLTREFIQStLHLDLPEDYLArlqaepttGSGPLLRLE 272
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-258 |
3.04e-42 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 150.91 E-value: 3.04e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 5 LLRIDNLSIAFSKQdetrTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLL-----PSppvsypQGDILFHDRSLl 79
Cdd:COG1126 1 MIEIENLHKSFGDL----EVLKGISLDVEKGEVVVIIGPSGSGKS----TLLRCInlleePD------SGTITVDGEDL- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 80 HADEQTLRGIRGnKIAMIFQE----P-M-----VSLNPLHslekqlyevlslHRGMRKEAARGEILDCLERTGIrnaAKR 149
Cdd:COG1126 66 TDSKKDINKLRR-KVGMVFQQfnlfPhLtvlenVTLAPIK------------VKKMSKAEAEERAMELLERVGL---ADK 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 150 LNDFPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDElNMSLLFITHNLSIVRKLADSVAV 229
Cdd:COG1126 130 ADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVF 208
|
250 260
....*....|....*....|....*....
gi 1278835479 230 MQNGRCVEQNAASTLLSAPQHPYTQRLLN 258
Cdd:COG1126 209 MDGGRIVEEGPPEEFFENPQHERTRAFLS 237
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
270-528 |
3.25e-42 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 151.49 E-value: 3.25e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 270 ADSTPLLRVEDLSVSFpirkgilrrivDRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEILF 344
Cdd:COG4598 3 DTAPPALEVRDLHKSF-----------GDLEVLKGVSLTARKGDVISIIGSSGSGKST----FLRCInlletPDSGEIRV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 345 DGMPLhRW-----------NRRQMLPVRPRMQVVFQDPNssLNPRLSVLQIVEEGlRVHQPGLSAQQREQEVMRVMVEVG 413
Cdd:COG4598 68 GGEEI-RLkpdrdgelvpaDRRQLQRIRTRLGMVFQSFN--LWSHMTVLENVIEA-PVHVLGRPKAEAIERAEALLAKVG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 414 LdPETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRlAYIFISHDLQVVRALC 493
Cdd:COG4598 144 L-ADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGR-TMLVVTHEMGFARDVS 221
|
250 260 270
....*....|....*....|....*....|....*
gi 1278835479 494 HQVIVLRQGEVVEQGECQRVFSAPTQRYTRQLLSS 528
Cdd:COG4598 222 SHVVFLHQGRIEEQGPPAEVFGNPKSERLRQFLSS 256
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
302-524 |
3.95e-42 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 151.64 E-value: 3.95e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 302 LKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEILFDGMPLHRWNRRQMLPVR-PRMQVVFQdpNSSL 375
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKST----LLRCInrliePTSGKVLIDGQDIAAMSRKELRELRrKKISMVFQ--SFAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 376 NPRLSVLQIVEEGLRVHqpGLSAQQREQEVMRVMVEVGLDPEtRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSS 455
Cdd:cd03294 114 LPHRTVLENVAFGLEVQ--GVPRAEREERAAEALELVGLEGW-EHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSA 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1278835479 456 LDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSAPTQRYTRQ 524
Cdd:cd03294 191 LDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVRE 259
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6-247 |
4.99e-42 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 150.21 E-value: 4.99e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 6 LRIDNLSIAFSKqdetRTVVSDLTLQIQRGETLALVGESGSGKSvSALSIL--RLLPSppvsypQGDILFHDRSLLHADE 83
Cdd:COG1131 1 IEVRGLTKRYGD----KTALDGVSLTVEPGEIFGLLGPNGAGKT-TTIRMLlgLLRPT------SGEVRVLGEDVARDPA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 84 QTLRgirgnKIAMIFQEPmvslnplhSLEKQL--YEVLSLH---RGMRKEAARGEILDCLERTGIRNAAKRLndfPHQLS 158
Cdd:COG1131 70 EVRR-----RIGYVPQEP--------ALYPDLtvRENLRFFarlYGLPRKEARERIDELLELFGLTDAADRK---VGTLS 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 159 GGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDElNMSLLFITHNLSIVRKLADSVAVMQNGRCVEQ 238
Cdd:COG1131 134 GGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVAD 212
|
....*....
gi 1278835479 239 NAASTLLSA 247
Cdd:COG1131 213 GTPDELKAR 221
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-252 |
1.36e-41 |
|
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: 149.19 E-value: 1.36e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 6 LRIDNLSIAFskqdETRTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLLPspPVSypqGDILFHDRSLLHADEQT 85
Cdd:cd03261 1 IELRGLTKSF----GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLR--PDS---GEVLIDGEDISGLSEAE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 86 LRGIRgNKIAMIFQEPMV--SLNPLHSLEKQLYEvlslHRGMRKEAARGEILDCLERTGIRNAAKRlndFPHQLSGGERQ 163
Cdd:cd03261 72 LYRLR-RRMGMLFQSGALfdSLTVFENVAFPLRE----HTRLSEEEIREIVLEKLEAVGLRGAEDL---YPAELSGGMKK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 164 RVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGRCVEQNAAST 243
Cdd:cd03261 144 RVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEE 223
|
....*....
gi 1278835479 244 LLsAPQHPY 252
Cdd:cd03261 224 LR-ASDDPL 231
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
276-503 |
1.39e-41 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 147.33 E-value: 1.39e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 276 LRVEDLSVSFPirkgilrrivdRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLH 350
Cdd:cd03229 1 LELKNVSKRYG-----------QKTVLNDVSLNIEAGEIVALLGPSGSGKST----LLRCIAgleepDSGSILIDGEDLT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 351 RwNRRQMLPVRPRMQVVFQDPNssLNPRLSVLQIVEEGLrvhqpglsaqqreqevmrvmvevgldpetrhrypaefSGGQ 430
Cdd:cd03229 66 D-LEDELPPLRRRIGMVFQDFA--LFPHLTVLENIALGL-------------------------------------SGGQ 105
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1278835479 431 RQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGE 503
Cdd:cd03229 106 QQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
254-508 |
2.16e-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: 156.46 E-value: 2.16e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 254 QRLLNSEPSGDP---VPLDADSTPLLRVEDLSVSFPirkgilrrivDRNPVLKNIRFSLRPGESLGLVGESGSGKSTTGL 330
Cdd:COG4988 312 FALLDAPEPAAPagtAPLPAAGPPSIELEDVSFSYP----------GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLN 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 331 ALLRLI-ASQGEILFDGMPLHRWNRRQmlpVRPRMQVVFQDP---NSSlnprlsvlqiVEEGLRVHQPGLSaqqrEQEVM 406
Cdd:COG4988 382 LLLGFLpPYSGSILINGVDLSDLDPAS---WRRQIAWVPQNPylfAGT----------IRENLRLGRPDAS----DEELE 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 407 RVMVEVGLDPETRhRYP-----------AEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKH 475
Cdd:COG4988 445 AALEAAGLDEFVA-ALPdgldtplgeggRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR 523
|
250 260 270
....*....|....*....|....*....|...
gi 1278835479 476 RLayIFISHDLQVVRAlCHQVIVLRQGEVVEQG 508
Cdd:COG4988 524 TV--ILITHRLALLAQ-ADRILVLDDGRIVEQG 553
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
270-506 |
2.89e-41 |
|
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: 147.97 E-value: 2.89e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 270 ADSTPLLRVEDLSVSFPIRKGILRrivdrnpVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILF 344
Cdd:COG4181 3 SSSAPIIELRGLTKTVGTGAGELT-------ILKGISLEVEAGESVAIVGASGSGKST----LLGLLAgldrpTSGTVRL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 345 DGMPLHRWNRRQMLPVRPR-MQVVFQdpNSSLNPRLSVLQIV-----EEGLRvhqpglSAQQREQEVMRvmvEVGLDPET 418
Cdd:COG4181 72 AGQDLFALDEDARARLRARhVGFVFQ--SFQLLPTLTALENVmlpleLAGRR------DARARARALLE---RVGLGHRL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 419 RHrYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVrALCHQVIV 498
Cdd:COG4181 141 DH-YPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALA-ARCDRVLR 218
|
....*...
gi 1278835479 499 LRQGEVVE 506
Cdd:COG4181 219 LRAGRLVE 226
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
292-504 |
6.12e-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: 6.12e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 292 LRRIVDRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLHRWNrrqmlPVRPRMQV 366
Cdd:COG4619 6 LSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKST----LLRALAdldppTSGEIYLDGKPLSAMP-----PPEWRRQV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 367 --VFQDPnsslnprlsvlQIVEEGLRVH--QPGLSAQQR--EQEVMRVMVEVGLDPETRHRYPAEFSGGQRQRIAIARAL 440
Cdd:COG4619 77 ayVPQEP-----------ALWGGTVRDNlpFPFQLRERKfdRERALELLERLGLPPDILDKPVERLSGGERQRLALIRAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1278835479 441 ILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEV 504
Cdd:COG4619 146 LLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
300-521 |
8.93e-41 |
|
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: 147.00 E-value: 8.93e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 300 PVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLHRwnrrqmLPVRPR-MQVVFQdpNS 373
Cdd:cd03300 14 VALDGVSLDIKEGEFFTLLGPSGCGKTT----LLRLIAgfetpTSGEILLDGKDITN------LPPHKRpVNTVFQ--NY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 374 SLNPRLSVLQIVEEGLRVHqpGLSAQQREQEVMRVMVEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPT 453
Cdd:cd03300 82 ALFPHLTVFENIAFGLRLK--KLPKAEIKERVAEALDLVQLE-GYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1278835479 454 SSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSAPTQRY 521
Cdd:cd03300 159 GALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRF 226
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
274-528 |
1.36e-40 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 146.90 E-value: 1.36e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 274 PLLRVEDLSVSFPIRKGilrrivdrnpvLKNIRFSLRPGESLGLVGESGSGKSTTGLALL-RLIASQGEILF---DGMP- 348
Cdd:TIGR02323 2 PLLQVSGLSKSYGGGKG-----------CRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAgRLAPDHGTATYimrSGAEl 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 349 ----LHRWNRRQMLpvRPRMQVVFQDPNSSLNPRLSVLQIVEEGLrvhqpgLSAQQRE-----QEVMRVMVEVGLDPETR 419
Cdd:TIGR02323 71 elyqLSEAERRRLM--RTEWGFVHQNPRDGLRMRVSAGANIGERL------MAIGARHygnirATAQDWLEEVEIDPTRI 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 420 HRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVL 499
Cdd:TIGR02323 143 DDLPRAFSGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVM 222
|
250 260
....*....|....*....|....*....
gi 1278835479 500 RQGEVVEQGECQRVFSAPTQRYTRQLLSS 528
Cdd:TIGR02323 223 QQGRVVESGLTDQVLDDPQHPYTQLLVSS 251
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
277-499 |
1.99e-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: 145.37 E-value: 1.99e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 277 RVEDLSVSFpirkgilrrivDRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLHR 351
Cdd:cd03235 1 EVEDLTVSY-----------GGHPVLEDVSFEVKPGEFLAIVGPNGAGKST----LLKAILgllkpTSGSIRVFGKPLEK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 352 wnrrqmlpVRPRMQVVFQDPNSSLNPRLSVLQIVEEGL---RVHQPGLSAQQREqEVMRVMVEVGLDpETRHRYPAEFSG 428
Cdd:cd03235 66 --------ERKRIGYVPQRRSIDRDFPISVRDVVLMGLyghKGLFRRLSKADKA-KVDEALERVGLS-ELADRQIGELSG 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1278835479 429 GQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAyIFISHDLQVVRALCHQVIVL 499
Cdd:cd03235 136 GQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTI-LVVTHDLGLVLEYFDRVLLL 205
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
299-504 |
2.16e-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: 144.98 E-value: 2.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 299 NPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLHRwNRRQMLPVRPRMQVVFQDPNs 373
Cdd:cd03262 13 FHVLKGIDLTVKKGEVVVIIGPSGSGKST----LLRCINlleepDSGTIIIDGLKLTD-DKKNINELRQKVGMVFQQFN- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 374 sLNPRLSVLQIVEEGLRVHQpGLSAQQREQEVMRVMVEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPT 453
Cdd:cd03262 87 -LFPHLTVLENITLAPIKVK-GMSKAEAEERALELLEKVGLA-DKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPT 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1278835479 454 SSLDRTVQAQILALLKGLQEKHrLAYIFISHDLQVVRALCHQVIVLRQGEV 504
Cdd:cd03262 164 SALDPELVGEVLDVMKDLAEEG-MTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-233 |
2.33e-40 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 146.39 E-value: 2.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 1 MTQPLLRIDNLSIAFSKQDETRTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLL-----PSppvsypQGDILFHD 75
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKS----TLLRLIaglekPT------SGEVLVDG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 76 RSLLHAdeqtlrgirGNKIAMIFQEPmvSLNPLHSLEKQLYEVLSLhRGMRKEAARGEILDCLERTGIRNAAKRlndFPH 155
Cdd:COG1116 73 KPVTGP---------GPDRGVVFQEP--ALLPWLTVLDNVALGLEL-RGVPKAERRERARELLELVGLAGFEDA---YPH 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1278835479 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLS-IVRkLADSVAVMQNG 233
Cdd:COG1116 138 QLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDeAVF-LADRVVVLSAR 215
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-248 |
2.60e-40 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 146.00 E-value: 2.60e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 1 MTQPLLRIDNLSIAFskqdETRTVVSDLTLQIQRGETLALVGESGSGKS--VSAlsILRLLPspPVSypqGDILFHDRSL 78
Cdd:COG1121 2 MMMPAIELENLTVSY----GGRPVLEDVSLTIPPGEFVAIVGPNGAGKStlLKA--ILGLLP--PTS---GTVRLFGKPP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 79 LHAdeqtlrgirGNKIAMIFQEPMVSLN-PLHslekqLYEVLSL----HRGMRK---EAARGEILDCLERTGIRNAAKRl 150
Cdd:COG1121 71 RRA---------RRRIGYVPQRAEVDWDfPIT-----VRDVVLMgrygRRGLFRrpsRADREAVDEALERVGLEDLADR- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 151 ndfP-HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDElNMSLLFITHNLSIVRKLADSVAV 229
Cdd:COG1121 136 ---PiGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLL 211
|
250
....*....|....*....
gi 1278835479 230 MqNGRCVEQNAASTLLSAP 248
Cdd:COG1121 212 L-NRGLVAHGPPEEVLTPE 229
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
276-503 |
3.60e-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: 142.91 E-value: 3.60e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 276 LRVEDLSVSFPIRKgilrrivdrNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEILFDGMPLHRWNR 354
Cdd:cd03228 1 IEFKNVSFSYPGRP---------KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYdPTSGEILIDGVDLRDLDL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 355 RQmlpVRPRMQVVFQDP---NSSlnprlsvlqiVEEGLrvhqpglsaqqreqevmrvmvevgldpetrhrypaeFSGGQR 431
Cdd:cd03228 72 ES---LRKNIAYVPQDPflfSGT----------IRENI------------------------------------LSGGQR 102
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1278835479 432 QRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLayIFISHDLQVVRaLCHQVIVLRQGE 503
Cdd:cd03228 103 QRIAIARALLRDPPILILDEATSALDPETEALILEALRALAKGKTV--IVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
5-247 |
3.71e-40 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 145.96 E-value: 3.71e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 5 LLRIDNLSIAFSKqdetRTVVSDLTLQIQRGETLALVGESGSGKSvSAL-SILRLLPspPVSypqGDILFHDRSL--LHA 81
Cdd:COG1120 1 MLEAENLSVGYGG----RPVLDDVSLSLPPGEVTALLGPNGSGKS-TLLrALAGLLK--PSS---GEVLLDGRDLasLSR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 82 DEqtlrgiRGNKIAMIFQEPMVSLnPLHslekqLYEVLSL----HRGM---RKEAARGEILDCLERTGIRNAAKRlnDFp 154
Cdd:COG1120 71 RE------LARRIAYVPQEPPAPF-GLT-----VRELVALgrypHLGLfgrPSAEDREAVEEALERTGLEHLADR--PV- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 155 HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGR 234
Cdd:COG1120 136 DELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGR 215
|
250
....*....|...
gi 1278835479 235 CVEQNAASTLLSA 247
Cdd:COG1120 216 IVAQGPPEEVLTP 228
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
302-528 |
5.17e-40 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 148.03 E-value: 5.17e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 302 LKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEILFDGMPLHRWNRRQMLPVRPRMQVVFQDPN--SS 374
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKST----LIRCInllerPTSGRVLVDGQDLTALSEKELRKARRQIGMIFQHFNllSS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 375 LNprlsVLQIVEEGLRVhqPGLSAQQREQEVMRVMVEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTS 454
Cdd:PRK11153 97 RT----VFDNVALPLEL--AGTPKAEIKARVTELLELVGLS-DKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATS 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1278835479 455 SLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSAPTQRYTRQLLSS 528
Cdd:PRK11153 170 ALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREFIQS 243
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
275-508 |
5.51e-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: 5.51e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 275 LLRVEDLSVSFPIRKgilrrivdrnPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIA-SQGEILFDGMPLHRWN 353
Cdd:TIGR02315 1 MLEVENLSKVYPNGK----------QALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEpSSGSILLEGTDITKLR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 354 RRQMLPVRPRMQVVFQDPNssLNPRLSVLQIVEEGLRVHQP------GLSAQQREQEVMRVMVEVGLDpETRHRYPAEFS 427
Cdd:TIGR02315 71 GKKLRKLRRRIGMIFQHYN--LIERLTVLENVLHGRLGYKPtwrsllGRFSEEDKERALSALERVGLA-DKAYQRADQLS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 428 GGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQ 507
Cdd:TIGR02315 148 GGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFD 227
|
.
gi 1278835479 508 G 508
Cdd:TIGR02315 228 G 228
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
302-518 |
5.77e-40 |
|
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: 146.06 E-value: 5.77e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 302 LKNIRFSLRPGESLGLVGESGSGKST-----TGLallrLIASQGEILFDGMPLHRWNRRQMLPVRPRMQVVFQDPNSsln 376
Cdd:TIGR04521 21 LDDVSLTIEDGEFVAIIGHTGSGKSTliqhlNGL----LKPTSGTVTIDGRDITAKKKKKLKDLRKKVGLVFQFPEH--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 377 prlsvlQIVEE--------GLRvhQPGLSAQQREQEVMRVMVEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPELII 448
Cdd:TIGR04521 94 ------QLFEEtvykdiafGPK--NLGLSEEEAEERVKEALELVGLDEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLI 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 449 LDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSAPT 518
Cdd:TIGR04521 166 LDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVD 235
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-252 |
5.78e-40 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 148.32 E-value: 5.78e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 1 MTQPLLRIDNLSIAFSKQdetrTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLL-----PSppvsypQGDILFHD 75
Cdd:COG3842 1 MAMPALELENVSKRYGDV----TALDDVSLSIEPGEFVALLGPSGCGKT----TLLRMIagfetPD------SGRILLDG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 76 RSLLH-ADEQtlrgiRGnkIAMIFQEP-----M-VSLN---PLHslekqlyevlslHRGMRKEAARGEILDCLERTGIRN 145
Cdd:COG3842 67 RDVTGlPPEK-----RN--VGMVFQDYalfphLtVAENvafGLR------------MRGVPKAEIRARVAELLELVGLEG 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 146 AAKRlndFPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHN----LSivr 221
Cdd:COG3842 128 LADR---YPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDqeeaLA--- 201
|
250 260 270
....*....|....*....|....*....|..
gi 1278835479 222 kLADSVAVMQNGRcVEQNA-ASTLLSAPQHPY 252
Cdd:COG3842 202 -LADRIAVMNDGR-IEQVGtPEEIYERPATRF 231
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
3-259 |
6.30e-40 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 145.36 E-value: 6.30e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 3 QPLLRIDNLSIAFSKQDETRtvvsDLTLQIQRGETLALVGESGSGKS--VSALSIlRLLPSppvsypQGDILFHDRS--- 77
Cdd:TIGR02323 1 KPLLQVSGLSKSYGGGKGCR----DVSFDLYPGEVLGIVGESGSGKStlLGCLAG-RLAPD------HGTATYIMRSgae 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 78 --LLHADEQTLRGIRGNKIAMIFQEPMVSLNPLHS----LEKQLYEVLSLHRGMRKEAARgeilDCLERTGIRnaAKRLN 151
Cdd:TIGR02323 70 leLYQLSEAERRRLMRTEWGFVHQNPRDGLRMRVSaganIGERLMAIGARHYGNIRATAQ----DWLEEVEID--PTRID 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 152 DFPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQ 231
Cdd:TIGR02323 144 DLPRAFSGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQ 223
|
250 260
....*....|....*....|....*...
gi 1278835479 232 NGRCVEQNAASTLLSAPQHPYTQRLLNS 259
Cdd:TIGR02323 224 QGRVVESGLTDQVLDDPQHPYTQLLVSS 251
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
272-508 |
9.06e-40 |
|
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: 144.80 E-value: 9.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 272 STPLLRVEDLSVSFpirkGILRrivdrnpVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEILFDG 346
Cdd:COG0411 1 SDPLLEVRGLTKRF----GGLV-------AVDDVSLEVERGEIVGLIGPNGAGKTT----LFNLItgfyrPTSGRILFDG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 347 MPLHRWNRRQmlpvRPRMQVV--FQdpNSSLNPRLSVLQIVEEGLRVHQ-----------PGLSAQQRE--QEVMRVMVE 411
Cdd:COG0411 66 RDITGLPPHR----IARLGIArtFQ--NPRLFPELTVLENVLVAAHARLgrgllaallrlPRARREEREarERAEELLER 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 412 VGLDPEtRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRA 491
Cdd:COG0411 140 VGLADR-ADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMG 218
|
250
....*....|....*..
gi 1278835479 492 LCHQVIVLRQGEVVEQG 508
Cdd:COG0411 219 LADRIVVLDFGRVIAEG 235
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
267-508 |
9.90e-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: 151.84 E-value: 9.90e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 267 PLDADSTPLLRVEDLSVSFPirkgilrriVDRNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEILFD 345
Cdd:COG4987 325 PAPAPGGPSLELEDVSFRYP---------GAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLdPQSGSITLG 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 346 GMPLHRWNRRQmlpVRPRMQVVFQDP---NSSlnprlsvlqiVEEGLRVHQPGLSaqqrEQEVMRVMVEVGLDP------ 416
Cdd:COG4987 396 GVDLRDLDEDD---LRRRIAVVPQRPhlfDTT----------LRENLRLARPDAT----DEELWAALERVGLGDwlaalp 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 417 ---ETR-HRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKG-LQEKhrlAYIFISHDLQVVrA 491
Cdd:COG4987 459 dglDTWlGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEaLAGR---TVLLITHRLAGL-E 534
|
250
....*....|....*..
gi 1278835479 492 LCHQVIVLRQGEVVEQG 508
Cdd:COG4987 535 RMDRILVLEDGRIVEQG 551
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
276-513 |
1.08e-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: 144.25 E-value: 1.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 276 LRVEDLSVSFPirkgilrrivDRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEILFDGMPLH 350
Cdd:cd03256 1 IEVENLSKTYP----------NGKKALKDVSLSINPGEFVALIGPSGAGKST----LLRCLnglvePTSGSVLIDGTDIN 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 351 RWNRRQMLPVRPRMQVVFQDPNssLNPRLSVLQIVEEG-------LRVHQPGLSAQQReQEVMRVMVEVGLDPETRHRyP 423
Cdd:cd03256 67 KLKGKALRQLRRQIGMIFQQFN--LIERLSVLENVLSGrlgrrstWRSLFGLFPKEEK-QRALAALERVGLLDKAYQR-A 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 424 AEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGE 503
Cdd:cd03256 143 DQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGR 222
|
250
....*....|
gi 1278835479 504 VVEQGECQRV 513
Cdd:cd03256 223 IVFDGPPAEL 232
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
300-528 |
1.28e-39 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 144.46 E-value: 1.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 300 PVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-----ASQGEILFDGMPLHRWNrrqmlpVRPRM-QVVFQDPNS 373
Cdd:PRK10418 17 PLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILpagvrQTAGRVLLDGKPVAPCA------LRGRKiATIMQNPRS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 374 SLNPRLSVLQIVEEGLRVhqpgLSAQQREQEVMRVMVEVGLDPETR--HRYPAEFSGGQRQRIAIARALILKPELIILDE 451
Cdd:PRK10418 91 AFNPLHTMHTHARETCLA----LGKPADDATLTAALEAVGLENAARvlKLYPFEMSGGMLQRMMIALALLCEAPFIIADE 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1278835479 452 PTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSAPTQRYTRQLLSS 528
Cdd:PRK10418 167 PTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSA 243
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
7-234 |
1.85e-39 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 142.61 E-value: 1.85e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 7 RIDNLSiaFSKQDETRTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLL-----PSppvsypQGDILFHDRSLlha 81
Cdd:cd03225 1 ELKNLS--FSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKS----TLLRLLngllgPT------SGEVLVDGKDL--- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 82 DEQTLRGIRGnKIAMIFQEPmvslnplhslEKQLY------EVLS--LHRGMRKEAARGEILDCLERTGIRNAAKRLndf 153
Cdd:cd03225 66 TKLSLKELRR-KVGLVFQNP----------DDQFFgptveeEVAFglENLGLPEEEIEERVEEALELVGLEGLRDRS--- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 154 PHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDElNMSLLFITHNLSIVRKLADSVAVMQNG 233
Cdd:cd03225 132 PFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDG 210
|
.
gi 1278835479 234 R 234
Cdd:cd03225 211 K 211
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
276-504 |
2.93e-39 |
|
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: 140.61 E-value: 2.93e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 276 LRVEDLSVSFPirkgilrrivdRNPVLKNIRFSLRPGESLGLVGESGSGKSTTglalLRLIA-----SQGEILFDGMPLH 350
Cdd:cd03230 1 IEVRNLSKRYG-----------KKTALDDISLTVEKGEIYGLLGPNGAGKTTL----IKIILgllkpDSGEIKVLGKDIK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 351 RWNRRqmlpVRPRMQVVFQDPnsSLNPRLSVLQIVEeglrvhqpglsaqqreqevmrvmvevgldpetrhrypaeFSGGQ 430
Cdd:cd03230 66 KEPEE----VKRRIGYLPEEP--SLYENLTVRENLK---------------------------------------LSGGM 100
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1278835479 431 RQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAyIFISHDLQVVRALCHQVIVLRQGEV 504
Cdd:cd03230 101 KQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKEGKTI-LLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
276-517 |
4.65e-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: 142.47 E-value: 4.65e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 276 LRVEDLSVSFpirkgilrrivdRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIAS-----QGEILFDGMPLh 350
Cdd:cd03299 1 LKVENLSKDW------------KEFKLKNVSLEVERGDYFVILGPTGSGKSV----LLETIAGfikpdSGKILLNGKDI- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 351 rwnrRQMLPVRPRMQVVFQdpNSSLNPRLSVLQIVEEGLRVHQpgLSAQQREQEVMRVMVEVGLDpETRHRYPAEFSGGQ 430
Cdd:cd03299 64 ----TNLPPEKRDISYVPQ--NYALFPHMTVYKNIAYGLKKRK--VDKKEIERKVLEIAEMLGID-HLLNRKPETLSGGE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 431 RQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGEC 510
Cdd:cd03299 135 QQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKP 214
|
....*..
gi 1278835479 511 QRVFSAP 517
Cdd:cd03299 215 EEVFKKP 221
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-506 |
5.06e-39 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 149.06 E-value: 5.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 8 IDNLSIAFSkqdeTRTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLLpsppvsypqgdilfhdRSLLHADEQTLR 87
Cdd:COG0488 1 LENLSKSFG----GRPLLDDVSLSINPGDRIGLVGRNGAGKS----TLLKIL----------------AGELEPDSGEVS 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 88 GIRGNKIAMIFQEP------------MVSLNPLHSLEKQLYEVLSLHRGMRKEAAR-GEILDCLERTG-------IRNAA 147
Cdd:COG0488 57 IPKGLRIGYLPQEPpldddltvldtvLDGDAELRALEAELEELEAKLAEPDEDLERlAELQEEFEALGgweaearAEEIL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 148 KRLN--DFPHQ-----LSGGERQRVMIAMALLTRPELLIADEPTTALDV-TVQaqiltLLRDLRDELNMSLLFITHNLSI 219
Cdd:COG0488 137 SGLGfpEEDLDrpvseLSGGWRRRVALARALLSEPDLLLLDEPTNHLDLeSIE-----WLEEFLKNYPGTVLVVSHDRYF 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 220 VRKLADSVAVMQNGRC----------VEQNA------------------------------AST--------------LL 245
Cdd:COG0488 212 LDRVATRILELDRGKLtlypgnysayLEQRAerleqeaaayakqqkkiakeeefirrfrakARKakqaqsrikaleklER 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 246 SAPQHPYTQ---RLLNSEPSGDPVpldadstplLRVEDLSVSFPirkgilrrivDRnPVLKNIRFSLRPGESLGLVGESG 322
Cdd:COG0488 292 EEPPRRDKTveiRFPPPERLGKKV---------LELEGLSKSYG----------DK-TLLDDLSLRIDRGDRIGLIGPNG 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 323 SGKSTtglaLLRLIA-----SQGEIlfdgmplhRWNrrqmlpvrPRMQVVF--QDpNSSLNPRLSVLQIVEEGlrvhqpg 395
Cdd:COG0488 352 AGKST----LLKLLAgelepDSGTV--------KLG--------ETVKIGYfdQH-QEELDPDKTVLDELRDG------- 403
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 396 lSAQQREQEVMRVMVEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLD-RTVQAQILALL--KGlq 472
Cdd:COG0488 404 -APGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDiETLEALEEALDdfPG-- 480
|
570 580 590
....*....|....*....|....*....|....
gi 1278835479 473 ekhrlAYIFISHDLQVVRALCHQVIVLRQGEVVE 506
Cdd:COG0488 481 -----TVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-236 |
5.65e-39 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 142.50 E-value: 5.65e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 4 PLLRIDNLSIAFSKQdetRTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLL-----PSppvsypQGDILFHDRSL 78
Cdd:COG3638 1 PMLELRNLSKRYPGG---TPALDDVSLEIERGEFVALIGPSGAGKS----TLLRCLnglvePT------SGEILVDGQDV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 79 LHADEQTLRGIRGnKIAMIFQEpmvslnplHSLEKQLYeVL-----------SLHRGMRKEAARGEI---LDCLERTGIr 144
Cdd:COG3638 68 TALRGRALRRLRR-RIGMIFQQ--------FNLVPRLS-VLtnvlagrlgrtSTWRSLLGLFPPEDReraLEALERVGL- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 145 naAKRLNDFPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLA 224
Cdd:COG3638 137 --ADKAYQRADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYA 214
|
250
....*....|..
gi 1278835479 225 DSVAVMQNGRCV 236
Cdd:COG3638 215 DRIIGLRDGRVV 226
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
302-454 |
8.53e-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: 138.55 E-value: 8.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 302 LKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLHRWNRRQmlpVRPRMQVVFQDPNssLN 376
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKST----LLKLIAgllspTEGTILLDGQDLTDDERKS---LRKEIGYVFQDPQ--LF 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 377 PRLSVLQIVEEGLRVhqPGLSAQQREQEVMRVMVEVGL--DPETR-HRYPAEFSGGQRQRIAIARALILKPELIILDEPT 453
Cdd:pfam00005 72 PRLTVRENLRLGLLL--KGLSKREKDARAEEALEKLGLgdLADRPvGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
.
gi 1278835479 454 S 454
Cdd:pfam00005 150 A 150
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
5-259 |
1.11e-38 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 142.24 E-value: 1.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 5 LLRIDNLSIAFSKQD-----ETRTVVSDLTLQIQRGETLALVGESGSGKSVSAlsilRLLpSPPVSYPQGDILFHDRSLL 79
Cdd:PRK15112 4 LLEVRNLSKTFRYRTgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLA----KML-AGMIEPTSGELLIDDHPLH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 80 HADeqtlRGIRGNKIAMIFQEPMVSLNPLHSLEKQLYEVLSLHRGMRKEAARGEILDCLERTGIRNaaKRLNDFPHQLSG 159
Cdd:PRK15112 79 FGD----YSYRSQRIRMIFQDPSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLP--DHASYYPHMLAP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 160 GERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGRCVEQN 239
Cdd:PRK15112 153 GQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERG 232
|
250 260
....*....|....*....|
gi 1278835479 240 AASTLLSAPQHPYTQRLLNS 259
Cdd:PRK15112 233 STADVLASPLHELTKRLIAG 252
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
277-508 |
1.28e-38 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 139.11 E-value: 1.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 277 RVEDLSVSFpirkgilrrivDRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLHR 351
Cdd:cd03214 1 EVENLSVGY-----------GGRTVLDDLSLSIEAGEIVGILGPNGAGKST----LLKTLAgllkpSSGEILLDGKDLAS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 352 WNRRQMlpvRPRMQVVFQdpnsslnprlsvlqiveeglrvhqpglsaqqreqevmrVMVEVGLDpETRHRYPAEFSGGQR 431
Cdd:cd03214 66 LSPKEL---ARKIAYVPQ--------------------------------------ALELLGLA-HLADRPFNELSGGER 103
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1278835479 432 QRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:cd03214 104 QRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
256-508 |
1.48e-38 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 148.77 E-value: 1.48e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 256 LLNSEPSGDPVPLDADSTPL---LRVEDLSVSFPirkgilrrivDRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaL 332
Cdd:COG1132 317 LLDEPPEIPDPPGAVPLPPVrgeIEFENVSFSYP----------GDRPVLKDISLTIPPGETVALVGPSGSGKST----L 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 333 LRLIA-----SQGEILFDGMPLHRWNRRQmlpVRPRMQVVFQDP---NSSlnprlsvlqiVEEGLRVHQPGLSaqqrEQE 404
Cdd:COG1132 383 VNLLLrfydpTSGRILIDGVDIRDLTLES---LRRQIGVVPQDTflfSGT----------IRENIRYGRPDAT----DEE 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 405 VMRVMVEVGLDPETRhRYP-----------AEFSGGQRQRIAIARALILKPELIILDEPTSSLD----RTVQAQILALLK 469
Cdd:COG1132 446 VEEAAKAAQAHEFIE-ALPdgydtvvgergVNLSGGQRQRIAIARALLKDPPILILDEATSALDteteALIQEALERLMK 524
|
250 260 270
....*....|....*....|....*....|....*....
gi 1278835479 470 GlqekhRLAyIFISHDLQVVRAlCHQVIVLRQGEVVEQG 508
Cdd:COG1132 525 G-----RTT-IVIAHRLSTIRN-ADRILVLDDGRIVEQG 556
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
276-515 |
2.18e-38 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 141.41 E-value: 2.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 276 LRVEDLSVSFPIRKgilrrivdrNPVLKNIRFSLRPGESLGLVGESGSGKST-----TGLallrLIASQGEILFDGMplH 350
Cdd:TIGR04520 1 IEVENVSFSYPESE---------KPALKNVSLSIEKGEFVAIIGHNGSGKSTlakllNGL----LLPTSGKVTVDGL--D 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 351 RWNRRQMLPVRPRMQVVFQDPNSSLnprlsVLQIVEE----GLRVHqpGLSAQQREQEVMRVMVEVGLDpETRHRYPAEF 426
Cdd:TIGR04520 66 TLDEENLWEIRKKVGMVFQNPDNQF-----VGATVEDdvafGLENL--GVPREEMRKRVDEALKLVGME-DFRDREPHLL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 427 SGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVrALCHQVIVLRQGEVVE 506
Cdd:TIGR04520 138 SGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIVA 216
|
....*....
gi 1278835479 507 QGECQRVFS 515
Cdd:TIGR04520 217 EGTPREIFS 225
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
276-517 |
2.31e-38 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 143.67 E-value: 2.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 276 LRVEDLSVSFpirkgilrrivDRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGmplH 350
Cdd:COG3839 4 LELENVSKSY-----------GGVEALKDIDLDIEDGEFLVLLGPSGCGKST----LLRMIAgledpTSGEILIGG---R 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 351 RWNRrqmLPVRPR---MqvVFQDPnsSLNPRLSVLQIVEEGLRVHqpGLSAQQREQEVMRVMVEVGLDPeTRHRYPAEFS 427
Cdd:COG3839 66 DVTD---LPPKDRniaM--VFQSY--ALYPHMTVYENIAFPLKLR--KVPKAEIDRRVREAAELLGLED-LLDRKPKQLS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 428 GGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDlQV-VRALCHQVIVLRQGEVVE 506
Cdd:COG3839 136 GGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHD-QVeAMTLADRIAVMNDGRIQQ 214
|
250
....*....|.
gi 1278835479 507 QGECQRVFSAP 517
Cdd:COG3839 215 VGTPEELYDRP 225
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-237 |
4.46e-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: 138.81 E-value: 4.46e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 6 LRIDNLSIAFSKQdetrTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLL-----PSppvsypQGDILFHDRSLLH 80
Cdd:cd03259 1 LELKGLSKTYGSV----RALDDLSLTVEPGEFLALLGPSGCGKT----TLLRLIaglerPD------SGEILIDGRDVTG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 81 adeqtlRGIRGNKIAMIFQEPmvSLNPLHSLEKQLYEVLSLhRGMRKEAARGEILDCLERTGIRNAAKRlndFPHQLSGG 160
Cdd:cd03259 67 ------VPPERRNIGMVFQDY--ALFPHLTVAENIAFGLKL-RGVPKAEIRARVRELLELVGLEGLLNR---YPHELSGG 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1278835479 161 ERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGRCVE 237
Cdd:cd03259 135 QQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQ 211
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
274-528 |
7.18e-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: 7.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 274 PLLRVEDLSVSFPIRKGILRrIVDRnpvlknIRFSLRPGESLGLVGESGSGKSTTGLALLRLIASQGEILFDGMplhRWN 353
Cdd:COG4170 2 PLLDIRNLTIEIDTPQGRVK-AVDR------VSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNWHVTADRF---RWN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 354 RRQMLPVRPR---------MQVVFQDPNSSLNPRLSVLQIVEEGLRVHQPGLS----AQQREQEVMRVMVEVGL-DPETR 419
Cdd:COG4170 72 GIDLLKLSPRerrkiigreIAMIFQEPSSCLDPSAKIGDQLIEAIPSWTFKGKwwqrFKWRKKRAIELLHRVGIkDHKDI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 420 HR-YPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIV 498
Cdd:COG4170 152 MNsYPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITV 231
|
250 260 270
....*....|....*....|....*....|
gi 1278835479 499 LRQGEVVEQGECQRVFSAPTQRYTRQLLSS 528
Cdd:COG4170 232 LYCGQTVESGPTEQILKSPHHPYTKALLRS 261
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
304-517 |
7.95e-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: 142.55 E-value: 7.95e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 304 NIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLHRWNRRQMLPV-RPRMQVVFQDPnsSLNP 377
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTT----LLRAIAglerpDSGRIRLGGEVLQDSARGIFLPPhRRRIGYVFQEA--RLFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 378 RLSVLQIVEEGLRVHQPGLSAQQREQevmrvMVEV-GLDPeTRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSL 456
Cdd:COG4148 91 HLSVRGNLLYGRKRAPRAERRISFDE-----VVELlGIGH-LLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAAL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1278835479 457 DRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSAP 517
Cdd:COG4148 165 DLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
275-518 |
8.28e-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: 8.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 275 LLRVEDLSVSfpirkgilrriVDRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPL 349
Cdd:COG4559 1 MLEAENLSVR-----------LGGRTLLDDVSLTLRPGELTAIIGPNGAGKST----LLKLLTgeltpSSGEVRLNGRPL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 350 HRWNRRQMLPVRPRMQvvfQdpNSSLNPRLSVLQIVEEGLRVHqpGLSAQQREQEVMRVMVEVGLDPeTRHRYPAEFSGG 429
Cdd:COG4559 66 AAWSPWELARRRAVLP---Q--HSSLAFPFTVEEVVALGRAPH--GSSAAQDRQIVREALALVGLAH-LAGRSYQTLSGG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 430 QRQRIAIARALI-------LKPELIILDEPTSSLDRTVQAQILALLKGLQEKhRLAYIFISHDLQVVRALCHQVIVLRQG 502
Cdd:COG4559 138 EQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQG 216
|
250
....*....|....*.
gi 1278835479 503 EVVEQGECQRVFSAPT 518
Cdd:COG4559 217 RLVAQGTPEEVLTDEL 232
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
307-526 |
1.08e-37 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 138.35 E-value: 1.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 307 FSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLHRwnrrqmLPV--RPrMQVVFQDPNssLNPRL 379
Cdd:COG3840 20 LTIAAGERVAILGPSGAGKST----LLNLIAgflppDSGRILWNGQDLTA------LPPaeRP-VSMLFQENN--LFPHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 380 SVLQIVEEGLRvhqPG--LSAQQREQeVMRVMVEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLD 457
Cdd:COG3840 87 TVAQNIGLGLR---PGlkLTAEQRAQ-VEQALERVGLA-GLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1278835479 458 RTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSAPTQRYTRQLL 526
Cdd:COG3840 162 PALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYL 230
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-242 |
1.33e-37 |
|
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: 138.34 E-value: 1.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 1 MTQPLLRIDNLSIAFSKQDETRTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLL-----PSppvsypQGDILFHD 75
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKS----TLLGLLagldrPT------SGTVRLAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 76 RSLLHADEQTLRGIRGNKIAMIFQEPMVsLNPLHSLEkqlYEVLSLH-RGMRKEAARGEILdcLERTGIrnaAKRLNDFP 154
Cdd:COG4181 74 QDLFALDEDARARLRARHVGFVFQSFQL-LPTLTALE---NVMLPLElAGRRDARARARAL--LERVGL---GHRLDHYP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 155 HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKlADSVAVMQNGR 234
Cdd:COG4181 145 AQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGR 223
|
....*...
gi 1278835479 235 CVEQNAAS 242
Cdd:COG4181 224 LVEDTAAT 231
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
276-508 |
1.57e-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: 137.95 E-value: 1.57e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 276 LRVEDLSVSFpirkGILRrivdrnpVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEILFDG---- 346
Cdd:cd03219 1 LEVRGLTKRF----GGLV-------ALDDVSFSVRPGEIHGLIGPNGAGKTT----LFNLIsgflrPTSGSVLFDGedit 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 347 -MPLHRWNRRQMlpVRprmqvVFQdpNSSLNPRLSVLQIVEEGLRVHQPGLSAQQR--------EQEVMRVMVEVGLDPE 417
Cdd:cd03219 66 gLPPHEIARLGI--GR-----TFQ--IPRLFPELTVLENVMVAAQARTGSGLLLARarreereaRERAEELLERVGLADL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 418 tRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRlAYIFISHDLQVVRALCHQVI 497
Cdd:cd03219 137 -ADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGI-TVLLVEHDMDVVMSLADRVT 214
|
250
....*....|.
gi 1278835479 498 VLRQGEVVEQG 508
Cdd:cd03219 215 VLDQGRVIAEG 225
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
276-509 |
2.14e-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: 137.70 E-value: 2.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 276 LRVEDLSVSFpirkgilrrivDRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA----------SQGEILFD 345
Cdd:cd03260 1 IELRDLNVYY-----------GDKHALKDISLDIPKGEITALIGPSGCGKST----LLRLLNrlndlipgapDEGEVLLD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 346 GMPLHRWNRRQMLpVRPRMQVVFQDPNsslnP-RLSVLQIVEEGLRVHQPgLSAQQREQEVMRVMVEVGLDPET-RHRYP 423
Cdd:cd03260 66 GKDIYDLDVDVLE-LRRRVGMVFQKPN----PfPGSIYDNVAYGLRLHGI-KLKEELDERVEEALRKAALWDEVkDRLHA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 424 AEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLqeKHRLAYIFISHDLQVVRALCHQVIVLRQGE 503
Cdd:cd03260 140 LGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAEL--KKEYTIVIVTHNMQQAARVADRTAFLLNGR 217
|
....*.
gi 1278835479 504 VVEQGE 509
Cdd:cd03260 218 LVEFGP 223
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
4-259 |
2.36e-37 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 138.67 E-value: 2.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 4 PLLRIDNLS-----IAFSKQDETRTVVSDLTLQIQRGETLALVGESGSGKSVSAlSILRLLPSPPvsypQGDILFHDRSL 78
Cdd:PRK10419 2 TLLNVSGLShhyahGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLA-RLLVGLESPS----QGNVSWRGEPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 79 LHADEQTLRGIRGNkIAMIFQEPMVSLNPLHSLEKQLYEVLSLHRGMRKEAARGEILDCLERTGIRNA-AKRLndfPHQL 157
Cdd:PRK10419 77 AKLNRAQRKAFRRD-IQMVFQDSISAVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSvLDKR---PPQL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGRCVE 237
Cdd:PRK10419 153 SGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
|
250 260
....*....|....*....|..
gi 1278835479 238 QNAASTLLSApQHPYTQRLLNS 259
Cdd:PRK10419 233 TQPVGDKLTF-SSPAGRVLQNA 253
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-504 |
3.63e-37 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 143.53 E-value: 3.63e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 1 MTQPLLRIDNLSIAFSkqdeTRTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLLPS--PPVSYpQGDILFHDrsl 78
Cdd:PRK13549 1 MMEYLLEMKNITKTFG----GVKALDNVSLKVRAGEIVSLCGENGAGKS----TLMKVLSGvyPHGTY-EGEIIFEG--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 79 lhaDEQTLRGIRGNK---IAMIFQEPMvslnplhsLEKQLYEVLSLHRGmrKEAARGEILD----------CLERTGIR- 144
Cdd:PRK13549 69 ---EELQASNIRDTEragIAIIHQELA--------LVKELSVLENIFLG--NEITPGGIMDydamylraqkLLAQLKLDi 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 145 NAAKRLNDfphqLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDElNMSLLFITHNLSIVRKLA 224
Cdd:PRK13549 136 NPATPVGN----LGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAIS 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 225 DSVAVMQNGRCVEQNAASTLlSAPQ-------------HPYTQRllnsePSGDPVpldadstplLRVEDLSVSFPIRKGi 291
Cdd:PRK13549 211 DTICVIRDGRHIGTRPAAGM-TEDDiitmmvgreltalYPREPH-----TIGEVI---------LEVRNLTAWDPVNPH- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 292 lRRIVDrnpvlkNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI--ASQGEILFDGMPLHRWNRRQ-------MLP--- 359
Cdd:PRK13549 275 -IKRVD------DVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYpgRWEGEIFIDGKPVKIRNPQQaiaqgiaMVPedr 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 360 ----VRPRMQVvfqdpnsSLNPRLSVLQIVEEGLRVHQpGLSAQQREQEVMRVMVEVGlDPETRhryPAEFSGGQRQRIA 435
Cdd:PRK13549 348 krdgIVPVMGV-------GKNITLAALDRFTGGSRIDD-AAELKTILESIQRLKVKTA-SPELA---IARLSGGNQQKAV 415
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1278835479 436 IARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHrLAYIFISHDLQVVRALCHQVIVLRQGEV 504
Cdd:PRK13549 416 LAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQG-VAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
272-513 |
1.01e-36 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 142.08 E-value: 1.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 272 STPLLRVEDLSVSFPirkgilrrivdRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDG 346
Cdd:COG1129 1 AEPLLEMRGISKSFG-----------GVKALDGVSLELRPGEVHALLGENGAGKST----LMKILSgvyqpDSGEILLDG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 347 MPLHRWNRRQMLpvRPRMQVVFQDPNssLNPRLSVLQ---IVEEGLRvhqPGL---SAQQRE-QEVMRvMVEVGLDPETR 419
Cdd:COG1129 66 EPVRFRSPRDAQ--AAGIAIIHQELN--LVPNLSVAEnifLGREPRR---GGLidwRAMRRRaRELLA-RLGLDIDPDTP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 420 HRypaEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRlAYIFISHDLQVVRALCHQVIVL 499
Cdd:COG1129 138 VG---DLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGV-AIIYISHRLDEVFEIADRVTVL 213
|
250
....*....|....
gi 1278835479 500 RQGEVVEQGECQRV 513
Cdd:COG1129 214 RDGRLVGTGPVAEL 227
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-235 |
1.07e-36 |
|
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: 135.29 E-value: 1.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 6 LRIDNLSIAFSKQDETRTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLLP--SPPVSypqGDILFhdrsllhaDE 83
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKS----TLLRIIAglERPTS---GEVLV--------DG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 84 QTLRGiRGNKIAMIFQEPmvSLNPLHSLEKQLyeVLSL-HRGMRKEAARGEILDCLERTGIRNAAKRlndFPHQLSGGER 162
Cdd:cd03293 66 EPVTG-PGPDRGYVFQQD--ALLPWLTVLDNV--ALGLeLQGVPKAEARERAEELLELVGLSGFENA---YPHQLSGGMR 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1278835479 163 QRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGRC 235
Cdd:cd03293 138 QRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSARPG 210
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
276-529 |
1.19e-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: 135.89 E-value: 1.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 276 LRVEDLSVSFPirkgilrrivDRNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIA-SQGEILFDGMPLHRWNR 354
Cdd:cd03295 1 IEFENVTKRYG----------GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEpTSGEIFIDGEDIREQDP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 355 RQMlpvRPRMQVVFQdpNSSLNPRLSVLQIVeeGLRVHQPGLSAQQREQEVMRVMVEVGLDPET-RHRYPAEFSGGQRQR 433
Cdd:cd03295 71 VEL---RRKIGYVIQ--QIGLFPHMTVEENI--ALVPKLLKWPKEKIRERADELLALVGLDPAEfADRYPHELSGGQQQR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 434 IAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRV 513
Cdd:cd03295 144 VGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
250
....*....|....*.
gi 1278835479 514 FSAPTQRYTRQLLSSD 529
Cdd:cd03295 224 LRSPANDFVAEFVGAD 239
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
6-237 |
1.50e-36 |
|
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: 135.39 E-value: 1.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 6 LRIDNLSIAFSKqdetRTVVSDLTLQIQRGETLALVGESGSGKSVsalsILRLL-------PSPPVSypqGDILFHDRSL 78
Cdd:cd03260 1 IELRDLNVYYGD----KHALKDISLDIPKGEITALIGPSGCGKST----LLRLLnrlndliPGAPDE---GEVLLDGKDI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 79 LHADEQTLRGIRgnKIAMIFQEPmvslNPLHsleKQLYEVLSL---HRGMRKEAARGEI-LDCLERTGI-RNAAKRLNdf 153
Cdd:cd03260 70 YDLDVDVLELRR--RVGMVFQKP----NPFP---GSIYDNVAYglrLHGIKLKEELDERvEEALRKAALwDEVKDRLH-- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 154 PHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDElnMSLLFITHNLSIVRKLADSVAVMQNG 233
Cdd:cd03260 139 ALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNG 216
|
....
gi 1278835479 234 RCVE 237
Cdd:cd03260 217 RLVE 220
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
276-505 |
1.58e-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: 132.94 E-value: 1.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 276 LRVEDLSVSFPirkgilrrivdRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLH 350
Cdd:cd03216 1 LELRGITKRFG-----------GVKALDGVSLSVRRGEVHALLGENGAGKST----LMKILSglykpDSGEILVDGKEVS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 351 RWNRRQMLpvRPRMQVVFQdpnsslnprlsvlqiveeglrvhqpglsaqqreqevmrvmvevgldpetrhrypaeFSGGQ 430
Cdd:cd03216 66 FASPRDAR--RAGIAMVYQ--------------------------------------------------------LSVGE 87
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1278835479 431 RQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHrLAYIFISHDLQVVRALCHQVIVLRQGEVV 505
Cdd:cd03216 88 RQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQG-VAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
5-244 |
1.76e-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: 135.50 E-value: 1.76e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 5 LLRIDNLSIAFSKQDetrTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLlpsppVSYPQGDILFHDRSLLHADEQ 84
Cdd:TIGR02315 1 MLEVENLSKVYPNGK---QALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRL-----VEPSSGSILLEGTDITKLRGK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 85 TLRGIRgNKIAMIFQEPMVsLNPLHSLEKQLYEVLSLHRGMR------KEAARGEILDCLERTGIRN-AAKRLNdfphQL 157
Cdd:TIGR02315 73 KLRKLR-RRIGMIFQHYNL-IERLTVLENVLHGRLGYKPTWRsllgrfSEEDKERALSALERVGLADkAYQRAD----QL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGRCVE 237
Cdd:TIGR02315 147 SGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVF 226
|
....*..
gi 1278835479 238 QNAASTL 244
Cdd:TIGR02315 227 DGAPSEL 233
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
274-518 |
2.70e-36 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 135.28 E-value: 2.70e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 274 PLLRVEDLSVSfpirkgilrriVDRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEILFDGMP 348
Cdd:PRK13548 1 AMLEARNLSVR-----------LGGRTLLDDVSLTLRPGEVVAILGPNGAGKST----LLRALsgelsPDSGEVRLNGRP 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 349 LHRWNRRQMLPVRPRM-QvvfqdpNSSLNPRLSVLQIVEEGLRVHqpGLSAQQREQEVMRVMVEVGLDpETRHRYPAEFS 427
Cdd:PRK13548 66 LADWSPAELARRRAVLpQ------HSSLSFPFTVEEVVAMGRAPH--GLSRAEDDALVAAALAQVDLA-HLAGRDYPQLS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 428 GGQRQRIAIARALI------LKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQ 501
Cdd:PRK13548 137 GGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQ 216
|
250
....*....|....*..
gi 1278835479 502 GEVVEQGECQRVFSAPT 518
Cdd:PRK13548 217 GRLVADGTPAEVLTPET 233
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
5-237 |
6.91e-36 |
|
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: 133.25 E-value: 6.91e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 5 LLRIDNLSIAFSKQDETRTVVSDLTLQIQRGETLALVGESGSGKSvSALSILRLLPSPPvsypQGDILFHDRSLLHADEQ 84
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKS-TLLHLLGGLDNPT----SGEVLFNGQSLSKLSSN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 85 TLRGIRGNKIAMIFQ--EPMVSLNPLHSLEKQLyevlsLHRGMRKEAARGEILDCLERTGIRnaaKRLNDFPHQLSGGER 162
Cdd:TIGR02211 76 ERAKLRNKKLGFIYQfhHLLPDFTALENVAMPL-----LIGKKSVKEAKERAYEMLEKVGLE---HRINHRPSELSGGER 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1278835479 163 QRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLaDSVAVMQNGRCVE 237
Cdd:TIGR02211 148 QRVAIARALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQLFN 221
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
6-237 |
7.73e-36 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 133.25 E-value: 7.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 6 LRIDNLSIAFSKQdetRTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLL-----PSppvsypQGDILFHDRSLLH 80
Cdd:COG2884 2 IRFENVSKRYPGG---REALSDVSLEIEKGEFVFLTGPSGAGKS----TLLKLLygeerPT------SGQVLVNGQDLSR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 81 ADEQTLRGIRgNKIAMIFQEpmvslnplHSL--EKQLYE--VLSLH-RGMRKEAARGEILDCLERTGIRNAAKRlndFPH 155
Cdd:COG2884 69 LKRREIPYLR-RRIGVVFQD--------FRLlpDRTVYEnvALPLRvTGKSRKEIRRRVREVLDLVGLSDKAKA---LPH 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRdELNMSLLFITHNLSIVRKLADSVAVMQNGRC 235
Cdd:COG2884 137 ELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEIN-RRGTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
..
gi 1278835479 236 VE 237
Cdd:COG2884 216 VR 217
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
304-508 |
9.18e-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: 132.80 E-value: 9.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 304 NIRFSLrPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLHRWNRRQMLPVRPR-MQVVFQdpNSSLNP 377
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKST----LLRCIAglekpDGGTIVLNGTVLFDSRKKINLPPQQRkIGLVFQ--QYALFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 378 RLSVLQIVEEGLRVHQPGlSAQQREQEVMRVMvevGLDPETRhRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLD 457
Cdd:cd03297 89 HLNVRENLAFGLKRKRNR-EDRISVDELLDLL---GLDHLLN-RYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1278835479 458 RTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:cd03297 164 RALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
7-238 |
1.28e-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: 1.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 7 RIDNLSIAFSKqdetRTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLLPSPpvsypQGDILFHDRSLLHADEQTL 86
Cdd:cd03214 1 EVENLSVGYGG----RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPS-----SGEILLDGKDLASLSPKEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 87 RgirgNKIAMIFQepmvslnplhslekqlyevlslhrgmrkeaargeildCLERTGIRNAAKRlnDFpHQLSGGERQRVM 166
Cdd:cd03214 72 A----RKIAYVPQ-------------------------------------ALELLGLAHLADR--PF-NELSGGERQRVL 107
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1278835479 167 IAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGRCVEQ 238
Cdd:cd03214 108 LARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQ 179
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
302-514 |
1.77e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 134.02 E-value: 1.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 302 LKNIRFSLRPGESLGLVGESGSGKST-----TGLallrLIASQGEILFDGMPLhrWNRRQMLP-VRPRMQVVFQDPNSsl 375
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTliqhlNGL----LKPTSGKIIIDGVDI--TDKKVKLSdIRKKVGLVFQYPEY-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 376 nprlsvlQIVEE--------GLRvhQPGLSAQQREQEVMRVMVEVGLDPET-RHRYPAEFSGGQRQRIAIARALILKPEL 446
Cdd:PRK13637 95 -------QLFEEtiekdiafGPI--NLGLSEEEIENRVKRAMNIVGLDYEDyKDKSPFELSGGQKRRVAIAGVVAMEPKI 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1278835479 447 IILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVF 514
Cdd:PRK13637 166 LILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
301-506 |
2.41e-35 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 131.71 E-value: 2.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 301 VLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLHRWNRRQMLPVRPR-MQVVFQdpNSS 374
Cdd:TIGR02211 20 VLKGVSLSIGKGEIVAIVGSSGSGKST----LLHLLGgldnpTSGEVLFNGQSLSKLSSNERAKLRNKkLGFIYQ--FHH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 375 LNPRLSVLQIVEEGLRV-HQPGLSAQQREQEVMRvmvEVGLDPETRHRyPAEFSGGQRQRIAIARALILKPELIILDEPT 453
Cdd:TIGR02211 94 LLPDFTALENVAMPLLIgKKSVKEAKERAYEMLE---KVGLEHRINHR-PSELSGGERQRVAIARALVNQPSLVLADEPT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1278835479 454 SSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALcHQVIVLRQGEVVE 506
Cdd:TIGR02211 170 GNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQLFN 221
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
273-502 |
2.63e-35 |
|
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: 131.79 E-value: 2.63e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 273 TPLLRVEDLSVSFPI--RKGIlrRIvdrnPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEILFD 345
Cdd:COG4778 2 TTLLEVENLSKTFTLhlQGGK--RL----PVLDGVSFSVAAGECVALTGPSGAGKST----LLKCIygnylPDSGSILVR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 346 ----GMPLHRWNRRQMLPVRPR--------MQVVfqdpnsslnPRLSVLQIVEEGLRVHqpGLSAQQREQEVMRVMVEVG 413
Cdd:COG4778 72 hdggWVDLAQASPREILALRRRtigyvsqfLRVI---------PRVSALDVVAEPLLER--GVDREEARARARELLARLN 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 414 LDPETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLqeKHR-LAYIFISHDLQVVRAL 492
Cdd:COG4778 141 LPERLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEA--KARgTAIIGIFHDEEVREAV 218
|
250
....*....|
gi 1278835479 493 CHQVIVLRQG 502
Cdd:COG4778 219 ADRVVDVTPF 228
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
277-505 |
6.46e-35 |
|
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: 130.07 E-value: 6.46e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 277 RVEDLSVSFPirkgilrrivDRNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEILFDGMPLHRWNRR 355
Cdd:cd03226 1 RIENISFSYK----------KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIkESSGSILLNGKPIKAKERR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 356 QMlpvrprMQVVFQDPNSSLnprlsVLQIVEEGLRVHQPGLSA-QQREQEVMRVMvevGL-DPETRHryPAEFSGGQRQR 433
Cdd:cd03226 71 KS------IGYVMQDVDYQL-----FTDSVREELLLGLKELDAgNEQAETVLKDL---DLyALKERH--PLSLSGGQKQR 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1278835479 434 IAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRQGEVV 505
Cdd:cd03226 135 LAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGK-AVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-234 |
6.52e-35 |
|
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: 129.23 E-value: 6.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 6 LRIDNLSIAFSKqdetRTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLLPSPpvsypQGDILFHDRSLlhADEQT 85
Cdd:cd03229 1 LELKNVSKRYGQ----KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPD-----SGSILIDGEDL--TDLED 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 86 LRGIRGNKIAMIFQEPmvslnplhslekQLYEVLSlhrgmrkeaargeILDclertgirNAAkrlndfpHQLSGGERQRV 165
Cdd:cd03229 70 ELPPLRRRIGMVFQDF------------ALFPHLT-------------VLE--------NIA-------LGLSGGQQQRV 109
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1278835479 166 MIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGR 234
Cdd:cd03229 110 ALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-236 |
7.02e-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: 131.15 E-value: 7.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 6 LRIDNLSIAFSkqdETRTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLLPspPVSypqGDILFHDRSLLHADEQT 85
Cdd:cd03256 1 IEVENLSKTYP---NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVE--PTS---GSVLIDGTDINKLKGKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 86 LRGIRGnKIAMIFQEP------MVSLNPLHSL--EKQLYEVLSlhrGMRKEAARGEILDCLERTGIRNAAKRLNDfphQL 157
Cdd:cd03256 73 LRQLRR-QIGMIFQQFnlierlSVLENVLSGRlgRRSTWRSLF---GLFPKEEKQRALAALERVGLLDKAYQRAD---QL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1278835479 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGRCV 236
Cdd:cd03256 146 SGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
274-501 |
1.14e-34 |
|
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: 129.52 E-value: 1.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 274 PLLRVEDLSVSFpirkgilrrivDRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMP 348
Cdd:COG4133 1 MMLEAENLSCRR-----------GERLLFSGLSFTLAAGEALALTGPNGSGKTT----LLRILAgllppSAGEVLWNGEP 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 349 LHRwnrrqmLPVRPRMQVVFQDPNSSLNPRLSVLqiveEGLRVHQPGLSAQQREQEVMRVMVEVGLDPEtRHRYPAEFSG 428
Cdd:COG4133 66 IRD------AREDYRRRLAYLGHADGLKPELTVR----ENLRFWAALYGLRADREAIDEALEAVGLAGL-ADLPVRQLSA 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1278835479 429 GQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAyIFISHDLqvVRALCHQVIVLRQ 501
Cdd:COG4133 135 GQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAV-LLTTHQP--LELAAARVLDLGD 204
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
6-234 |
1.16e-34 |
|
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: 128.27 E-value: 1.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 6 LRIDNLSiaFSKQDETRTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLLPsppvsyPQ-GDILFHDRSLLHADEQ 84
Cdd:cd03228 1 IEFKNVS--FSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYD------PTsGEILIDGVDLRDLDLE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 85 TLRgirgNKIAMIFQEPmvslnplhslekQLYEvlslhrgmrkeaarGEILDCLertgirnaakrlndfphqLSGGERQR 164
Cdd:cd03228 73 SLR----KNIAYVPQDP------------FLFS--------------GTIRENI------------------LSGGQRQR 104
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 165 VMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDelNMSLLFITHNLSIVRKlADSVAVMQNGR 234
Cdd:cd03228 105 IAIARALLRDPPILILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
301-527 |
1.29e-34 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 130.64 E-value: 1.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 301 VLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI----------ASQGEILFDG-MPLhrwNRRQMLPVRPRMQVVFQ 369
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTT----LLRCInlleqpeagtIRVGDITIDTaRSL---SQQKGLIRQLRQHVGFV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 370 DPNSSLNPRLSVLQIVEEGLRV--HQPGLSAQQREQEVMrvmVEVGLDPEtRHRYPAEFSGGQRQRIAIARALILKPELI 447
Cdd:PRK11264 91 FQNFNLFPHRTVLENIIEGPVIvkGEPKEEATARARELL---AKVGLAGK-ETSYPRRLSGGQQQRVAIARALAMRPEVI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 448 ILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIfISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSAPTQRYTRQLLS 527
Cdd:PRK11264 167 LFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQFLE 245
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
299-525 |
1.74e-34 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 130.13 E-value: 1.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 299 NPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRL-----IASQGEILFDGMPL---HRWNRRQMLPVRPRMQVVFQD 370
Cdd:COG4161 15 HQALFDINLECPSGETLVLLGPSGAGKSS----LLRVlnlleTPDSGQLNIAGHQFdfsQKPSEKAIRLLRQKVGMVFQQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 371 PNssLNPRLSVLQ-IVEEGLRVHqpGLSAQQREQEVMRVMVEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPELIIL 449
Cdd:COG4161 91 YN--LWPHLTVMEnLIEAPCKVL--GLSKEQAREKAMKLLARLRLT-DKADRFPLHLSGGQQQRVAIARALMMEPQVLLF 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1278835479 450 DEPTSSLDRTVQAQILALLKGLQEKHrLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQrVFSAP-TQRYTRQL 525
Cdd:COG4161 166 DEPTAALDPEITAQVVEIIRELSQTG-ITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDAS-HFTQPqTEAFAHYL 240
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
277-503 |
1.78e-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: 127.36 E-value: 1.78e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 277 RVEDLSVSFPirkgilrrivdRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLHR 351
Cdd:cd00267 1 EIENLSFRYG-----------GRTALDNVSLTLKAGEIVALVGPNGSGKST----LLRAIAgllkpTSGEILIDGKDIAK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 352 WNRRQmlpVRPRMQVVFQdpnsslnprlsvlqiveeglrvhqpglsaqqreqevmrvmvevgldpetrhrypaeFSGGQR 431
Cdd:cd00267 66 LPLEE---LRRRIGYVPQ--------------------------------------------------------LSGGQR 86
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1278835479 432 QRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRQGE 503
Cdd:cd00267 87 QRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEEGR-TVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
274-519 |
2.71e-34 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 130.52 E-value: 2.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 274 PLLRVEDLSVSFPirkgilrriVDRNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIA-SQGEILFDGMPLhrw 352
Cdd:PRK13635 4 EIIRVEHISFRYP---------DAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLpEAGTITVGGMVL--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 353 NRRQMLPVRPRMQVVFQDPNSSLnprlsVLQIVEEGLRVhqpGLSAQQ--REQEVMRV---MVEVGLDpETRHRYPAEFS 427
Cdd:PRK13635 72 SEETVWDVRRQVGMVFQNPDNQF-----VGATVQDDVAF---GLENIGvpREEMVERVdqaLRQVGME-DFLNREPHRLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 428 GGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVrALCHQVIVLRQGEVVEQ 507
Cdd:PRK13635 143 GGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEA-AQADRVIVMNKGEILEE 221
|
250
....*....|..
gi 1278835479 508 GECQRVFSAPTQ 519
Cdd:PRK13635 222 GTPEEIFKSGHM 233
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
25-185 |
3.61e-34 |
|
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: 126.22 E-value: 3.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 25 VSDLTLQIQRGETLALVGESGSGKSVSALSILRLLpsppvSYPQGDILFHDRSLLHADEQTLRGirgnKIAMIFQEPmvS 104
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLL-----SPTEGTILLDGQDLTDDERKSLRK----EIGYVFQDP--Q 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 105 LNPLHSLEKQLYEVLSLhRGMRKEAARGEILDCLERTGIRNAAKR-LNDFPHQLSGGERQRVMIAMALLTRPELLIADEP 183
Cdd:pfam00005 70 LFPRLTVRENLRLGLLL-KGLSKREKDARAEEALEKLGLGDLADRpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
..
gi 1278835479 184 TT 185
Cdd:pfam00005 149 TA 150
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
6-234 |
4.08e-34 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 126.74 E-value: 4.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 6 LRIDNLSIAFSKqdetRTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLL-----PSppvsypQGDILFHDRSLLH 80
Cdd:cd03230 1 IEVRNLSKRYGK----KTALDDISLTVEKGEIYGLLGPNGAGKT----TLIKIIlgllkPD------SGEIKVLGKDIKK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 81 ADEQTLRgirgnKIAMIFQEPMvslnplhslekqLYEVLSLHrgmrkeaargEILDclertgirnaakrlndfphqLSGG 160
Cdd:cd03230 67 EPEEVKR-----RIGYLPEEPS------------LYENLTVR----------ENLK--------------------LSGG 99
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1278835479 161 ERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDElNMSLLFITHNLSIVRKLADSVAVMQNGR 234
Cdd:cd03230 100 MKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGR 172
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
292-527 |
5.24e-34 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 129.32 E-value: 5.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 292 LRRIVDRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEILFDGMPLHR----------WNRRQ 356
Cdd:PRK10619 11 LHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKST----FLRCInflekPSEGSIVVNGQTINLvrdkdgqlkvADKNQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 357 MLPVRPRMQVVFQDPNssLNPRLSVLQIVEEGlRVHQPGLSAQQREQEVMRVMVEVGLDPETRHRYPAEFSGGQRQRIAI 436
Cdd:PRK10619 87 LRLLRTRLTMVFQHFN--LWSHMTVLENVMEA-PIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 437 ARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSA 516
Cdd:PRK10619 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGK-TMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGN 242
|
250
....*....|.
gi 1278835479 517 PTQRYTRQLLS 527
Cdd:PRK10619 243 PQSPRLQQFLK 253
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
299-520 |
7.56e-34 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 128.29 E-value: 7.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 299 NPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEILFDGMPLhRWNRRQMLPVRPRMQVVFQDPNs 373
Cdd:PRK09493 14 TQVLHNIDLNIDQGEVVVIIGPSGSGKST----LLRCInkleeITSGDLIVDGLKV-NDPKVDERLIRQEAGMVFQQFY- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 374 sLNPRLSVLQIVEEGlRVHQPGLSAQQREQEVMRVMVEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPT 453
Cdd:PRK09493 88 -LFPHLTALENVMFG-PLRVRGASKEEAEKQARELLAKVGLA-ERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1278835479 454 SSLDRTVQAQILALLKGLQEKHrLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSAP-TQR 520
Cdd:PRK09493 165 SALDPELRHEVLKVMQDLAEEG-MTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPpSQR 231
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6-234 |
9.66e-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: 127.26 E-value: 9.66e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 6 LRIDNLSIAFSKQdetrTVVSDLTLQIQRGETLALVGESGSGKSvsalSILR---LLPSPPvsypQGDILFHDRSLLHaD 82
Cdd:cd03262 1 IEIKNLHKSFGDF----HVLKGIDLTVKKGEVVVIIGPSGSGKS----TLLRcinLLEEPD----SGTIIIDGLKLTD-D 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 83 EQTLRGIRgNKIAMIFQEpmVSLNPLHSLEKQLYEVLSLHRGMRKEAARGEILDCLERTGIrnaAKRLNDFPHQLSGGER 162
Cdd:cd03262 68 KKNINELR-QKVGMVFQQ--FNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGL---ADKADAYPAQLSGGQQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1278835479 163 QRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDElNMSLLFITHNLSIVRKLADSVAVMQNGR 234
Cdd:cd03262 142 QRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
6-257 |
1.24e-33 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 127.18 E-value: 1.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 6 LRIDNLSIAFskQDETRTvvsdLTLQIQRGETLALVGESGSGKSvsalSILRLLPS--PPVSypqGDILFHDRSLLHade 83
Cdd:COG3840 2 LRLDDLTYRY--GDFPLR----FDLTIAAGERVAILGPSGAGKS----TLLNLIAGflPPDS---GRILWNGQDLTA--- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 84 qTLRGIRgnKIAMIFQEpmvslNPL--H-SLEKQLYevLSLHRGMR-KEAARGEILDCLERTGIRNAAKRLndfPHQLSG 159
Cdd:COG3840 66 -LPPAER--PVSMLFQE-----NNLfpHlTVAQNIG--LGLRPGLKlTAEQRAQVEQALERVGLAGLLDRL---PGQLSG 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 160 GERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGRCVEQN 239
Cdd:COG3840 133 GQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADG 212
|
250
....*....|....*...
gi 1278835479 240 AASTLLSAPQHPYTQRLL 257
Cdd:COG3840 213 PTAALLDGEPPPALAAYL 230
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
299-508 |
1.48e-33 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 126.96 E-value: 1.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 299 NPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRL-IASQGEILFDGMPLHRWNRRQmlpVRPRMQVVFQDP---NSS 374
Cdd:cd03254 16 KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFyDPQKGQILIDGIDIRDISRKS---LRSMIGVVLQDTflfSGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 375 L--NPRLSVLQIVEEglrvhqpglsaqqreqEVMRVMVEVGLDPETRHR------YPAE----FSGGQRQRIAIARALIL 442
Cdd:cd03254 93 ImeNIRLGRPNATDE----------------EVIEAAKEAGAHDFIMKLpngydtVLGEnggnLSQGERQLLAIARAMLR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 443 KPELIILDEPTSSLD----RTVQAQILALLKGlqekhRLAYIfISHDLQVVRAlCHQVIVLRQGEVVEQG 508
Cdd:cd03254 157 DPKILILDEATSNIDteteKLIQEALEKLMKG-----RTSII-IAHRLSTIKN-ADKILVLDDGKIIEEG 219
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
6-252 |
1.60e-33 |
|
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: 134.96 E-value: 1.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 6 LRIDNLSiaFSKQDETRTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLL-----PSppvsypQGDILFHDRSLLH 80
Cdd:COG2274 474 IELENVS--FRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKS----TLLKLLlglyePT------SGRILIDGIDLRQ 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 81 ADEQTLRgirgNKIAMIFQEPMVslnplhsLEKQLYEVLSLHRgmrKEAARGEILDCLERTGIRNAAKRLndfPH----- 155
Cdd:COG2274 542 IDPASLR----RQIGVVLQDVFL-------FSGTIRENITLGD---PDATDEEIIEAARLAGLHDFIEAL---PMgydtv 604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 156 ------QLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDelNMSLLFITHNLSIVRkLADSVAV 229
Cdd:COG2274 605 vgeggsNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIR-LADRIIV 681
|
250 260
....*....|....*....|...
gi 1278835479 230 MQNGRCVEQNAASTLLSAPQHPY 252
Cdd:COG2274 682 LDKGRIVEDGTHEELLARKGLYA 704
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
27-249 |
2.42e-33 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 127.05 E-value: 2.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 27 DLTLQIQRGETLALVGESGSGKSvSALSILRLLPSPpvSYPQGDILFHDRSLLHA-DEQTLRGIRgNKIAMIFQEpmVSL 105
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKS-SLLRVLNLLEMP--RSGTLNIAGNHFDFSKTpSDKAIRELR-RNVGMVFQQ--YNL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 106 NPLHSLEKQLYEVLSLHRGMRKEAARGEILDCLERTGIRNAAKRlndFPHQLSGGERQRVMIAMALLTRPELLIADEPTT 185
Cdd:PRK11124 94 WPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADR---FPLHLSGGQQQRVAIARALMMEPQVLLFDEPTA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1278835479 186 ALDVTVQAQILTLLRDLRdELNMSLLFITHNLSIVRKLADSVAVMQNGRCVEQNAASTlLSAPQ 249
Cdd:PRK11124 171 ALDPEITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASC-FTQPQ 232
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
6-238 |
2.47e-33 |
|
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: 127.55 E-value: 2.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 6 LRIDNLSiaFSKQDETRTVVSDLTLQIQRGETLALVGESGSGKSVSA--LSILrLLPSppvsypQGDILFHDRSLLhaDE 83
Cdd:TIGR04520 1 IEVENVS--FSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAklLNGL-LLPT------SGKVTVDGLDTL--DE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 84 QTLRGIRgNKIAMIFQepmvslNPlhslEKQLyeVLSL----------HRGMRKEAARGEILDCLERTGIRNAAKRLndf 153
Cdd:TIGR04520 70 ENLWEIR-KKVGMVFQ------NP----DNQF--VGATveddvafgleNLGVPREEMRKRVDEALKLVGMEDFRDRE--- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 154 PHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRkLADSVAVMQNG 233
Cdd:TIGR04520 134 PHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAV-LADRVIVMNKG 212
|
....*
gi 1278835479 234 RCVEQ 238
Cdd:TIGR04520 213 KIVAE 217
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
16-256 |
3.13e-33 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 126.75 E-value: 3.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 16 SKQDETRTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLLPSPPVsYPQGDILFHDRSLL--HADEQTLRGIRGnk 93
Cdd:PRK09493 8 SKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKS----TLLRCINKLEE-ITSGDLIVDGLKVNdpKVDERLIRQEAG-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 94 iaMIFQEpmVSLNP-LHSLEKQLYEVLSLhRGMRKEAARGEILDCLERTGIrnaAKRLNDFPHQLSGGERQRVMIAMALL 172
Cdd:PRK09493 81 --MVFQQ--FYLFPhLTALENVMFGPLRV-RGASKEEAEKQARELLAKVGL---AERAHHYPSELSGGQQQRVAIARALA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 173 TRPELLIADEPTTALDVTVQAQILTLLRDLRDElNMSLLFITHNLSIVRKLADSVAVMQNGRCVEQNAASTLLSapqHPY 252
Cdd:PRK09493 153 VKPKLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIK---NPP 228
|
....
gi 1278835479 253 TQRL 256
Cdd:PRK09493 229 SQRL 232
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
299-527 |
3.30e-33 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 126.67 E-value: 3.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 299 NPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRL-----IASQGEI-----LFDGMplHRWNRRQMLPVRPRMQVVF 368
Cdd:PRK11124 15 HQALFDITLDCPQGETLVLLGPSGAGKSS----LLRVlnlleMPRSGTLniagnHFDFS--KTPSDKAIRELRRNVGMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 369 QDPNssLNPRLSVLQ-IVEEGLRVHqpGLSAQQREQEVMRVMVEVGLDPETrHRYPAEFSGGQRQRIAIARALILKPELI 447
Cdd:PRK11124 89 QQYN--LWPHLTVQQnLIEAPCRVL--GLSKDQALARAEKLLERLRLKPYA-DRFPLHLSGGQQQRVAIARALMMEPQVL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 448 ILDEPTSSLDRTVQAQILALLKGLQEKHrLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRvFSAPTQRYTRQLLS 527
Cdd:PRK11124 164 LFDEPTAALDPEITAQIVSIIRELAETG-ITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASC-FTQPQTEAFKNYLS 241
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-258 |
9.68e-33 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 131.81 E-value: 9.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 2 TQPLLRIDNLSiaFSKQDETRTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLLPsppvsYPQGDILFHDRSLLHA 81
Cdd:COG4987 330 GGPSLELEDVS--FRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLD-----PQSGSITLGGVDLRDL 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 82 DEQTLRgirgNKIAMIFQEPmvslnplHSLEKQLYEVLSLHRGmrkEAARGEILDCLERTGIrnaAKRLNDFPH------ 155
Cdd:COG4987 403 DEDDLR----RRIAVVPQRP-------HLFDTTLRENLRLARP---DATDEELWAALERVGL---GDWLAALPDgldtwl 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 156 -----QLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDelNMSLLFITHNLSIVRKlADSVAVM 230
Cdd:COG4987 466 geggrRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGLER-MDRILVL 542
|
250 260
....*....|....*....|....*...
gi 1278835479 231 QNGRCVEQNAASTLLSapQHPYTQRLLN 258
Cdd:COG4987 543 EDGRIVEQGTHEELLA--QNGRYRQLYQ 568
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
278-518 |
9.81e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 126.45 E-value: 9.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 278 VEDLSVSFPIRKgilrrivdrNPVLKNIRFSLRPGESLGLVGESGSGKST-----TGLaLLRLIASQGEILFDGMPLhrw 352
Cdd:PRK13640 8 FKHVSFTYPDSK---------KPALNDISFSIPRGSWTALIGHNGSGKSTiskliNGL-LLPDDNPNSKITVDGITL--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 353 NRRQMLPVRPRMQVVFQDPNSSLnprlsVLQIVEE----GLRvhQPGLSAQQREQEVMRVMVEVGL----DPEtrhryPA 424
Cdd:PRK13640 75 TAKTVWDIREKVGIVFQNPDNQF-----VGATVGDdvafGLE--NRAVPRPEMIKIVRDVLADVGMldyiDSE-----PA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 425 EFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVrALCHQVIVLRQGEV 504
Cdd:PRK13640 143 NLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKL 221
|
250
....*....|....
gi 1278835479 505 VEQGECQRVFSAPT 518
Cdd:PRK13640 222 LAQGSPVEIFSKVE 235
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
291-508 |
1.09e-32 |
|
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: 124.29 E-value: 1.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 291 ILRRIVDR---NPVLKNIRFSLRPGESLGLVGESGSGKSTTglalLRLIA-----SQGEILFDGmplhrwNRRQMLPVRP 362
Cdd:cd03301 2 ELENVTKRfgnVTALDDLNLDIADGEFVVLLGPSGCGKTTT----LRMIAgleepTSGRIYIGG------RDVTDLPPKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 363 R-MQVVFQdpNSSLNPRLSVLQIVEEGLRV-HQPGLSAQQREQEVMRVMvevGLDpETRHRYPAEFSGGQRQRIAIARAL 440
Cdd:cd03301 72 RdIAMVFQ--NYALYPHMTVYDNIAFGLKLrKVPKDEIDERVREVAELL---QIE-HLLDRKPKQLSGGQRQRVALGRAI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1278835479 441 ILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:cd03301 146 VREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-234 |
1.26e-32 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 123.77 E-value: 1.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 6 LRIDNLSIafskQDETRTVVSDLTLQIQRGETLALVGESGSGKSVsalsILRLLPS--PPVSypqGDILFHDRSLLHADE 83
Cdd:COG4619 1 LELEGLSF----RVGGKPILSPVSLTLEAGECVAITGPSGSGKST----LLRALADldPPTS---GEIYLDGKPLSAMPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 84 QTLRGirgnKIAMIFQEPMVslnplhsLEKQLYEVLSLHRGMRKEAARGE-ILDCLERTGIRNAAkrLNDFPHQLSGGER 162
Cdd:COG4619 70 PEWRR----QVAYVPQEPAL-------WGGTVRDNLPFPFQLRERKFDRErALELLERLGLPPDI--LDKPVERLSGGER 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1278835479 163 QRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGR 234
Cdd:COG4619 137 QRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGR 208
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
275-517 |
1.27e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 125.96 E-value: 1.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 275 LLRVEDLSVSFPirkgilrrivDRNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEILFDGMPLhRWN 353
Cdd:PRK13639 1 ILETRDLKYSYP----------DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILkPTSGEVLIKGEPI-KYD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 354 RRQMLPVRPRMQVVFQDPNSSL-NPRlsVLQIVEEGlrvhqP---GLSAQQREQEVMRVMVEVGLDPETRhRYPAEFSGG 429
Cdd:PRK13639 70 KKSLLEVRKTVGIVFQNPDDQLfAPT--VEEDVAFG-----PlnlGLSKEEVEKRVKEALKAVGMEGFEN-KPPHHLSGG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 430 QRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHrLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGE 509
Cdd:PRK13639 142 QKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEG-ITIIISTHDVDLVPVYADKVYVMSDGKIIKEGT 220
|
....*...
gi 1278835479 510 CQRVFSAP 517
Cdd:PRK13639 221 PKEVFSDI 228
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-247 |
1.39e-32 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 131.42 E-value: 1.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 2 TQPLLRIDNLSIAFskqDETRTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLLPsppvsyP-QGDILFHDRSLLH 80
Cdd:COG4988 333 GPPSIELEDVSFSY---PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLP------PySGSILINGVDLSD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 81 ADEQTLRgirgNKIAMIFQEPMVslnplhsLEKQLYEVLSLHRgmrKEAARGEILDCLERTGIRNAAKRLN---DFP--- 154
Cdd:COG4988 404 LDPASWR----RQIAWVPQNPYL-------FAGTIRENLRLGR---PDASDEELEAALEAAGLDEFVAALPdglDTPlge 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 155 --HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELnmSLLFITHNLSIVRkLADSVAVMQN 232
Cdd:COG4988 470 ggRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLALLA-QADRILVLDD 546
|
250
....*....|....*
gi 1278835479 233 GRCVEQNAASTLLSA 247
Cdd:COG4988 547 GRIVEQGTHEELLAK 561
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
301-521 |
1.80e-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: 1.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 301 VLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLHRwnrrqmLPVRPR-MQVVFQdpNSS 374
Cdd:TIGR00968 15 ALDDVNLEVPTGSLVALLGPSGSGKST----LLRIIAgleqpDSGRIRLNGQDATR------VHARDRkIGFVFQ--HYA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 375 LNPRLSVLQIVEEGLRVHQ-PGLSAQQREQEVMRVMVEVGLdpetRHRYPAEFSGGQRQRIAIARALILKPELIILDEPT 453
Cdd:TIGR00968 83 LFKHLTVRDNIAFGLEIRKhPKAKIKARVEELLELVQLEGL----GDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPF 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1278835479 454 SSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSAPTQRY 521
Cdd:TIGR00968 159 GALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPF 226
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
11-248 |
1.92e-32 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 127.52 E-value: 1.92e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 11 LSIAFSKQdetrtvVSDLTLQIQ-----RGETlALVGESGSGKSvsalSILRL---LPSPPvsypQGDILFHDRSLLHAD 82
Cdd:COG4148 3 LEVDFRLR------RGGFTLDVDftlpgRGVT-ALFGPSGSGKT----TLLRAiagLERPD----SGRIRLGGEVLQDSA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 83 EQTLRGIRGNKIAMIFQEPmvSLNPlHslekqlYEVLS-LHRGMR---KEAARGEILDCLERTGIrnaAKRLNDFPHQLS 158
Cdd:COG4148 68 RGIFLPPHRRRIGYVFQEA--RLFP-H------LSVRGnLLYGRKrapRAERRISFDEVVELLGI---GHLLDRRPATLS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 159 GGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGRCVEQ 238
Cdd:COG4148 136 GGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVAS 215
|
250
....*....|
gi 1278835479 239 NAASTLLSAP 248
Cdd:COG4148 216 GPLAEVLSRP 225
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
24-255 |
1.93e-32 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 124.35 E-value: 1.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 24 VVSDLTLQIQRGETLALVGESGSGKSvSALSILRLLPSPpvSYPQGDILFHDRSL-LHADEQTLRGIRGnKIAMIFQEpm 102
Cdd:COG4161 17 ALFDINLECPSGETLVLLGPSGAGKS-SLLRVLNLLETP--DSGQLNIAGHQFDFsQKPSEKAIRLLRQ-KVGMVFQQ-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 103 VSLNPLHSLEKQLYE----VLslhrGMRKEAARGEILDCLERTGIRNAAKRlndFPHQLSGGERQRVMIAMALLTRPELL 178
Cdd:COG4161 91 YNLWPHLTVMENLIEapckVL----GLSKEQAREKAMKLLARLRLTDKADR---FPLHLSGGQQQRVAIARALMMEPQVL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1278835479 179 IADEPTTALDVTVQAQILTLLRDLRdELNMSLLFITHNLSIVRKLADSVAVMQNGRCVEQNAASTLlsapQHPYTQR 255
Cdd:COG4161 164 LFDEPTAALDPEITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDASHF----TQPQTEA 235
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
25-252 |
2.01e-32 |
|
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: 125.06 E-value: 2.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 25 VSDLTLQIQRGETLALVGESGSGKSVSALSILRLLPspPVSypqGDILFHDRSLLHADEQTLRGIRGNKIAMIFQE--PM 102
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIE--PTS---GKVLIDGQDIAAMSRKELRELRRKKISMVFQSfaLL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 103 VSLNPLHSLEKQLyEVLSLHRGMRKEAARgeilDCLERTGIRNAAKRlndFPHQLSGGERQRVMIAMALLTRPELLIADE 182
Cdd:cd03294 115 PHRTVLENVAFGL-EVQGVPRAEREERAA----EALELVGLEGWEHK---YPDELSGGMQQRVGLARALAVDPDILLMDE 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 183 PTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGRCVEQNAASTLLSAPQHPY 252
Cdd:cd03294 187 AFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDY 256
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
16-227 |
2.25e-32 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 123.11 E-value: 2.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 16 SKQDETRTVVSDLTLQIQRGETLALVGESGSGKSvSALSILRLLPSppvsYPQGDILFHDRSLLHADEQTLRGIRGNKIA 95
Cdd:TIGR03608 5 SKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKS-TLLNIIGLLEK----FDSGQVYLNGQETPPLNSKKASKFRREKLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 96 MIFQEpmVSLNPLHSLEKQLYEVLSLHRGMRKEAaRGEILDCLERTGIRNaakRLNDFPHQLSGGERQRVMIAMALLTRP 175
Cdd:TIGR03608 80 YLFQN--FALIENETVEENLDLGLKYKKLSKKEK-REKKKEALEKVGLNL---KLKQKIYELSGGEQQRVALARAILKPP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1278835479 176 ELLIADEPTTALDVTVQAQILTLLRDLRDElNMSLLFITHNLSIVRKlADSV 227
Cdd:TIGR03608 154 PLILADEPTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDPEVAKQ-ADRV 203
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
252-508 |
3.04e-32 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 131.38 E-value: 3.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 252 YTQRLLNSEPSGDPVPLDAdsTPLLRVEDLSVSFPIRKgilrrivdRNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLA 331
Cdd:TIGR00958 457 YLDRKPNIPLTGTLAPLNL--EGLIEFQDVSFSYPNRP--------DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAAL 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 332 LLRL-IASQGEILFDGMPL----HRWNRRQMlpvrprmQVVFQDPnssLNPRLSVLQIVEEGLRvhqpglsaQQREQEVM 406
Cdd:TIGR00958 527 LQNLyQPTGGQVLLDGVPLvqydHHYLHRQV-------ALVGQEP---VLFSGSVRENIAYGLT--------DTPDEEIM 588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 407 RVMVEVGLDP---ETRHRYPAE-------FSGGQRQRIAIARALILKPELIILDEPTSSLDrtvqAQILALLKGLQEKHR 476
Cdd:TIGR00958 589 AAAKAANAHDfimEFPNGYDTEvgekgsqLSGGQKQRIAIARALVRKPRVLILDEATSALD----AECEQLLQESRSRAS 664
|
250 260 270
....*....|....*....|....*....|..
gi 1278835479 477 LAYIFISHDLQVVRAlCHQVIVLRQGEVVEQG 508
Cdd:TIGR00958 665 RTVLLIAHRLSTVER-ADQILVLKKGSVVEMG 695
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
275-515 |
3.09e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 124.96 E-value: 3.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 275 LLRVEDLSVSFPirkgilrrivDRNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIA-SQGEILFDGMPLHrWN 353
Cdd:PRK13636 5 ILKVEELNYNYS----------DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKpSSGRILFDGKPID-YS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 354 RRQMLPVRPRMQVVFQDPNSSLNPRlSVLQIVEEGlrVHQPGLSAQQREQEVMRVMVEVGLDPeTRHRYPAEFSGGQRQR 433
Cdd:PRK13636 74 RKGLMKLRESVGMVFQDPDNQLFSA-SVYQDVSFG--AVNLKLPEDEVRKRVDNALKRTGIEH-LKDKPTHCLSFGQKKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 434 IAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRV 513
Cdd:PRK13636 150 VAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEV 229
|
..
gi 1278835479 514 FS 515
Cdd:PRK13636 230 FA 231
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
275-521 |
3.76e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 124.71 E-value: 3.76e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 275 LLRVEDLSVSFPirkgilrrivDRNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIASQ-GEILFDGMPLHRWN 353
Cdd:PRK13644 1 MIRLENVSYSYP----------DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQkGKVLVSGIDTGDFS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 354 RRQmlPVRPRMQVVFQDPNSSLnprlsVLQIVEEGLRVHQPGLSAQQRE--QEVMRVMVEVGLDpETRHRYPAEFSGGQR 431
Cdd:PRK13644 71 KLQ--GIRKLVGIVFQNPETQF-----VGRTVEEDLAFGPENLCLPPIEirKRVDRALAEIGLE-KYRHRSPKTLSGGQG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 432 QRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRlAYIFISHDLQVVRAlCHQVIVLRQGEVVEQGECQ 511
Cdd:PRK13644 143 QCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGK-TIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPE 220
|
250
....*....|
gi 1278835479 512 RVFSAPTQRY 521
Cdd:PRK13644 221 NVLSDVSLQT 230
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
292-518 |
3.76e-32 |
|
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: 123.60 E-value: 3.76e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 292 LRRIVDRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLHRwnrrqmLPVRPRmQV 366
Cdd:cd03296 8 VSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTT----LLRLIAglerpDSGTILFGGEDATD------VPVQER-NV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 367 --VFQdpNSSLNPRLSVLQIVEEGLRVH--QPGLSAQQREQEVMRVMVEVGLDPETRhRYPAEFSGGQRQRIAIARALIL 442
Cdd:cd03296 77 gfVFQ--HYALFRHMTVFDNVAFGLRVKprSERPPEAEIRAKVHELLKLVQLDWLAD-RYPAQLSGGQRQRVALARALAV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1278835479 443 KPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSAPT 518
Cdd:cd03296 154 EPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPA 229
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
6-257 |
4.83e-32 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 126.03 E-value: 4.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 6 LRIDNLSiafsKQDETRTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLL-----PSppvsypQGDILFHDRSL-- 78
Cdd:COG1118 3 IEVRNIS----KRFGSFTLLDDVSLEIASGELVALLGPSGSGKT----TLLRIIagletPD------SGRIVLNGRDLft 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 79 -LHADEqtlrgiRgnKIAMIFQEPM------VSLNPLHSLEkqlyevlslHRGMRKEAARGEILDCLERTGIRNAAKRln 151
Cdd:COG1118 69 nLPPRE------R--RVGFVFQHYAlfphmtVAENIAFGLR---------VRPPSKAEIRARVEELLELVQLEGLADR-- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 152 dFPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQ 231
Cdd:COG1118 130 -YPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMN 208
|
250 260
....*....|....*....|....*.
gi 1278835479 232 NGRCVEQNAASTLLSAPQHPYTQRLL 257
Cdd:COG1118 209 QGRIEQVGTPDEVYDRPATPFVARFL 234
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
7-230 |
5.58e-32 |
|
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: 122.26 E-value: 5.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 7 RIDNLSIAFSKqdetRTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLLPsppvsyP-QGDILFHDRSLlhadeqt 85
Cdd:cd03235 1 EVEDLTVSYGG----HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLK------PtSGSIRVFGKPL------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 86 lrGIRGNKIAMIFQEPMVSLN-PLHSLE---KQLYEVLSLHRGMRKEAARgEILDCLERTGIRNAAKRLNDfphQLSGGE 161
Cdd:cd03235 64 --EKERKRIGYVPQRRSIDRDfPISVRDvvlMGLYGHKGLFRRLSKADKA-KVDEALERVGLSELADRQIG---ELSGGQ 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1278835479 162 RQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDElNMSLLFITHNLSIVRKLADSVAVM 230
Cdd:cd03235 138 QQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
23-504 |
5.65e-32 |
|
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: 128.79 E-value: 5.65e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 23 TVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLLPS--PPVSYpQGDILFHDRSLlhaDEQTLRGIRGNKIAMIFQE 100
Cdd:TIGR02633 15 KALDGIDLEVRPGECVGLCGENGAGKS----TLMKILSGvyPHGTW-DGEIYWSGSPL---KASNIRDTERAGIVIIHQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 101 PMVSLNpLHSLEKQLYEVLSLHRGMRKEAA----RGEILDCLERTGIRNAAKRLNDfphqLSGGERQRVMIAMALLTRPE 176
Cdd:TIGR02633 87 LTLVPE-LSVAENIFLGNEITLPGGRMAYNamylRAKNLLRELQLDADNVTRPVGD----YGGGQQQLVEIAKALNKQAR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 177 LLIADEPTTALDVTVQAQILTLLRDLRDElNMSLLFITHNLSIVRKLADSVAVMQNGRCVEQNAASTlLSAPQhPYTQRL 256
Cdd:TIGR02633 162 LLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMST-MSEDD-IITMMV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 257 LNSEPSGDPVPLDADSTPLLRVEDLSVSFPIRKGILRriVDrnpvlkNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI 336
Cdd:TIGR02633 239 GREITSLYPHEPHEIGDVILEARNLTCWDVINPHRKR--VD------DVSFSLRRGEILGVAGLVGAGRTELVQALFGAY 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 337 ASQ--GEILFDGMPLHRWNRRQ-------MLPVRPRMQVVFQDPNSSLNPRLSVLQIVEEGLRVhqpglSAQQREQEVMR 407
Cdd:TIGR02633 311 PGKfeGNVFINGKPVDIRNPAQairagiaMVPEDRKRHGIVPILGVGKNITLSVLKSFCFKMRI-----DAAAELQIIGS 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 408 VMVEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHrLAYIFISHDLQ 487
Cdd:TIGR02633 386 AIQRLKVKTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEG-VAIIVVSSELA 464
|
490
....*....|....*..
gi 1278835479 488 VVRALCHQVIVLRQGEV 504
Cdd:TIGR02633 465 EVLGLSDRVLVIGEGKL 481
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-238 |
8.04e-32 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 123.59 E-value: 8.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 1 MTQPLLRIDNLSiaFSKQDETRTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLLPspPVSypqGDILFHDRSLlh 80
Cdd:PRK13635 1 MKEEIIRVEHIS--FRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLL--PEA---GTITVGGMVL-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 81 aDEQTLRGIRgNKIAMIFQEP-------MVSLNPLHSLEKQlyevlslhrGMRKEAARGEILDCLERTGIRNAAKRLndf 153
Cdd:PRK13635 72 -SEETVWDVR-RQVGMVFQNPdnqfvgaTVQDDVAFGLENI---------GVPREEMVERVDQALRQVGMEDFLNRE--- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 154 PHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKlADSVAVMQNG 233
Cdd:PRK13635 138 PHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKG 216
|
....*
gi 1278835479 234 RCVEQ 238
Cdd:PRK13635 217 EILEE 221
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-254 |
9.43e-32 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 122.84 E-value: 9.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 2 TQPLLRIDNLSIAFSKqdetRTVVSDLTLQIQRGETLALVGESGSGKSvsalSILR-------LLPSPPVSypqGDILFH 74
Cdd:COG1117 8 LEPKIEVRNLNVYYGD----KQALKDINLDIPENKVTALIGPSGCGKS----TLLRclnrmndLIPGARVE---GEILLD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 75 DRSLLHA--DEQTLRgiRgnKIAMIFQEPmvslNPL-HSLekqlYE-V---LSLHrGMRKEAARGEIL-DCLERTGIRNA 146
Cdd:COG1117 77 GEDIYDPdvDVVELR--R--RVGMVFQKP----NPFpKSI----YDnVaygLRLH-GIKSKSELDEIVeESLRKAALWDE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 147 AK-RLNDFPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDElnMSLLFITHNLSIVRKLAD 225
Cdd:COG1117 144 VKdRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD--YTIVIVTHNMQQAARVSD 221
|
250 260
....*....|....*....|....*....
gi 1278835479 226 SVAVMQNGRCVEQNAASTLLSAPQHPYTQ 254
Cdd:COG1117 222 YTAFFYLGELVEFGPTEQIFTNPKDKRTE 250
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
300-504 |
1.12e-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: 1.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 300 PVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLHRWNRRQMLPVRPRMQVVFQDpnSS 374
Cdd:cd03292 15 AALDGINISISAGEFVFLVGPSGAGKST----LLKLIYkeelpTSGTIRVNGQDVSDLRGRAIPYLRRKIGVVFQD--FR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 375 LNPRLSVLQIVEEGLRVHQ-PGLSAQQReqeVMRVMVEVGLdpETRHR-YPAEFSGGQRQRIAIARALILKPELIILDEP 452
Cdd:cd03292 89 LLPDRNVYENVAFALEVTGvPPREIRKR---VPAALELVGL--SHKHRaLPAELSGGEQQRVAIARAIVNSPTILIADEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1278835479 453 TSSLDRTVQAQILALLKGLQEkhRLAYIFIS-HDLQVVRALCHQVIVLRQGEV 504
Cdd:cd03292 164 TGNLDPDTTWEIMNLLKKINK--AGTTVVVAtHAKELVDTTRHRVIALERGKL 214
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
274-507 |
1.22e-31 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 122.66 E-value: 1.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 274 PLLRVEDLSVSFPIRKGilrrivdRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMP 348
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQ-------PQPALQDVSLTIESGEFVVALGASGCGKTT----LLNLIAgflapSSGEITLDGVP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 349 LHRwnrrqmlPVRPRmQVVFQDpnSSLNPRLSVLQIVEEGLRVHqpGLSAQQREQEVMRVMVEVGLDpETRHRYPAEFSG 428
Cdd:COG4525 71 VTG-------PGADR-GVVFQK--DALLPWLNVLDNVAFGLRLR--GVPKAERRARAEELLALVGLA-DFARRRIWQLSG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 429 GQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVL--RQGEVVE 506
Cdd:COG4525 138 GMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMspGPGRIVE 217
|
.
gi 1278835479 507 Q 507
Cdd:COG4525 218 R 218
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
7-234 |
1.24e-31 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 119.27 E-value: 1.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 7 RIDNLSIAFskqdETRTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLLPSPpvsypQGDILFHDRSLLHADEQTL 86
Cdd:cd00267 1 EIENLSFRY----GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPT-----SGEILIDGKDIAKLPLEEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 87 RgirgNKIAMIFQepmvslnplhslekqlyevlslhrgmrkeaargeildclertgirnaakrlndfphqLSGGERQRVM 166
Cdd:cd00267 72 R----RRIGYVPQ---------------------------------------------------------LSGGQRQRVA 90
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1278835479 167 IAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDElNMSLLFITHNLSIVRKLADSVAVMQNGR 234
Cdd:cd00267 91 LARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
305-517 |
1.50e-31 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 124.84 E-value: 1.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 305 IRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLHRWNRRQMLPV-RPRMQVVFQDpnSSLNPR 378
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTT----LIRLIAgltrpDEGEIVLNGRTLFDSRKGIFLPPeKRRIGYVFQE--ARLFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 379 LSVLQIVEEGLRVHQPGLSaQQREQEVMRVMvevGLDPETRhRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDR 458
Cdd:TIGR02142 90 LSVRGNLRYGMKRARPSER-RISFERVIELL---GIGHLLG-RLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1278835479 459 TVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSAP 517
Cdd:TIGR02142 165 PRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
17-258 |
1.63e-31 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 122.17 E-value: 1.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 17 KQDETRTVVSDLTLQIQRGETLALVGESGSGKSvSALSILRLLPSPPVSYPQ-GDILFHDRSLLHADEQTLRGIRgNKIA 95
Cdd:PRK11264 11 KKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKT-TLLRCINLLEQPEAGTIRvGDITIDTARSLSQQKGLIRQLR-QHVG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 96 MIFQEpmVSLNPLHSLEKQLYEVLSLHRGMRKEAARGEILDCLERTGIrnaAKRLNDFPHQLSGGERQRVMIAMALLTRP 175
Cdd:PRK11264 89 FVFQN--FNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGL---AGKETSYPRRLSGGQQQRVAIARALAMRP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 176 ELLIADEPTTALDVTVQAQILTLLRDLRDElNMSLLFITHNLSIVRKLADSVAVMQNGRCVEQNAASTLLSAPQHPYTQR 255
Cdd:PRK11264 164 EVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQ 242
|
...
gi 1278835479 256 LLN 258
Cdd:PRK11264 243 FLE 245
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
6-249 |
1.64e-31 |
|
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: 121.67 E-value: 1.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 6 LRIDNLSIAFSKqdetrTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLLPspPVSypqGDILFHDrsllhADEQT 85
Cdd:cd03299 1 LKVENLSKDWKE-----FKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIK--PDS---GKILLNG-----KDITN 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 86 LRGIRGNkIAMIFQEpmVSLNPLHSLEKQLYEVLSLHRGMRKEAARgEILDCLERTGIRNAakrLNDFPHQLSGGERQRV 165
Cdd:cd03299 66 LPPEKRD-ISYVPQN--YALFPHMTVYKNIAYGLKKRKVDKKEIER-KVLEIAEMLGIDHL---LNRKPETLSGGEQQRV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 166 MIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGRCVEQNAASTLL 245
Cdd:cd03299 139 AIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVF 218
|
....
gi 1278835479 246 SAPQ 249
Cdd:cd03299 219 KKPK 222
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
6-260 |
1.67e-31 |
|
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: 121.64 E-value: 1.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 6 LRIDNLSIAFSKqdeTRTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLL-PSppvsypQGDILFHDRSLLHADEQ 84
Cdd:cd03295 1 IEFENVTKRYGG---GKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIePT------SGEIFIDGEDIREQDPV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 85 TLRgirgNKIAMIFQEpmVSLNPLHSLEKQLYEVLSLhRGMRKEAARGEILDCLERTGIrNAAKRLNDFPHQLSGGERQR 164
Cdd:cd03295 72 ELR----RKIGYVIQQ--IGLFPHMTVEENIALVPKL-LKWPKEKIRERADELLALVGL-DPAEFADRYPHELSGGQQQR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 165 VMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGRCVEQNAASTL 244
Cdd:cd03295 144 VGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
250
....*....|....*.
gi 1278835479 245 LSAPQHPYTQRLLNSE 260
Cdd:cd03295 224 LRSPANDFVAEFVGAD 239
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
27-234 |
2.65e-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: 2.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 27 DLTLQIQ---RGETLALVGESGSGKSvSALSILRLLPSPPVsypqGDILFHDRSLLHADEQTLRGIRGNKIAMIFQEpmV 103
Cdd:cd03297 12 DFTLKIDfdlNEEVTGIFGASGAGKS-TLLRCIAGLEKPDG----GTIVLNGTVLFDSRKKINLPPQQRKIGLVFQQ--Y 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 104 SLNPLHSLEKQLYEVLSLHRGMRKEAARGEILDCLERTGIrnaakrLNDFPHQLSGGERQRVMIAMALLTRPELLIADEP 183
Cdd:cd03297 85 ALFPHLNVRENLAFGLKRKRNREDRISVDELLDLLGLDHL------LNRYPAQLSGGEKQRVALARALAAQPELLLLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1278835479 184 TTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGR 234
Cdd:cd03297 159 FSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGR 209
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
273-522 |
2.74e-31 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 124.67 E-value: 2.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 273 TPLLRVEDLSVSFpirkgilrrivDRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGM 347
Cdd:PRK09452 12 SPLVELRGISKSF-----------DGKEVISNLDLTINNGEFLTLLGPSGCGKTT----VLRLIAgfetpDSGRIMLDGQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 348 PLHRwnrrqmLPVRPR-MQVVFQdpNSSLNPRLSVLQIVEEGLRVHQpgLSAQQREQEVMRVMVEVGLDpETRHRYPAEF 426
Cdd:PRK09452 77 DITH------VPAENRhVNTVFQ--SYALFPHMTVFENVAFGLRMQK--TPAAEITPRVMEALRMVQLE-EFAQRKPHQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 427 SGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVE 506
Cdd:PRK09452 146 SGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQ 225
|
250
....*....|....*.
gi 1278835479 507 QGECQRVFSAPTQRYT 522
Cdd:PRK09452 226 DGTPREIYEEPKNLFV 241
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
269-527 |
3.15e-31 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 121.30 E-value: 3.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 269 DADSTPLLRVEDLSVSFpirkgilrrivDRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLR-------LIASQ-- 339
Cdd:COG1117 5 ASTLEPKIEVRNLNVYY-----------GDKQALKDINLDIPENKVTALIGPSGCGKST----LLRclnrmndLIPGArv 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 340 -GEILFDGMPLHRwnrRQMLPVRPRMQV--VFQDPNsslnP-RLSVLQIVEEGLRVHqpGLsaqqREQEVMRVMVE---- 411
Cdd:COG1117 70 eGEILLDGEDIYD---PDVDVVELRRRVgmVFQKPN----PfPKSIYDNVAYGLRLH--GI----KSKSELDEIVEeslr 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 412 -VGLDPETRHR---YPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLqeKHRLAYIFISHDLQ 487
Cdd:COG1117 137 kAALWDEVKDRlkkSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILEL--KKDYTIVIVTHNMQ 214
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1278835479 488 VVRALCHQVIVLRQGEVVEQGECQRVFSAPTQRYTRQLLS 527
Cdd:COG1117 215 QAARVSDYTAFFYLGELVEFGPTEQIFTNPKDKRTEDYIT 254
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-506 |
3.24e-31 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 126.82 E-value: 3.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 1 MTQPLLRIDNLSIAFSKQdetrTVVSDLTLQIQRGETLALVGESGSGKSvSALSILRLLPSPPvsypQGDILFHDRS--- 77
Cdd:PRK09700 1 MATPYISMAGIGKSFGPV----HALKSVNLTVYPGEIHALLGENGAGKS-TLMKVLSGIHEPT----KGTITINNINynk 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 78 LLHADEQTLrgirgnKIAMIFQEPMVsLNPLhSLEKQLY-------EVLSL----HRGMRKEAArgEILDcleRTGIRna 146
Cdd:PRK09700 72 LDHKLAAQL------GIGIIYQELSV-IDEL-TVLENLYigrhltkKVCGVniidWREMRVRAA--MMLL---RVGLK-- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 147 aKRLNDFPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDElNMSLLFITHNLSIVRKLADS 226
Cdd:PRK09700 137 -VDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDR 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 227 VAVMQNGRCVeqnaASTLLSAPQHPYTQRLLNSEPSGDPVPLDADSTpllRVEDLSVSFPIRKgILRRivDRNPVlKNIR 306
Cdd:PRK09700 215 YTVMKDGSSV----CSGMVSDVSNDDIVRLMVGRELQNRFNAMKENV---SNLAHETVFEVRN-VTSR--DRKKV-RDIS 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 307 FSLRPGESLGLVGESGSGKSTTGLALLRL--IASqGEILFDGMPLHrwNRRQMLPVRPRMQVVFQD-------PNSSLNP 377
Cdd:PRK09700 284 FSVCRGEILGFAGLVGSGRTELMNCLFGVdkRAG-GEIRLNGKDIS--PRSPLDAVKKGMAYITESrrdngffPNFSIAQ 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 378 RLSVLQIVEEGLRVHQPGLSAQQREQEVMRVMVE-VGLDPETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSL 456
Cdd:PRK09700 361 NMAISRSLKDGGYKGAMGLFHEVDEQRTAENQRElLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGI 440
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1278835479 457 DRTVQAQILALLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRQGEVVE 506
Cdd:PRK09700 441 DVGAKAEIYKVMRQLADDGK-VILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
317-521 |
3.71e-31 |
|
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: 122.99 E-value: 3.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 317 LVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLhrwnrRQMLPVRPRMQVVFQdpNSSLNPRLSVLQIVEEGLRv 391
Cdd:TIGR01187 1 LLGPSGCGKTT----LLRLLAgfeqpDSGSIMLDGEDV-----TNVPPHLRHINMVFQ--SYALFPHMTVEENVAFGLK- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 392 hQPGLSAQQREQEVMRVMVEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGL 471
Cdd:TIGR01187 69 -MRKVPRAEIKPRVLEALRLVQLE-EFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTI 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1278835479 472 QEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSAPTQRY 521
Cdd:TIGR01187 147 QEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLF 196
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
273-509 |
1.04e-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: 119.80 E-value: 1.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 273 TPLLRVEDLSVSFpirkgilrrivDRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI------ASQGEI-LFd 345
Cdd:COG1119 1 DPLLELRNVTVRR-----------GGKTILDDISWTVKPGEHWAILGPNGAGKST----LLSLItgdlppTYGNDVrLF- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 346 GMPLHRWNrrqMLPVRPRMQVVFQDPNSSLNPRLSVLQIVEEGL-----RVHQPglSAQQREQeVMRVMVEVGLDpETRH 420
Cdd:COG1119 65 GERRGGED---VWELRKRIGLVSPALQLRFPRDETVLDVVLSGFfdsigLYREP--TDEQRER-ARELLELLGLA-HLAD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 421 RYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLR 500
Cdd:COG1119 138 RPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLK 217
|
....*....
gi 1278835479 501 QGEVVEQGE 509
Cdd:COG1119 218 DGRVVAAGP 226
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
19-238 |
1.46e-30 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 125.28 E-value: 1.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 19 DETRTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLLPS--PPVSypqGDILFHDRSLLHADEQTLRgirgNKIAM 96
Cdd:COG1132 350 PGDRPVLKDISLTIPPGETVALVGPSGSGKS----TLVNLLLRfyDPTS---GRILIDGVDIRDLTLESLR----RQIGV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 97 IFQEPMVslnplhsLEKQLYEVLSLhrGmRKEAARGEILDCLERTgirNAAKRLNDFPHQ-----------LSGGERQRV 165
Cdd:COG1132 419 VPQDTFL-------FSGTIRENIRY--G-RPDATDEEVEEAAKAA---QAHEFIEALPDGydtvvgergvnLSGGQRQRI 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1278835479 166 MIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDelNMSLLFITHNLSIVRKlADSVAVMQNGRCVEQ 238
Cdd:COG1132 486 AIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQ 555
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-246 |
1.98e-30 |
|
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: 118.81 E-value: 1.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 5 LLRIDNLSIAFSKqdetRTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLL-----PSppvsypQGDILFHDRSLL 79
Cdd:COG4555 1 MIEVENLSKKYGK----VPALKDVSFTAKDGEITGLLGPNGAGKT----TLLRMLagllkPD------SGSILIDGEDVR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 80 HADEQTLRgirgnKIAMIFQEPMVSLNplHSLEKQLYEVLSLHrGMRKEAARGEILDCLERTGIRNAAKRLndfPHQLSG 159
Cdd:COG4555 67 KEPREARR-----QIGVLPDERGLYDR--LTVRENIRYFAELY-GLFDEELKKRIEELIELLGLEEFLDRR---VGELST 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 160 GERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDElNMSLLFITHNLSIVRKLADSVAVMQNGRCVEQN 239
Cdd:COG4555 136 GMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQG 214
|
....*..
gi 1278835479 240 AASTLLS 246
Cdd:COG4555 215 SLDELRE 221
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
275-508 |
3.65e-30 |
|
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: 117.47 E-value: 3.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 275 LLRVEDLSVSFPIRKGILRrivdrnpVLKNIRFSLRPGESLGLVGESGSGKSTTglalLRLIA-----SQGEILFDGMPL 349
Cdd:cd03266 1 MITADALTKRFRDVKKTVQ-------AVDGVSFTVKPGEVTGLLGPNGAGKTTT----LRMLAgllepDAGFATVDGFDV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 350 HRwnrrQMLPVRPRMQVVFQdpNSSLNPRLSVLQIVEEGLRVHqpGLSAQQREQEVMRVMVEVGLDpETRHRYPAEFSGG 429
Cdd:cd03266 70 VK----EPAEARRRLGFVSD--STGLYDRLTARENLEYFAGLY--GLKGDELTARLEELADRLGME-ELLDRRVGGFSTG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1278835479 430 QRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:cd03266 141 MRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGK-CILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
299-515 |
6.40e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 118.30 E-value: 6.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 299 NPVLKNIRFSLRPGESLGLVGESGSGKSTTglalLRLI-----ASQGEILFDGMPL---HRWNRRQmlpvrpRMQVVFQD 370
Cdd:PRK13650 20 KYTLNDVSFHVKQGEWLSIIGHNGSGKSTT----VRLIdglleAESGQIIIDGDLLteeNVWDIRH------KIGMVFQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 371 PNSSLnprlsVLQIVEE----GLRvhQPGLSAQQREQEVMRVMVEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPEL 446
Cdd:PRK13650 90 PDNQF-----VGATVEDdvafGLE--NKGIPHEEMKERVNEALELVGMQ-DFKEREPARLSGGQKQRVAIAGAVAMRPKI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1278835479 447 IILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVrALCHQVIVLRQGEVVEQGECQRVFS 515
Cdd:PRK13650 162 IILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPRELFS 229
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
297-512 |
6.80e-30 |
|
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: 116.84 E-value: 6.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 297 DRNPVLKNIRFSLRPGESLGLVGESGSGKSTTgLALL--RLIASQGEILFDGMPLhrwnRRQMLPVRPRMQVVFQDpnSS 374
Cdd:cd03263 13 GTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTT-LKMLtgELRPTSGTAYINGYSI----RTDRKAARQSLGYCPQF--DA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 375 LNPRLSVLQIVEEGLRVHqpGLSAQQREQEVMRVMVEVGLDPEtRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTS 454
Cdd:cd03263 86 LFDELTVREHLRFYARLK--GLPKSEIKEEVELLLRVLGLTDK-ANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTS 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1278835479 455 SLDRTVQAQILALLKGLQEKHrlAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQR 512
Cdd:cd03263 163 GLDPASRRAIWDLILEVRKGR--SIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQE 218
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
299-508 |
7.46e-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: 116.44 E-value: 7.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 299 NPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEILFDG-----MPLHRWnrrqmlpvRPRMQVVFQDPN 372
Cdd:cd03244 17 PPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVeLSSGSILIDGvdiskIGLHDL--------RSRISIIPQDPV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 373 -------SSLNPRLS-----VLQIVEeglRVHQPGLSAQQREQEVMRVMvEVGLDpetrhrypaeFSGGQRQRIAIARAL 440
Cdd:cd03244 89 lfsgtirSNLDPFGEysdeeLWQALE---RVGLKEFVESLPGGLDTVVE-EGGEN----------LSVGQRQLLCLARAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1278835479 441 ILKPELIILDEPTSSLDRTVQAQILALLKGlQEKHRlAYIFISHDLQVVrALCHQVIVLRQGEVVEQG 508
Cdd:cd03244 155 LRKSKILVLDEATASVDPETDALIQKTIRE-AFKDC-TVLTIAHRLDTI-IDSDRILVLDKGRVVEFD 219
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
301-496 |
7.55e-30 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 116.84 E-value: 7.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 301 VLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLHRWNRRQMLPVRPRmQVVFQDPNSSL 375
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKST----LLHLLGgldtpTSGDVIFNGQPMSKLSSAAKAELRNQ-KLGFIYQFHHL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 376 NPRLSVLQIVEEGLRV-HQPGLSAQQREQEVMRVmveVGLDPETRHRyPAEFSGGQRQRIAIARALILKPELIILDEPTS 454
Cdd:PRK11629 99 LPDFTALENVAMPLLIgKKKPAEINSRALEMLAA---VGLEHRANHR-PSELSGGERQRVAIARALVNNPRLVLADEPTG 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1278835479 455 SLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQV 496
Cdd:PRK11629 175 NLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQL 216
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
297-529 |
7.88e-30 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 119.04 E-value: 7.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 297 DRNPVLKNIRFSLRPGESLGLVGESGSGKSTTglalLRLI-----ASQGEILFDGMPLhrwnrRQMLPVRPRMQV--VFQ 369
Cdd:COG1125 13 DGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTT----LRMInrliePTSGRILIDGEDI-----RDLDPVELRRRIgyVIQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 370 dpNSSLNPRLSVLQ---IVeeglrvhqPGL---SAQQREQEVMRVMVEVGLDPET-RHRYPAEFSGGQRQRIAIARALIL 442
Cdd:COG1125 84 --QIGLFPHMTVAEniaTV--------PRLlgwDKERIRARVDELLELVGLDPEEyRDRYPHELSGGQQQRVGVARALAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 443 KPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSAPTQRYT 522
Cdd:COG1125 154 DPPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFV 233
|
....*..
gi 1278835479 523 RQLLSSD 529
Cdd:COG1125 234 ADFVGAD 240
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
274-528 |
1.42e-29 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 118.75 E-value: 1.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 274 PLLRVEDLSVSFPIRKGILRrIVDRnpvlknIRFSLRPGESLGLVGESGSGKSTTGLALLRLIASQGEILFDGMplhRWN 353
Cdd:PRK15093 2 PLLDIRNLTIEFKTSDGWVK-AVDR------VSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRVTADRM---RFD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 354 RRQMLPVRPR---------MQVVFQDPNSSLNPRLSV-LQIVEEGLRVHQPGLSAQQ---REQEVMRVMVEVGLD--PET 418
Cdd:PRK15093 72 DIDLLRLSPRerrklvghnVSMIFQEPQSCLDPSERVgRQLMQNIPGWTYKGRWWQRfgwRKRRAIELLHRVGIKdhKDA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 419 RHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIV 498
Cdd:PRK15093 152 MRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINV 231
|
250 260 270
....*....|....*....|....*....|
gi 1278835479 499 LRQGEVVEQGECQRVFSAPTQRYTRQLLSS 528
Cdd:PRK15093 232 LYCGQTVETAPSKELVTTPHHPYTQALIRA 261
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
266-520 |
1.78e-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: 122.16 E-value: 1.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 266 VPLDADSTPL------LRVEDLSVSFPIRKgilrrivdrNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI--- 336
Cdd:COG4618 315 VPAEPERMPLprpkgrLSVENLTVVPPGSK---------RPILRGVSFSLEPGEVLGVIGPSGSGKST----LARLLvgv 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 337 --ASQGEILFDGMPLHRWNRRQM------LPvrprmQVV-------------FQDPNSSlnprlsvlQIVEEGLR--VHQ 393
Cdd:COG4618 382 wpPTAGSVRLDGADLSQWDREELgrhigyLP-----QDVelfdgtiaeniarFGDADPE--------KVVAAAKLagVHE 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 394 pglsaqqreqevmrvMV---------EVGldpETRHRypaeFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQI 464
Cdd:COG4618 449 ---------------MIlrlpdgydtRIG---EGGAR----LSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAAL 506
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1278835479 465 LALLKGLQEKHRLAyIFISHDLQVVRAlCHQVIVLRQGEVVEQGECQRVFSAPTQR 520
Cdd:COG4618 507 AAAIRALKARGATV-VVITHRPSLLAA-VDKLLVLRDGRVQAFGPRDEVLARLARP 560
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
276-504 |
1.81e-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: 1.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 276 LRVEDLSVSFPIRKgilrrivdrNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLH 350
Cdd:cd03246 1 LEVENVSFRYPGAE---------PPVLRNVSFSIEPGESLAIIGPSGSGKST----LARLILgllrpTSGRVRLDGADIS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 351 RWNRRQmlpvrprmqvvfqdpnsslnprlsvlqiveegLRVHqpglsaqqreqeVMRVMVEVGLDPETRhrypAE--FSG 428
Cdd:cd03246 68 QWDPNE--------------------------------LGDH------------VGYLPQDDELFSGSI----AEniLSG 99
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1278835479 429 GQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQeKHRLAYIFISHDLQVVrALCHQVIVLRQGEV 504
Cdd:cd03246 100 GQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALK-AAGATRIVIAHRPETL-ASADRILVLEDGRV 173
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
302-526 |
1.99e-29 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 119.75 E-value: 1.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 302 LKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEILFDGMPLHRWNRRQMLPVR-PRMQVVFQdpNSSLNPRL 379
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIePTRGQVLIDGVDIAKISDAELREVRrKKIAMVFQ--SFALMPHM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 380 SVLQIVEEGLRVhqPGLSAQQREQEVMRVMVEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRT 459
Cdd:PRK10070 122 TVLDNTAFGMEL--AGINAEERREKALDALRQVGLE-NYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1278835479 460 VQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSAPTQRYTRQLL 526
Cdd:PRK10070 199 IRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFF 265
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
276-491 |
2.17e-29 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 114.89 E-value: 2.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 276 LRVEDLSVsfpirkgilrrIVDRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA--------SQGEILFDGM 347
Cdd:COG4136 2 LSLENLTI-----------TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKST----LLAAIAgtlspafsASGEVLLNGR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 348 PLHRwnrrqmLPVRPR-MQVVFQDPnsSLNPRLSVLQIVEEGLRvhqPGLSAQQREQEVMRVMVEVGLDpETRHRYPAEF 426
Cdd:COG4136 67 RLTA------LPAEQRrIGILFQDD--LLFPHLSVGENLAFALP---PTIGRAQRRARVEQALEEAGLA-GFADRDPATL 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1278835479 427 SGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRA 491
Cdd:COG4136 135 SGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPA 199
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
297-527 |
2.93e-29 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 118.26 E-value: 2.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 297 DRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLHRWNRRQMlpvrpRMQVVFQdp 371
Cdd:PRK10851 13 GRTQVLNDISLDIPSGQMVALLGPSGSGKTT----LLRIIAglehqTSGHIRFHGTDVSRLHARDR-----KVGFVFQ-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 372 NSSLNPRLSVLQIVEEGLRVhqpgLSAQQR------EQEVMRVMVEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPE 445
Cdd:PRK10851 82 HYALFRHMTVFDNIAFGLTV----LPRRERpnaaaiKAKVTQLLEMVQL-AHLADRYPAQLSGGQKQRVALARALAVEPQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 446 LIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSAPTQRYTRQL 525
Cdd:PRK10851 157 ILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEF 236
|
..
gi 1278835479 526 LS 527
Cdd:PRK10851 237 MG 238
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-236 |
5.30e-29 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 114.46 E-value: 5.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 6 LRIDNLSIAFSKQdetrTVVSDLTLQIQRGETLALVGESGSGKS--VSALS-ILRllPSppvsypQGDILFHDRSLLH-- 80
Cdd:cd03219 1 LEVRGLTKRFGGL----VALDDVSFSVRPGEIHGLIGPNGAGKTtlFNLISgFLR--PT------SGSVLFDGEDITGlp 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 81 ADEQTLRGI-RGNKIAMIFQEPMVSLNPLHSLEKQLYEVLSLHRGMRKE-AARGEILDCLERTGIRNAAKRLndfPHQLS 158
Cdd:cd03219 69 PHEIARLGIgRTFQIPRLFPELTVLENVMVAAQARTGSGLLLARARREErEARERAEELLERVGLADLADRP---AGELS 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1278835479 159 GGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDElNMSLLFITHNLSIVRKLADSVAVMQNGRCV 236
Cdd:cd03219 146 YGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVI 222
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
302-515 |
5.69e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 115.62 E-value: 5.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 302 LKNIRFSLRPGESLGLVGESGSGKSTtgLALLRL---IASQGEILFDGMPLHRWNRRQmlpVRPRMQVVFQDPNSSLnpr 378
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKST--IAKLMIgieKVKSGEIFYNNQAITDDNFEK---LRKHIGIVFQNPDNQF--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 379 lsVLQIVEE----GLRVHQpgLSAQQREQEVMRVMVEVGLDPETRHRyPAEFSGGQRQRIAIARALILKPELIILDEPTS 454
Cdd:PRK13648 97 --VGSIVKYdvafGLENHA--VPYDEMHRRVSEALKQVDMLERADYE-PNALSGGQKQRVAIAGVLALNPSVIILDEATS 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1278835479 455 SLDRTVQAQILALLKGLQEKHRLAYIFISHDL-QVVRAlcHQVIVLRQGEVVEQGECQRVFS 515
Cdd:PRK13648 172 MLDPDARQNLLDLVRKVKSEHNITIISITHDLsEAMEA--DHVIVMNKGTVYKEGTPTEIFD 231
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
297-508 |
6.76e-29 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 114.25 E-value: 6.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 297 DRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEILFDGMPLHRWNR---RQMLPVRPRMQVVF 368
Cdd:cd03253 12 PGRPVLKDVSFTIPAGKKVAIVGPSGSGKST----ILRLLfrfydVSSGSILIDGQDIREVTLdslRRAIGVVPQDTVLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 369 QDpnsslnprlsvlqIVEEGLRVHQPGLSaqqrEQEVMRVMVEVGLDPETRhRYPAEF-----------SGGQRQRIAIA 437
Cdd:cd03253 88 ND-------------TIGYNIRYGRPDAT----DEEVIEAAKAAQIHDKIM-RFPDGYdtivgerglklSGGEKQRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1278835479 438 RALILKPELIILDEPTSSLD----RTVQAQILALLKGlqekhRLAyIFISHDLQVVrALCHQVIVLRQGEVVEQG 508
Cdd:cd03253 150 RAILKNPPILLLDEATSALDthteREIQAALRDVSKG-----RTT-IVIAHRLSTI-VNADKIIVLKDGRIVERG 217
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
299-508 |
1.13e-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: 1.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 299 NPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEILFDGMplhrwNRRQMLPVRPRMQVVFQDPnsSLNP 377
Cdd:cd03268 13 KRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIkPDSGEITFDGK-----SYQKNIEALRRIGALIEAP--GFYP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 378 RLSVlqivEEGLRVHQPGLsaQQREQEVMRVMVEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLD 457
Cdd:cd03268 86 NLTA----RENLRLLARLL--GIRKKRIDEVLDVVGLK-DSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1278835479 458 RTVQAQILALLKGLQEKHRLayIFI-SHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:cd03268 159 PDGIKELRELILSLRDQGIT--VLIsSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
275-497 |
1.23e-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: 113.25 E-value: 1.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 275 LLRVEDLSVSFPI-RKGILRRivdrnPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEILF---- 344
Cdd:TIGR02324 1 LLEVEDLSKTFTLhQQGGVRL-----PVLKNVSLTVNAGECVALSGPSGAGKST----LLKSLyanylPDSGRILVrheg 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 345 DGMPLHRWNRRQMLPVRpRMQVVFQDPNSSLNPRLSVLQIVEEGLRVHqpGLSAQQREQEVMRVMVEVGLDPETRHRYPA 424
Cdd:TIGR02324 72 AWVDLAQASPREVLEVR-RKTIGYVSQFLRVIPRVSALEVVAEPLLER--GVPREAARARARELLARLNIPERLWHLPPA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1278835479 425 EFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKglQEKHR-LAYIFISHDLQVVRALCHQVI 497
Cdd:TIGR02324 149 TFSGGEQQRVNIARGFIADYPILLLDEPTASLDAANRQVVVELIA--EAKARgAALIGIFHDEEVRELVADRVM 220
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
269-514 |
1.55e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 114.32 E-value: 1.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 269 DADSTPLLRVEDLSVSFPirkgilrriVDRNPVLKNIRFSLRPGESLGLVGESGSGKST-----TGLallrLIASQGEIL 343
Cdd:PRK13632 1 IKNKSVMIKVENVSFSYP---------NSENNALKNVSFEINEGEYVAILGHNGSGKSTiskilTGL----LKPQSGEIK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 344 FDGMPLHRWNRRQmlpVRPRMQVVFQDPNSslnprlsvlQIVeeGLRVHQP---GLSAQQREQEVMRVMVE-----VGLD 415
Cdd:PRK13632 68 IDGITISKENLKE---IRKKIGIIFQNPDN---------QFI--GATVEDDiafGLENKKVPPKKMKDIIDdlakkVGME 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 416 pETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVrALCHQ 495
Cdd:PRK13632 134 -DYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADK 211
|
250
....*....|....*....
gi 1278835479 496 VIVLRQGEVVEQGECQRVF 514
Cdd:PRK13632 212 VIVFSEGKLIAQGKPKEIL 230
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
277-508 |
1.60e-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: 113.40 E-value: 1.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 277 RVEDLSVSFPIRKGIlrrivdrnPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEILFDGMPLHRWNRR 355
Cdd:cd03249 2 EFKNVSFRYPSRPDV--------PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYdPTSGEILLDGVDIRDLNLR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 356 QmlpVRPRMQVVFQDP---NSSlnprlsvlqiVEEGLRVHQPGLSaqqrEQEVMRVMVEVGLD------PETRH----RY 422
Cdd:cd03249 74 W---LRSQIGLVSQEPvlfDGT----------IAENIRYGKPDAT----DEEVEEAAKKANIHdfimslPDGYDtlvgER 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 423 PAEFSGGQRQRIAIARALILKPELIILDEPTSSLD----RTVQAQILALLKGlqekhRLAyIFISHDLQVVRAlCHQVIV 498
Cdd:cd03249 137 GSQLSGGQKQRIAIARALLRNPKILLLDEATSALDaeseKLVQEALDRAMKG-----RTT-IVIAHRLSTIRN-ADLIAV 209
|
250
....*....|
gi 1278835479 499 LRQGEVVEQG 508
Cdd:cd03249 210 LQNGQVVEQG 219
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
11-255 |
1.75e-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: 116.36 E-value: 1.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 11 LSIAFSKQDETRTVVSDLTLQIQrgETLALVGESGSGKSvSALSILRLLPSPPVsypqGDILFHDRSLLHADEQTLRGIR 90
Cdd:TIGR02142 1 LSARFSKRLGDFSLDADFTLPGQ--GVTAIFGRSGSGKT-TLIRLIAGLTRPDE----GEIVLNGRTLFDSRKGIFLPPE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 91 GNKIAMIFQEpmVSLNPLHSLEKQLYEVLSLHRGMRKEAARGEILDCLertGIRNAAKRLndfPHQLSGGERQRVMIAMA 170
Cdd:TIGR02142 74 KRRIGYVFQE--ARLFPHLSVRGNLRYGMKRARPSERRISFERVIELL---GIGHLLGRL---PGRLSGGEKQRVAIGRA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 171 LLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGRCVEQNAASTLLSAPQH 250
Cdd:TIGR02142 146 LLSSPRLLLMDEPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDL 225
|
....*
gi 1278835479 251 PYTQR 255
Cdd:TIGR02142 226 PWLAR 230
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
302-520 |
1.95e-28 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 112.94 E-value: 1.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 302 LKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLHRwnrrqmlPVRPRMqVVFQdpNSSLN 376
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKST----LLNLISglaqpTSGGVILEGKQITE-------PGPDRM-VVFQ--NYSLL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 377 PRLSVLQIVEEGLRVHQPGLSAQQREQEVMRVMVEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSL 456
Cdd:TIGR01184 67 PWLTVRENIALAVDRVLPDLSKSERRAIVEEHIALVGLT-EAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1278835479 457 DRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRV-FSAPTQR 520
Cdd:TIGR01184 146 DALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRPRDR 210
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
16-238 |
1.98e-28 |
|
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: 113.20 E-value: 1.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 16 SKQDETRTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRL---LPSPPvsypQGDILFHDRsllhadEQTLRGIRGN 92
Cdd:cd03296 9 SKRFGDFVALDDVSLDIPSGELVALLGPSGSGKT----TLLRLiagLERPD----SGTILFGGE------DATDVPVQER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 93 KIAMIFQ------EPMVSLNPLHSLEKQlyevlslHRGMRKEAA--RGEILDCLERTGIRNAAKRlndFPHQLSGGERQR 164
Cdd:cd03296 75 NVGFVFQhyalfrHMTVFDNVAFGLRVK-------PRSERPPEAeiRAKVHELLKLVQLDWLADR---YPAQLSGGQRQR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1278835479 165 VMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGRcVEQ 238
Cdd:cd03296 145 VALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGR-IEQ 217
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
6-276 |
3.93e-28 |
|
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: 115.48 E-value: 3.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 6 LRIDNLSIAFSkqdeTRTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLLPS-PPVSYPQGDILFHDRSLLHADEQ 84
Cdd:TIGR03258 6 IRIDHLRVAYG----ANTVLDDLSLEIEAGELLALIGKSGCGKT----TLLRAIAGfVKAAGLTGRIAIADRDLTHAPPH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 85 TlrgiRGnkIAMIFQEpmVSLNPLHSLEKQLYEVLSLHRGMRKEAARgEILDCLERTGIRNAAKRLndfPHQLSGGERQR 164
Cdd:TIGR03258 78 K----RG--LALLFQN--YALFPHLKVEDNVAFGLRAQKMPKADIAE-RVADALKLVGLGDAAAHL---PAQLSGGMQQR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 165 VMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDEL-NMSLLFITHNLSIVRKLADSVAVMQNGRCVEQNAAST 243
Cdd:TIGR03258 146 IAIARAIAIEPDVLLLDEPLSALDANIRANMREEIAALHEELpELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQA 225
|
250 260 270
....*....|....*....|....*....|...
gi 1278835479 244 LLSAPQHPYTQRLLNSEPSGDPVPLDADSTPLL 276
Cdd:TIGR03258 226 LYDAPADGFAAEFLGAANILPAIALGITEAPGL 258
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
301-521 |
5.34e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 112.31 E-value: 5.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 301 VLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIA------SQGEILFDGMPLHRWNrrqMLPVRPRMQVVFQDPNSS 374
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypearVSGEVYLDGQDIFKMD---VIELRRRVQMVFQIPNPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 375 lnPRLSVLQIVEEGLRVHQPGLSAQQREQEVMRVMVEVGLDPETRHRYPA---EFSGGQRQRIAIARALILKPELIILDE 451
Cdd:PRK14247 95 --PNLSIFENVALGLKLNRLVKSKKELQERVRWALEKAQLWDEVKDRLDApagKLSGGQQQRLCIARALAFQPEVLLADE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1278835479 452 PTSSLDRTVQAQILALLkgLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSAP----TQRY 521
Cdd:PRK14247 173 PTANLDPENTAKIESLF--LELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPrhelTEKY 244
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
275-504 |
5.60e-28 |
|
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: 111.41 E-value: 5.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 275 LLRVEDLSVSFPIRKGilrrivdrNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIASQ-GEILFDGMPL---- 349
Cdd:cd03248 11 IVKFQNVTFAYPTRPD--------TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQgGQVLLDGKPIsqye 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 350 HRWNRRQMLPVrPRMQVVF----QDPNSSLNPRLSVLQIVEEGLRVHQPGLSAQqreqevmrvmVEVGLDPETRHRyPAE 425
Cdd:cd03248 83 HKYLHSKVSLV-GQEPVLFarslQDNIAYGLQSCSFECVKEAAQKAHAHSFISE----------LASGYDTEVGEK-GSQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 426 FSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRlaYIFISHDLQVV-RAlcHQVIVLRQGEV 504
Cdd:cd03248 151 LSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRT--VLVIAHRLSTVeRA--DQILVLDGGRI 226
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-264 |
7.07e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 112.88 E-value: 7.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 4 PLLRIDNLSIAFSKqdetRTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLLPSPPVSYPQGDILFHDRSLL-HAD 82
Cdd:PRK14271 20 PAMAAVNLTLGFAG----KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFnYRD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 83 EQTLRgirgNKIAMIFQEPmvslNPL-HSLEKQLYEVLSLHRGMRKEAARGEILDCLERTGIRNAAK-RLNDFPHQLSGG 160
Cdd:PRK14271 96 VLEFR----RRVGMLFQRP----NPFpMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKdRLSDSPFRLSGG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 161 ERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELnmSLLFITHNLSIVRKLADSVAVMQNGRCVEQNA 240
Cdd:PRK14271 168 QQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGP 245
|
250 260
....*....|....*....|....
gi 1278835479 241 ASTLLSAPQHPYTQRLLnSEPSGD 264
Cdd:PRK14271 246 TEQLFSSPKHAETARYV-AGLSGD 268
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-238 |
7.63e-28 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 110.83 E-value: 7.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 6 LRIDNLSIAFSkqdeTRTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLLPspPVSypqGDILFHDRSLLHADeqt 85
Cdd:cd03269 1 LEVENVTKRFG----RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIIL--PDS---GEVLFDGKPLDIAA--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 86 lrgirGNKIAMIFQEPmvSLNPLHSLEKQLYEVLSLhRGMRKEAARGEILDCLERTGIRN-AAKRLNdfphQLSGGERQR 164
Cdd:cd03269 69 -----RNRIGYLPEER--GLYPKMKVIDQLVYLAQL-KGLKKEEARRRIDEWLERLELSEyANKRVE----ELSKGNQQK 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1278835479 165 VMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDElNMSLLFITHNLSIVRKLADSVAVMQNGRCVEQ 238
Cdd:cd03269 137 VQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLY 209
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
298-515 |
7.83e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 112.49 E-value: 7.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 298 RNPVLKNIRFSLRPGESLGLVGESGSGKSTTGL---ALLrlIASQGEILFDGMPL----HRWNrrqmlpVRPRMQVVFQD 370
Cdd:PRK13633 22 EKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKhmnALL--IPSEGKVYVDGLDTsdeeNLWD------IRNKAGMVFQN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 371 PNSSLnprlsVLQIVEEGLRVHQPGLSAQQREqevMRVMVEVGLDP----ETRHRYPAEFSGGQRQRIAIARALILKPEL 446
Cdd:PRK13633 94 PDNQI-----VATIVEEDVAFGPENLGIPPEE---IRERVDESLKKvgmyEYRRHAPHLLSGGQKQRVAIAGILAMRPEC 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 447 IILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDL-QVVRAlcHQVIVLRQGEVVEQGECQRVFS 515
Cdd:PRK13633 166 IIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMeEAVEA--DRIIVMDSGKVVMEGTPKEIFK 233
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
273-516 |
8.20e-28 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 111.71 E-value: 8.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 273 TPLLRVEDLSVSFPIRKGILRRI-----------VDRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA---- 337
Cdd:COG1134 2 SSMIEVENVSKSYRLYHEPSRSLkelllrrrrtrREEFWALKDVSFEVERGESVGIIGRNGAGKST----LLKLIAgile 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 338 -SQGEILFDGmplhrwnrrqmlpvrpRMQVVFqDPNSSLNPRLSVLQIVEEGLRVHqpGLSaqqrEQEVMRVMVEVgldp 416
Cdd:COG1134 78 pTSGRVEVNG----------------RVSALL-ELGAGFHPELTGRENIYLNGRLL--GLS----RKEIDEKFDEI---- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 417 etrhrypAEFSG--------------GQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRlAYIFI 482
Cdd:COG1134 131 -------VEFAElgdfidqpvktyssGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGR-TVIFV 202
|
250 260 270
....*....|....*....|....*....|....
gi 1278835479 483 SHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSA 516
Cdd:COG1134 203 SHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
297-508 |
9.16e-28 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 117.75 E-value: 9.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 297 DRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIAS-----QGEILFDGMPLHRWNRRQmlpVRPRMQVVFQdp 371
Cdd:TIGR03797 464 DGPLILDDVSLQIEPGEFVAIVGPSGSGKST----LLRLLLGfetpeSGSVFYDGQDLAGLDVQA---VRRQLGVVLQ-- 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 372 NSSLNPRlSVLQIVEEGLRVHQpglsaqqreQEVMRVMVEVGLDPETR------HRYPAE----FSGGQRQRIAIARALI 441
Cdd:TIGR03797 535 NGRLMSG-SIFENIAGGAPLTL---------DEAWEAARMAGLAEDIRampmgmHTVISEgggtLSGGQRQRLLIARALV 604
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1278835479 442 LKPELIILDEPTSSLDRTVQAQILALLKGLQekhrLAYIFISHDLQVVRAlCHQVIVLRQGEVVEQG 508
Cdd:TIGR03797 605 RKPRILLFDEATSALDNRTQAIVSESLERLK----VTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQG 666
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
6-238 |
9.94e-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: 111.17 E-value: 9.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 6 LRIDNLSIAFSKQdetrTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLL-----PSppvsypQGDILFHDRSLLH 80
Cdd:cd03300 1 IELENVSKFYGGF----VALDGVSLDIKEGEFFTLLGPSGCGKT----TLLRLIagfetPT------SGEILLDGKDITN 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 81 adeqtlrgIRGNK--IAMIFQEpmVSLNPLHSLEKQLYEVLSLhRGMRKEAARGEILDCLERTGIRNAAKRlndFPHQLS 158
Cdd:cd03300 67 --------LPPHKrpVNTVFQN--YALFPHLTVFENIAFGLRL-KKLPKAEIKERVAEALDLVQLEGYANR---KPSQLS 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 159 GGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGRcVEQ 238
Cdd:cd03300 133 GGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGK-IQQ 211
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-254 |
1.52e-27 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 111.02 E-value: 1.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 1 MTQPLLRIDNLSIAFSKQDETRTVvsdlTLQIQRGETLALVGESGSGKSVSALSILRLLPSPPVSYPQGDILF--HDRSL 78
Cdd:PRK14239 1 MTEPILQVSDLSVYYNKKKALNSV----SLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYngHNIYS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 79 LHADEQTLRgirgNKIAMIFQEPmvslNPLhslEKQLYEvlSLHRGMRKEAARG-EILDCLERTGIRNAA------KRLN 151
Cdd:PRK14239 77 PRTDTVDLR----KEIGMVFQQP----NPF---PMSIYE--NVVYGLRLKGIKDkQVLDEAVEKSLKGASiwdevkDRLH 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 152 DFPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMslLFITHNLSIVRKLADSVAVMQ 231
Cdd:PRK14239 144 DSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTM--LLVTRSMQQASRISDRTGFFL 221
|
250 260
....*....|....*....|...
gi 1278835479 232 NGRCVEQNAASTLLSAPQHPYTQ 254
Cdd:PRK14239 222 DGDLIEYNDTKQMFMNPKHKETE 244
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
301-516 |
2.29e-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: 110.27 E-value: 2.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 301 VLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRL-IASQGEILFDGMPL----HRWNRRQMlpvrprmQVVFQDpNSSL 375
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFyVPENGRVLVDGHDLaladPAWLRRQV-------GVVLQE-NVLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 376 NprlsvlQIVEEGLRVHQPGLSaQQREQEVMRVMVEVGLDPETRHRYP-------AEFSGGQRQRIAIARALILKPELII 448
Cdd:cd03252 89 N------RSIRDNIALADPGMS-MERVIEAAKLAGAHDFISELPEGYDtivgeqgAGLSGGQRQRIAIARALIHNPRILI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1278835479 449 LDEPTSSLD----RTVQAQILALLKGlqekhRLAyIFISHDLQVVRAlCHQVIVLRQGEVVEQGECQRVFSA 516
Cdd:cd03252 162 FDEATSALDyeseHAIMRNMHDICAG-----RTV-IIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-256 |
2.52e-27 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 115.69 E-value: 2.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 2 TQPLLRIDNLSiaFSKQDETRTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLL-----PSppvsypQGDILFHDR 76
Cdd:PRK11160 335 DQVSLTLNNVS--FTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKS----TLLQLLtrawdPQ------QGEILLNGQ 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 77 SLLHADEQTLRgirgNKIAMIFQEPmvslnplHSLEKQLYEVLSLhrgmRKEAARGEIL-DCLERTGIRN---AAKRLN- 151
Cdd:PRK11160 403 PIADYSEAALR----QAISVVSQRV-------HLFSATLRDNLLL----AAPNASDEALiEVLQQVGLEKlleDDKGLNa 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 152 ---DFPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDelNMSLLFITHNLSIVRKLaDSVA 228
Cdd:PRK11160 468 wlgEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQF-DRIC 544
|
250 260
....*....|....*....|....*...
gi 1278835479 229 VMQNGRCVEQNAASTLLSapQHPYTQRL 256
Cdd:PRK11160 545 VMDNGQIIEQGTHQELLA--QQGRYYQL 570
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
261-499 |
2.62e-27 |
|
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: 115.46 E-value: 2.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 261 PSGDPVPLDADSTPLLRVEDLSVSFPirkgilrrivDRNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQ 339
Cdd:TIGR02857 307 PLAGKAPVTAAPASSLEFSGVSVAYP----------GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVdPTE 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 340 GEILFDGMPLHRWN----RRQM--LPVRPRMqvvfqdpnsslnprlsVLQIVEEGLRVHQPGLSAQQREQEVMRVmvevG 413
Cdd:TIGR02857 377 GSIAVNGVPLADADadswRDQIawVPQHPFL----------------FAGTIAENIRLARPDASDAEIREALERA----G 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 414 LD------PETRH----RYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLayIFIS 483
Cdd:TIGR02857 437 LDefvaalPQGLDtpigEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTV--LLVT 514
|
250
....*....|....*.
gi 1278835479 484 HDLqVVRALCHQVIVL 499
Cdd:TIGR02857 515 HRL-ALAALADRIVVL 529
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-234 |
6.28e-27 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 108.68 E-value: 6.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 1 MTqPLLRIDNLSIAFS--KQDETR-TVVSDLTLQIQRGETLALVGESGSGKSvsalSILRL-----LPSppvsypQGDIL 72
Cdd:COG4778 1 MT-TLLEVENLSKTFTlhLQGGKRlPVLDGVSFSVAAGECVALTGPSGAGKS----TLLKCiygnyLPD------SGSIL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 73 FHDRS----LLHADEQTLRGIRGNKIAMIFQ----EPMVS-----LNPLhslekqlyevlsLHRGMRKEAARGEILDCLE 139
Cdd:COG4778 70 VRHDGgwvdLAQASPREILALRRRTIGYVSQflrvIPRVSaldvvAEPL------------LERGVDREEARARARELLA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 140 RTGIRnaaKRLND-FPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDElNMSLLFITHNLS 218
Cdd:COG4778 138 RLNLP---ERLWDlPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEE 213
|
250
....*....|....*.
gi 1278835479 219 IVRKLADSVAVMQNGR 234
Cdd:COG4778 214 VREAVADRVVDVTPFS 229
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
272-510 |
6.89e-27 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 113.97 E-value: 6.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 272 STPLLRVEDLSVSFPirkGILrrivdrnpVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEILFDG 346
Cdd:COG3845 2 MPPALELRGITKRFG---GVV--------ANDDVSLTVRPGEIHALLGENGAGKST----LMKILyglyqPDSGEILIDG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 347 MPLHRWNrrqmlpvrPR--------MqvVFQDPnsSLNPRLSVLQIVEEGL-RVHQPGLSAQQREQEVMRVMVEVGL--D 415
Cdd:COG3845 67 KPVRIRS--------PRdaialgigM--VHQHF--MLVPNLTVAENIVLGLePTKGGRLDRKAARARIRELSERYGLdvD 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 416 PetrHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLdrTVQ--AQILALLKGLQEKHRlAYIFISHDLQVVRALC 493
Cdd:COG3845 135 P---DAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVL--TPQeaDELFEILRRLAAEGK-SIIFITHKLREVMAIA 208
|
250
....*....|....*..
gi 1278835479 494 HQVIVLRQGEVVeqGEC 510
Cdd:COG3845 209 DRVTVLRRGKVV--GTV 223
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
302-519 |
7.44e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 109.87 E-value: 7.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 302 LKNIRFSLRPGESLGLVGESGSGKST-----TGLallrLIASQGEILFDGMPLHRWNRRQML-PVRPRMQVVFQDPNSSL 375
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTliqniNAL----LKPTTGTVTVDDITITHKTKDKYIrPVRKRIGMVFQFPESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 376 NPRlSVLQIVEEGLRvhQPGLSAQQREQEVMRVMVEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSS 455
Cdd:PRK13646 99 FED-TVEREIIFGPK--NFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAG 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1278835479 456 LDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSAPTQ 519
Cdd:PRK13646 176 LDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKKK 239
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
24-246 |
8.87e-27 |
|
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: 108.40 E-value: 8.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 24 VVSDLTLQIQRGETLALVGESGSGKSVSALSILRL-LPSppvsypQGDILFHDrslLHADEQTLRGIRgNKIAMIFQEPM 102
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFyDPT------SGEILLDG---VDIRDLNLRWLR-SQIGLVSQEPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 103 VSLNPLhsLEKQLYEVLSLHRGMRKEAARgeildclertgIRNAAKRLNDFPH-----------QLSGGERQRVMIAMAL 171
Cdd:cd03249 88 LFDGTI--AENIRYGKPDATDEEVEEAAK-----------KANIHDFIMSLPDgydtlvgergsQLSGGQKQRIAIARAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1278835479 172 LTRPELLIADEPTTALDVTVQAQILTLLRDLRdeLNMSLLFITHNLSIVRKlADSVAVMQNGRCVEQNAASTLLS 246
Cdd:cd03249 155 LRNPKILLLDEATSALDAESEKLVQEALDRAM--KGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDELMA 226
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
5-260 |
9.18e-27 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 111.32 E-value: 9.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 5 LLRIDNLSiafskQDETRTVVSDLTLQIQRGETLALVGESGSGKSVsalsILRLLPS--PPVSypqGDILFHDRSL-LHA 81
Cdd:NF040840 1 MIRIENLS-----KDWKEFKLRDISLEVKEGEYFIILGPSGAGKTV----LLELIAGiwPPDS---GKIYLDGKDItNLP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 82 DEQtlrgiRGnkIAMIFQEPMvsLNPLHSLEKQLYEVLSLHRGMRKEAAR--GEILDCLertGIRNAAKRLndfPHQLSG 159
Cdd:NF040840 69 PEK-----RG--IAYVYQNYM--LFPHKTVFENIAFGLKLRKVPKEEIERkvKEIMELL---GISHLLHRK---PRTLSG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 160 GERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGRCVEQN 239
Cdd:NF040840 134 GEQQRVALARALIIEPKLLLLDEPLSALDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVG 213
|
250 260
....*....|....*....|.
gi 1278835479 240 AASTLLSAPQHPYTQRLLNSE 260
Cdd:NF040840 214 DVREVFRRPKNEFVARFVGFE 234
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
292-508 |
9.35e-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: 9.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 292 LRRIVDRNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEILFDGMPLhrwnRRQMLPVRPRMQVVFQD 370
Cdd:cd03265 6 LVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLkPTSGRATVAGHDV----VREPREVRRRIGIVFQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 371 PnsSLNPRLSVLQIVEEGLRVHqpGLSAQQREQEVMRVMVEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPELIILD 450
Cdd:cd03265 82 L--SVDDELTGWENLYIHARLY--GVPGAERRERIDELLDFVGL-LEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1278835479 451 EPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:cd03265 157 EPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEG 214
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
304-508 |
9.72e-27 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 107.58 E-value: 9.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 304 NIRFSLR--PGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMplhrwNRRQMLPVRPRMQVVFQDPNssLN 376
Cdd:cd03298 14 PMHFDLTfaQGEITAIVGPSGSGKST----LLNLIAgfetpQSGRVLINGV-----DVTAAPPADRPVSMLFQENN--LF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 377 PRLSVLQIVEEGLrvhQPGL--SAQQReQEVMRVMVEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTS 454
Cdd:cd03298 83 AHLTVEQNVGLGL---SPGLklTAEDR-QAIEVALARVGLA-GLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1278835479 455 SLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:cd03298 158 ALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
297-508 |
1.23e-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: 114.07 E-value: 1.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 297 DRNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIASQ-GEILFDGMPLHR----WNRRQMlpvrprmQVVFQDp 371
Cdd:TIGR01846 468 DSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQhGQVLVDGVDLAIadpaWLRRQM-------GVVLQE- 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 372 nsslnprlSVL--QIVEEGLRVHQPGLSaqqrEQEVMRVMVEVGLDP---ETRHRYPAE-------FSGGQRQRIAIARA 439
Cdd:TIGR01846 540 --------NVLfsRSIRDNIALCNPGAP----FEHVIHAAKLAGAHDfisELPQGYNTEvgekganLSGGQRQRIAIARA 607
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1278835479 440 LILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLayIFISHDLQVVRAlCHQVIVLRQGEVVEQG 508
Cdd:TIGR01846 608 LVGNPRILIFDEATSALDYESEALIMRNMREICRGRTV--IIIAHRLSTVRA-CDRIIVLEKGQIAESG 673
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
276-508 |
1.27e-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: 107.28 E-value: 1.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 276 LRVEDLSVSFPIRKgilrrivdrnpVLKNIRFSLRPGeSLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLh 350
Cdd:cd03264 1 LQLENLTKRYGKKR-----------ALDGVSLTLGPG-MYGLLGPNGAGKTT----LMRILAtltppSSGTIRIDGQDV- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 351 rwnRRQMLPVRPRMQVVFQDPNSSlnPRLSVLQIVEEGLRVHqpGLSAQQREQEVMRVMVEVGLDpETRHRYPAEFSGGQ 430
Cdd:cd03264 64 ---LKQPQKLRRRIGYLPQEFGVY--PNFTVREFLDYIAWLK--GIPSKEVKARVDEVLELVNLG-DRAKKKIGSLSGGM 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1278835479 431 RQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHrlAYIFISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:cd03264 136 RRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDR--IVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
273-528 |
1.81e-26 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 110.70 E-value: 1.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 273 TPLLRVEDLSVSFpirkgilrrivDRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGM 347
Cdd:PRK11607 17 TPLLEIRNLTKSF-----------DGQHAVDDVSLTIYKGEIFALLGASGCGKST----LLRMLAgfeqpTAGQIMLDGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 348 PLhrwnrRQMLPVRPRMQVVFQdpNSSLNPRLSVLQIVEEGLRvhQPGLSAQQREQEVMRVMVEVGLDpETRHRYPAEFS 427
Cdd:PRK11607 82 DL-----SHVPPYQRPINMMFQ--SYALFPHMTVEQNIAFGLK--QDKLPKAEIASRVNEMLGLVHMQ-EFAKRKPHQLS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 428 GGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQ 507
Cdd:PRK11607 152 GGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQI 231
|
250 260
....*....|....*....|.
gi 1278835479 508 GECQRVFSAPTQRYTRQLLSS 528
Cdd:PRK11607 232 GEPEEIYEHPTTRYSAEFIGS 252
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
258-486 |
2.51e-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: 2.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 258 NSEPSGDPV-PLDADST---PLLRVEDLSVSFPirkgilrrivDRNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALL 333
Cdd:TIGR02868 313 AAGPVAEGSaPAAGAVGlgkPTLELRDLSAGYP----------GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLA 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 334 RLIA-SQGEILFDGMPLHRWNRRQmlpVRPRMQVVFQDPN---SSlnprlsvlqiVEEGLRVHQPGLSaqqrEQEVMRVM 409
Cdd:TIGR02868 383 GLLDpLQGEVTLDGVPVSSLDQDE---VRRRVSVCAQDAHlfdTT----------VRENLRLARPDAT----DEELWAAL 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 410 VEVGLDPETR----------HRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILA-LLKGLQEKhrlA 478
Cdd:TIGR02868 446 ERVGLADWLRalpdgldtvlGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEdLLAALSGR---T 522
|
....*...
gi 1278835479 479 YIFISHDL 486
Cdd:TIGR02868 523 VVLITHHL 530
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
300-515 |
3.22e-26 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 107.79 E-value: 3.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 300 PVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIASQ-GEILFDGMPLHrWNRRQMLPVRPRMQVVFQDP------- 371
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQkGAVLWQGKPLD-YSKRGLLALRQQVATVFQDPeqqifyt 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 372 --NSSLNPRLSVLQIVEEGLrvhqpglsaQQREQEVMRVMVEVGLdpetRHRYPAEFSGGQRQRIAIARALILKPELIIL 449
Cdd:PRK13638 94 diDSDIAFSLRNLGVPEAEI---------TRRVDEALTLVDAQHF----RHQPIQCLSHGQKKRVAIAGALVLQARYLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1278835479 450 DEPTSSLDRTVQAQILALLKGLQEKHRLAYIfISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFS 515
Cdd:PRK13638 161 DEPTAGLDPAGRTQMIAIIRRIVAQGNHVII-SSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFA 225
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
291-521 |
3.26e-26 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 109.81 E-value: 3.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 291 ILRRIVDR---NPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPL-HRwnrrqmlPVR 361
Cdd:PRK11432 8 VLKNITKRfgsNTVIDNLNLTIKQGTMVTLLGPSGCGKTT----VLRLVAglekpTEGQIFIDGEDVtHR-------SIQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 362 PR-MQVVFQdpNSSLNPRLSVLQIVEEGLRVHqpGLSAQQREQEVMRVMVEVGLDPeTRHRYPAEFSGGQRQRIAIARAL 440
Cdd:PRK11432 77 QRdICMVFQ--SYALFPHMSLGENVGYGLKML--GVPKEERKQRVKEALELVDLAG-FEDRYVDQISGGQQQRVALARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 441 ILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSAPTQR 520
Cdd:PRK11432 152 ILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASR 231
|
.
gi 1278835479 521 Y 521
Cdd:PRK11432 232 F 232
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
297-508 |
4.62e-26 |
|
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: 106.16 E-value: 4.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 297 DRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLHRWNRRQMlpvRPRMQVVFQDP 371
Cdd:cd03251 13 DGPPVLRDISLDIPAGETVALVGPSGSGKST----LVNLIPrfydvDSGRILIDGHDVRDYTLASL---RRQIGLVSQDV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 372 ---NSSlnprlsvlqiVEEGLRVHQPGLSAQQRE--------QEVMRVMVEvGLDPETRHRyPAEFSGGQRQRIAIARAL 440
Cdd:cd03251 86 flfNDT----------VAENIAYGRPGATREEVEeaaraanaHEFIMELPE-GYDTVIGER-GVKLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1278835479 441 ILKPELIILDEPTSSLD----RTVQAQILALLKGlqekhRLAYIfISHDLQVVRAlCHQVIVLRQGEVVEQG 508
Cdd:cd03251 154 LKDPPILILDEATSALDteseRLVQAALERLMKN-----RTTFV-IAHRLSTIEN-ADRIVVLEDGKIVERG 218
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
276-508 |
4.76e-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: 105.98 E-value: 4.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 276 LRVEDLSVSFpirkgilrrivDRNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEILFDGMPLHRWNR 354
Cdd:cd03224 1 LEVENLNAGY-----------GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLpPRSGSIRFDGRDITGLPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 355 RQmlpvRPRMQVVFQDPNSSLNPRLSVlqivEEGLRVhqpGLSAQQREqEVMRVMVEV-GLDP---ETRHRYPAEFSGGQ 430
Cdd:cd03224 70 HE----RARAGIGYVPEGRRIFPELTV----EENLLL---GAYARRRA-KRKARLERVyELFPrlkERRKQLAGTLSGGE 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1278835479 431 RQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKhRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:cd03224 138 QQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEG 214
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
301-507 |
5.18e-26 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 106.02 E-value: 5.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 301 VLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLHRWNRRQMLPVRPR-MQVVFQdpNSS 374
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKST----LLAILAglddgSSGEVSLVGQPLHQMDEEARAKLRAKhVGFVFQ--SFM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 375 LNPRLSVLQIVEegLRVHQPGLSAQQREQEVMRVMVEVGLDPETRHrYPAEFSGGQRQRIAIARALILKPELIILDEPTS 454
Cdd:PRK10584 99 LIPTLNALENVE--LPALLRGESSRQSRNGAKALLEQLGLGKRLDH-LPAQLSGGEQQRVALARAFNGRPDVLFADEPTG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1278835479 455 SLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVrALCHQVIVLRQGEVVEQ 507
Cdd:PRK10584 176 NLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLA-ARCDRRLRLVNGQLQEE 227
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-257 |
5.36e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 106.85 E-value: 5.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 24 VVSDLTLQIQRGETLALVGESGSGKSVSALSILRLLPSPPVSYPQGDILFHDRSLLHADEQTLRGIRgnKIAMIFQEPmv 103
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRLFGRNIYSPDVDPIEVRR--EVGMVFQYP-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 104 slNPLHSLekQLYEVLSLHRGMRKEAARGEILDCLERTGIRNAA------KRLNDFPHQLSGGERQRVMIAMALLTRPEL 177
Cdd:PRK14267 95 --NPFPHL--TIYDNVAIGVKLNGLVKSKKELDERVEWALKKAAlwdevkDRLNDYPSNLSGGQRQRLVIARALAMKPKI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 178 LIADEPTTALDVTVQAQILTLLRDLRDELnmSLLFITHNLSIVRKLADSVAVMQNGRCVEQNAASTLLSAPQHPYTQRLL 257
Cdd:PRK14267 171 LLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEKYV 248
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
27-257 |
5.94e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 107.44 E-value: 5.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 27 DLTLQIQRGETLALVGESGSGKSVSALSILRLLPspPVSypqGDILFHDRSLlhADEQT-LRGIRgNKIAMIFQEPmvsl 105
Cdd:PRK13637 25 NVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLK--PTS---GKIIIDGVDI--TDKKVkLSDIR-KKVGLVFQYP---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 106 nplhslEKQLYEvlslhRGMRKEAARGEILDCLERTGIRNAAKR--------LNDF----PHQLSGGERQRVMIAMALLT 173
Cdd:PRK13637 93 ------EYQLFE-----ETIEKDIAFGPINLGLSEEEIENRVKRamnivgldYEDYkdksPFELSGGQKRRVAIAGVVAM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 174 RPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGRCVEQ-------NAASTL-- 244
Cdd:PRK13637 162 EPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQgtprevfKEVETLes 241
|
250
....*....|....*
gi 1278835479 245 --LSAPQHPYTQRLL 257
Cdd:PRK13637 242 igLAVPQVTYLVRKL 256
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
297-508 |
6.04e-26 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 105.75 E-value: 6.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 297 DRNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRL-IASQGEILFDGMPLhrwnrRQMLPV--RPRMQVVFQDP-- 371
Cdd:cd03245 15 QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLyKPTSGSVLLDGTDI-----RQLDPAdlRRNIGYVPQDVtl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 372 -NSSLNPRLSVlqiveeGLRVHQpglsaqqrEQEVMRVMVEVGLDPETRhRYPAEF-----------SGGQRQRIAIARA 439
Cdd:cd03245 90 fYGTLRDNITL------GAPLAD--------DERILRAAELAGVTDFVN-KHPNGLdlqigergrglSGGQRQAVALARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1278835479 440 LILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLayIFISHDLQVVrALCHQVIVLRQGEVVEQG 508
Cdd:cd03245 155 LLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTL--IIITHRPSLL-DLVDRIIVMDSGRIVADG 220
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
300-516 |
7.25e-26 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 111.88 E-value: 7.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 300 PVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLhrwnrRQMLP--VRPRMQVVFQDP- 371
Cdd:TIGR03375 479 PALDNVSLTIRPGEKVAIIGRIGSGKST----LLKLLLglyqpTEGSVLLDGVDI-----RQIDPadLRRNIGYVPQDPr 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 372 --NSSLnprlsvlqivEEGLRVHQPGLSaqqrEQEVMRVMVEVGLDPETRhRYPAEF-----------SGGQRQRIAIAR 438
Cdd:TIGR03375 550 lfYGTL----------RDNIALGAPYAD----DEEILRAAELAGVTEFVR-RHPDGLdmqigergrslSGGQRQAVALAR 614
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1278835479 439 ALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLayIFISHDLQVVRaLCHQVIVLRQGEVVEQGECQRVFSA 516
Cdd:TIGR03375 615 ALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGKTL--VLVTHRTSLLD-LVDRIIVMDNGRIVADGPKDQVLEA 689
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
3-238 |
1.07e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 106.23 E-value: 1.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 3 QPLLRIDNLSiaFSKQDETRTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLLPSppVSYPQGDILFHDRSLLHAD 82
Cdd:PRK13632 5 SVMIKVENVS--FSYPNSENNALKNVSFEINEGEYVAILGHNGSGKS----TISKILTG--LLKPQSGEIKIDGITISKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 83 eqTLRGIRgNKIAMIFQEP-------MVSLNPLHSLEKQLYEvlslhrgmRKEAARgEILDCLERTGIRNAAKRLndfPH 155
Cdd:PRK13632 77 --NLKEIR-KKIGIIFQNPdnqfigaTVEDDIAFGLENKKVP--------PKKMKD-IIDDLAKKVGMEDYLDKE---PQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVrKLADSVAVMQNGRC 235
Cdd:PRK13632 142 NLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKL 220
|
...
gi 1278835479 236 VEQ 238
Cdd:PRK13632 221 IAQ 223
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-234 |
1.14e-25 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 105.28 E-value: 1.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 1 MTQPLLRIDNLSIAFSKQDETRTVVSDLTLQIQRGETLALVGESGSGKSvSALSILRLLPSPPvsypQGDILFHDRSLLH 80
Cdd:PRK11629 1 MNKILLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKS-TLLHLLGGLDTPT----SGDVIFNGQPMSK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 81 ADEQTLRGIRGNKIAMIFQ--EPMVSLNPLHSLEKQLyevlsLHRGMRKEAARGEILDCLERTGIrnaAKRLNDFPHQLS 158
Cdd:PRK11629 76 LSSAAKAELRNQKLGFIYQfhHLLPDFTALENVAMPL-----LIGKKKPAEINSRALEMLAAVGL---EHRANHRPSELS 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1278835479 159 GGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAvMQNGR 234
Cdd:PRK11629 148 GGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLE-MRDGR 222
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
7-238 |
1.18e-25 |
|
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: 105.00 E-value: 1.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 7 RIDNLSIAFSkQDETRTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLLPsppvsyPQ-GDILFHDRSLLHADEQT 85
Cdd:cd03254 2 EIEFENVNFS-YDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYD------PQkGQILIDGIDIRDISRKS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 86 LRgirgNKIAMIFQEPMVslnplhsLEKQLYEVLSLHrgmRKEAARGEILDCLERTGIRNAAKRL--------NDFPHQL 157
Cdd:cd03254 75 LR----SMIGVVLQDTFL-------FSGTIMENIRLG---RPNATDEEVIEAAKEAGAHDFIMKLpngydtvlGENGGNL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDelNMSLLFITHNLSIVRKlADSVAVMQNGRCVE 237
Cdd:cd03254 141 SQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKN-ADKILVLDDGKIIE 217
|
.
gi 1278835479 238 Q 238
Cdd:cd03254 218 E 218
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
272-527 |
1.27e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 105.63 E-value: 1.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 272 STPLLRVEDLSVSFPIRKGilrrivdrnpvLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRL------IASQGEILFD 345
Cdd:PRK14239 2 TEPILQVSDLSVYYNKKKA-----------LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpeVTITGSIVYN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 346 GMPLHRwNRRQMLPVRPRMQVVFQDPNSSlnPrLSVLQIVEEGLRVhqpglsAQQREQEVMRVMVEVGLD--------PE 417
Cdd:PRK14239 71 GHNIYS-PRTDTVDLRKEIGMVFQQPNPF--P-MSIYENVVYGLRL------KGIKDKQVLDEAVEKSLKgasiwdevKD 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 418 TRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLayIFISHDLQVVRALCHQVI 497
Cdd:PRK14239 141 RLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTM--LLVTRSMQQASRISDRTG 218
|
250 260 270
....*....|....*....|....*....|
gi 1278835479 498 VLRQGEVVEQGECQRVFSAPTQRYTRQLLS 527
Cdd:PRK14239 219 FFLDGDLIEYNDTKQMFMNPKHKETEDYIS 248
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
6-238 |
1.36e-25 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 107.85 E-value: 1.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 6 LRIDNLSIAFSKQdetrTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLL-----PSppvsypQGDILFHDRSLLH 80
Cdd:COG3839 4 LELENVSKSYGGV----EALKDIDLDIEDGEFLVLLGPSGCGKS----TLLRMIagledPT------SGEILIGGRDVTD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 81 ADEQTlrgiRGnkIAMIFQEPMvslnplhslekqLYEVLSLH---------RGMRKEAARGEILDCLERTGIRNAAKRLn 151
Cdd:COG3839 70 LPPKD----RN--IAMVFQSYA------------LYPHMTVYeniafplklRKVPKAEIDRRVREAAELLGLEDLLDRK- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 152 dfPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQ 231
Cdd:COG3839 131 --PKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMN 208
|
....*..
gi 1278835479 232 NGRcVEQ 238
Cdd:COG3839 209 DGR-IQQ 214
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-504 |
1.41e-25 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 110.14 E-value: 1.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 4 PLLRIDNLSIAFSKQDETRTVvsDLTLQiqRGETLALVGESGSGKSVSALSILRLLPSPpvsypQGDILFHDRSLLH--- 80
Cdd:PRK15439 10 PLLCARSISKQYSGVEVLKGI--DFTLH--AGEVHALLGGNGAGKSTLMKIIAGIVPPD-----SGTLEIGGNPCARltp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 81 ADEQTLrgirgnKIAMIFQEPMVSLNpLHSLEKQLYevlslhrGMRKEAARGEILDCLertgIRNAAKRLNdfPHQLSG- 159
Cdd:PRK15439 81 AKAHQL------GIYLVPQEPLLFPN-LSVKENILF-------GLPKRQASMQKMKQL----LAALGCQLD--LDSSAGs 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 160 ---GERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDElNMSLLFITHNLSIVRKLADSVAVMQNGRCV 236
Cdd:PRK15439 141 levADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQ-GVGIVFISHKLPEIRQLADRISVMRDGTIA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 237 eqnaastlLSAPQHPY--------------------TQRLLNSEPSGDPVplDADSTPLLRVEDLSvsfpirkgilrriv 296
Cdd:PRK15439 220 --------LSGKTADLstddiiqaitpaarekslsaSQKLWLELPGNRRQ--QAAGAPVLTVEDLT-------------- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 297 drNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLAL--LRLIASqGEILFDGMPLHRWNRRQ-------MLPVRPRMQVV 367
Cdd:PRK15439 276 --GEGFRNISLEVRAGEILGLAGVVGAGRTELAETLygLRPARG-GRIMLNGKEINALSTAQrlarglvYLPEDRQSSGL 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 368 FQDPNSSLNPrlsvlqiveEGLRVHQPGLSAQ-QREQEVM-RVMVEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPE 445
Cdd:PRK15439 353 YLDAPLAWNV---------CALTHNRRGFWIKpARENAVLeRYRRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQ 423
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1278835479 446 LIILDEPTSSLDRTVQAQILALLKGLQEKHrLAYIFISHDLQVVRALCHQVIVLRQGEV 504
Cdd:PRK15439 424 LLIVDEPTRGVDVSARNDIYQLIRSIAAQN-VAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
6-246 |
1.51e-25 |
|
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: 105.00 E-value: 1.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 6 LRIDNLSIAFskqDETRTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLL-----PSppvsypQGDILFHDRSLLH 80
Cdd:cd03253 1 IEFENVTFAY---DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKS----TILRLLfrfydVS------SGSILIDGQDIRE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 81 ADEQTLRgirgNKIAMIFQEpMVSLNplhslEKQLYEVlslhRGMRKEAARGEIldclertgiRNAAK------RLNDFP 154
Cdd:cd03253 68 VTLDSLR----RAIGVVPQD-TVLFN-----DTIGYNI----RYGRPDATDEEV---------IEAAKaaqihdKIMRFP 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 155 HQ-----------LSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDelNMSLLFITHNLSIVRKl 223
Cdd:cd03253 125 DGydtivgerglkLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN- 201
|
250 260
....*....|....*....|...
gi 1278835479 224 ADSVAVMQNGRCVEQNAASTLLS 246
Cdd:cd03253 202 ADKIIVLKDGRIVERGTHEELLA 224
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
296-524 |
1.51e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 105.51 E-value: 1.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 296 VDRNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-------ASQGEILFDGMPLHRWNrrqMLPVRPRMQVVF 368
Cdd:PRK14246 20 INDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIeiydskiKVDGKVLYFGKDIFQID---AIKLRKEVGMVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 369 QDPNSSlnPRLSVLQIVEEGLRVHqpGLSAQQREQEVMR-VMVEVGLDPETRHRY--PA-EFSGGQRQRIAIARALILKP 444
Cdd:PRK14246 97 QQPNPF--PHLSIYDNIAYPLKSH--GIKEKREIKKIVEeCLRKVGLWKEVYDRLnsPAsQLSGGQQQRLTIARALALKP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 445 ELIILDEPTSSLDRTVQAQILALLKGLqeKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSAPTQRYTRQ 524
Cdd:PRK14246 173 KVLLMDEPTSMIDIVNSQAIEKLITEL--KNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEK 250
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
305-510 |
2.21e-25 |
|
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: 103.79 E-value: 2.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 305 IRFSL--RPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMplhrwNRRQMLPVRPRMQVVFQDPNssLNP 377
Cdd:TIGR01277 15 MEFDLnvADGEIVAIMGPSGAGKST----LLNLIAgfiepASGSIKVNDQ-----SHTGLAPYQRPVSMLFQENN--LFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 378 RLSVLQIVEEGLRvhqPGLSAQQREQE-VMRVMVEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSL 456
Cdd:TIGR01277 84 HLTVRQNIGLGLH---PGLKLNAEQQEkVVDAAQQVGIA-DYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1278835479 457 DRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGEC 510
Cdd:TIGR01277 160 DPLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSDC 213
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-215 |
2.30e-25 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 103.71 E-value: 2.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 4 PLLRIDNLSIAFSKqdetRTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLLP--SPPVSypqGDILFHDRSLLHA 81
Cdd:COG4133 1 MMLEAENLSCRRGE----RLLFSGLSFTLAAGEALALTGPNGSGKT----TLLRILAglLPPSA---GEVLWNGEPIRDA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 82 DEQTLRgirgnKIAMIFQEPMV--SLNPLhslekqlyEVLSLHRGMRK-EAARGEILDCLERTGIrnaAKRLNDFPHQLS 158
Cdd:COG4133 70 REDYRR-----RLAYLGHADGLkpELTVR--------ENLRFWAALYGlRADREAIDEALEAVGL---AGLADLPVRQLS 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1278835479 159 GGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMsLLFITH 215
Cdd:COG4133 134 AGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGA-VLLTTH 189
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
274-508 |
2.31e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 109.91 E-value: 2.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 274 PLLRVEDLSVSFPIRKgilrrivdrNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEILFDGMP 348
Cdd:PRK11160 337 VSLTLNNVSFTYPDQP---------QPVLKGLSLQIKAGEKVALLGRTGCGKST----LLQLLtrawdPQQGEILLNGQP 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 349 LHRWNRRQMlpvRPRMQVVFQDP---NSSLnprlsvlqivEEGLRVHQPGLSaqqrEQEVMRVMVEVGLDP--ETRHRYP 423
Cdd:PRK11160 404 IADYSEAAL---RQAISVVSQRVhlfSATL----------RDNLLLAAPNAS----DEALIEVLQQVGLEKllEDDKGLN 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 424 A-------EFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALL-KGLQEKhrlAYIFISHDLqvvRALCH- 494
Cdd:PRK11160 467 AwlgeggrQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLaEHAQNK---TVLMITHRL---TGLEQf 540
|
250
....*....|....*
gi 1278835479 495 -QVIVLRQGEVVEQG 508
Cdd:PRK11160 541 dRICVMDNGQIIEQG 555
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-255 |
2.85e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 104.74 E-value: 2.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 22 RTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLLPSPPVSYP-QGDILFHDRSLLHADEQTLRgirgNKIAMIFQE 100
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKvDGKVLYFGKDIFQIDAIKLR----KEVGMVFQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 101 PmvslNPLH--SLEKQLYEVLSLHRGMRKEAARGEILDCLERTGI-RNAAKRLNDFPHQLSGGERQRVMIAMALLTRPEL 177
Cdd:PRK14246 99 P----NPFPhlSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLwKEVYDRLNSPASQLSGGQQQRLTIARALALKPKV 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1278835479 178 LIADEPTTALDVTVQAQILTLLRDLRDElnMSLLFITHNLSIVRKLADSVAVMQNGRCVEQNAASTLLSAPQHPYTQR 255
Cdd:PRK14246 175 LLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEK 250
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
5-248 |
3.09e-25 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 104.81 E-value: 3.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 5 LLRIDNLSIAFSKqdetRTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLL-----PSppvsypQGDILFHDRSLL 79
Cdd:COG4559 1 MLEAENLSVRLGG----RTLLDDVSLTLRPGELTAIIGPNGAGKS----TLLKLLtgeltPS------SGEVRLNGRPLA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 80 HADEQTLRGIRgnkiAMIFQEpmVSLN-PLHSLEkqlyeVLSLHR---GMRKEAARGEILDCLERTGIRNAAKRlnDFPh 155
Cdd:COG4559 67 AWSPWELARRR----AVLPQH--SSLAfPFTVEE-----VVALGRaphGSSAAQDRQIVREALALVGLAHLAGR--SYQ- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 156 QLSGGERQRVMIAMALL-------TRPELLIADEPTTALDVTVQAQILTLLRDLRDElNMSLLFITHNLSIVRKLADSVA 228
Cdd:COG4559 133 TLSGGEQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRIL 211
|
250 260
....*....|....*....|
gi 1278835479 229 VMQNGRCVEQNAASTLLSAP 248
Cdd:COG4559 212 LLHQGRLVAQGTPEEVLTDE 231
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
302-505 |
3.13e-25 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 108.76 E-value: 3.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 302 LKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIAS-------QGEILFDGMPLHRWNRRQMlpvrPRMQVVFQDPNSS 374
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKST----LMKILSGvyphgtwDGEIYWSGSPLKASNIRDT----ERAGIVIIHQELT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 375 LNPRLSVLQ-------IVEEGLRVHQPGLSaqQREQEVMRvmvEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPELI 447
Cdd:TIGR02633 89 LVPELSVAEniflgneITLPGGRMAYNAMY--LRAKNLLR---ELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1278835479 448 ILDEPTSSLDRTVQAQILALLKGLQeKHRLAYIFISHDLQVVRALCHQVIVLRQGEVV 505
Cdd:TIGR02633 164 ILDEPSSSLTEKETEILLDIIRDLK-AHGVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
274-520 |
3.53e-25 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 107.62 E-value: 3.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 274 PLLRVEDLSVSFpirkgilrrivDRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEILFDGMP 348
Cdd:PRK09536 2 PMIDVSDLSVEF-----------GDTTVLDGVDLSVREGSLVGLVGPNGAGKTT----LLRAIngtltPTAGTVLVAGDD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 349 LHRWNRRQmlpVRPRMQVVFQDpnSSLNPRLSVLQIVEEGlrvHQPGLSAQQREQEVMRVMVEVGLDPETRHRYPA---- 424
Cdd:PRK09536 67 VEALSARA---ASRRVASVPQD--TSLSFEFDVRQVVEMG---RTPHRSRFDTWTETDRAAVERAMERTGVAQFADrpvt 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 425 EFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFIsHDLQVVRALCHQVIVLRQGEV 504
Cdd:PRK09536 139 SLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAI-HDLDLAARYCDELVLLADGRV 217
|
250
....*....|....*.
gi 1278835479 505 VEQGECQRVFSAPTQR 520
Cdd:PRK09536 218 RAAGPPADVLTADTLR 233
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
23-236 |
4.48e-25 |
|
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: 101.35 E-value: 4.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 23 TVVSDLTLQIQRGETLALVGESGSGKS--VSALSilrllpsppvsypqGdilfhdrsLLHADEQTLRgIRGNKIAMifqe 100
Cdd:cd03216 14 KALDGVSLSVRRGEVHALLGENGAGKStlMKILS--------------G--------LYKPDSGEIL-VDGKEVSF---- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 101 pmvsLNPLHSLekqlyevlslhrgmrkeaargeildcleRTGIRnaakrlndFPHQLSGGERQRVMIAMALLTRPELLIA 180
Cdd:cd03216 67 ----ASPRDAR----------------------------RAGIA--------MVYQLSVGERQMVEIARALARNARLLIL 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1278835479 181 DEPTTALDVTVQAQILTLLRDLRDElNMSLLFITHNLSIVRKLADSVAVMQNGRCV 236
Cdd:cd03216 107 DEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
6-238 |
4.91e-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: 102.68 E-value: 4.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 6 LRIDNLSIAFSKqdetRTVVSDLTLQIQRGETLALVGESGSGKSvSALSILRLLPSPPvsypQGDILFHDRSLLHADEQT 85
Cdd:cd03268 1 LKTNDLTKTYGK----KRVLDDISLHVKKGEIYGFLGPNGAGKT-TTMKIILGLIKPD----SGEITFDGKSYQKNIEAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 86 lrgirgNKIAMIFQEPmvSLNPLHSLEKQLYeVLSLHRGMRKEaargEILDCLERTGIRNAAKRLndfPHQLSGGERQRV 165
Cdd:cd03268 72 ------RRIGALIEAP--GFYPNLTARENLR-LLARLLGIRKK----RIDEVLDVVGLKDSAKKK---VKGFSLGMKQRL 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1278835479 166 MIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDElNMSLLFITHNLSIVRKLADSVAVMQNGRCVEQ 238
Cdd:cd03268 136 GIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIEE 207
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
275-506 |
4.93e-25 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 104.01 E-value: 4.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 275 LLRVEDLSVSFPIRkgilrrivdrnPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPL 349
Cdd:PRK11248 1 MLQISHLYADYGGK-----------PALEDINLTLESGELLVVLGPSGCGKTT----LLNLIAgfvpyQHGSITLDGKPV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 350 HRwnrrqmlPVRPRmQVVFQdpNSSLNPRLSVLQIVEEGLRVhqPGLSAQQREQEVMRVMVEVGLDpETRHRYPAEFSGG 429
Cdd:PRK11248 66 EG-------PGAER-GVVFQ--NEGLLPWRNVQDNVAFGLQL--AGVEKMQRLEIAHQMLKKVGLE-GAEKRYIWQLSGG 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1278835479 430 QRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLR--QGEVVE 506
Cdd:PRK11248 133 QRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSpgPGRVVE 211
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
276-502 |
5.29e-25 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 108.74 E-value: 5.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 276 LRVEDLSVSFPirkgilrrivDRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILfdgMPLH 350
Cdd:COG4178 363 LALEDLTLRTP----------DGRPLLEDLSLSLKPGERLLITGPSGSGKST----LLRAIAglwpyGSGRIA---RPAG 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 351 RwnrRQM-LPVRPRMqvvfqdPNSSLnpRLSVLQiveeglrvhqPGLSAQQREQEVMRVMVEVGLDP-----ETRHRYPA 424
Cdd:COG4178 426 A---RVLfLPQRPYL------PLGTL--REALLY----------PATAEAFSDAELREALEAVGLGHlaerlDEEADWDQ 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1278835479 425 EFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKglQEKHRLAYIFISHDlQVVRALCHQVIVLRQG 502
Cdd:COG4178 485 VLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLR--EELPGTTVISVGHR-STLAAFHDRVLELTGD 559
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
27-238 |
5.67e-25 |
|
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: 102.57 E-value: 5.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 27 DLTLQIQRGETLALVGESGSGKSvsalSILRLLPSPPVsyPQ-GDILFHDRSLLHADEQTlrgirgNKIAMIFQEPmvSL 105
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKS----TLLNLIAGFET--PQsGRVLINGVDVTAAPPAD------RPVSMLFQEN--NL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 106 NPLHSLEKQLyeVLSLHRGMR-KEAARGEILDCLERTGIRNAAKRLndfPHQLSGGERQRVMIAMALLTRPELLIADEPT 184
Cdd:cd03298 82 FAHLTVEQNV--GLGLSPGLKlTAEDRQAIEVALARVGLAGLEKRL---PGELSGGERQRVALARVLVRDKPVLLLDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1278835479 185 TALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGRCVEQ 238
Cdd:cd03298 157 AALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQ 210
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
302-518 |
6.08e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 104.72 E-value: 6.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 302 LKNIRFSLRPGESLGLVGESGSGKSTtglaLLR-----LIASQGEI-LFDGMPLHRWNRRQMLPVRPRMQVVFQDPNSsl 375
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKST----LLQhlnglLQPTSGTVtIGERVITAGKKNKKLKPLRKKVGIVFQFPEH-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 376 nprlsvlQIVEEGLR---VHQP---GLSAQQREQEVMRVMVEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPELIIL 449
Cdd:PRK13634 97 -------QLFEETVEkdiCFGPmnfGVSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1278835479 450 DEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSAPT 518
Cdd:PRK13634 170 DEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-247 |
8.49e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 103.31 E-value: 8.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 4 PLLRIDNLSIAFSKqdetRTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLLpSPPVSYPQGDILFHDRSLLHADE 83
Cdd:PRK13548 1 AMLEARNLSVRLGG----RTLLDDVSLTLRPGEVVAILGPNGAGKS----TLLRAL-SGELSPDSGEVRLNGRPLADWSP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 84 QTLRGIRgnkiAMIFQEPMVSLnPLhSLEkqlyEVLSL----HRGMRKEAARgEILDCLERTGIRNAAKRlnDFPhQLSG 159
Cdd:PRK13548 72 AELARRR----AVLPQHSSLSF-PF-TVE----EVVAMgrapHGLSRAEDDA-LVAAALAQVDLAHLAGR--DYP-QLSG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 160 GERQRVMIAMAL--LTRPE----LLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNG 233
Cdd:PRK13548 138 GEQQRVQLARVLaqLWEPDgpprWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQG 217
|
250
....*....|....
gi 1278835479 234 RCVEQNAASTLLSA 247
Cdd:PRK13548 218 RLVADGTPAEVLTP 231
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
8-238 |
8.81e-25 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 105.55 E-value: 8.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 8 IDNLSIAFSKqdetRTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLLPSPPvSYPQGDILFH--DRSLLHAdeqt 85
Cdd:PRK10851 5 IANIKKSFGR----TQVLNDISLDIPSGQMVALLGPSGSGKT----TLLRIIAGLE-HQTSGHIRFHgtDVSRLHA---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 86 lrgiRGNKIAMIFQ------EPMVSLNPLHSLekqlyEVLSLHRGMRKEAARGEILDCLERTGIRNAAKRlndFPHQLSG 159
Cdd:PRK10851 72 ----RDRKVGFVFQhyalfrHMTVFDNIAFGL-----TVLPRRERPNAAAIKAKVTQLLEMVQLAHLADR---YPAQLSG 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1278835479 160 GERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGrCVEQ 238
Cdd:PRK10851 140 GQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQG-NIEQ 217
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
302-515 |
8.96e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 104.02 E-value: 8.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 302 LKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIAS-QGEILFDGmplHRWNRRQMLPVRPRMQVVFQDPNSSLnprls 380
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEfEGKVKIDG---ELLTAENVWNLRRKIGMVFQNPDNQF----- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 381 VLQIVEE--GLRVHQPGLSAQQREQEVMRVMVEVG-LDPETRHryPAEFSGGQRQRIAIARALILKPELIILDEPTSSLD 457
Cdd:PRK13642 95 VGATVEDdvAFGMENQGIPREEMIKRVDEALLAVNmLDFKTRE--PARLSGGQKQRVAVAGIIALRPEIIILDESTSMLD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1278835479 458 RTVQAQILALLKGLQEKHRLAYIFISHDLQVVrALCHQVIVLRQGEVVEQGECQRVFS 515
Cdd:PRK13642 173 PTGRQEIMRVIHEIKEKYQLTVLSITHDLDEA-ASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
278-517 |
9.30e-25 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 107.88 E-value: 9.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 278 VEDLSVSFPIRKGILRRIVD-------RNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEILFD 345
Cdd:PRK10789 300 VKDGSEPVPEGRGELDVNIRqftypqtDHPALENVNFTLKPGQMLGICGPTGSGKST----LLSLIqrhfdVSEGDIRFH 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 346 GMPLHRWnrrQMLPVRPRMQVVFQDP---------NSSL-NPRLSVLQIvEEGLR---VHQPGLSAQQreqevmrvmvev 412
Cdd:PRK10789 376 DIPLTKL---QLDSWRSRLAVVSQTPflfsdtvanNIALgRPDATQQEI-EHVARlasVHDDILRLPQ------------ 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 413 GLDPETRHRyPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLayIFISHDLQvvrAL 492
Cdd:PRK10789 440 GYDTEVGER-GVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTV--IISAHRLS---AL 513
|
250 260
....*....|....*....|....*..
gi 1278835479 493 --CHQVIVLRQGEVVEQGECQRVFSAP 517
Cdd:PRK10789 514 teASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
289-504 |
1.01e-24 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 103.22 E-value: 1.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 289 KGILRRIVDRNpVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLHRwnrrqmlpVRPR 363
Cdd:PRK11247 16 NAVSKRYGERT-VLNQLDLHIPAGQFVAVVGRSGCGKST----LLRLLAgletpSAGELLAGTAPLAE--------ARED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 364 MQVVFQDpnSSLNPRLSVLQIVeeGLrvhqpGLSAQQREQeVMRVMVEVGLDpETRHRYPAEFSGGQRQRIAIARALILK 443
Cdd:PRK11247 83 TRLMFQD--ARLLPWKKVIDNV--GL-----GLKGQWRDA-ALQALAAVGLA-DRANEWPAALSGGQKQRVALARALIHR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1278835479 444 PELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEV 504
Cdd:PRK11247 152 PGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
23-244 |
1.03e-24 |
|
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: 102.06 E-value: 1.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 23 TVVSDLTLQIQRGETLALVGESGSGKSvSALSILRLLpSPPVSyPQGDILFHDRSllhadeQTLRGIRgNKIAMIFQEPm 102
Cdd:cd03265 14 EAVRGVSFRVRRGEIFGLLGPNGAGKT-TTIKMLTTL-LKPTS-GRATVAGHDVV------REPREVR-RRIGIVFQDL- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 103 vslnplhSLEKQL--YEVLSLH---RGMRKEAARGEILDCLERTGIRNAAKRLndfPHQLSGGERQRVMIAMALLTRPEL 177
Cdd:cd03265 83 -------SVDDELtgWENLYIHarlYGVPGAERRERIDELLDFVGLLEAADRL---VKTYSGGMRRRLEIARSLVHRPEV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1278835479 178 LIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGRCVEQNAASTL 244
Cdd:cd03265 153 LFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
2-216 |
1.28e-24 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 102.16 E-value: 1.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 2 TQPLLRIDNLSIAFSKQDETRTVVSDLTLQIQRGETLALVGESGSGKSvSALSILRLLPSPPvsypQGDILFHDRSLLHA 81
Cdd:PRK10584 3 AENIVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKS-TLLAILAGLDDGS----SGEVSLVGQPLHQM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 82 DEQTLRGIRGNKIAMIFQEPMV--SLNPLHSLEkqlyeVLSLHRGMRKEAARGEILDCLERTGIrnaAKRLNDFPHQLSG 159
Cdd:PRK10584 78 DEEARAKLRAKHVGFVFQSFMLipTLNALENVE-----LPALLRGESSRQSRNGAKALLEQLGL---GKRLDHLPAQLSG 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1278835479 160 GERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHN 216
Cdd:PRK10584 150 GEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
5-236 |
1.50e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 103.24 E-value: 1.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 5 LLRIDNLSIAFSKQDET--RTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLL-PSPPVSYPQGdilfhdrsLLHA 81
Cdd:PRK13633 4 MIKCKNVSYKYESNEESteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLiPSEGKVYVDG--------LDTS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 82 DEQTLRGIRgNKIAMIFQEPM-----------VSLNPlhslekqlyEVLslhrGMRKEAARGEILDCLERTGIRNAAKRL 150
Cdd:PRK13633 76 DEENLWDIR-NKAGMVFQNPDnqivativeedVAFGP---------ENL----GIPPEEIRERVDESLKKVGMYEYRRHA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 151 ndfPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKlADSVAVM 230
Cdd:PRK13633 142 ---PHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVM 217
|
....*.
gi 1278835479 231 QNGRCV 236
Cdd:PRK13633 218 DSGKVV 223
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
276-508 |
2.06e-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: 100.95 E-value: 2.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 276 LRVEDLSVSFPirkgilrriVDRNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEILFDG-----MPL 349
Cdd:cd03369 7 IEVENLSVRYA---------PDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLeAEEGKIEIDGidistIPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 350 HRwnrrqmlpVRPRMQVVFQDP-------NSSLNP--RLSVLQIVeEGLRVHQPGLSaqqreqevmrvmvevgldpetrh 420
Cdd:cd03369 78 ED--------LRSSLTIIPQDPtlfsgtiRSNLDPfdEYSDEEIY-GALRVSEGGLN----------------------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 421 rypaeFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKglQEKHRLAYIFISHDLQVVrALCHQVIVLR 500
Cdd:cd03369 126 -----LSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIR--EEFTNSTILTIAHRLRTI-IDYDKILVMD 197
|
....*...
gi 1278835479 501 QGEVVEQG 508
Cdd:cd03369 198 AGEVKEYD 205
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-311 |
2.15e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 103.26 E-value: 2.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 6 LRIDNLSiafsKQDETRTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLLpsppvsYP-QGDILFHDRSLlhaDEQ 84
Cdd:COG4152 2 LELKGLT----KRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGIL------APdSGEVLWDGEPL---DPE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 85 TLRGI------RGnkiamifqepmvsLNPLHSLEKQLYEVLSLHrGMRKEAARGEILDCLERTGIrnaAKRLNDFPHQLS 158
Cdd:COG4152 69 DRRRIgylpeeRG-------------LYPKMKVGEQLVYLARLK-GLSKAEAKRRADEWLERLGL---GDRANKKVEELS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 159 GGERQRVMIAMALLTRPELLIADEPTTALD-VTVQAqILTLLRDLRDElNMSLLFITHNLSIVRKLADSVAVMQNGRCVE 237
Cdd:COG4152 132 KGNQQKVQLIAALLHDPELLILDEPFSGLDpVNVEL-LKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 238 QNAASTLLSApqhpYTQRLLNSEPSGDPVPLDADSTPL-LRVEDLSVSFPIRKG-----ILRRIVDRNPVlknIRFSLRP 311
Cdd:COG4152 210 SGSVDEIRRQ----FGRNTLRLEADGDAGWLRALPGVTvVEEDGDGAELKLEDGadaqeLLRALLARGPV---REFEEVR 282
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
306-515 |
2.29e-24 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 101.58 E-value: 2.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 306 RFSL--RPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMplhrwNRRQMLPVRPRMQVVFQDPNssLNPR 378
Cdd:PRK10771 17 RFDLtvERGERVAILGPSGAGKST----LLNLIAgfltpASGSLTLNGQ-----DHTTTPPSRRPVSMLFQENN--LFSH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 379 LSVLQIVeeGLRVHqPGL--SAQQREQeVMRVMVEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSL 456
Cdd:PRK10771 86 LTVAQNI--GLGLN-PGLklNAAQREK-LHAIARQMGIE-DLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSAL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1278835479 457 DRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFS 515
Cdd:PRK10771 161 DPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
233-516 |
2.44e-24 |
|
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: 106.71 E-value: 2.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 233 GRCVEQNAASTLLSAPQHPYTQrllnsepsgdPVPLDADstplLRVEDLSVSFPIRKgilrrivdRNPVLKNIRFSLRPG 312
Cdd:TIGR02204 309 ERLIELLQAEPDIKAPAHPKTL----------PVPLRGE----IEFEQVNFAYPARP--------DQPALDGLNLTVRPG 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 313 ESLGLVGESGSGKSTTGLALLRLI-ASQGEILFDGMPLhrwnrRQMLP--VRPRMQVVFQDPN---SSlnprlsvlqiVE 386
Cdd:TIGR02204 367 ETVALVGPSGAGKSTLFQLLLRFYdPQSGRILLDGVDL-----RQLDPaeLRARMALVPQDPVlfaAS----------VM 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 387 EGLRVHQPGLSAQQ-REQEVMRVMVE-VGLDPETRHRYPAE----FSGGQRQRIAIARALILKPELIILDEPTSSLDRTV 460
Cdd:TIGR02204 432 ENIRYGRPDATDEEvEAAARAAHAHEfISALPEGYDTYLGErgvtLSGGQRQRIAIARAILKDAPILLLDEATSALDAES 511
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1278835479 461 QAQILALLKGLQeKHRLAYIfISHDLQVVRAlCHQVIVLRQGEVVEQGECQRVFSA 516
Cdd:TIGR02204 512 EQLVQQALETLM-KGRTTLI-IAHRLATVLK-ADRIVVMDQGRIVAQGTHAELIAK 564
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
24-246 |
2.71e-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: 100.97 E-value: 2.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 24 VVSDLTLQIQRGETLALVGESGSGKSVSALSILRLLPspPVSypqGDILFHDRSLLHA--DEQTLRGIrgnkiAMIFQEP 101
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLP--PRS---GSIRFDGRDITGLppHERARAGI-----GYVPEGR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 102 MV--SLNPLHSLEkqlyevLSLHRGMRKEAARG--EILDCLERTgirnaAKRLNDFPHQLSGGERQRVMIAMALLTRPEL 177
Cdd:cd03224 85 RIfpELTVEENLL------LGAYARRRAKRKARleRVYELFPRL-----KERRKQLAGTLSGGEQQMLAIARALMSRPKL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1278835479 178 LIADEPTTALDVTVQAQILTLLRDLRDElNMSLLFITHNLSIVRKLADSVAVMQNGRCVEQNAASTLLS 246
Cdd:cd03224 154 LLLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
273-508 |
4.46e-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: 100.83 E-value: 4.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 273 TPLLRVEDLSVSFpirkgilrrivDRNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEILFDGMPLHR 351
Cdd:COG0410 1 MPMLEVENLHAGY-----------GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLpPRSGSIRFDGEDITG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 352 WNRRQmlpvRPRM---QV-----VFqdpnsslnPRLSVlqivEEGLRVHQPGLSAQQREQEVMRVMVEvgLDP---ETRH 420
Cdd:COG0410 70 LPPHR----IARLgigYVpegrrIF--------PSLTV----EENLLLGAYARRDRAEVRADLERVYE--LFPrlkERRR 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 421 RYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKhRLAYIFISHDLQVVRALCHQVIVLR 500
Cdd:COG0410 132 QRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLE 210
|
....*...
gi 1278835479 501 QGEVVEQG 508
Cdd:COG0410 211 RGRIVLEG 218
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
6-238 |
5.31e-24 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 100.02 E-value: 5.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 6 LRIDNLSIAFskqdETRTVVSDLTLQIQRGETLALVGESGSGKSVsalsILRLLPS--PPVSypqGDILFHDRSLlhade 83
Cdd:cd03301 1 VELENVTKRF----GNVTALDDLNLDIADGEFVVLLGPSGCGKTT----TLRMIAGleEPTS---GRIYIGGRDV----- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 84 qTLRGIRGNKIAMIFQEpmVSLNPLHSLEKQLYEVLSLhRGMRKEAARGEILDCLERTGIRNAakrLNDFPHQLSGGERQ 163
Cdd:cd03301 65 -TDLPPKDRDIAMVFQN--YALYPHMTVYDNIAFGLKL-RKVPKDEIDERVREVAELLQIEHL---LDRKPKQLSGGQRQ 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1278835479 164 RVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGRcVEQ 238
Cdd:cd03301 138 RVALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQ-IQQ 211
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
302-517 |
5.39e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 101.83 E-value: 5.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 302 LKNIRFSLRPGESLGLVGESGSGKST-----TGLallrLIASQGEILFDGMPLH-RWNRRQMLPVRPRMQVVFQDPNSSL 375
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTlmqhfNAL----LKPSSGTITIAGYHITpETGNKNLKKLRKKVSLVFQFPEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 376 NPRlSVLQIVEEGLRvhQPGLSAQQREQEVMRVMVEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSS 455
Cdd:PRK13641 99 FEN-TVLKDVEFGPK--NFGFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAG 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1278835479 456 LDRTVQAQILALLKGLQ-EKHRLayIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSAP 517
Cdd:PRK13641 176 LDPEGRKEMMQLFKDYQkAGHTV--ILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-255 |
5.42e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 101.14 E-value: 5.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 6 LRIDNLSIAFSKQDetrtVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLLPSPPVSYPQGDILFHDRSLLHADEQT 85
Cdd:PRK14247 4 IEIRDLKVSFGQVE----VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARVSGEVYLDGQDIFKMDVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 86 LRgirgNKIAMIFQEPmvslNPLHSLE--KQLYEVLSLHRGMR-KEAARGEILDCLERTGIRNAAK-RLNDFPHQLSGGE 161
Cdd:PRK14247 80 LR----RRVQMVFQIP----NPIPNLSifENVALGLKLNRLVKsKKELQERVRWALEKAQLWDEVKdRLDAPAGKLSGGQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 162 RQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDElnMSLLFITHNLSIVRKLADSVAVMQNGRCVEQNAA 241
Cdd:PRK14247 152 QQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPT 229
|
250
....*....|....
gi 1278835479 242 STLLSAPQHPYTQR 255
Cdd:PRK14247 230 REVFTNPRHELTEK 243
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
25-254 |
6.07e-24 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 103.96 E-value: 6.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 25 VSDLTLQIQRGETLALVGESGSGKSVSALSILRLLPSPpvsypQGDILFHDRSLLHADEQTLRGIRGNKIAMIFQEpmVS 104
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPT-----RGQVLIDGVDIAKISDAELREVRRKKIAMVFQS--FA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 105 LNPLHSLEKQLYEVLSLhRGMRKEAARGEILDCLERTGIRNAAkrlNDFPHQLSGGERQRVMIAMALLTRPELLIADEPT 184
Cdd:PRK10070 117 LMPHMTVLDNTAFGMEL-AGINAEERREKALDALRQVGLENYA---HSYPDELSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 185 TALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGRCVEQNAASTLLSAPQHPYTQ 254
Cdd:PRK10070 193 SALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVR 262
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
285-527 |
6.88e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 100.69 E-value: 6.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 285 FPIRKGILRRIVDRNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIA------SQGEILFDGMPLHRwnrRQML 358
Cdd:PRK14267 3 FAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneearVEGEVRLFGRNIYS---PDVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 359 PVRPRMQV--VFQDPNSSlnPRLSVLQIVEEGLRVHQPGLSAQQREQEVMRVMVEVGLDPETRHR---YPAEFSGGQRQR 433
Cdd:PRK14267 80 PIEVRREVgmVFQYPNPF--PHLTIYDNVAIGVKLNGLVKSKKELDERVEWALKKAALWDEVKDRlndYPSNLSGGQRQR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 434 IAIARALILKPELIILDEPTSSLDRTVQAQILALLkgLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRV 513
Cdd:PRK14267 158 LVIARALAMKPKILLMDEPTANIDPVGTAKIEELL--FELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKV 235
|
250
....*....|....
gi 1278835479 514 FSAPTQRYTRQLLS 527
Cdd:PRK14267 236 FENPEHELTEKYVT 249
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
300-508 |
6.98e-24 |
|
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: 105.80 E-value: 6.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 300 PVLKNIRFSLRPGESLGLVGESGSGKSTTGlallRLIA-----SQGEILFDGMPLHRWNRRQmlpVRPRMQVVFQDpnss 374
Cdd:TIGR03796 493 PLIENFSLTLQPGQRVALVGGSGSGKSTIA----KLVAglyqpWSGEILFDGIPREEIPREV---LANSVAMVDQD---- 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 375 lnprLSVLQ-IVEEGLRVHQPGLSaqqrEQEVMRVMVEVGLDPETRHR---YPAE-------FSGGQRQRIAIARALILK 443
Cdd:TIGR03796 562 ----IFLFEgTVRDNLTLWDPTIP----DADLVRACKDAAIHDVITSRpggYDAElaegganLSGGQRQRLEIARALVRN 633
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1278835479 444 PELIILDEPTSSLDRTVQAQILALLKglqeKHRLAYIFISHDLQVVRAlCHQVIVLRQGEVVEQG 508
Cdd:TIGR03796 634 PSILILDEATSALDPETEKIIDDNLR----RRGCTCIIVAHRLSTIRD-CDEIIVLERGKVVQRG 693
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
301-508 |
8.02e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 101.72 E-value: 8.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 301 VLKNIRFSLRPGESLGLVGESGSGKSTTglalLRLI-----ASQGEILFDGMPLHRWNRRQM--LP-VRprmqvvfqdpn 372
Cdd:COG4152 16 AVDDVSFTVPKGEIFGLLGPNGAGKTTT----IRIIlgilaPDSGEVLWDGEPLDPEDRRRIgyLPeER----------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 373 sSLNPRLSVL-QIVEEG-LRvhqpGLSAQQREQEVMRVMVEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPELIILD 450
Cdd:COG4152 81 -GLYPKMKVGeQLVYLArLK----GLSKAEAKRRADEWLERLGL-GDRANKKVEELSKGNQQKVQLIAALLHDPELLILD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1278835479 451 EPTSSLDrTVQAQILA-LLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:COG4152 155 EPFSGLD-PVNVELLKdVIRELAAKGT-TVIFSSHQMELVEELCDRIVIINKGRKVLSG 211
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
26-234 |
8.39e-24 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 99.24 E-value: 8.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 26 SDLTLQIQRGETLALVGESGSGKSvsalSILRLL-----PSppvsypQGDILFHDRSLLHADEQTLRGIRgNKIAMIFQE 100
Cdd:TIGR02673 19 HDVSLHIRKGEFLFLTGPSGAGKT----TLLKLLygaltPS------RGQVRIAGEDVNRLRGRQLPLLR-RRIGVVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 101 PMVSLNplhsleKQLYE--VLSLH-RGMRKEAARGEILDCLERTGIrnaAKRLNDFPHQLSGGERQRVMIAMALLTRPEL 177
Cdd:TIGR02673 88 FRLLPD------RTVYEnvALPLEvRGKKEREIQRRVGAALRQVGL---EHKADAFPEQLSGGEQQRVAIARAIVNSPPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1278835479 178 LIADEPTTALDVTVQAQILTLLRDLRDeLNMSLLFITHNLSIVRKLADSVAVMQNGR 234
Cdd:TIGR02673 159 LLADEPTGNLDPDLSERILDLLKRLNK-RGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
276-508 |
8.40e-24 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 100.14 E-value: 8.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 276 LRVEDLSVSfpirkgilrriVDRNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALL---RLIASQGEILFDGMPLhrw 352
Cdd:COG0396 1 LEIKNLHVS-----------VEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMghpKYEVTSGSILLDGEDI--- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 353 nrrQMLPV--RPRMQV--VFQDP-------NSSLnprlsvLQIVEEGLRvhQPGLSAQQREQEVMRVMVEVGLDPETRHR 421
Cdd:COG0396 67 ---LELSPdeRARAGIflAFQYPveipgvsVSNF------LRTALNARR--GEELSAREFLKLLKEKMKELGLDEDFLDR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 422 YPAE-FSGGQRQRIAIARALILKPELIILDEPTSSLDrtVQA-QILA-LLKGLQEKHRlAYIFISHD---LQVVRAlcHQ 495
Cdd:COG0396 136 YVNEgFSGGEKKRNEILQMLLLEPKLAILDETDSGLD--IDAlRIVAeGVNKLRSPDR-GILIITHYqriLDYIKP--DF 210
|
250
....*....|...
gi 1278835479 496 VIVLRQGEVVEQG 508
Cdd:COG0396 211 VHVLVDGRIVKSG 223
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
276-508 |
8.85e-24 |
|
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: 98.78 E-value: 8.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 276 LRVEDLSVSFPIRKGILRRivdrnPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIASQ-------GEILFDGMP 348
Cdd:cd03213 4 LSFRNLTVTVKSSPSKSGK-----QLLKNVSGKAKPGELTAIMGPSGAGKST----LLNALAGRrtglgvsGEVLINGRP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 349 LHRWNrrqmlpVRPRMQVVFQDpnSSLNPRLSVlqivEEGLRVhqpglSAQQReqevmrvmvevGLdpetrhrypaefSG 428
Cdd:cd03213 75 LDKRS------FRKIIGYVPQD--DILHPTLTV----RETLMF-----AAKLR-----------GL------------SG 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 429 GQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAyIFISHDL-QVVRALCHQVIVLRQGEVVEQ 507
Cdd:cd03213 115 GERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTI-ICSIHQPsSEIFELFDKLLLLSQGRVIYF 193
|
.
gi 1278835479 508 G 508
Cdd:cd03213 194 G 194
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
259-508 |
9.42e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 104.93 E-value: 9.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 259 SEPSGDPVPLDADSTPLLRVEDLSVSFPirkgilrrivDRNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIAS 338
Cdd:PRK11174 333 AHPQQGEKELASNDPVTIEAEDLEILSP----------DGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 339 QGEILFDGMPLHRWNRRQMlpvrpRMQV--VFQdpnsslNPRLsVLQIVEEGLRVHQPGLSAQQREQEVMRVMV------ 410
Cdd:PRK11174 403 QGSLKINGIELRELDPESW-----RKHLswVGQ------NPQL-PHGTLRDNVLLGNPDASDEQLQQALENAWVseflpl 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 411 -EVGLDPETRHRyPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKglQEKHRLAYIFISHDLQVV 489
Cdd:PRK11174 471 lPQGLDTPIGDQ-AAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALN--AASRRQTTLMVTHQLEDL 547
|
250
....*....|....*....
gi 1278835479 490 RAlCHQVIVLRQGEVVEQG 508
Cdd:PRK11174 548 AQ-WDQIWVMQDGQIVQQG 565
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
276-508 |
1.35e-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: 97.77 E-value: 1.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 276 LRVEDLSVSFPirkgilrriVDRNPVLKNIRFSLRPGESLGLVGESGSGKSTTgLALLR--LIASQGEILFDGMPLHRWN 353
Cdd:cd03247 1 LSINNVSFSYP---------EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTL-LQLLTgdLKPQQGEITLDGVPVSDLE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 354 RRqmlpVRPRMQVVFQDP---NSSLNPRLsvlqiveeGLRvhqpglsaqqreqevmrvmvevgldpetrhrypaeFSGGQ 430
Cdd:cd03247 71 KA----LSSLISVLNQRPylfDTTLRNNL--------GRR-----------------------------------FSGGE 103
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1278835479 431 RQRIAIARALILKPELIILDEPTSSLDRTVQAQILALL-KGLQEKhrlAYIFISHDLQVVRALcHQVIVLRQGEVVEQG 508
Cdd:cd03247 104 RQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIfEVLKDK---TLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
276-508 |
1.36e-23 |
|
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: 99.14 E-value: 1.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 276 LRVEDLSVSFPIRKGILRRIVDRN-----------PVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQ 339
Cdd:cd03220 1 IELENVSKSYPTYKGGSSSLKKLGilgrkgevgefWALKDVSFEVPRGERIGLIGRNGAGKST----LLRLLAgiyppDS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 340 GEILFDGMplhrwnrrqmlpVRPRMqvvfqDPNSSLNPRLSVLQIVEEGLRVHqpGLSAQQREQEVMRVMV--EVGLDPE 417
Cdd:cd03220 77 GTVTVRGR------------VSSLL-----GLGGGFNPELTGRENIYLNGRLL--GLSRKEIDEKIDEIIEfsELGDFID 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 418 TRHRypaEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRlAYIFISHDLQVVRALCHQVI 497
Cdd:cd03220 138 LPVK---TYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGK-TVILVSHDPSSIKRLCDRAL 213
|
250
....*....|.
gi 1278835479 498 VLRQGEVVEQG 508
Cdd:cd03220 214 VLEKGKIRFDG 224
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
5-234 |
1.65e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 100.19 E-value: 1.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 5 LLRIDNLSIAFsKQDETRTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLLPSPpvsypQGDILFHDRSLlhaDEQ 84
Cdd:PRK13650 4 IIEVKNLTFKY-KEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAE-----SGQIIIDGDLL---TEE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 85 TLRGIRgNKIAMIFQEP-------MVSLNPLHSLEKQlyevlslhrGMRKEAARGEILDCLERTGIRNAAKRLndfPHQL 157
Cdd:PRK13650 75 NVWDIR-HKIGMVFQNPdnqfvgaTVEDDVAFGLENK---------GIPHEEMKERVNEALELVGMQDFKERE---PARL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1278835479 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVrKLADSVAVMQNGR 234
Cdd:PRK13650 142 SGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQ 217
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
292-508 |
2.40e-23 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 98.12 E-value: 2.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 292 LRRIVDRNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIAS-QGEILFDGMPLHRWNRRQM--LPvrprmqvvf 368
Cdd:cd03269 6 VTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPdSGEVLFDGKPLDIAARNRIgyLP--------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 369 qdPNSSLNPRLSVLQIVEEGLRVHqpGLSAQQREQEVMRVMVEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPELII 448
Cdd:cd03269 77 --EERGLYPKMKVIDQLVYLAQLK--GLKKEEARRRIDEWLERLELS-EYANKRVEELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 449 LDEPTSSLDRTVQAQILALLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDVIRELARAGK-TVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
279-508 |
2.64e-23 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 103.50 E-value: 2.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 279 EDLSVSFPirkgilrrivDRNPVLKNIRFSLRPGESLGLVGESGSGKSTTgLALLRLI--ASQGEILFDGMPLHRWNRRQ 356
Cdd:PRK13657 338 DDVSFSYD----------NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTL-INLLQRVfdPQSGRILIDGTDIRTVTRAS 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 357 MlpvRPRMQVVFQDP---NSSlnprlsvlqiVEEGLRVHQPGLSaqqrEQEVMRVMV-----------EVGLDPETRHRy 422
Cdd:PRK13657 407 L---RRNIAVVFQDAglfNRS----------IEDNIRVGRPDAT----DEEMRAAAEraqahdfierkPDGYDTVVGER- 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 423 PAEFSGGQRQRIAIARALILKPELIILDEPTSSLD----RTVQAQILALLKGlqekhRLAYIfISHDLQVVRAlCHQVIV 498
Cdd:PRK13657 469 GRQLSGGERQRLAIARALLKDPPILILDEATSALDveteAKVKAALDELMKG-----RTTFI-IAHRLSTVRN-ADRILV 541
|
250
....*....|
gi 1278835479 499 LRQGEVVEQG 508
Cdd:PRK13657 542 FDNGRVVESG 551
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
5-238 |
2.73e-23 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 103.50 E-value: 2.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 5 LLRIDNLSIAFskqDETRTVVSDLTLQIQRGETLALVGESGSGKSvSALSILRllpspPVSYPQGDILFHD----RSLlh 80
Cdd:PRK13657 334 AVEFDDVSFSY---DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKS-TLINLLQ-----RVFDPQSGRILIDgtdiRTV-- 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 81 adeqTLRGIRGNkIAMIFQEPMVslnplhsLEKQLYEVLSLHRG------MRKEAARGEILDCLERTGIR---NAAKRLN 151
Cdd:PRK13657 403 ----TRASLRRN-IAVVFQDAGL-------FNRSIEDNIRVGRPdatdeeMRAAAERAQAHDFIERKPDGydtVVGERGR 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 152 dfphQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDelNMSLLFITHNLSIVRKlADSVAVMQ 231
Cdd:PRK13657 471 ----QLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAHRLSTVRN-ADRILVFD 543
|
....*..
gi 1278835479 232 NGRCVEQ 238
Cdd:PRK13657 544 NGRVVES 550
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
6-230 |
4.54e-23 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 102.75 E-value: 4.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 6 LRIDNLSIAFSkqdETRTVVSDLTLQIQRGETLALVGESGSGKSvSALS-ILRLLPSPpvsypQGDILFHDRSLLHADEQ 84
Cdd:TIGR02857 322 LEFSGVSVAYP---GRRPALRPVSFTVPPGERVALVGPSGAGKS-TLLNlLLGFVDPT-----EGSIAVNGVPLADADAD 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 85 TLRGirgnKIAMIFQEPmvslnplHSLEKQLYEVLSLHRgmrKEAARGEILDCLERTGI--------RNAAKRLNDFPHQ 156
Cdd:TIGR02857 393 SWRD----QIAWVPQHP-------FLFAGTIAENIRLAR---PDASDAEIREALERAGLdefvaalpQGLDTPIGEGGAG 458
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1278835479 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDelNMSLLFITHNLSIVRkLADSVAVM 230
Cdd:TIGR02857 459 LSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAA-LADRIVVL 529
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
25-238 |
6.49e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 98.77 E-value: 6.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 25 VSDLTLQIQRGETLALVGESGSGKSVSALSILRLLPspPVSypqGDILFHDRSLLHAdEQTLRGIRGNkIAMIFQEPMVS 104
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILK--PSS---GRILFDGKPIDYS-RKGLMKLRES-VGMVFQDPDNQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 105 LNPLHSLEKQLYEVLSLhrGMRKEAARGEILDCLERTGIrnaaKRLNDFP-HQLSGGERQRVMIAMALLTRPELLIADEP 183
Cdd:PRK13636 95 LFSASVYQDVSFGAVNL--KLPEDEVRKRVDNALKRTGI----EHLKDKPtHCLSFGQKKRVAIAGVLVMEPKVLVLDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1278835479 184 TTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGRCVEQ 238
Cdd:PRK13636 169 TAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQ 223
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
317-525 |
7.39e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 98.24 E-value: 7.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 317 LVGESGSGKSTTGLALLRL------IASQGEILFDGMPLhrWNRRQMLPVRPRMQVVFQDPNSSlnpRLSVLQIVEEGLR 390
Cdd:PRK14271 52 LMGPTGSGKTTFLRTLNRMndkvsgYRYSGDVLLGGRSI--FNYRDVLEFRRRVGMLFQRPNPF---PMSIMDNVLAGVR 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 391 VHQPGLSAQQREQEVMRvMVEVGLDPETRHRY---PAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILAL 467
Cdd:PRK14271 127 AHKLVPRKEFRGVAQAR-LTEVGLWDAVKDRLsdsPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEF 205
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1278835479 468 LKGLQEkhRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSAP----TQRYTRQL 525
Cdd:PRK14271 206 IRSLAD--RLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPkhaeTARYVAGL 265
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
276-508 |
7.69e-23 |
|
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: 97.40 E-value: 7.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 276 LRVEDLSVSFPIR------KGILRRIVDRN----PVLKNIRFSLRPGESLGLVGESGSGKSTTgLALLR--LIASQGEIL 343
Cdd:cd03267 1 IEVSNLSKSYRVYskepglIGSLKSLFKRKyrevEALKGISFTIEKGEIVGFIGPNGAGKTTT-LKILSglLQPTSGEVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 344 FDGmpLHRWNRRQMLpvRPRMQVVFQDpNSSLNPRLSVLqiveEGLRVHQP--GLSAQQREQEVMRV--MVEVG--LDPE 417
Cdd:cd03267 80 VAG--LVPWKRRKKF--LRRIGVVFGQ-KTQLWWDLPVI----DSFYLLAAiyDLPPARFKKRLDELseLLDLEelLDTP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 418 TRhrypaEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVI 497
Cdd:cd03267 151 VR-----QLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVL 225
|
250
....*....|.
gi 1278835479 498 VLRQGEVVEQG 508
Cdd:cd03267 226 VIDKGRLLYDG 236
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-254 |
8.11e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 97.93 E-value: 8.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 2 TQPLLRIDNLSIAFSKQdetrTVVSDLTLQIQRGETLALVGESGSGKSvsalSILR-------LLPSPPVsypQGDILFH 74
Cdd:PRK14243 7 TETVLRTENLNVYYGSF----LAVKNVWLDIPKNQITAFIGPSGCGKS----TILRcfnrlndLIPGFRV---EGKVTFH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 75 DRSLL--HADEQTLRgirgNKIAMIFQEPmvslNPLhslEKQLYEVLSLhrGMRKEAARGEILDCLERTgIRNAA----- 147
Cdd:PRK14243 76 GKNLYapDVDPVEVR----RRIGMVFQKP----NPF---PKSIYDNIAY--GARINGYKGDMDELVERS-LRQAAlwdev 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 148 -KRLNDFPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDElnMSLLFITHNLSIVRKLADS 226
Cdd:PRK14243 142 kDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAARVSDM 219
|
250 260 270
....*....|....*....|....*....|....*..
gi 1278835479 227 VAVM---------QNGRCVEQNAASTLLSAPQHPYTQ 254
Cdd:PRK14243 220 TAFFnveltegggRYGYLVEFDRTEKIFNSPQQQATR 256
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
299-507 |
8.45e-23 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 99.92 E-value: 8.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 299 NPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGmplhrwnRR--QMLPVRPRMQVVFQdp 371
Cdd:PRK11650 17 TQVIKGIDLDVADGEFIVLVGPSGCGKST----LLRMVAgleriTSGEIWIGG-------RVvnELEPADRDIAMVFQ-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 372 NSSLNPRLSVLQIVEEGLRVHqpGLSAQQREQEVMRV--MVEVG--LDpetrhRYPAEFSGGQRQRIAIARALILKPELI 447
Cdd:PRK11650 84 NYALYPHMSVRENMAYGLKIR--GMPKAEIEERVAEAarILELEplLD-----RKPRELSGGQRQRVAMGRAIVREPAVF 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1278835479 448 ILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDlQV-VRALCHQVIVLRQGeVVEQ 507
Cdd:PRK11650 157 LFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHD-QVeAMTLADRVVVMNGG-VAEQ 215
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
6-247 |
8.96e-23 |
|
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: 96.92 E-value: 8.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 6 LRIDNLSiaFSKQDETRTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLLPSPpVSYPQGDILFHDRSLLHADEQT 85
Cdd:cd03251 1 VEFKNVT--FRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKS----TLVNLIPRF-YDVDSGRILIDGHDVRDYTLAS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 86 LRgirgNKIAMIFQEPMVSLNPLHslEKQLYEvlslhrgmRKEAARGEILDCLErtgIRNAAKRLNDFPH---------- 155
Cdd:cd03251 74 LR----RQIGLVSQDVFLFNDTVA--ENIAYG--------RPGATREEVEEAAR---AANAHEFIMELPEgydtvigerg 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 156 -QLSGGERQRVMIAMALLTRPELLIADEPTTALDVT----VQAQILTLLRdlrdelNMSLLFITHNLSIVRKlADSVAVM 230
Cdd:cd03251 137 vKLSGGQRQRIAIARALLKDPPILILDEATSALDTEserlVQAALERLMK------NRTTFVIAHRLSTIEN-ADRIVVL 209
|
250
....*....|....*..
gi 1278835479 231 QNGRCVEQNAASTLLSA 247
Cdd:cd03251 210 EDGKIVERGTHEELLAQ 226
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
298-508 |
1.02e-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: 101.82 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 298 RNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEILFDGMPLhrwnrRQMLP--VRPRMQVVFQDP--- 371
Cdd:COG5265 370 ERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYdVTSGRILIDGQDI-----RDVTQasLRAAIGIVPQDTvlf 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 372 NSSLnprlsvlqivEEGLRVHQPGLSaqqrEQEVMRV-------------------MV-EVGLdpetrhrypaEFSGGQR 431
Cdd:COG5265 445 NDTI----------AYNIAYGRPDAS----EEEVEAAaraaqihdfieslpdgydtRVgERGL----------KLSGGEK 500
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1278835479 432 QRIAIARALILKPELIILDEPTSSLD-RTVQAqILALLKGLQEKHrlAYIFISHDLQ-VVRAlcHQVIVLRQGEVVEQG 508
Cdd:COG5265 501 QRVAIARTLLKNPPILIFDEATSALDsRTERA-IQAALREVARGR--TTLVIAHRLStIVDA--DEILVLEAGRIVERG 574
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
13-258 |
1.29e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 97.95 E-value: 1.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 13 IAFSKQDETRTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLLpsppvsypQGDILFHD--RSLLHAD-----EQT 85
Cdd:PRK13640 11 VSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKS----TISKLI--------NGLLLPDDnpNSKITVDgitltAKT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 86 LRGIRgNKIAMIFQEP-------MVSLNPLHSLEkqlyevlslHRGMRKEAARGEILDCLERTGIRNAAKRLndfPHQLS 158
Cdd:PRK13640 79 VWDIR-EKVGIVFQNPdnqfvgaTVGDDVAFGLE---------NRAVPRPEMIKIVRDVLADVGMLDYIDSE---PANLS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 159 GGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVrKLADSVAVMQNGRCVEQ 238
Cdd:PRK13640 146 GGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQ 224
|
250 260
....*....|....*....|....*...
gi 1278835479 239 NAASTLLSAPQH--------PYTQRLLN 258
Cdd:PRK13640 225 GSPVEIFSKVEMlkeigldiPFVYKLKN 252
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
24-258 |
1.50e-22 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 96.96 E-value: 1.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 24 VVSDLTLQIQRGETLALVGESGSGKSvSALSILRLLPSP---PVSYPQGDILF---HDRSLLHADEQTLRGIRgNKIAMI 97
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKS-TFLRCINFLEKPsegSIVVNGQTINLvrdKDGQLKVADKNQLRLLR-TRLTMV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 98 FQEPMV--SLNPLHSLEKQLYEVLslhrGMRKEAARGEILDCLERTGIRNAAKrlNDFPHQLSGGERQRVMIAMALLTRP 175
Cdd:PRK10619 98 FQHFNLwsHMTVLENVMEAPIQVL----GLSKQEARERAVKYLAKVGIDERAQ--GKYPVHLSGGQQQRVSIARALAMEP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 176 ELLIADEPTTALDVTVQAQILTLLRDLRDElNMSLLFITHNLSIVRKLADSVAVMQNGRCVEQNAASTLLSAPQHPYTQR 255
Cdd:PRK10619 172 EVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQ 250
|
...
gi 1278835479 256 LLN 258
Cdd:PRK10619 251 FLK 253
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
5-236 |
2.18e-22 |
|
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: 95.51 E-value: 2.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 5 LLRIDNLSIAFSKQDETRTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLLpSPPVSYPQGDILFHDRSLLHADEQ 84
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKT----TTLRML-AGLLEPDAGFATVDGFDVVKEPAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 85 TLRGIrgnkiamifqepmvslnPLHSLEKQLYEVLS----------LHrGMRKEAARGEILDCLERTGIRN-AAKRLNDF 153
Cdd:cd03266 76 ARRRL-----------------GFVSDSTGLYDRLTarenleyfagLY-GLKGDELTARLEELADRLGMEElLDRRVGGF 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 154 phqlSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDElNMSLLFITHNLSIVRKLADSVAVMQNG 233
Cdd:cd03266 138 ----STGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRAL-GKCILFSTHIMQEVERLCDRVVVLHRG 212
|
...
gi 1278835479 234 RCV 236
Cdd:cd03266 213 RVV 215
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
220-508 |
3.37e-22 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 100.18 E-value: 3.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 220 VRKLADSVAVMQNGRCVEQnAASTLLSAPQHPYTQRLLNSEPSGDpvpldadstplLRVEDLSVSFPIRkgilrrivDRn 299
Cdd:TIGR02203 287 LKSLTNVNAPMQRGLAAAE-SLFTLLDSPPEKDTGTRAIERARGD-----------VEFRNVTFRYPGR--------DR- 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 300 PVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEILFDGMPLHRWN----RRQMLPVRprMQVVFQDPNSS 374
Cdd:TIGR02203 346 PALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYePDSGQILLDGHDLADYTlaslRRQVALVS--QDVVLFNDTIA 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 375 LNPRLSVL-QIVEEGLRvhqpGLSAQQREQEVMRVMVEvGLDPETRHRyPAEFSGGQRQRIAIARALILKPELIILDEPT 453
Cdd:TIGR02203 424 NNIAYGRTeQADRAEIE----RALAAAYAQDFVDKLPL-GLDTPIGEN-GVLLSGGQRQRLAIARALLKDAPILILDEAT 497
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1278835479 454 SSLD----RTVQAQILALLKGlqekhRLAYIfISHDLQVVRAlCHQVIVLRQGEVVEQG 508
Cdd:TIGR02203 498 SALDneseRLVQAALERLMQG-----RTTLV-IAHRLSTIEK-ADRIVVMDDGRIVERG 549
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
25-246 |
3.84e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 96.39 E-value: 3.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 25 VSDLTLQIQRGETLALVGESGSGKSVSALSILRLLPSPPVSYPQGDILFHDRSllhaDEQTLRGIRgNKIAMIFQEPmvs 104
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKT----KDKYIRPVR-KRIGMVFQFP--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 105 lnplhslEKQLYEVlSLHR---------GMRKEAARGEILDCLERTGI-RNAakrLNDFPHQLSGGERQRVMIAMALLTR 174
Cdd:PRK13646 95 -------ESQLFED-TVEReiifgpknfKMNLDEVKNYAHRLLMDLGFsRDV---MSQSPFQMSGGQMRKIAIVSILAMN 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1278835479 175 PELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGRCVEQNAASTLLS 246
Cdd:PRK13646 164 PDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK 235
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
301-517 |
4.00e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 96.41 E-value: 4.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 301 VLKNIRFSLRPGESLGLVGESGSGKSTtglaLLR-----LIASQGEILFDGMPLHRWNRRQmlpVRPRMQVVFQDPNSSL 375
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKST----LFRhfngiLKPTSGSVLIRGEPITKENIRE---VRKFVGLVFQNPDDQI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 376 -NPrlSVLQIVEEGlrvhqP---GLSAQQREQEVMRVMVEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPELIILDE 451
Cdd:PRK13652 92 fSP--TVEQDIAFG-----PinlGLDEETVAHRVSSALHMLGLE-ELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1278835479 452 PTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSAP 517
Cdd:PRK13652 164 PTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
278-508 |
4.12e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 95.96 E-value: 4.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 278 VEDLSVSFPirkgilrrivDRNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRL-IASQGEILFDGMPLHRWNRRQ 356
Cdd:PRK13647 7 VEDLHFRYK----------DGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIyLPQRGRVKVMGREVNAENEKW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 357 mlpVRPRMQVVFQDPNSSLNPrLSVLQIVEEGLRvhQPGLSAQQREQEVMRVMVEVGLDpETRHRYPAEFSGGQRQRIAI 436
Cdd:PRK13647 77 ---VRSKVGLVFQDPDDQVFS-STVWDDVAFGPV--NMGLDKDEVERRVEEALKAVRMW-DFRDKPPYHLSYGQKKRVAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1278835479 437 ARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:PRK13647 150 AGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGK-TVIVATHDVDLAAEWADQVIVLKEGRVLAEG 220
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
6-259 |
4.27e-22 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 95.47 E-value: 4.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 6 LRIDNLSIAFSKQdetrTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLLPspPVSypqGDILFHDRSLLHADEQT 85
Cdd:PRK11231 3 LRTENLTVGYGTK----RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLT--PQS---GTVFLGDKPISMLSSRQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 86 LrgirGNKIAMIFQEPM----VSLNPLHSLEKQLYevLSLHrGMRKEAARGEILDCLERTGIRN-AAKRLNDfphqLSGG 160
Cdd:PRK11231 74 L----ARRLALLPQHHLtpegITVRELVAYGRSPW--LSLW-GRLSAEDNARVNQAMEQTRINHlADRRLTD----LSGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 161 ERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDElNMSLLFITHNLSIVRKLADSVAVMQNGRCVEQna 240
Cdd:PRK11231 143 QRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQ-- 219
|
250
....*....|....*....
gi 1278835479 241 astllSAPQHPYTQRLLNS 259
Cdd:PRK11231 220 -----GTPEEVMTPGLLRT 233
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
276-516 |
4.74e-22 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 95.47 E-value: 4.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 276 LRVEDLSVSFpirkgilrrivDRNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIASQ-GEILFDGMPLHRWNR 354
Cdd:PRK11231 3 LRTENLTVGY-----------GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQsGTVFLGDKPISMLSS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 355 RQmlpvrprmqvvfqdpnssLNPRLSVL-QI--VEEGLRVHQ-------PGLS-----AQQREQEVMRVMVEVGLDpETR 419
Cdd:PRK11231 72 RQ------------------LARRLALLpQHhlTPEGITVRElvaygrsPWLSlwgrlSAEDNARVNQAMEQTRIN-HLA 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 420 HRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRlAYIFISHDLQVVRALCHQVIVL 499
Cdd:PRK11231 133 DRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGK-TVVTVLHDLNQASRYCDHLVVL 211
|
250
....*....|....*..
gi 1278835479 500 RQGEVVEQGECQRVFSA 516
Cdd:PRK11231 212 ANGHVMAQGTPEEVMTP 228
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
6-238 |
5.12e-22 |
|
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: 93.15 E-value: 5.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 6 LRIDNLSiaFSKQDETRTVVSDLTLQIQRGETLALVGESGSGKSVSALSILR-LLPSppvsypQGDILFhDRSLLHADEQ 84
Cdd:cd03247 1 LSINNVS--FSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGdLKPQ------QGEITL-DGVPVSDLEK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 85 TLRgirgNKIAMIFQEPMvslnplhslekqlyevlslhrgmrkeaargeildcLERTGIRNAAKRlndfphQLSGGERQR 164
Cdd:cd03247 72 ALS----SLISVLNQRPY-----------------------------------LFDTTLRNNLGR------RFSGGERQR 106
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1278835479 165 VMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRD-LRDElnmSLLFITHNLSIVRKlADSVAVMQNGRCVEQ 238
Cdd:cd03247 107 LALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEvLKDK---TLIWITHHLTGIEH-MDKILFLENGKIIMQ 177
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
6-238 |
5.99e-22 |
|
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: 94.10 E-value: 5.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 6 LRIDNLSIAFSkqDETRTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLLPSppvsyPQGDILFHDRSLLHADEQT 85
Cdd:cd03244 3 IEFKNVSLRYR--PNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVEL-----SSGSILIDGVDISKIGLHD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 86 LRgirgNKIAMIFQEPMV-------SLNPLHslekqlyevlslhrgmrkEAARGEILDCLERTGIRNAAKRLN---DFPH 155
Cdd:cd03244 76 LR----SRISIIPQDPVLfsgtirsNLDPFG------------------EYSDEELWQALERVGLKEFVESLPgglDTVV 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 156 -----QLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDelNMSLLFITHNLSIVRKlADSVAVM 230
Cdd:cd03244 134 eeggeNLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREAFK--DCTVLTIAHRLDTIID-SDRILVL 210
|
....*...
gi 1278835479 231 QNGRCVEQ 238
Cdd:cd03244 211 DKGRVVEF 218
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
278-508 |
6.28e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 96.69 E-value: 6.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 278 VEDLSVSFPIRK------GILRRIVDRN----PVLKNIRFSLRPGESLGLVGESGSGKSTT-----GLallrLIASQGEI 342
Cdd:COG4586 4 VENLSKTYRVYEkepglkGALKGLFRREyrevEAVDDISFTIEPGEIVGFIGPNGAGKSTTikmltGI----LVPTSGEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 343 LFDGM-PlhrWNRRQMLpVRpRMQVVF-QdpNSSLNPRLSVLqiveEGLRVHQP--GLSAQQREQEvMRVMVEV-GLDP- 416
Cdd:COG4586 80 RVLGYvP---FKRRKEF-AR-RIGVVFgQ--RSQLWWDLPAI----DSFRLLKAiyRIPDAEYKKR-LDELVELlDLGEl 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 417 -ETRHRypaEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQ 495
Cdd:COG4586 148 lDTPVR---QLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDR 224
|
250
....*....|...
gi 1278835479 496 VIVLRQGEVVEQG 508
Cdd:COG4586 225 VIVIDHGRIIYDG 237
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
26-512 |
6.97e-22 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 98.71 E-value: 6.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 26 SDLTLQIQRGETLALVGESGSGKSvsalSILRLLPS--PPVSYpQGDILFHDrsllhaDEQTLRGIRGNK---IAMIFQE 100
Cdd:NF040905 18 DDVNLSVREGEIHALCGENGAGKS----TLMKVLSGvyPHGSY-EGEILFDG------EVCRFKDIRDSEalgIVIIHQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 101 pmVSLNPLHSLEKQLYevlslhrgMRKEAARGEILDcLERTGIRNAA--KR--LNDFPHQLSG----GERQRVMIAMALL 172
Cdd:NF040905 87 --LALIPYLSIAENIF--------LGNERAKRGVID-WNETNRRAREllAKvgLDESPDTLVTdigvGKQQLVEIAKALS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 173 TRPELLIADEPTTALDVTVQAQILTLLRDLRDElNMSLLFITHNLSIVRKLADSVAVMQNGRCVEQnaastlLSAPQHPY 252
Cdd:NF040905 156 KDVKLLILDEPTAALNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSITVLRDGRTIET------LDCRADEV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 253 TQ---------R-LLNSEPSGDPVPLDadstPLLRVEDLSVSFPIRKGilRRIVDrnpvlkNIRFSLRPGESLGLVGESG 322
Cdd:NF040905 229 TEdriirgmvgRdLEDRYPERTPKIGE----VVFEVKNWTVYHPLHPE--RKVVD------DVSLNVRRGEIVGIAGLMG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 323 SGKstTGLALL-------RLIAsqGEILFDGMPLHRWNRRQMLPV--------RPRMQVVFQDP---NSSLnPRLSvlqi 384
Cdd:NF040905 297 AGR--TELAMSvfgrsygRNIS--GTVFKDGKEVDVSTVSDAIDAglayvtedRKGYGLNLIDDikrNITL-ANLG---- 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 385 veeglRVHQPGLSAQQREQEV-------MR-----VMVEVGldpetrhrypaEFSGGQRQRIAIARALILKPELIILDEP 452
Cdd:NF040905 368 -----KVSRRGVIDENEEIKVaeeyrkkMNiktpsVFQKVG-----------NLSGGNQQKVVLSKWLFTDPDVLILDEP 431
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 453 TSSLDRTVQAQILALLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRQGEVVeqGECQR 512
Cdd:NF040905 432 TRGIDVGAKYEIYTIINELAAEGK-GVIVISSELPELLGMCDRIYVMNEGRIT--GELPR 488
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-248 |
1.09e-21 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 96.33 E-value: 1.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 1 MTQPLLRIDNLSIAFSKQdetrTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRL---LPSPPvsypQGDIlFHDrs 77
Cdd:PRK11432 2 TQKNFVVLKNITKRFGSN----TVIDNLNLTIKQGTMVTLLGPSGCGKT----TVLRLvagLEKPT----EGQI-FID-- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 78 llhADEQTLRGIRGNKIAMIFQE----PMVSL--NPLHSLEKQlyevlslhrGMRKEAARGEILDCLERTGIRNAAKRLN 151
Cdd:PRK11432 67 ---GEDVTHRSIQQRDICMVFQSyalfPHMSLgeNVGYGLKML---------GVPKEERKQRVKEALELVDLAGFEDRYV 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 152 DfphQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQ 231
Cdd:PRK11432 135 D---QISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMN 211
|
250
....*....|....*..
gi 1278835479 232 NGRCVEQNAASTLLSAP 248
Cdd:PRK11432 212 KGKIMQIGSPQELYRQP 228
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
29-246 |
1.27e-21 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 93.49 E-value: 1.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 29 TLQIQRGETLALVGESGSGKSvsalSILRLLPS--PPVSypqGDILfhdrslLHADEQTLRGIRGNKIAMIFQEPmvSLN 106
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKS----TLLNLIAGflTPAS---GSLT------LNGQDHTTTPPSRRPVSMLFQEN--NLF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 107 PLHSLEKQLyeVLSLHRGMRKEAA-RGEILDCLERTGIRNAAKRLndfPHQLSGGERQRVMIAMALLTRPELLIADEPTT 185
Cdd:PRK10771 84 SHLTVAQNI--GLGLNPGLKLNAAqREKLHAIARQMGIEDLLARL---PGQLSGGQRQRVALARCLVREQPILLLDEPFS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1278835479 186 ALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGRCVEQNAASTLLS 246
Cdd:PRK10771 159 ALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-247 |
1.28e-21 |
|
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: 94.00 E-value: 1.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 3 QPLLRIDNLSIAFskqdETRTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLLPS--PPVSYPQGDILfhDRSLLH 80
Cdd:COG1119 1 DPLLELRNVTVRR----GGKTILDDISWTVKPGEHWAILGPNGAGKS----TLLSLITGdlPPTYGNDVRLF--GERRGG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 81 ADEQTLR---GIRGNKIAMIFQEPMVSLNPLHSlekQLYEVLSLHRGMrKEAARGEILDCLERTGIRNAAKRLndFpHQL 157
Cdd:COG1119 71 EDVWELRkriGLVSPALQLRFPRDETVLDVVLS---GFFDSIGLYREP-TDEQRERARELLELLGLAHLADRP--F-GTL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGRCVE 237
Cdd:COG1119 144 SQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVA 223
|
250
....*....|
gi 1278835479 238 QNAASTLLSA 247
Cdd:COG1119 224 AGPKEEVLTS 233
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-259 |
1.37e-21 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 96.44 E-value: 1.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 1 MTQPLLRIDNLSIAFSKQdetrTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLLP--SPPVsypQGDILFHDRSL 78
Cdd:PRK11607 15 ALTPLLEIRNLTKSFDGQ----HAVDDVSLTIYKGEIFALLGASGCGKS----TLLRMLAgfEQPT---AGQIMLDGVDL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 79 LHADEQTlrgirgNKIAMIFQEpmVSLNPLHSLEKQLYEVLSLHRGMRKEAArGEILDCLERTGIRNAAKRLndfPHQLS 158
Cdd:PRK11607 84 SHVPPYQ------RPINMMFQS--YALFPHMTVEQNIAFGLKQDKLPKAEIA-SRVNEMLGLVHMQEFAKRK---PHQLS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 159 GGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGRCVEQ 238
Cdd:PRK11607 152 GGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQI 231
|
250 260
....*....|....*....|.
gi 1278835479 239 NAASTLLSAPQHPYTQRLLNS 259
Cdd:PRK11607 232 GEPEEIYEHPTTRYSAEFIGS 252
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
276-484 |
1.63e-21 |
|
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: 91.45 E-value: 1.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 276 LRVEDLSVSFPirkgilrrivDRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIlfdGMPLH 350
Cdd:cd03223 1 IELENLSLATP----------DGRVLLKDLSFEIKPGDRLLITGPSGTGKSS----LFRALAglwpwGSGRI---GMPEG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 351 rwNRRQMLPVRPRMqvvfqdPNSSLnprlsvlqiveeglrvhqpglsaqqREQEVmrvmvevgldpetrhrYP--AEFSG 428
Cdd:cd03223 64 --EDLLFLPQRPYL------PLGTL-------------------------REQLI----------------YPwdDVLSG 94
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1278835479 429 GQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKglqeKHRLAYIFISH 484
Cdd:cd03223 95 GEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLK----ELGITVISVGH 146
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
24-248 |
1.64e-21 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 98.26 E-value: 1.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 24 VVSDLTLQIQRGETLALVGESGSGKSVSALSILRLLPspPVSypqGDILFHDRSLLHADEQTLRgirgNKIAMIFQEPmv 103
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQ--PTG---GQVLLDGVPLVQYDHHYLH----RQVALVGQEP-- 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 104 slnplhslekQLYEvlslhRGMRKEAARGeiLDCLERTGIRNAAKRLN------DFPH-----------QLSGGERQRVM 166
Cdd:TIGR00958 565 ----------VLFS-----GSVRENIAYG--LTDTPDEEIMAAAKAANahdfimEFPNgydtevgekgsQLSGGQKQRIA 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 167 IAMALLTRPELLIADEPTTALDVTVQAqiltLLRDLRDELNMSLLFITHNLSIVRKlADSVAVMQNGRCVEQNAASTLLS 246
Cdd:TIGR00958 628 IARALVRKPRVLILDEATSALDAECEQ----LLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLME 702
|
..
gi 1278835479 247 AP 248
Cdd:TIGR00958 703 DQ 704
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
254-516 |
1.71e-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: 97.80 E-value: 1.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 254 QRLLNSEPSGDPVPLDADSTPLLRVEDLSVSFPIRKgilrrivdrNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLL 333
Cdd:TIGR01842 295 NELLANYPSRDPAMPLPEPEGHLSVENVTIVPPGGK---------KPTLRGISFSLQAGEALAIIGPSGSGKST----LA 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 334 RLIA-----SQGEILFDGMPLHRWNRRQmlpvrprmqvvfqdpnssLNPRLSVL-QIVEeglrvHQPGLSAQQ------- 400
Cdd:TIGR01842 362 RLIVgiwppTSGSVRLDGADLKQWDRET------------------FGKHIGYLpQDVE-----LFPGTVAENiarfgen 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 401 -REQEVMRVMVEVGLDpETRHRYP-----------AEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALL 468
Cdd:TIGR01842 419 aDPEKIIEAAKLAGVH-ELILRLPdgydtvigpggATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAI 497
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1278835479 469 KGLQEKHRLAyIFISHDLQVVrALCHQVIVLRQGEVVEQGECQRVFSA 516
Cdd:TIGR01842 498 KALKARGITV-VVITHRPSLL-GCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
6-234 |
1.82e-21 |
|
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: 92.95 E-value: 1.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 6 LRIDNLSIAFSKQdeTRTVVSDLTLQIQRGETLALVGESGSGKSvSALSIL--RLLPSppvsypQGDILFHDRSLlhade 83
Cdd:cd03263 1 LQIRNLTKTYKKG--TKPAVDDLSLNVYKGEIFGLLGHNGAGKT-TTLKMLtgELRPT------SGTAYINGYSI----- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 84 QTLRGIRGNKIAMIFQEPMV--SLNPLHSLEkqLYevlSLHRGMRKEAARGEILDCLERTGIRNAAKRLndfPHQLSGGE 161
Cdd:cd03263 67 RTDRKAARQSLGYCPQFDALfdELTVREHLR--FY---ARLKGLPKSEIKEEVELLLRVLGLTDKANKR---ARTLSGGM 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1278835479 162 RQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDelNMSLLFITHNLSIVRKLADSVAVMQNGR 234
Cdd:cd03263 139 KRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGK 209
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
300-509 |
1.87e-21 |
|
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: 98.27 E-value: 1.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 300 PVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEILFDGMPLHRWNR---RQMLPVRPRMQVVFQDpnssl 375
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFqARSGEILLNGFSLKDIDRhtlRQFINYLPQEPYIFSG----- 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 376 nprlsvlQIVEEGLRVHQPGLSaqqrEQEVMRV--MVEVGLD----PETRHRYPAE----FSGGQRQRIAIARALILKPE 445
Cdd:TIGR01193 563 -------SILENLLLGAKENVS----QDEIWAAceIAEIKDDienmPLGYQTELSEegssISGGQKQRIALARALLTDSK 631
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1278835479 446 LIILDEPTSSLDRTVQAQILALLKGLQEKhrlAYIFISHDLQVVRaLCHQVIVLRQGEVVEQGE 509
Cdd:TIGR01193 632 VLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAK-QSDKIIVLDHGKIIEQGS 691
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
300-526 |
2.80e-21 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 93.68 E-value: 2.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 300 PVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIASQ-----GEILFDGMPLHRWNRRQMLPVRPRMQVVFQdpNSS 374
Cdd:PRK11831 21 CIFDNISLTVPRGKITAIMGPSGIGKTT----LLRLIGGQiapdhGEILFDGENIPAMSRSRLYTVRKRMSMLFQ--SGA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 375 LNPRLSVLQIVEEGLRVHQpGLSAQQREQEVMRVMVEVGLDPETrHRYPAEFSGGQRQRIAIARALILKPELIILDEPTS 454
Cdd:PRK11831 95 LFTDMNVFDNVAYPLREHT-QLPAPLLHSTVMMKLEAVGLRGAA-KLMPSELSGGMARRAALARAIALEPDLIMFDEPFV 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1278835479 455 SLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSAPTQRyTRQLL 526
Cdd:PRK11831 173 GQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDPR-VRQFL 243
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
302-514 |
2.90e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 94.03 E-value: 2.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 302 LKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIA-SQGEI-LFDGMPLHRWNRRQMLPVRPRMQVVFQDPNSSLNPRl 379
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQpTEGKVtVGDIVVSSTSKQKEIKPVRKKVGVVFQFPESQLFEE- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 380 SVLQIVEEGLRvhQPGLSAQQREQEVMRVMVEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRT 459
Cdd:PRK13643 101 TVLKDVAFGPQ--NFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1278835479 460 VQAQILALLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVF 514
Cdd:PRK13643 179 ARIEMMQLFESIHQSGQ-TVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
4-249 |
2.98e-21 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 92.74 E-value: 2.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 4 PLLRIDNLSIAFSKqdetRTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLLPspPVSypqGDILFHDRSL--LHA 81
Cdd:COG0410 2 PMLEVENLHAGYGG----IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLP--PRS---GSIRFDGEDItgLPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 82 DEQTLRGI------RGnkiamIFQEpmvslnplhslekqlyevLS----LHRGMRKEAARGEILDCLERTgirnaakrLN 151
Cdd:COG0410 73 HRIARLGIgyvpegRR-----IFPS------------------LTveenLLLGAYARRDRAEVRADLERV--------YE 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 152 DFP------HQ----LSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDElNMSLLFITHNLSIVR 221
Cdd:COG0410 122 LFPrlkerrRQragtLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFAL 200
|
250 260
....*....|....*....|....*...
gi 1278835479 222 KLADSVAVMQNGRCVEQNAASTLLSAPQ 249
Cdd:COG0410 201 EIADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
302-505 |
3.02e-21 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 92.25 E-value: 3.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 302 LKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLHRWNRRQMLPVRPRMQVVFQDPNSSLN 376
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKST----LLKLICgierpSAGKIWFSGHDITRLKNREVPFLRRQIGMIFQDHHLLMD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 377 PrlSVLQIVEEGLRVhqPGLSAQQREQEVMRVMVEVGLDPETRHrYPAEFSGGQRQRIAIARALILKPELIILDEPTSSL 456
Cdd:PRK10908 94 R--TVYDNVAIPLII--AGASGDDIRRRVSAALDKVGLLDKAKN-FPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1278835479 457 DRTVQAQILALlkgLQEKHRLA--YIFISHDLQVVRALCHQVIVLRQGEVV 505
Cdd:PRK10908 169 DDALSEGILRL---FEEFNRVGvtVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
277-518 |
3.10e-21 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 93.31 E-value: 3.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 277 RVEDLSVSFPIRKgilrrivdrnpVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEILFDGMPLHR 351
Cdd:PRK10575 13 ALRNVSFRVPGRT-----------LLHPLSLTFPAGKVTGLIGHNGSGKST----LLKMLgrhqpPSEGEILLDAQPLES 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 352 WNRR----------QMLPVRPRMqvvfqdpnsslnprlSVLQIVEEGlRVHQPG----LSAQQREQeVMRVMVEVGLDPe 417
Cdd:PRK10575 78 WSSKafarkvaylpQQLPAAEGM---------------TVRELVAIG-RYPWHGalgrFGAADREK-VEEAISLVGLKP- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 418 TRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVI 497
Cdd:PRK10575 140 LAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLV 219
|
250 260
....*....|....*....|.
gi 1278835479 498 VLRQGEVVEQGECQRVFSAPT 518
Cdd:PRK10575 220 ALRGGEMIAQGTPAELMRGET 240
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-246 |
3.20e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 93.28 E-value: 3.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 1 MTQPLLRIDNLSiaFSKQDETRTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLLpsppvSYPQGDILFHDRSLlh 80
Cdd:PRK13648 3 DKNSIIVFKNVS--FQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIE-----KVKSGEIFYNNQAI-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 81 aDEQTLRGIRgNKIAMIFQEP-------MVSLNPLHSLEKQLYEVLSLHRGMRKEAARGEILDclertgirnaakRLNDF 153
Cdd:PRK13648 74 -TDDNFEKLR-KHIGIVFQNPdnqfvgsIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLE------------RADYE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 154 PHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKlADSVAVMQNG 233
Cdd:PRK13648 140 PNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKG 218
|
250
....*....|...
gi 1278835479 234 RCVEQNAASTLLS 246
Cdd:PRK13648 219 TVYKEGTPTEIFD 231
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
5-234 |
3.38e-21 |
|
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: 92.15 E-value: 3.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 5 LLRIDNLSIAFSKQDETRtVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLLPsppvsyPQ-GDILFHDRSLLHADE 83
Cdd:cd03248 11 IVKFQNVTFAYPTRPDTL-VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQ------PQgGQVLLDGKPISQYEH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 84 QTLRgirgNKIAMIFQEPMVSLNPLHslEKQLYEVLSLHRGMRKEAARGEildclertgirNAAKRLNDFPH-------- 155
Cdd:cd03248 84 KYLH----SKVSLVGQEPVLFARSLQ--DNIAYGLQSCSFECVKEAAQKA-----------HAHSFISELASgydtevge 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 156 ---QLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDlrDELNMSLLFITHNLSIVRKlADSVAVMQN 232
Cdd:cd03248 147 kgsQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYD--WPERRTVLVIAHRLSTVER-ADQILVLDG 223
|
..
gi 1278835479 233 GR 234
Cdd:cd03248 224 GR 225
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-504 |
4.52e-21 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 96.23 E-value: 4.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 2 TQPLLRIDNLSIAFS--KqdetrtVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLLPSppvSYP--QGDILFHDRs 77
Cdd:PRK10762 1 MQALLQLKGIDKAFPgvK------ALSGAALNVYPGRVMALVGENGAGKS----TMMKVLTG---IYTrdAGSILYLGK- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 78 llhadEQTLRGIRGNK---IAMIFQEpmVSLNPLHSLEKQLY---EVLS-----LHRGMRKEAARgeildCLERTGIRNA 146
Cdd:PRK10762 67 -----EVTFNGPKSSQeagIGIIHQE--LNLIPQLTIAENIFlgrEFVNrfgriDWKKMYAEADK-----LLARLNLRFS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 147 AKRLNDfphQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDElNMSLLFITHNLSIVRKLADS 226
Cdd:PRK10762 135 SDKLVG---ELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQ-GRGIVYISHRLKEIFEICDD 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 227 VAVMQNGRCVEQNAASTLLS------------APQHPytqRLlnSEPSGDPVpldadstplLRVEDLSvsfpirkgilrr 294
Cdd:PRK10762 211 VTVFRDGQFIAEREVADLTEdsliemmvgrklEDQYP---RL--DKAPGEVR---------LKVDNLS------------ 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 295 ivdrNPVLKNIRFSLRPGESLGLVGESGSGKSttglALLRLI-----ASQGEILFDGMPLHRWNRRQMLPV--------R 361
Cdd:PRK10762 265 ----GPGVNDVSFTLRKGEILGVSGLMGAGRT----ELMKVLygalpRTSGYVTLDGHEVVTRSPQDGLANgivyisedR 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 362 PR------MQVvfqDPNSSLNprlSVLQIVEEGLRVHqpglsaQQREQEVMRVMVEV-GLDPETRHRYPAEFSGGQRQRI 434
Cdd:PRK10762 337 KRdglvlgMSV---KENMSLT---ALRYFSRAGGSLK------HADEQQAVSDFIRLfNIKTPSMEQAIGLLSGGNQQKV 404
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 435 AIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHrLAYIFISHDLQVVRALCHQVIVLRQGEV 504
Cdd:PRK10762 405 AIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEG-LSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
276-508 |
4.59e-21 |
|
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: 91.84 E-value: 4.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 276 LRVEDLSVSFPIRKgilrrivdrnpVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEILFDG-----MPL 349
Cdd:cd03218 1 LRAENLSKRYGKRK-----------VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVkPDSGKILLDGqditkLPM 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 350 HRwnrrqmlpvRPRMQVVFQDPNSSLNPRLSVLQIVEEGLRVHqpGLSAQQREQEVMRVMVEVGLDPeTRHRYPAEFSGG 429
Cdd:cd03218 70 HK---------RARLGIGYLPQEASIFRKLTVEENILAVLEIR--GLSKKEREEKLEELLEEFHITH-LRKSKASSLSGG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 430 QRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLqeKHRLAYIFIS-HDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:cd03218 138 ERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKIL--KDRGIGVLITdHNVRETLSITDRAYIIYEGKVLAEG 215
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
4-248 |
4.62e-21 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 95.29 E-value: 4.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 4 PLLRIDNLSIAFSKQdetrTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLLPSPpVSYPQGDILFHDRSLLHADE 83
Cdd:PRK09536 2 PMIDVSDLSVEFGDT----TVLDGVDLSVREGSLVGLVGPNGAGKT----TLLRAINGT-LTPTAGTVLVAGDDVEALSA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 84 QTLrgirGNKIAMIFQEPMVSLNplHSLEKQLYEVLSLHRG---MRKEAARGEILDCLERTGIRNAAKRLNDfphQLSGG 160
Cdd:PRK09536 73 RAA----SRRVASVPQDTSLSFE--FDVRQVVEMGRTPHRSrfdTWTETDRAAVERAMERTGVAQFADRPVT---SLSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 161 ERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFItHNLSIVRKLADSVAVMQNGRCVEQNA 240
Cdd:PRK09536 144 ERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAI-HDLDLAARYCDELVLLADGRVRAAGP 222
|
....*...
gi 1278835479 241 ASTLLSAP 248
Cdd:PRK09536 223 PADVLTAD 230
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
276-505 |
5.67e-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: 5.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 276 LRVEDLSVSFPIRKgilrriVDRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLH 350
Cdd:COG1101 2 LELKNLSKTFNPGT------VNEKRALDGLNLTIEEGDFVTVIGSNGAGKST----LLNAIAgslppDSGSILIDGKDVT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 351 RWN--RRQMLPVRprmqvVFQDPNSSLNPRLSVlqivEE------------GLRvhqPGLSAQQREQevMRVMVE-VGLD 415
Cdd:COG1101 72 KLPeyKRAKYIGR-----VFQDPMMGTAPSMTI----EEnlalayrrgkrrGLR---RGLTKKRREL--FRELLAtLGLG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 416 PETRHRYPAEF-SGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCH 494
Cdd:COG1101 138 LENRLDTKVGLlSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGN 217
|
250
....*....|.
gi 1278835479 495 QVIVLRQGEVV 505
Cdd:COG1101 218 RLIMMHEGRII 228
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
7-247 |
7.77e-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: 95.94 E-value: 7.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 7 RIDNLSIAFSKQDETRTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLLPSPpVSYPQGDILFHDRSLLHADEQTL 86
Cdd:TIGR02203 330 DVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKS----TLVNLIPRF-YEPDSGQILLDGHDLADYTLASL 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 87 RgirgNKIAMIFQEPMVSLNPLHSlekqlyevlSLHRGMRKEAARGEILDCLERTGIRNAAKRLNDFPHQ--------LS 158
Cdd:TIGR02203 405 R----RQVALVSQDVVLFNDTIAN---------NIAYGRTEQADRAEIERALAAAYAQDFVDKLPLGLDTpigengvlLS 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 159 GGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDelNMSLLFITHNLSIVRKlADSVAVMQNGRCVEQ 238
Cdd:TIGR02203 472 GGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIEK-ADRIVVMDDGRIVER 548
|
....*....
gi 1278835479 239 NAASTLLSA 247
Cdd:TIGR02203 549 GTHNELLAR 557
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
274-524 |
7.84e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 92.02 E-value: 7.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 274 PLLRVEDLSVSFpirkgilrrivDRNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIASQGEILFDG----MPL 349
Cdd:PRK14258 6 PAIKVNNLSFYY-----------DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGrvefFNQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 350 HRWNRRQMLPvRPRMQVVFQDPNSSLNPrLSVLQIVEEGLRV--HQPGLsaqQREQEVMRVMVEVGLDPETR---HRYPA 424
Cdd:PRK14258 75 NIYERRVNLN-RLRRQVSMVHPKPNLFP-MSVYDNVAYGVKIvgWRPKL---EIDDIVESALKDADLWDEIKhkiHKSAL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 425 EFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVL----- 499
Cdd:PRK14258 150 DLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFkgnen 229
|
250 260
....*....|....*....|....*
gi 1278835479 500 RQGEVVEQGECQRVFSAPTQRYTRQ 524
Cdd:PRK14258 230 RIGQLVEFGLTKKIFNSPHDSRTRE 254
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
300-514 |
8.08e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 92.50 E-value: 8.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 300 PVLKNIRFSLRPGESLGLVGESGSGKSTTgLALLR--LIASQGEILFDGMPLHRWNR-RQMLPVRPRMQVVFQDPNSSLN 376
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTI-MQLLNglHVPTQGSVRVDDTLITSTSKnKDIKQIRKKVGLVFQFPESQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 377 PRlSVLQIVEEGLRvhQPGLSAQQREQEVMRVMVEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSL 456
Cdd:PRK13649 100 EE-TVLKDVAFGPQ--NFGVSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1278835479 457 DRTVQAQILALLKGLQEKHrLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVF 514
Cdd:PRK13649 177 DPKGRKELMTLFKKLHQSG-MTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
13-247 |
8.19e-21 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 91.39 E-value: 8.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 13 IAFSKQDETRTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLLPSPpvsypQGDILFHDRSLLHADEQTLRgirgN 92
Cdd:cd03252 6 VRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPE-----NGRVLVDGHDLALADPAWLR----R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 93 KIAMIFQEPMVslnplhslekqlyevlsLHRGMRKEAARGEILDCLERtgIRNAAKRL--NDFPHQ-------------- 156
Cdd:cd03252 77 QVGVVLQENVL-----------------FNRSIRDNIALADPGMSMER--VIEAAKLAgaHDFISElpegydtivgeqga 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 157 -LSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDelNMSLLFITHNLSIVRKlADSVAVMQNGRC 235
Cdd:cd03252 138 gLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRI 214
|
250
....*....|..
gi 1278835479 236 VEQNAASTLLSA 247
Cdd:cd03252 215 VEQGSHDELLAE 226
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
276-508 |
8.58e-21 |
|
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: 91.05 E-value: 8.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 276 LRVEDLSVSFpirkgilrrivDRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEILFDG---- 346
Cdd:TIGR03410 1 LEVSNLNVYY-----------GQSHILRGVSLEVPKGEVTCVLGRNGVGKTT----LLKTLmgllpVKSGSIRLDGedit 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 347 -MPLHRWNRRQMLPVrPRMQVVFqdpnsslnPRLSVlqivEEGLRVhqpGLSAQ-QREQEVMRVMVEvgLDP---ETRHR 421
Cdd:TIGR03410 66 kLPPHERARAGIAYV-PQGREIF--------PRLTV----EENLLT---GLAALpRRSRKIPDEIYE--LFPvlkEMLGR 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 422 YPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQ 501
Cdd:TIGR03410 128 RGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMER 207
|
....*..
gi 1278835479 502 GEVVEQG 508
Cdd:TIGR03410 208 GRVVASG 214
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
30-234 |
8.77e-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: 90.69 E-value: 8.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 30 LQIQRGETLALVGESGSGKSvSALSILRLLPSPPvsypQGDILFHDRSLLHADEQTlrgirgNKIAMIFQEPmvslNPLH 109
Cdd:TIGR01277 19 LNVADGEIVAIMGPSGAGKS-TLLNLIAGFIEPA----SGSIKVNDQSHTGLAPYQ------RPVSMLFQEN----NLFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 110 SLEKQLYEVLSLHRGMRKEAARGE-ILDCLERTGIRNAAKRLndfPHQLSGGERQRVMIAMALLTRPELLIADEPTTALD 188
Cdd:TIGR01277 84 HLTVRQNIGLGLHPGLKLNAEQQEkVVDAAQQVGIADYLDRL---PEQLSGGQRQRVALARCLVRPNPILLLDEPFSALD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1278835479 189 VTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGR 234
Cdd:TIGR01277 161 PLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGK 206
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
307-508 |
8.79e-21 |
|
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: 91.07 E-value: 8.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 307 FSLRPGESLGLVGESGSGKSTTGLALLRLIA-SQGEILFDGMPlHRWNRRQMLPVRPRMQVVFQDPnsslnprLSVLQIV 385
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPpAKGTVKVAGAS-PGKGWRHIGYVPQRHEFAWDFP-------ISVAHTV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 386 EEGlRVHQPGLSAQQREQE---VMRVMVEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQA 462
Cdd:TIGR03771 73 MSG-RTGHIGWLRRPCVADfaaVRDALRRVGLT-ELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQE 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1278835479 463 QILALLKGL-QEKHrlAYIFISHDLQVVRALCHQViVLRQGEVVEQG 508
Cdd:TIGR03771 151 LLTELFIELaGAGT--AILMTTHDLAQAMATCDRV-VLLNGRVIADG 194
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-237 |
9.04e-21 |
|
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: 95.64 E-value: 9.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 3 QPLLRIDNLSIAFSKQDetRTV---VSDLTLQIQRGETLALVGESGSGKSVSALSILRLLP--SPPVSYPQGDiLFHDRS 77
Cdd:TIGR03269 277 EPIIKVRNVSKRYISVD--RGVvkaVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEptSGEVNVRVGD-EWVDMT 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 78 LLHADEqtlRGIRGNKIAMIFQEpmVSLNPLHSLEKQLYEVLSLHrgMRKEAARGEILDCLERTGI--RNAAKRLNDFPH 155
Cdd:TIGR03269 354 KPGPDG---RGRAKRYIGILHQE--YDLYPHRTVLDNLTEAIGLE--LPDELARMKAVITLKMVGFdeEKAEEILDKYPD 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGRC 235
Cdd:TIGR03269 427 ELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
..
gi 1278835479 236 VE 237
Cdd:TIGR03269 507 VK 508
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
40-259 |
9.40e-21 |
|
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: 93.33 E-value: 9.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 40 LVGESGSGKSvsalSILRLL-----PSppvsypQGDILFHDRSLLHADEQtLRGIrgnkiAMIFQEpmVSLNPLHSLEKQ 114
Cdd:TIGR01187 1 LLGPSGCGKT----TLLRLLagfeqPD------SGSIMLDGEDVTNVPPH-LRHI-----NMVFQS--YALFPHMTVEEN 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 115 LYEVLSLhRGMRKEAARGEILDCLERTGIRNAAKRlndFPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQ 194
Cdd:TIGR01187 63 VAFGLKM-RKVPRAEIKPRVLEALRLVQLEEFADR---KPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQ 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1278835479 195 ILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGRCVEQNAASTLLSAPQHPYTQRLLNS 259
Cdd:TIGR01187 139 MQLELKTIQEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGE 203
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-215 |
1.22e-20 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 91.46 E-value: 1.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 4 PLLRIDNLSIAFSKQDETRTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLL-----PSppvsypQGDILFhdrsl 78
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKT----TLLNLIagflaPS------SGEITL----- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 79 lhaDEQTLRGiRGNKIAMIFQEP--MVSLNPLHSLEkqlyevLSLH-RGMRKEAARGEILDCLERTGIRNAAKRlndFPH 155
Cdd:COG4525 67 ---DGVPVTG-PGADRGVVFQKDalLPWLNVLDNVA------FGLRlRGVPKAERRARAEELLALVGLADFARR---RIW 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITH 215
Cdd:COG4525 134 QLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITH 193
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
303-521 |
1.31e-20 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 93.56 E-value: 1.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 303 KNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGmplhrwnrRQMLPVRPRMQ---VVFQdpNSS 374
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKST----LLRMIAglediTSGDLFIGE--------KRMNDVPPAERgvgMVFQ--SYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 375 LNPRLSVLQIVEEGLRVHQPGLS-AQQREQEVMRVM-VEVGLDpetrhRYPAEFSGGQRQRIAIARALILKPELIILDEP 452
Cdd:PRK11000 86 LYPHLSVAENMSFGLKLAGAKKEeINQRVNQVAEVLqLAHLLD-----RKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1278835479 453 TSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSAPTQRY 521
Cdd:PRK11000 161 LSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRF 229
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
4-227 |
1.32e-20 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 91.33 E-value: 1.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 4 PLLRIDNLSIAFSKqdetRTVVSDLTLQIQRGETLALVGESGSGKSVSALSILrllpsppvsypqgdilfhdrSLLHADE 83
Cdd:PRK09544 3 SLVSLENVSVSFGQ----RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVL--------------------GLVAPDE 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 84 QTLRGIRGNKIAMIFQEpmVSLNPlhSLEKQLYEVLSLHRGMRKeaarGEILDCLERTgirnAAKRLNDFPHQ-LSGGER 162
Cdd:PRK09544 59 GVIKRNGKLRIGYVPQK--LYLDT--TLPLTVNRFLRLRPGTKK----EDILPALKRV----QAGHLIDAPMQkLSGGET 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1278835479 163 QRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSV 227
Cdd:PRK09544 127 QRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEV 191
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
6-237 |
1.52e-20 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 89.85 E-value: 1.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 6 LRIDNLSIAFskqdETRTVVSDLTLQIQRGETLALVGESGSGKSvSALSILRLLPSPPVSYpQGDILFHDRSLLHAdeQT 85
Cdd:COG4136 2 LSLENLTITL----GGRPLLAPLSLTVAPGEILTLMGPSGSGKS-TLLAAIAGTLSPAFSA-SGEVLLNGRRLTAL--PA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 86 LRgirgNKIAMIFQEPMvsLNPLHSLEKQLyeVLSLHRGMRKEAARGEILDCLERTGIRNAAKRlndFPHQLSGGERQRV 165
Cdd:COG4136 74 EQ----RRIGILFQDDL--LFPHLSVGENL--AFALPPTIGRAQRRARVEQALEEAGLAGFADR---DPATLSGGQRARV 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1278835479 166 MIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHnlsivrklaDSVAVMQNGRCVE 237
Cdd:COG4136 143 ALLRALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTH---------DEEDAPAAGRVLD 205
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
280-508 |
1.55e-20 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 95.11 E-value: 1.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 280 DLSVSFPirKGILRRIVDRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIAS--------QGEILFDGMPLhr 351
Cdd:TIGR00955 21 KQLVSRL--RGCFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTT----LMNALAFrspkgvkgSGSVLLNGMPI-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 352 wNRRQMlpvRPRMQVVFQDpnsSLN-PRLSVLQ--IVEEGLRVHQpGLSAQQREQEVMRVMVEVGLDP--ETRHRYPAE- 425
Cdd:TIGR00955 93 -DAKEM---RAISAYVQQD---DLFiPTLTVREhlMFQAHLRMPR-RVTKKEKRERVDEVLQALGLRKcaNTRIGVPGRv 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 426 --FSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGE 503
Cdd:TIGR00955 165 kgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGR 244
|
....*
gi 1278835479 504 VVEQG 508
Cdd:TIGR00955 245 VAYLG 249
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-236 |
1.56e-20 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 95.18 E-value: 1.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 1 MTqPLLRIDNLSIAFSKQDETRTVVSDLTLQIQRGETLALVGESGSGKSvSALSILRLL--PSPPVSYPQGdilfHDRSL 78
Cdd:PRK10535 1 MT-ALLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKS-TLMNILGCLdkPTSGTYRVAG----QDVAT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 79 LHADEqtLRGIRGNKIAMIFQEpmVSLNPlHSLEKQLYEVLSLHRGMRKEAARGEILDCLERTGIrnaAKRLNDFPHQLS 158
Cdd:PRK10535 75 LDADA--LAQLRREHFGFIFQR--YHLLS-HLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGL---EDRVEYQPSQLS 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1278835479 159 GGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDElNMSLLFITHNLSIVRKlADSVAVMQNGRCV 236
Cdd:PRK10535 147 GGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVAAQ-AERVIEIRDGEIV 222
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
2-512 |
1.71e-20 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 94.59 E-value: 1.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 2 TQPLLRIDNLSIAFSKQdetrTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLL-----PSppvsypQGDIlfhdr 76
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGV----KALDDISFDCRAGQVHALMGENGAGKS----TLLKILsgnyqPD------AGSI----- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 77 sLLHADEQTLRGIR---GNKIAMIFQEpmvslnpLHSL-EKQLYEVLSL----HRG--MRKEAARGEILDCLERTGIR-N 145
Cdd:PRK11288 62 -LIDGQEMRFASTTaalAAGVAIIYQE-------LHLVpEMTVAENLYLgqlpHKGgiVNRRLLNYEAREQLEHLGVDiD 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 146 AAKRLNDfphqLSGGERQRVMIAMALLtRPELLIA-DEPTTALDVTVQAQILTLLRDLRDElNMSLLFITHNLSIVRKLA 224
Cdd:PRK11288 134 PDTPLKY----LSIGQRQMVEIAKALA-RNARVIAfDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALC 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 225 DSVAVMQNGRCVEQNAASTLLSAPQ-------------HPYTQRllnsePSGDpvpldadstPLLRVEDLSvsfpirkgi 291
Cdd:PRK11288 208 DAITVFKDGRYVATFDDMAQVDRDQlvqamvgreigdiYGYRPR-----PLGE---------VRLRLDGLK--------- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 292 lrrivdrNPVLKN-IRFSLRPGESLGLVGESGSGKSttglALLRLI-----ASQGEILFDGMPLHRWNRRQmlPVRPRMQ 365
Cdd:PRK11288 265 -------GPGLREpISFSVRAGEIVGLFGLVGAGRS----ELMKLLygatrRTAGQVYLDGKPIDIRSPRD--AIRAGIM 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 366 VVFQD-------PNSSlnprlsvlqiVEEGL-----RVHQPG--LSAQQREQEVMRVMVEvGLDPETRHRYPA--EFSGG 429
Cdd:PRK11288 332 LCPEDrkaegiiPVHS----------VADNInisarRHHLRAgcLINNRWEAENADRFIR-SLNIKTPSREQLimNLSGG 400
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 430 QRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRQGEVVeqGE 509
Cdd:PRK11288 401 NQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGV-AVLFVSSDLPEVLGVADRIVVMREGRIA--GE 477
|
...
gi 1278835479 510 CQR 512
Cdd:PRK11288 478 LAR 480
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
11-234 |
1.87e-20 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 92.63 E-value: 1.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 11 LSIAFSKQdetrtvVSDLTLQIQ-----RGETlALVGESGSGKSvSALSILRLLPSPPvsypQGDILFHDRSLLHADEQT 85
Cdd:PRK11144 2 LELNFKQQ------LGDLCLTVNltlpaQGIT-AIFGRSGAGKT-SLINAISGLTRPQ----KGRIVLNGRVLFDAEKGI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 86 LRGIRGNKIAMIFQEpmVSLNPLHSLEKqlyevlSLHRGMRKEAaRGEILDCLERTGIRNAAKRlndFPHQLSGGERQRV 165
Cdd:PRK11144 70 CLPPEKRRIGYVFQD--ARLFPHYKVRG------NLRYGMAKSM-VAQFDKIVALLGIEPLLDR---YPGSLSGGEKQRV 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1278835479 166 MIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGR 234
Cdd:PRK11144 138 AIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGK 206
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
276-503 |
1.92e-20 |
|
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: 87.50 E-value: 1.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 276 LRVEDLSVSFpirkgilrrivDRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIASQGEIlfdgmplhrwnrr 355
Cdd:cd03221 1 IELENLSKTY-----------GGKLLLKDISLTINPGDRIGLVGRNGAGKST----LLKLIAGELEP------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 356 qmlpvrprmqvvfqdpnsslnprlsvlqivEEGlrvhqpglsaqqreqevmrvmvEVGLDPETRHRYPAEFSGGQRQRIA 435
Cdd:cd03221 53 ------------------------------DEG----------------------IVTWGSTVKIGYFEQLSGGEKMRLA 80
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1278835479 436 IARALILKPELIILDEPTSSLDrtVQAqILALLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRQGE 503
Cdd:cd03221 81 LAKLLLENPNLLLLDEPTNHLD--LES-IEALEEALKEYPG-TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
23-234 |
2.00e-20 |
|
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: 89.77 E-value: 2.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 23 TVVSDLTLQIQRGETLALVGESGSGKSVSALSILRL-LPSppvsypQGDILFHDRSLLHADEQTLRGIRgNKIAMIFQEP 101
Cdd:cd03292 15 AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEeLPT------SGTIRVNGQDVSDLRGRAIPYLR-RKIGVVFQDF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 102 --MVSLNPLHSLEKQLYEVLSLHRGMRKEAArgeilDCLERTGIRNaakRLNDFPHQLSGGERQRVMIAMALLTRPELLI 179
Cdd:cd03292 88 rlLPDRNVYENVAFALEVTGVPPREIRKRVP-----AALELVGLSH---KHRALPAELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1278835479 180 ADEPTTALDVTVQAQILTLLRDLRDElNMSLLFITHNLSIVRKLADSVAVMQNGR 234
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGK 213
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
7-233 |
2.13e-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: 89.24 E-value: 2.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 7 RIDNLSIAFSKQdetRTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLLPSPpvsypQGDILFHDRSLLHADeqtl 86
Cdd:cd03226 1 RIENISFSYKKG---TEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKES-----SGSILLNGKPIKAKE---- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 87 rgiRGNKIAMIFQEPmvslnplhslEKQLYE--VLS-LHRGMRKEAARGEILDCLERTGIRNAAKRLNdfPHQLSGGERQ 163
Cdd:cd03226 69 ---RRKSIGYVMQDV----------DYQLFTdsVREeLLLGLKELDAGNEQAETVLKDLDLYALKERH--PLSLSGGQKQ 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 164 RVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLfITHNLSIVRKLADSVAVMQNG 233
Cdd:cd03226 134 RLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIV-ITHDYEFLAKVCDRVLLLANG 202
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
13-249 |
2.47e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 90.91 E-value: 2.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 13 IAFSKQDETRtVVSDLTLQIQRGETLALVGESGSGKSVSAL---SILRllPSppvsypQGDILFHDRSLLHaDEQTLRGI 89
Cdd:PRK13639 7 LKYSYPDGTE-ALKGINFKAEKGEMVALLGPNGAGKSTLFLhfnGILK--PT------SGEVLIKGEPIKY-DKKSLLEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 90 RgNKIAMIFQEPMVSLNPLHSLEKQLYEVLSLhrGMRKEAARGEILDCLERTGIRNAAKRLndfPHQLSGGERQRVMIAM 169
Cdd:PRK13639 77 R-KTVGIVFQNPDDQLFAPTVEEDVAFGPLNL--GLSKEEVEKRVKEALKAVGMEGFENKP---PHHLSGGQKKRVAIAG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 170 ALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDElNMSLLFITHNLSIVRKLADSVAVMQNGRCVEQNAASTLLSAPQ 249
Cdd:PRK13639 151 ILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIE 229
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
6-215 |
3.85e-20 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 93.72 E-value: 3.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 6 LRIDNLSIAFSkqdETRTVVSDLTLQIQRGETLALVGESGSGKSvsalSILR----LLPsppvsYPQGDILFHDrsllha 81
Cdd:COG4178 363 LALEDLTLRTP---DGRPLLEDLSLSLKPGERLLITGPSGSGKS----TLLRaiagLWP-----YGSGRIARPA------ 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 82 deqtlrgirGNKIAMIFQEPMVslnPLHSLEKQLyevlsLHRGMRKEAARGEILDCLERTGIRNAAKRLN---DFPHQLS 158
Cdd:COG4178 425 ---------GARVLFLPQRPYL---PLGTLREAL-----LYPATAEAFSDAELREALEAVGLGHLAERLDeeaDWDQVLS 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1278835479 159 GGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLlrdLRDEL-NMSLLFITH 215
Cdd:COG4178 488 LGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQL---LREELpGTTVISVGH 542
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
275-511 |
4.44e-20 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 90.07 E-value: 4.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 275 LLRVEDLSVSFpirkgilrrivDRNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI----ASQGEILFDGMPLH 350
Cdd:PRK09984 4 IIRVEKLAKTF-----------NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdkSAGSHIELLGRTVQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 351 RWNR--RQMLPVRPRMQVVFQDPNssLNPRLSVLQIVEEGLRVHQP------GLSAQQREQEVMRVMVEVGLdPETRHRY 422
Cdd:PRK09984 73 REGRlaRDIRKSRANTGYIFQQFN--LVNRLSVLENVLIGALGSTPfwrtcfSWFTREQKQRALQALTRVGM-VHFAHQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 423 PAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQG 502
Cdd:PRK09984 150 VSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQG 229
|
....*....
gi 1278835479 503 EVVEQGECQ 511
Cdd:PRK09984 230 HVFYDGSSQ 238
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
301-509 |
4.89e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 90.92 E-value: 4.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 301 VLKNIRFSLRPGESLGLVGESGSGKST-----TGLallrLIASQGEILF---DGMPLHRWNR------------------ 354
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTfiehlNAL----LLPDTGTIEWifkDEKNKKKTKEkekvleklviqktrfkki 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 355 RQMLPVRPRMQVVFQdpnsslnprLSVLQIVEEGLR---VHQP---GLSAQQREQEVMRVMVEVGLDPETRHRYPAEFSG 428
Cdd:PRK13651 98 KKIKEIRRRVGVVFQ---------FAEYQLFEQTIEkdiIFGPvsmGVSKEEAKKRAAKYIELVGLDESYLQRSPFELSG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 429 GQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:PRK13651 169 GQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGK-TIILVTHDLDNVLEWTKRTIFFKDGKIIKDG 247
|
.
gi 1278835479 509 E 509
Cdd:PRK13651 248 D 248
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
16-234 |
4.91e-20 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 89.74 E-value: 4.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 16 SKQDETRTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLL-----PSppvsypQGDILFHDRSLLHADEQTlrgir 90
Cdd:PRK11247 19 SKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKS----TLLRLLagletPS------AGELLAGTAPLAEAREDT----- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 91 gnkiAMIFQEpmVSLNPLhsleKQLYEVLSLH-RGMRKEAArgeiLDCLERTGIrnaAKRLNDFPHQLSGGERQRVMIAM 169
Cdd:PRK11247 84 ----RLMFQD--ARLLPW----KKVIDNVGLGlKGQWRDAA----LQALAAVGL---ADRANEWPAALSGGQKQRVALAR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1278835479 170 ALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGR 234
Cdd:PRK11247 147 ALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
300-508 |
6.71e-20 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 88.99 E-value: 6.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 300 PVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLHRWNRRQMlpVRpRMQVVFQDPNss 374
Cdd:COG4604 15 VVLDDVSLTIPKGGITALIGPNGAGKST----LLSMISrllppDSGEVLVDGLDVATTPSREL--AK-RLAILRQENH-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 375 LNPRLSVLQIVEEGLRVHQPG-LSAQQRE--QEVMRVMvevGLDPeTRHRYPAEFSGGQRQRIAIARALILKPELIILDE 451
Cdd:COG4604 86 INSRLTVRELVAFGRFPYSKGrLTAEDREiiDEAIAYL---DLED-LADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1278835479 452 PTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:COG4604 162 PLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQG 218
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-234 |
8.06e-20 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 87.10 E-value: 8.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 4 PLLRIDNLSIAfskqdetrTVVSDLTLQIQRGETLALVGESGSGKS--VSALSILRllpsPPVSypqGDILFHDRSLLHA 81
Cdd:cd03215 3 PVLEVRGLSVK--------GAVRDVSFEVRAGEIVGIAGLVGNGQTelAEALFGLR----PPAS---GEITLDGKPVTRR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 82 DeqtLRGIRGNKIAMIFQEPmvslnplhslekqlyevlsLHRGMrkeaargeildCLERTGIRNAAkrlndFPHQLSGGE 161
Cdd:cd03215 68 S---PRDAIRAGIAYVPEDR-------------------KREGL-----------VLDLSVAENIA-----LSSLLSGGN 109
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1278835479 162 RQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDElNMSLLFITHNLSIVRKLADSVAVMQNGR 234
Cdd:cd03215 110 QQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGR 181
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
274-504 |
8.46e-20 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 87.10 E-value: 8.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 274 PLLRVEDLSVSfpirkgilrrivdrnPVLKNIRFSLRPGESLGLVGESGSGKSTTGLAL--LRLIASqGEILFDGMPLHR 351
Cdd:cd03215 3 PVLEVRGLSVK---------------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALfgLRPPAS-GEITLDGKPVTR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 352 WNRRQMlpvrprmqvvfqdpnsslnprlsvlqiVEEGlrvhqpglsaqqreqevmrvmveVGLDPETRHRY--------- 422
Cdd:cd03215 67 RSPRDA---------------------------IRAG-----------------------IAYVPEDRKREglvldlsva 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 423 -----PAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKhRLAYIFISHDLQVVRALCHQVI 497
Cdd:cd03215 97 enialSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRIL 175
|
....*..
gi 1278835479 498 VLRQGEV 504
Cdd:cd03215 176 VMYEGRI 182
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
299-508 |
9.46e-20 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 92.77 E-value: 9.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 299 NPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEILFDGMPLHRWNRRQMlpvrpRMQVVFQDPNSSL-- 375
Cdd:PRK11176 356 VPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYdIDEGEILLDGHDLRDYTLASL-----RNQVALVSQNVHLfn 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 376 -----------NPRLSVLQIVEEGLRVHQPGLsAQQREQEVMRVMVEVGldpetrhrypAEFSGGQRQRIAIARALILKP 444
Cdd:PRK11176 431 dtianniayarTEQYSREQIEEAARMAYAMDF-INKMDNGLDTVIGENG----------VLLSGGQRQRIAIARALLRDS 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1278835479 445 ELIILDEPTSSLDRTVQAQILALLKGLQeKHRLAYIfISHDLQVVRAlCHQVIVLRQGEVVEQG 508
Cdd:PRK11176 500 PILILDEATSALDTESERAIQAALDELQ-KNRTSLV-IAHRLSTIEK-ADEILVVEDGEIVERG 560
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
6-237 |
1.38e-19 |
|
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: 86.81 E-value: 1.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 6 LRIDNLSIAfskqDETRTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLlPSPPVSypQGDILFHDRSLLHA--DE 83
Cdd:cd03217 1 LEIKDLHVS----VGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH-PKYEVT--EGEILFKGEDITDLppEE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 84 QTLRGIrgnkiAMIFQEPMvslnplhslekqlyevlslhrgmrkeaargEIldclerTGIRNAaKRLNDFPHQLSGGERQ 163
Cdd:cd03217 74 RARLGI-----FLAFQYPP------------------------------EI------PGVKNA-DFLRYVNEGFSGGEKK 111
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1278835479 164 RVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDElNMSLLFITHNLSIVRKL-ADSVAVMQNGRCVE 237
Cdd:cd03217 112 RNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREE-GKSVLIITHYQRLLDYIkPDRVHVLYDGRIVK 185
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
273-505 |
2.27e-19 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 91.71 E-value: 2.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 273 TPLLRVEDLSVSFPIRKGILRrivdrnpVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEILFDGM 347
Cdd:PRK10535 2 TALLELKDIRRSYPSGEEQVE-------VLKGISLDIYAGEMVAIVGASGSGKST----LMNILgcldkPTSGTYRVAGQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 348 PLHRWNRRQMLPVR-PRMQVVFQdpNSSLNPRLSVLQIVEegLRVHQPGLSAQQREQEVMRVMVEVGLDPETRHRyPAEF 426
Cdd:PRK10535 71 DVATLDADALAQLRrEHFGFIFQ--RYHLLSHLTAAQNVE--VPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQ-PSQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 427 SGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEK-HRLayIFISHDLQVVrALCHQVIVLRQGEVV 505
Cdd:PRK10535 146 SGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRgHTV--IIVTHDPQVA-AQAERVIEIRDGEIV 222
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
21-236 |
2.28e-19 |
|
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: 86.07 E-value: 2.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 21 TRTVVSDLTLQIQRGETLALVGESGSGKSvSALSILR-LLPSPPVSypqGDILFHDRSLlhaDEQTLRGIrgnkIAMIFQ 99
Cdd:cd03213 21 GKQLLKNVSGKAKPGELTAIMGPSGAGKS-TLLNALAgRRTGLGVS---GEVLINGRPL---DKRSFRKI----IGYVPQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 100 EPMvslnplhslekqLYEVLSLHRGMRKEAA-RGeildclertgirnaakrlndfphqLSGGERQRVMIAMALLTRPELL 178
Cdd:cd03213 90 DDI------------LHPTLTVRETLMFAAKlRG------------------------LSGGERKRVSIALELVSNPSLL 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1278835479 179 IADEPTTALDVTVQAQILTLLRDLRDElNMSLLFITHNLSI-VRKLADSVAVMQNGRCV 236
Cdd:cd03213 134 FLDEPTSGLDSSSALQVMSLLRRLADT-GRTIICSIHQPSSeIFELFDKLLLLSQGRVI 191
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
223-528 |
3.29e-19 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 91.96 E-value: 3.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 223 LADSVAVMQNGRCVEQNA-AST-------------LLSA--PQHPYTQRLLNS-EPSGDPVPLDADSTPLLRVEDLSVSF 285
Cdd:PLN03232 1150 LTATFAVLRNGNAENQAGfASTmglllsytlnittLLSGvlRQASKAENSLNSvERVGNYIDLPSEATAIIENNRPVSGW 1229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 286 PIRKGI------LRRIVDRNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIA-SQGEILFDGMPLHRW---NRR 355
Cdd:PLN03232 1230 PSRGSIkfedvhLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVElEKGRIMIDDCDVAKFgltDLR 1309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 356 QMLPVRPRMQVVFQ-------DPNSSLNPRlsvlQIVEEGLRVHQpglsaqqreQEVMRvMVEVGLDPETRHRyPAEFSG 428
Cdd:PLN03232 1310 RVLSIIPQSPVLFSgtvrfniDPFSEHNDA----DLWEALERAHI---------KDVID-RNPFGLDAEVSEG-GENFSV 1374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 429 GQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKglQEKHRLAYIFISHDLQVVRAlCHQVIVLRQGEVVEQG 508
Cdd:PLN03232 1375 GQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIR--EEFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYD 1451
|
330 340
....*....|....*....|
gi 1278835479 509 ECQRVFSAPTQRYTRQLLSS 528
Cdd:PLN03232 1452 SPQELLSRDTSAFFRMVHST 1471
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-238 |
4.83e-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: 85.71 E-value: 4.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 6 LRIDNLSIAFSKQDetrtVVSDLTLQIQRGeTLALVGESGSGKSvsalSILRLLPS--PPVSypqGDILFHDRSLLhADE 83
Cdd:cd03264 1 LQLENLTKRYGKKR----ALDGVSLTLGPG-MYGLLGPNGAGKT----TLMRILATltPPSS---GTIRIDGQDVL-KQP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 84 QTLRGIrgnkIAMIFQEPMVSlnPLHSLEKQLYEVLSLHrGMRKEAARGEILDCLERTGIRNAAKRLndfPHQLSGGERQ 163
Cdd:cd03264 68 QKLRRR----IGYLPQEFGVY--PNFTVREFLDYIAWLK-GIPSKEVKARVDEVLELVNLGDRAKKK---IGSLSGGMRR 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1278835479 164 RVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDelNMSLLFITHNLSIVRKLADSVAVMQNGRCVEQ 238
Cdd:cd03264 138 RVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
265-518 |
5.26e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 87.98 E-value: 5.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 265 PVPLDADStpLLRVEDLSVSFPirkgilRRIVDRNPVLKNIRFSLRPGESLGLVGESGSGKSTT------------GLAL 332
Cdd:PRK13631 13 PNPLSDDI--ILRVKNLYCVFD------EKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLvthfnglikskyGTIQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 333 LRLIASQGEILFDGMPLHRWNRR--QMLPVRPRMQVVFQDPNSSLNPRLSVLQIVEEGLRVHQPGLSAQQREQEVMRVMv 410
Cdd:PRK13631 85 VGDIYIGDKKNNHELITNPYSKKikNFKELRRRVSMVFQFPEYQLFKDTIEKDIMFGPVALGVKKSEAKKLAKFYLNKM- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 411 evGLDPETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIfISHDLQVVR 490
Cdd:PRK13631 164 --GLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFV-ITHTMEHVL 240
|
250 260
....*....|....*....|....*...
gi 1278835479 491 ALCHQVIVLRQGEVVEQGECQRVFSAPT 518
Cdd:PRK13631 241 EVADEVIVMDKGKILKTGTPYEIFTDQH 268
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
276-508 |
5.30e-19 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 86.16 E-value: 5.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 276 LRVEDLSVSfpirkgilrriVDRNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALL---RLIASQGEILFDGMPLHrw 352
Cdd:TIGR01978 1 LKIKDLHVS-----------VEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAghpSYEVTSGTILFKGQDLL-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 353 nrrQMLP---VRPRMQVVFQDPNSSlnPRLSVLQIVEEGLRVH-----QPGLSAQQREQEVMRVMVEVGLDPETRHRYPA 424
Cdd:TIGR01978 68 ---ELEPderARAGLFLAFQYPEEI--PGVSNLEFLRSALNARrsargEEPLDLLDFEKLLKEKLALLDMDEEFLNRSVN 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 425 E-FSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRlAYIFISHDLQVVRALCHQVI-VLRQG 502
Cdd:TIGR01978 143 EgFSGGEKKRNEILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLREPDR-SFLIITHYQRLLNYIKPDYVhVLLDG 221
|
....*.
gi 1278835479 503 EVVEQG 508
Cdd:TIGR01978 222 RIVKSG 227
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
301-516 |
6.39e-19 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 86.58 E-value: 6.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 301 VLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIASQ-GEILFDGMPLHRWNRRQmlpVRPRMQVVFQdpNSSLNPRL 379
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAhGHVWLDGEHIQHYASKE---VARRIGLLAQ--NATTPGDI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 380 SVLQIVEEGLRVHQPGLSAQQREQE--VMRVMVEVGLDPETRHRYPAeFSGGQRQRIAIARALILKPELIILDEPTSSLD 457
Cdd:PRK10253 97 TVQELVARGRYPHQPLFTRWRKEDEeaVTKAMQATGITHLADQSVDT-LSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 458 RTVQAQILALLKGLQEKHRLAYIFISHDL-QVVRALCHqVIVLRQGEVVEQGECQRVFSA 516
Cdd:PRK10253 176 ISHQIDLLELLSELNREKGYTLAAVLHDLnQACRYASH-LIALREGKIVAQGAPKEIVTA 234
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
5-236 |
6.46e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 87.60 E-value: 6.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 5 LLRIDNLSIAF-SKQDETRTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLLPSPpvsypQGDILFHD-------R 76
Cdd:PRK13631 21 ILRVKNLYCVFdEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSK-----YGTIQVGDiyigdkkN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 77 SLLHADEQTLRGIRGNK-----IAMIFQEPMVSLNPlHSLEKQL-YEVLSLhrGMRKEAARGEILDCLERTGIRNAAkrL 150
Cdd:PRK13631 96 NHELITNPYSKKIKNFKelrrrVSMVFQFPEYQLFK-DTIEKDImFGPVAL--GVKKSEAKKLAKFYLNKMGLDDSY--L 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 151 NDFPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDElNMSLLFITHNLSIVRKLADSVAVM 230
Cdd:PRK13631 171 ERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVM 249
|
....*.
gi 1278835479 231 QNGRCV 236
Cdd:PRK13631 250 DKGKIL 255
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-217 |
8.56e-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: 89.34 E-value: 8.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 4 PLLRIDNLSIAFSKQDEtrtVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLLPSPpvsypQGDILFHDRSLLHADE 83
Cdd:TIGR02868 333 PTLELRDLSAGYPGAPP---VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPL-----QGEVTLDGVPVSSLDQ 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 84 QTLRGIrgnkIAMIFQEPmvslnplHSLEKQLYEVLSLHRGmrkEAARGEILDCLERTGIRNAAKRLNDFPH-------- 155
Cdd:TIGR02868 405 DEVRRR----VSVCAQDA-------HLFDTTVRENLRLARP---DATDEELWAALERVGLADWLRALPDGLDtvlgegga 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1278835479 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELnmSLLFITHNL 217
Cdd:TIGR02868 471 RLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGR--TVVLITHHL 530
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
271-485 |
1.06e-18 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 85.15 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 271 DSTPLLRVEDLSVSfpirkgilrriVDRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIAS-----QGEILFD 345
Cdd:PRK10247 3 ENSPLLQLQNVGYL-----------AGDAKILNNISFSLRAGEFKLITGPSGCGKST----LLKIVASlisptSGTLLFE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 346 GMPLHRWNrrqmlPVRPRMQV--VFQDP---NSSLNPRLsvlqIVEEGLRVHQPglsaqqREQEVMRVMVEVGLDPETRH 420
Cdd:PRK10247 68 GEDISTLK-----PEIYRQQVsyCAQTPtlfGDTVYDNL----IFPWQIRNQQP------DPAIFLDDLERFALPDTILT 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1278835479 421 RYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHD 485
Cdd:PRK10247 133 KNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHD 197
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
27-249 |
1.15e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 86.23 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 27 DLTLQIQRGETLALVGESGSGKSvSALSILRLLPSPPvsypQGDILFHDRSLL-HADEQTLRGIRgNKIAMIFQEPmvsl 105
Cdd:PRK13634 25 DVNVSIPSGSYVAIIGHTGSGKS-TLLQHLNGLLQPT----SGTVTIGERVITaGKKNKKLKPLR-KKVGIVFQFP---- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 106 nplhslEKQLYE--VLS------LHRGMRKEAARGEILDCLERTGIrnAAKRLNDFPHQLSGGERQRVMIAMALLTRPEL 177
Cdd:PRK13634 95 ------EHQLFEetVEKdicfgpMNFGVSEEDAKQKAREMIELVGL--PEELLARSPFELSGGQMRRVAIAGVLAMEPEV 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1278835479 178 LIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGRCVEQNAASTLLSAPQ 249
Cdd:PRK13634 167 LVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
27-249 |
1.18e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 86.42 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 27 DLTLQIQRGETLALVGESGSGKSV-----SALsilrLLPSppvsypQGDILFHDRSL-LHADEQTLRGIRgNKIAMIFQE 100
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTlmqhfNAL----LKPS------SGTITIAGYHItPETGNKNLKKLR-KKVSLVFQF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 101 PmvslnplhslEKQLYE--VLS------LHRGMRKEAARGEILDCLERTGIRNAAkrLNDFPHQLSGGERQRVMIAMALL 172
Cdd:PRK13641 94 P----------EAQLFEntVLKdvefgpKNFGFSEDEAKEKALKWLKKVGLSEDL--ISKSPFELSGGQMRRVAIAGVMA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1278835479 173 TRPELLIADEPTTALDVTVQAQILTLLRDLRDElNMSLLFITHNLSIVRKLADSVAVMQNGRCVEQNAASTLLSAPQ 249
Cdd:PRK13641 162 YEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
6-249 |
1.22e-18 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 85.28 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 6 LRIDNLSIAfskqdeTRtvVSDLTLQIQRGETLALVGESGSGKSvSALSILR-LLPSppvsypQGDILFHDRSLLHADEQ 84
Cdd:COG4138 1 LQLNDVAVA------GR--LGPISAQVNAGELIHLIGPNGAGKS-TLLARMAgLLPG------QGEILLNGRPLSDWSAA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 85 TLRGIRgnkiAMIFQEPMvslnPLHSLekQLYEVLSLHR--GMRKEAARGEILDCLERTGIrnaAKRLNDFPHQLSGGER 162
Cdd:COG4138 66 ELARHR----AYLSQQQS----PPFAM--PVFQYLALHQpaGASSEAVEQLLAQLAEALGL---EDKLSRPLTQLSGGEW 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 163 QRVMIAMALLT-------RPELLIADEPTTALDVTVQAQILTLLRDLRdELNMSLLFITHNLSIVRKLADSVAVMQNGRC 235
Cdd:COG4138 133 QRVRLAAVLLQvwptinpEGQLLLLDEPMNSLDVAQQAALDRLLRELC-QQGITVVMSSHDLNHTLRHADRVWLLKQGKL 211
|
250
....*....|....
gi 1278835479 236 VEQNAASTLLSAPQ 249
Cdd:COG4138 212 VASGETAEVMTPEN 225
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
27-233 |
1.24e-18 |
|
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: 84.82 E-value: 1.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 27 DLTLQIQRGETLALVGESGSGKSvSALSILRLLPSPPvsypQGDILFHDRSLLHAdeqtlrgirGNKIAMIFQEpmVSLN 106
Cdd:TIGR01184 3 GVNLTIQQGEFISLIGHSGCGKS-TLLNLISGLAQPT----SGGVILEGKQITEP---------GPDRMVVFQN--YSLL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 107 PLHSLEKQLY-EVLSLHRGMRKEAARGEILDCLERTGIRNAAKRlndFPHQLSGGERQRVMIAMALLTRPELLIADEPTT 185
Cdd:TIGR01184 67 PWLTVRENIAlAVDRVLPDLSKSERRAIVEEHIALVGLTEAADK---RPGQLSGGMKQRVAIARALSIRPKVLLLDEPFG 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1278835479 186 ALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNG 233
Cdd:TIGR01184 144 ALDALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-247 |
1.31e-18 |
|
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: 89.11 E-value: 1.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 2 TQPLLRIDNLSIAFskqDETRTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLL-----PSppvsypQGDILFHDR 76
Cdd:COG5265 354 GGGEVRFENVSFGY---DPERPILKGVSFEVPAGKTVAIVGPSGAGKS----TLARLLfrfydVT------SGRILIDGQ 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 77 SLLHADEQTLRGIrgnkIAMIFQEPmvslnplhslekqlyeVL-------SLHRGmRKEAARGEIldclertgiRNAAK- 148
Cdd:COG5265 421 DIRDVTQASLRAA----IGIVPQDT----------------VLfndtiayNIAYG-RPDASEEEV---------EAAARa 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 149 -RLNDF----PHQ-----------LSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDelNMSLLF 212
Cdd:COG5265 471 aQIHDFieslPDGydtrvgerglkLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVAR--GRTTLV 548
|
250 260 270
....*....|....*....|....*....|....*.
gi 1278835479 213 ITHNLS-IVRklADSVAVMQNGRCVEQNAASTLLSA 247
Cdd:COG5265 549 IAHRLStIVD--ADEILVLEAGRIVERGTHAELLAQ 582
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
268-509 |
1.41e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 88.57 E-value: 1.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 268 LDADSTPLLRVEDLSVSFpirKGIlrrivdrnPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEI 342
Cdd:PRK15439 4 SDTTAPPLLCARSISKQY---SGV--------EVLKGIDFTLHAGEVHALLGGNGAGKST----LMKIIAgivppDSGTL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 343 LFDGMPLHRWNrrqmlPVRPR---MQVVFQDPNssLNPRLSVLQIVEEGLRVHQpglSAQQREQEVMRVMvEVGLDPETR 419
Cdd:PRK15439 69 EIGGNPCARLT-----PAKAHqlgIYLVPQEPL--LFPNLSVKENILFGLPKRQ---ASMQKMKQLLAAL-GCQLDLDSS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 420 hryPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHrLAYIFISHDLQVVRALCHQVIVL 499
Cdd:PRK15439 138 ---AGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQG-VGIVFISHKLPEIRQLADRISVM 213
|
250
....*....|
gi 1278835479 500 RQGEVVEQGE 509
Cdd:PRK15439 214 RDGTIALSGK 223
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-238 |
1.68e-18 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 87.31 E-value: 1.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 1 MTQPLLRIDNLSIAFskqdETRTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLL-----PSppvsypQGDILFHD 75
Cdd:PRK09452 10 SLSPLVELRGISKSF----DGKEVISNLDLTINNGEFLTLLGPSGCGKT----TVLRLIagfetPD------SGRIMLDG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 76 RSLLHAD-EQtlrgirgNKIAMIFQEpmVSLNPLHSLekqlYEVLSLHRGMRKEAARgEIldcleRTGIRNAAK--RLND 152
Cdd:PRK09452 76 QDITHVPaEN-------RHVNTVFQS--YALFPHMTV----FENVAFGLRMQKTPAA-EI-----TPRVMEALRmvQLEE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 153 F----PHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVA 228
Cdd:PRK09452 137 FaqrkPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIV 216
|
250
....*....|
gi 1278835479 229 VMQNGRcVEQ 238
Cdd:PRK09452 217 VMRDGR-IEQ 225
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
5-249 |
1.85e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 85.53 E-value: 1.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 5 LLRIDNLSIAFSKQDETRTVvSDLTLQIQRGETLALVGESGSGKSVSALSILRLLPSPpvsypQGDILFHDRSLLHADEQ 84
Cdd:PRK13642 4 ILEVENLVFKYEKESDVNQL-NGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEF-----EGKVKIDGELLTAENVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 85 TLRgirgNKIAMIFQEP-------MVSLNPLHSLEKQlyevlslhrGMRKEAARGEILDCLERTGIRNAAKRLndfPHQL 157
Cdd:PRK13642 78 NLR----RKIGMVFQNPdnqfvgaTVEDDVAFGMENQ---------GIPREEMIKRVDEALLAVNMLDFKTRE---PARL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKlADSVAVMQNGRCVE 237
Cdd:PRK13642 142 SGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIK 220
|
250
....*....|..
gi 1278835479 238 QNAASTLLSAPQ 249
Cdd:PRK13642 221 EAAPSELFATSE 232
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
131-486 |
2.44e-18 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 88.33 E-value: 2.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 131 RGEILDCLERTGIRNAAKRlnDFpHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDelNMSL 210
Cdd:PRK13409 190 RGKLDEVVERLGLENILDR--DI-SELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAE--GKYV 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 211 LFITHNLSIVRKLADSVAVMQNgrcveQNAASTLLSapqHPYTQRL-LNSEPSGDpvpLDADStplLRVEDLSVSF---- 285
Cdd:PRK13409 265 LVVEHDLAVLDYLADNVHIAYG-----EPGAYGVVS---KPKGVRVgINEYLKGY---LPEEN---MRIRPEPIEFeerp 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 286 PIRKGILRRIVDRNPVLKNI-RFSL-------RPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDgmplhrw 352
Cdd:PRK13409 331 PRDESERETLVEYPDLTKKLgDFSLeveggeiYEGEVIGIVGPNGIGKTT----FAKLLAgvlkpDEGEVDPE------- 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 353 nrrqmLPVRPRMQVVFQDPNSSlnprlsvlqiVEEGLRVHQPGLSAQQREQEVMRVMvevGLDP--EtrhRYPAEFSGGQ 430
Cdd:PRK13409 400 -----LKISYKPQYIKPDYDGT----------VEDLLRSITDDLGSSYYKSEIIKPL---QLERllD---KNVKDLSGGE 458
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1278835479 431 RQRIAIARALILKPELIILDEPTSSLDrtVQAQILA--LLKGLQEKHRLAYIFISHDL 486
Cdd:PRK13409 459 LQRVAIAACLSRDADLYLLDEPSAHLD--VEQRLAVakAIRRIAEEREATALVVDHDI 514
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-254 |
2.52e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 84.70 E-value: 2.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 4 PLLRIDNLSIAFskqdETRTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLLPSPPVSYPQGDILFHDRSLlHADE 83
Cdd:PRK14258 6 PAIKVNNLSFYY----DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGRVEFFNQNI-YERR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 84 QTLRGIRgNKIAMIFQEPmvSLNPLHSLEKQLYEVLSLhrGMRKEAargEILDCLErTGIRNA------AKRLNDFPHQL 157
Cdd:PRK14258 81 VNLNRLR-RQVSMVHPKP--NLFPMSVYDNVAYGVKIV--GWRPKL---EIDDIVE-SALKDAdlwdeiKHKIHKSALDL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQN----- 232
Cdd:PRK14258 152 SGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenri 231
|
250 260
....*....|....*....|..
gi 1278835479 233 GRCVEQNAASTLLSAPQHPYTQ 254
Cdd:PRK14258 232 GQLVEFGLTKKIFNSPHDSRTR 253
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
274-468 |
3.39e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 83.00 E-value: 3.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 274 PLLRVEDLSVsfpIRKGILrrivdrnpVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMP 348
Cdd:PRK13539 1 MMLEGEDLAC---VRGGRV--------LFSGLSFTLAAGEALVLTGPNGSGKTT----LLRLIAgllppAAGTIKLDGGD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 349 LHrwnrrqmLPvRPRMQVVFQDPNSSLNPRLSVLQIVEEGLRVHQpglsaqQREQEVMRVMVEVGLDPETrHRYPAEFSG 428
Cdd:PRK13539 66 ID-------DP-DVAEACHYLGHRNAMKPALTVAENLEFWAAFLG------GEELDIAAALEAVGLAPLA-HLPFGYLSA 130
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1278835479 429 GQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALL 468
Cdd:PRK13539 131 GQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELI 170
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
275-527 |
5.04e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 84.06 E-value: 5.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 275 LLRVEDLSVSFpirkgilrrivDRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLR-------LIAS---QGEILF 344
Cdd:PRK14243 10 VLRTENLNVYY-----------GSFLAVKNVWLDIPKNQITAFIGPSGCGKST----ILRcfnrlndLIPGfrvEGKVTF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 345 DGMPLHRwNRRQMLPVRPRMQVVFQDPNS---------SLNPRLSVLQ-----IVEEGLRvhQPGLSaqqreQEVMRVMV 410
Cdd:PRK14243 75 HGKNLYA-PDVDPVEVRRRIGMVFQKPNPfpksiydniAYGARINGYKgdmdeLVERSLR--QAALW-----DEVKDKLK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 411 EVGLdpetrhrypaEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLayIFISHDLQVVR 490
Cdd:PRK14243 147 QSGL----------SLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTI--IIVTHNMQQAA 214
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1278835479 491 ALCHQVIVL---------RQGEVVEQGECQRVFSAPTQRYTRQLLS 527
Cdd:PRK14243 215 RVSDMTAFFnveltegggRYGYLVEFDRTEKIFNSPQQQATRDYVS 260
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
278-515 |
5.53e-18 |
|
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: 84.14 E-value: 5.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 278 VEDLSVSFpirkgilrrIVDRNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIASQGEILFDG-----MPLHRW 352
Cdd:cd03289 5 VKDLTAKY---------TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIQIDGvswnsVPLQKW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 353 nrRQMLPVRPRMQVVFQDP-NSSLNPrlsvlqiveeglrvhqpglSAQQREQEVMRVMVEVGLDpETRHRYPAE------ 425
Cdd:cd03289 76 --RKAFGVIPQKVFIFSGTfRKNLDP-------------------YGKWSDEEIWKVAEEVGLK-SVIEQFPGQldfvlv 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 426 -----FSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKglQEKHRLAYIFISHDLQVVRAlCHQVIVLR 500
Cdd:cd03289 134 dggcvLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLK--QAFADCTVILSEHRIEAMLE-CQRFLVIE 210
|
250
....*....|....*
gi 1278835479 501 QGEVVEQGECQRVFS 515
Cdd:cd03289 211 ENKVRQYDSIQKLLN 225
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
301-508 |
8.15e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 84.09 E-value: 8.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 301 VLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIA-SQGEILFDGMPLHRWNRRqmlpVRPRMQVVFQDPNssLNPRL 379
Cdd:PRK13537 22 VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHpDAGSISLCGEPVPSRARH----ARQRVGVVPQFDN--LDPDF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 380 SVlqivEEGLRVHQP--GLSAQQREQEVMRVMVEVGLDPETRHRYpAEFSGGQRQRIAIARALILKPELIILDEPTSSLD 457
Cdd:PRK13537 96 TV----RENLLVFGRyfGLSAAAARALVPPLLEFAKLENKADAKV-GELSGGMKRRLTLARALVNDPDVLVLDEPTTGLD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1278835479 458 RTVQAQILALLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:PRK13537 171 PQARHLMWERLRSLLARGK-TILLTTHFMEEAERLCDRLCVIEEGRKIAEG 220
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
6-234 |
8.24e-18 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 81.11 E-value: 8.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 6 LRIDNLSiaFSKQDETRTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLLPspPVSypqGDILfhdrsLLHAD-EQ 84
Cdd:cd03246 1 LEVENVS--FRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLR--PTS---GRVR-----LDGADiSQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 85 TLRGIRGNKIAMIFQEpmvslnplhsleKQLYEvlslhrgmrkeaarGEILDCLertgirnaakrlndfphqLSGGERQR 164
Cdd:cd03246 69 WDPNELGDHVGYLPQD------------DELFS--------------GSIAENI------------------LSGGQRQR 104
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 165 VMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRdELNMSLLFITHNLSIVRkLADSVAVMQNGR 234
Cdd:cd03246 105 LGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALK-AAGATRIVIAHRPETLA-SADRILVLEDGR 172
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
131-498 |
8.68e-18 |
|
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: 86.38 E-value: 8.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 131 RGEILDCLERTGIRNAAKR-LNDfphqLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDElNMS 209
Cdd:COG1245 190 RGKLDELAEKLGLENILDRdISE----LSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEE-GKY 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 210 LLFITHNLSIVRKLADSVAVMQNgrcveQNAASTLLSapqHPYTQRL---------LNSEPsgdpvpldadstplLRVED 280
Cdd:COG1245 265 VLVVEHDLAILDYLADYVHILYG-----EPGVYGVVS---KPKSVRVginqyldgyLPEEN--------------VRIRD 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 281 LSVSFPIRKgiLRRIVDRNPVLK--NIR-----FSL-------RPGESLGLVGESGSGKSTtglaLLRLIAsqGEIlfdg 346
Cdd:COG1245 323 EPIEFEVHA--PRREKEEETLVEypDLTksyggFSLeveggeiREGEVLGIVGPNGIGKTT----FAKILA--GVL---- 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 347 mplhrwnrrqmlpvrprmqvvfqDPNS-SLNPRLSV------LQI-----VEEGLR-VHQPGLSAQQREQEVMRVMvevG 413
Cdd:COG1245 391 -----------------------KPDEgEVDEDLKIsykpqyISPdydgtVEEFLRsANTDDFGSSYYKTEIIKPL---G 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 414 LDPeTRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDrtVQAQILA--LLKGLQEKHRLAYIFISHDLQVVRA 491
Cdd:COG1245 445 LEK-LLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD--VEQRLAVakAIRRFAENRGKTAMVVDHDIYLIDY 521
|
....*..
gi 1278835479 492 LCHQVIV 498
Cdd:COG1245 522 ISDRLMV 528
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-247 |
9.57e-18 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 86.31 E-value: 9.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 2 TQPL----LRIDNLSIAFSKQdetRTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLLPsppvsYPQGDILFHDRS 77
Cdd:PRK10790 333 DRPLqsgrIDIDNVSFAYRDD---NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYP-----LTEGEIRLDGRP 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 78 LLHADEQTLRgirgNKIAMIFQEPMVslnplhsLEKQLYEVLSLHRGMRKEAargeILDCLERTGIRNAAKRLNDFPH-- 155
Cdd:PRK10790 405 LSSLSHSVLR----QGVAMVQQDPVV-------LADTFLANVTLGRDISEEQ----VWQALETVQLAELARSLPDGLYtp 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 156 ------QLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDelNMSLLFITHNLS-IVRklADSVA 228
Cdd:PRK10790 470 lgeqgnNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVRE--HTTLVVIAHRLStIVE--ADTIL 545
|
250
....*....|....*....
gi 1278835479 229 VMQNGRCVEQNAASTLLSA 247
Cdd:PRK10790 546 VLHRGQAVEQGTHQQLLAA 564
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
22-230 |
1.06e-17 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 81.13 E-value: 1.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 22 RTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLLPspPVSypqgdilfhdrsllhadeQTLRGIRGNKIAMIFQEP 101
Cdd:NF040873 5 RPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLR--PTS------------------GTVRRAGGARVAYVPQRS 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 102 MVSlnplHSLEKQLYEVLSL----HRGMRKE---AARGEILDCLERTGIRNAAKRLNDfphQLSGGERQRVMIAMALLTR 174
Cdd:NF040873 65 EVP----DSLPLTVRDLVAMgrwaRRGLWRRltrDDRAAVDDALERVGLADLAGRQLG---ELSGGQRQRALLAQGLAQE 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1278835479 175 PELLIADEPTTALDVTVQAQILTLLRDLRDElNMSLLFITHNLSIVRkLADSVAVM 230
Cdd:NF040873 138 ADLLLLDEPTTGLDAESRERIIALLAEEHAR-GATVVVVTHDLELVR-RADPCVLL 191
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
124-248 |
1.07e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 83.31 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 124 GMRKEAARGEILDCLERTGIRNAAKRLndfPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLR 203
Cdd:PRK13652 108 GLDEETVAHRVSSALHMLGLEELRDRV---PHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLP 184
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1278835479 204 DELNMSLLFITHNLSIVRKLADSVAVMQNGRCVEQNAASTLLSAP 248
Cdd:PRK13652 185 ETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
274-508 |
1.09e-17 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 82.38 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 274 PLLRVEDLSVSFPIRkgilrrivdrnPVLKNIRFSLRPGESLGLVGESGSGKSTT-----GLallrLIASQGEILFDG-- 346
Cdd:COG1137 2 MTLEAENLVKSYGKR-----------TVVKDVSLEVNQGEIVGLLGPNGAGKTTTfymivGL----VKPDSGRIFLDGed 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 347 ---MPLHRWNRRQM--LPvrprmqvvfQDPnsSLNPRLSVLQ----IVEegLRvhqpGLSAQQREQEVMRVMVEVGLDpE 417
Cdd:COG1137 67 ithLPMHKRARLGIgyLP---------QEA--SIFRKLTVEDnilaVLE--LR----KLSKKEREERLEELLEEFGIT-H 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 418 TRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLqeKHRLAYIFIS-HDlqvVR---ALC 493
Cdd:COG1137 129 LRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHL--KERGIGVLITdHN---VRetlGIC 203
|
250
....*....|....*
gi 1278835479 494 HQVIVLRQGEVVEQG 508
Cdd:COG1137 204 DRAYIISEGKVLAEG 218
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
277-492 |
2.46e-17 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 81.16 E-value: 2.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 277 RVEDLSVSFpirkGILRRIVDRnPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIasqgeilfdgmplhrWNRRQ 356
Cdd:COG2401 26 RVAIVLEAF----GVELRVVER-YVLRDLNLEIEPGEIVLIVGASGSGKST----LLRLL---------------AGALK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 357 MLPVrprmQVVFQDPNSSLNPRLSVLQIVeegLRVHQPGlsaqqreqEVMRVMVEVGL-DPETRHRYPAEFSGGQRQRIA 435
Cdd:COG2401 82 GTPV----AGCVDVPDNQFGREASLIDAI---GRKGDFK--------DAVELLNAVGLsDAVLWLRRFKELSTGQKFRFR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 436 IARALILKPELIILDEPTSSLDRTVqAQILAllKGLQE---KHRLAYIFISHDLQVVRAL 492
Cdd:COG2401 147 LALLLAERPKLLVIDEFCSHLDRQT-AKRVA--RNLQKlarRAGITLVVATHHYDVIDDL 203
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
22-234 |
2.56e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 81.07 E-value: 2.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 22 RTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLL-----PSppvsypQGDILF--HDRSLLHADEQT-LRgirgNK 93
Cdd:PRK10908 15 RQALQGVTFHMRPGEMAFLTGHSGAGKS----TLLKLIcgierPS------AGKIWFsgHDITRLKNREVPfLR----RQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 94 IAMIFQEpmvslnplHSL--EKQLYEVLSLH---RGMRKEAARGEILDCLERTGIRNAAKrlnDFPHQLSGGERQRVMIA 168
Cdd:PRK10908 81 IGMIFQD--------HHLlmDRTVYDNVAIPliiAGASGDDIRRRVSAALDKVGLLDKAK---NFPIQLSGGEQQRVGIA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1278835479 169 MALLTRPELLIADEPTTALDVTVQAQILTLLRDLrDELNMSLLFITHNLSIVRKLADSVAVMQNGR 234
Cdd:PRK10908 150 RAVVNKPAVLLADEPTGNLDDALSEGILRLFEEF-NRVGVTVLMATHDIGLISRRSYRMLTLSDGH 214
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
273-513 |
2.68e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 84.84 E-value: 2.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 273 TPLLRVEDLSVSFPirkgilrrivdrnPV--LKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFD 345
Cdd:PRK09700 3 TPYISMAGIGKSFG-------------PVhaLKSVNLTVYPGEIHALLGENGAGKST----LMKVLSgihepTKGTITIN 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 346 GMPLHRWNRRqmLPVRPRMQVVFQDpnSSLNPRLSVLQ-------IVEEGLRVHQPGLSAQQREQEVMRVMVEVGLDPET 418
Cdd:PRK09700 66 NINYNKLDHK--LAAQLGIGIIYQE--LSVIDELTVLEnlyigrhLTKKVCGVNIIDWREMRVRAAMMLLRVGLKVDLDE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 419 RhryPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRlAYIFISHDLQVVRALCHQVIV 498
Cdd:PRK09700 142 K---VANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGT-AIVYISHKLAEIRRICDRYTV 217
|
250
....*....|....*
gi 1278835479 499 LRQGEVVEQGECQRV 513
Cdd:PRK09700 218 MKDGSSVCSGMVSDV 232
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
297-497 |
2.73e-17 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 79.97 E-value: 2.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 297 DRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILfdgmplhrwnrrqmlpVRPRMQVVFQDP 371
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKST----LLKVLAgvlrpTSGTVR----------------RAGGARVAYVPQ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 372 NSSLNPRL--SVLQIVEEGLRVHQPGLSAQQRE--QEVMRVMVEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPELI 447
Cdd:NF040873 63 RSEVPDSLplTVRDLVAMGRWARRGLWRRLTRDdrAAVDDALERVGLA-DLAGRQLGELSGGQRQRALLAQGLAQEADLL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1278835479 448 ILDEPTSSLDRTVQAQILALLKGLQEKHRlAYIFISHDLQVVRALCHQVI 497
Cdd:NF040873 142 LLDEPTTGLDAESRERIIALLAEEHARGA-TVVVVTHDLELVRRADPCVL 190
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-234 |
2.74e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 81.67 E-value: 2.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 6 LRIDNLSIAFSKQ--DEtRTVVSDLTLQIQRGETLALVGESGSGKSvSALSIL--RLLPSppvsypQGDILFHDRSLLH- 80
Cdd:COG1101 2 LELKNLSKTFNPGtvNE-KRALDGLNLTIEEGDFVTVIGSNGAGKS-TLLNAIagSLPPD------SGSILIDGKDVTKl 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 81 ADEQtlrgiRGNKIAMIFQEPMVSLNPLHSLEKQLyeVLSLHRGMR-------KEAARGEILDCLERTGIrNAAKRLNDF 153
Cdd:COG1101 74 PEYK-----RAKYIGRVFQDPMMGTAPSMTIEENL--ALAYRRGKRrglrrglTKKRRELFRELLATLGL-GLENRLDTK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 154 PHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNG 233
Cdd:COG1101 146 VGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEG 225
|
.
gi 1278835479 234 R 234
Cdd:COG1101 226 R 226
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
7-457 |
2.83e-17 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 85.18 E-value: 2.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 7 RIDNLSIAFSKQdetrTVVSDLTLQIQRGETLALVGESGSGKSvSALSIL---RLLPSPPVSYPQGDIL--FHDRSLLHa 81
Cdd:NF033858 3 RLEGVSHRYGKT----VALDDVSLDIPAGCMVGLIGPDGVGKS-SLLSLIagaRKIQQGRVEVLGGDMAdaRHRRAVCP- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 82 deqtlrgirgnKIAMIFQepmvslnplhSLEKQLYEVLSLHR---------GMRKEAARGEILDCLERTGI-----RNAA 147
Cdd:NF033858 77 -----------RIAYMPQ----------GLGKNLYPTLSVFEnldffgrlfGQDAAERRRRIDELLRATGLapfadRPAG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 148 KrlndfphqLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDEL-NMSLLFIThnlsivrklA-- 224
Cdd:NF033858 136 K--------LSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERpGMSVLVAT---------Aym 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 225 ------DSVAVMQNGRCV---------EQNAASTLLSApqhpYTqRLLNSEPSGDPVPLDAdsTPllRVEDLSVSFPIR- 288
Cdd:NF033858 199 eeaerfDWLVAMDAGRVLatgtpaellARTGADTLEAA----FI-ALLPEEKRRGHQPVVI--PP--RPADDDDEPAIEa 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 289 KGILRRI-----VDrnpvlkNIRFSLRPGESLGLVGESGSGKST-----TGLallrLIASQGEILFDGMPLhrwNRRQMl 358
Cdd:NF033858 270 RGLTMRFgdftaVD------HVSFRIRRGEIFGFLGSNGCGKSTtmkmlTGL----LPASEGEAWLFGQPV---DAGDI- 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 359 pvRPRMQVVFQDPNSSLNPRLSVLQIVEEGLRV-HQPGLSAQQREQEVMRvmvEVGLDPETRHRyPAEFSGGQRQRIAIA 437
Cdd:NF033858 336 --ATRRRVGYMSQAFSLYGELTVRQNLELHARLfHLPAAEIAARVAEMLE---RFDLADVADAL-PDSLPLGIRQRLSLA 409
|
490 500
....*....|....*....|
gi 1278835479 438 RALILKPELIILDEPTSSLD 457
Cdd:NF033858 410 VAVIHKPELLILDEPTSGVD 429
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
272-516 |
3.77e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 81.47 E-value: 3.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 272 STPLLRVEDLSVSFpiRKGilrrivdrNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEILFDGMPLH 350
Cdd:PRK15056 3 QQAGIVVNDVTVTW--RNG--------HTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVrLASGKISILGQPTR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 351 RWNRRQMLPVRPRMQVVfqdpNSSLnPRLsVLQIVEEGLRVHQPGLS-AQQREQE-VMRVMVEVGLdPETRHRYPAEFSG 428
Cdd:PRK15056 73 QALQKNLVAYVPQSEEV----DWSF-PVL-VEDVVMMGRYGHMGWLRrAKKRDRQiVTAALARVDM-VEFRHRQIGELSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 429 GQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRqGEVVEQG 508
Cdd:PRK15056 146 GQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGK-TMLVSTHNLGSVTEFCDYTVMVK-GTVLASG 223
|
....*...
gi 1278835479 509 ECQRVFSA 516
Cdd:PRK15056 224 PTETTFTA 231
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
27-236 |
5.16e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 81.33 E-value: 5.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 27 DLTLQIQRGETLALVGESGSGKSvsalSILRLL-----PSppvsypQGDILFHDRSLL-HADEQTLRGIRgNKIAMIFQE 100
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKS----TIMQLLnglhvPT------QGSVRVDDTLITsTSKNKDIKQIR-KKVGLVFQF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 101 PmvslnplhslEKQLYEVLSL--------HRGMRKEAARGEILDCLERTGIRNAAKRLNdfPHQLSGGERQRVMIAMALL 172
Cdd:PRK13649 94 P----------ESQLFEETVLkdvafgpqNFGVSQEEAEALAREKLALVGISESLFEKN--PFELSGGQMRRVAIAGILA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1278835479 173 TRPELLIADEPTTALDVTVQAQILTLLRDLRdELNMSLLFITHNLSIVRKLADSVAVMQNGRCV 236
Cdd:PRK13649 162 MEPKILVLDEPTAGLDPKGRKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLV 224
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
14-236 |
5.50e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 83.94 E-value: 5.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 14 AFSKQDETRTVVSDLTLQIQRGETLALVGESGSGKSvSALSILRLLPSPPVSYpQGDILFHDRSLlHADEQTLRGirgnk 93
Cdd:TIGR00955 30 CFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKT-TLMNALAFRSPKGVKG-SGSVLLNGMPI-DAKEMRAIS----- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 94 iAMIFQEPMvsLNPLHSLEKQLY--EVLSLHRGMRKEAARGEILDCLERTGIRNAAKRLNDFPHQ---LSGGERQRVMIA 168
Cdd:TIGR00955 102 -AYVQQDDL--FIPTLTVREHLMfqAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGVPGRvkgLSGGERKRLAFA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1278835479 169 MALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGRCV 236
Cdd:TIGR00955 179 SELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVA 246
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
25-267 |
5.51e-17 |
|
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: 83.79 E-value: 5.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 25 VSDLTLQIQRGETLALVGESGSGKSvSALSILRLLPSPPVsypqGDILFHDRSLLHADEQTLRgirgNKIAMIFQEPMVs 104
Cdd:TIGR01192 351 VFDVSFEAKAGQTVAIVGPTGAGKT-TLINLLQRVYDPTV----GQILIDGIDINTVTRESLR----KSIATVFQDAGL- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 105 lnplhsLEKQLYEVLSLHRgmrKEAARGEILDCLERTGIRN-AAKRLNDFP-------HQLSGGERQRVMIAMALLTRPE 176
Cdd:TIGR01192 421 ------FNRSIRENIRLGR---EGATDEEVYEAAKAAAAHDfILKRSNGYDtlvgergNRLSGGERQRLAIARAILKNAP 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 177 LLIADEPTTALDVTVQAQILTLLRDLRDelNMSLLFITHNLSIVRKlADSVAVMQNGRCVEQNAASTLLSAPQHPY---- 252
Cdd:TIGR01192 492 ILVLDEATSALDVETEARVKNAIDALRK--NRTTFIIAHRLSTVRN-ADLVLFLDQGRLIEKGSFQELIQKDGRFYkllr 568
|
250
....*....|....*
gi 1278835479 253 TQRLLNSEPSGDPVP 267
Cdd:TIGR01192 569 RSGLLTNQPATKPLR 583
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
319-520 |
6.32e-17 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 82.23 E-value: 6.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 319 GESGSGKSTtglaLLRLIA-----SQGEILFDGMPLHRWNRRQMLPV-RPRMQVVFQDpnSSLNPRLSVlqivEEGLRVh 392
Cdd:PRK11144 31 GRSGAGKTS----LINAISgltrpQKGRIVLNGRVLFDAEKGICLPPeKRRIGYVFQD--ARLFPHYKV----RGNLRY- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 393 qpGLSAQQREQeVMRVMVEVGLDPETRhRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQ 472
Cdd:PRK11144 100 --GMAKSMVAQ-FDKIVALLGIEPLLD-RYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1278835479 473 EKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSAPTQR 520
Cdd:PRK11144 176 REINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSAMR 223
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
27-236 |
7.77e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 80.93 E-value: 7.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 27 DLTLQIQRGETLALVGESGSGKSVSALSILRLLPSPPVSYPQGDILFHDRSllhaDEQTLRGIRgNKIAMIFQEPmvsln 106
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTS----KQKEIKPVR-KKVGVVFQFP----- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 107 plhslEKQLYEVLSL--------HRGMRKEAARGEILDCLERTGIrnAAKRLNDFPHQLSGGERQRVMIAMALLTRPELL 178
Cdd:PRK13643 94 -----ESQLFEETVLkdvafgpqNFGIPKEKAEKIAAEKLEMVGL--ADEFWEKSPFELSGGQMRRVAIAGILAMEPEVL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1278835479 179 IADEPTTALDVTVQAQILTLLRDLRdELNMSLLFITHNLSIVRKLADSVAVMQNGRCV 236
Cdd:PRK13643 167 VLDEPTAGLDPKARIEMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEKGHII 223
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
307-518 |
1.04e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 79.59 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 307 FSLRPGESLGLVGESGSGKSTTGLALLRLIASQGEILFDGMPLHRWNRRQMlpVRPRMQVVFQDPNSSLNPrlsVLQIve 386
Cdd:PRK03695 17 AEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSGSIQFAGQPLEAWSAAEL--ARHRAYLSQQQTPPFAMP---VFQY-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 387 egLRVHQPGLSAQQREQEVMRVMVE-VGLDPETrHRYPAEFSGGQRQRIAIARALI-----LKPE--LIILDEPTSSLDR 458
Cdd:PRK03695 90 --LTLHQPDKTRTEAVASALNEVAEaLGLDDKL-GRSVNQLSGGEWQRVRLAAVVLqvwpdINPAgqLLLLDEPMNSLDV 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 459 TVQAQILALLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSAPT 518
Cdd:PRK03695 167 AQQAALDRLLSELCQQGI-AVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPEN 225
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
6-249 |
1.05e-16 |
|
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: 79.63 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 6 LRIDNLSIAFSKqdetRTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLLPSPpvsypQGDILFHDRSLLHA--DE 83
Cdd:TIGR04406 2 LVAENLIKSYKK----RKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPD-----AGKILIDGQDITHLpmHE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 84 QTLRGIrgnkiAMIFQEPmvSLNPLHSLEKQLYEVLSLHRGMRKEAARGEILDCLERTGIrnaaKRLNDFPHQ-LSGGER 162
Cdd:TIGR04406 73 RARLGI-----GYLPQEA--SIFRKLTVEENIMAVLEIRKDLDRAEREERLEALLEEFQI----SHLRDNKAMsLSGGER 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 163 QRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDElNMSLLFITHNLSIVRKLADSVAVMQNGRCVEQNAAS 242
Cdd:TIGR04406 142 RRVEIARALATNPKFILLDEPFAGVDPIAVGDIKKIIKHLKER-GIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPA 220
|
....*..
gi 1278835479 243 TLLSAPQ 249
Cdd:TIGR04406 221 EIVANEK 227
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
13-236 |
1.21e-16 |
|
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: 78.79 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 13 IAFSKQDETRTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLL-----PSppvsypQGDILF--HDRSLLHADEqt 85
Cdd:cd03245 8 VSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKS----TLLKLLaglykPT------SGSVLLdgTDIRQLDPAD-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 86 lrgIRGNkIAMIFQEPMVslnplhsLEKQLYEVLSLHRGMRKEAargEILDCLERTGIRNAAKRLndfPH---------- 155
Cdd:cd03245 76 ---LRRN-IGYVPQDVTL-------FYGTLRDNITLGAPLADDE---RILRAAELAGVTDFVNKH---PNgldlqigerg 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 156 -QLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDElnMSLLFITHNLSIVrKLADSVAVMQNGR 234
Cdd:cd03245 139 rGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGD--KTLIIITHRPSLL-DLVDRIIVMDSGR 215
|
..
gi 1278835479 235 CV 236
Cdd:cd03245 216 IV 217
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
302-515 |
1.24e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 80.44 E-value: 1.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 302 LKNIRFSLRPGESLGLVGESGSGKST-----TGLallrLIASQGEILFD--GMPLHRWNRRQMLPVRPRMQVVFQDPNSS 374
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTmiqltNGL----IISETGQTIVGdyAIPANLKKIKEVKRLRKEIGLVFQFPEYQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 375 LnprlsVLQIVEEGLRVHQPGLSAQQRE--QEVMRVMVEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPELIILDEP 452
Cdd:PRK13645 103 L-----FQETIEKDIAFGPVNLGENKQEayKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEP 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1278835479 453 TSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFS 515
Cdd:PRK13645 178 TGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFS 240
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
300-491 |
1.39e-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: 78.17 E-value: 1.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 300 PVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLHRwnrrqmLPVRPRMQVVFQDPNSS 374
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTT----LLRILAgllrpDSGEVRWNGTPLAE------QRDEPHENILYLGHLPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 375 LNPRLSVLqiveEGLRVHQPGLSAQQREqeVMRVMVEVGLDPETrHRYPAEFSGGQRQRIAIARALILKPELIILDEPTS 454
Cdd:TIGR01189 84 LKPELSAL----ENLHFWAAIHGGAQRT--IEDALAAVGLTGFE-DLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 1278835479 455 SLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRA 491
Cdd:TIGR01189 157 ALDKAGVALLAGLLRAHLARGGIVLLTTHQDLGLVEA 193
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
6-237 |
1.60e-16 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 78.96 E-value: 1.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 6 LRIDNLSIAFskqdETRTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLlPSPPVSypQGDILFHDRSLLH--ADE 83
Cdd:COG0396 1 LEIKNLHVSV----EGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGH-PKYEVT--SGSILLDGEDILElsPDE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 84 QTLRGIrgnkiAMIFQEPM----VSL-NPLH-SLEKQLYEVLSLhrgmrkEAARGEILDCLERTGIRNA-AKR-LNDfph 155
Cdd:COG0396 74 RARAGI-----FLAFQYPVeipgVSVsNFLRtALNARRGEELSA------REFLKLLKEKMKELGLDEDfLDRyVNE--- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 156 QLSGGERQRVMIA-MALLtRPELLIADEPTTALDVTVqAQILT-LLRDLRDElNMSLLFITHNLSIVRKL-ADSVAVMQN 232
Cdd:COG0396 140 GFSGGEKKRNEILqMLLL-EPKLAILDETDSGLDIDA-LRIVAeGVNKLRSP-DRGILIITHYQRILDYIkPDFVHVLVD 216
|
....*
gi 1278835479 233 GRCVE 237
Cdd:COG0396 217 GRIVK 221
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
271-529 |
1.60e-16 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 82.46 E-value: 1.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 271 DSTPLL--RVEDLSVSFPIRKGilrrivdrNPVLKNIRFSLRPGESLGLVGESGSGKSTtgLALLRL---IASQGEILFD 345
Cdd:PRK10790 332 DDRPLQsgRIDIDNVSFAYRDD--------NLVLQNINLSVPSRGFVALVGHTGSGKST--LASLLMgyyPLTEGEIRLD 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 346 GMPLHRWNRRQMlpvRPRMQVVFQDPnsslnprlsvlqIVEEGLRVHQPGLSAQQREQEVMRVMVEVGLD------PETR 419
Cdd:PRK10790 402 GRPLSSLSHSVL---RQGVAMVQQDP------------VVLADTFLANVTLGRDISEEQVWQALETVQLAelarslPDGL 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 420 HRYPAE----FSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLayIFISHDLQ-VVRAlcH 494
Cdd:PRK10790 467 YTPLGEqgnnLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTL--VVIAHRLStIVEA--D 542
|
250 260 270
....*....|....*....|....*....|....*...
gi 1278835479 495 QVIVLRQGEVVEQGECQRVFSAPT---QRYTRQLLSSD 529
Cdd:PRK10790 543 TILVLHRGQAVEQGTHQQLLAAQGrywQMYQLQLAGEE 580
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
12-234 |
1.73e-16 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 78.73 E-value: 1.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 12 SIAFSKQDETRTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLLP--SPPVSypqGDIlfhdrsllhadeqtlrgI 89
Cdd:cd03220 25 ILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKS----TLLRLLAgiYPPDS---GTV-----------------T 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 90 RGNKIAMIFqEPMVSLNPLHSLEKQLYEVLSLHrGMRKEAARGEILDCLERTGirnaakrLNDFPHQ----LSGGERQRV 165
Cdd:cd03220 81 VRGRVSSLL-GLGGGFNPELTGRENIYLNGRLL-GLSRKEIDEKIDEIIEFSE-------LGDFIDLpvktYSSGMKARL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1278835479 166 MIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDElNMSLLFITHNLSIVRKLADSVAVMQNGR 234
Cdd:cd03220 152 AFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGK 219
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
272-508 |
1.96e-16 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 79.26 E-value: 1.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 272 STPLLRVEDLSVSFpirKGILrrIVDrnpvlkNIRFSLRPGESLGLVGESGSGKST-----TGLallrLIASQGEILFDG 346
Cdd:PRK11300 2 SQPLLSVSGLMMRF---GGLL--AVN------NVNLEVREQEIVSLIGPNGAGKTTvfnclTGF----YKPTGGTILLRG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 347 MPLHRWNRRQMlpvrPRMQVV--FQdpnsslNPRLSVLQIVEEGLRVHQ---------PGL----SAQQREQEVM-RVMV 410
Cdd:PRK11300 67 QHIEGLPGHQI----ARMGVVrtFQ------HVRLFREMTVIENLLVAQhqqlktglfSGLlktpAFRRAESEALdRAAT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 411 ---EVGLDpETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQ 487
Cdd:PRK11300 137 wleRVGLL-EHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMK 215
|
250 260
....*....|....*....|.
gi 1278835479 488 VVRALCHQVIVLRQGEVVEQG 508
Cdd:PRK11300 216 LVMGISDRIYVVNQGTPLANG 236
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
7-238 |
2.00e-16 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 78.97 E-value: 2.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 7 RIDNLSiafsKQDETRTVVSDLTLQIQRGETLALVGESGSGKSvSALSIL-RLLPSPpvsypQGDILFHDRSLLHADEQT 85
Cdd:COG4604 3 EIKNVS----KRYGGKVVLDDVSLTIPKGGITALIGPNGAGKS-TLLSMIsRLLPPD-----SGEVLVDGLDVATTPSRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 86 LrgirGNKIAMIFQEPMVSLNplhslekqL--YEVLSL-----HRGMRKEAARGEI---LDCLERTGIRNAakrlndFPH 155
Cdd:COG4604 73 L----AKRLAILRQENHINSR--------LtvRELVAFgrfpySKGRLTAEDREIIdeaIAYLDLEDLADR------YLD 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGRC 235
Cdd:COG4604 135 ELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRV 214
|
...
gi 1278835479 236 VEQ 238
Cdd:COG4604 215 VAQ 217
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
301-508 |
2.34e-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: 2.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 301 VLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIASQ--------GEILFDGMPLHRWNrrqmlpVRPRMQVVFQDPN 372
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTT----LLDAISGRvegggttsGQILFNGQPRKPDQ------FQKCVAYVRQDDI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 373 --SSLNPRLSVLQIVEEGLRVHQPglSAQQREQEVMRVMVEVGLDPeTRHRYPAEFSGGQRQRIAIARALILKPELIILD 450
Cdd:cd03234 92 llPGLTVRETLTYTAILRLPRKSS--DAIRKKRVEDVLLRDLALTR-IGGNLVKGISGGERRRVSIAVQLLWDPKVLILD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1278835479 451 EPTSSLDRTVQAQILALLKGLQEKHRLAYIFIshdlqvvralcHQ-----------VIVLRQGEVVEQG 508
Cdd:cd03234 169 EPTSGLDSFTALNLVSTLSQLARRNRIVILTI-----------HQprsdlfrlfdrILLLSSGEIVYSG 226
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
297-465 |
2.45e-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: 82.65 E-value: 2.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 297 DRNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIASQGEILFDGMP-----LHRWnrRQMLPVRPRMQVVFQDP 371
Cdd:TIGR01271 1230 AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGEIQIDGVSwnsvtLQTW--RKAFGVIPQKVFIFSGT 1307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 372 -NSSLNPRlsvlqiveeglrvhqpglsAQQREQEVMRVMVEVGLDpETRHRYPAE-----------FSGGQRQRIAIARA 439
Cdd:TIGR01271 1308 fRKNLDPY-------------------EQWSDEEIWKVAEEVGLK-SVIEQFPDKldfvlvdggyvLSNGHKQLMCLARS 1367
|
170 180
....*....|....*....|....*.
gi 1278835479 440 LILKPELIILDEPTSSLDrTVQAQIL 465
Cdd:TIGR01271 1368 ILSKAKILLLDEPSAHLD-PVTLQII 1392
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
6-247 |
2.47e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 79.26 E-value: 2.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 6 LRIDNLSIAFSKqdetRTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLL-PSPPVSYPQGDILFHdrsllHADEQ 84
Cdd:PRK10253 8 LRGEQLTLGYGK----YTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMtPAHGHVWLDGEHIQH-----YASKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 85 TLRgirgnKIAMIFQEPM----VSLNPLhsLEKQLYEVLSLHRGMRKEAARGeILDCLERTGIRNAAKRLNDfphQLSGG 160
Cdd:PRK10253 79 VAR-----RIGLLAQNATtpgdITVQEL--VARGRYPHQPLFTRWRKEDEEA-VTKAMQATGITHLADQSVD---TLSGG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 161 ERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGRCVEQNA 240
Cdd:PRK10253 148 QRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGA 227
|
....*..
gi 1278835479 241 ASTLLSA 247
Cdd:PRK10253 228 PKEIVTA 234
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
15-236 |
3.16e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 79.75 E-value: 3.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 15 FSKQDETRTVVSDLTLQIQRGETLALVGESGSGKSvSALSILR--LLPSppvsypQGDILFHDRSLlHADEQTLRgirgN 92
Cdd:COG4586 28 FRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKS-TTIKMLTgiLVPT------SGEVRVLGYVP-FKRRKEFA----R 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 93 KIAMIF---QEPMVSLNPLHSLE--KQLYEV-LSLHRGMRKEAArgEILDclertgirnaakrLNDFPH----QLSGGER 162
Cdd:COG4586 96 RIGVVFgqrSQLWWDLPAIDSFRllKAIYRIpDAEYKKRLDELV--ELLD-------------LGELLDtpvrQLSLGQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1278835479 163 QRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGRCV 236
Cdd:COG4586 161 MRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRII 234
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
5-217 |
3.61e-16 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 78.20 E-value: 3.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 5 LLRIDNLSIAFSKqdetRTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLLpSPPVSYPQGDIlfhdrsllhadeq 84
Cdd:PRK11248 1 MLQISHLYADYGG----KPALEDINLTLESGELLVVLGPSGCGKT----TLLNLI-AGFVPYQHGSI------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 85 TLRGIR----GNKIAMIFQEPmvSLNPLHSLEKQLYEVLSLhRGMRKEAARGEILDCLERTGIRNAAKRlndFPHQLSGG 160
Cdd:PRK11248 59 TLDGKPvegpGAERGVVFQNE--GLLPWRNVQDNVAFGLQL-AGVEKMQRLEIAHQMLKKVGLEGAEKR---YIWQLSGG 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1278835479 161 ERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNL 217
Cdd:PRK11248 133 QRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
6-234 |
4.10e-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: 75.18 E-value: 4.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 6 LRIDNLSIAFSKqdetRTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLLpsppvsypQGDILfhdrsllhADEQT 85
Cdd:cd03221 1 IELENLSKTYGG----KLLLKDISLTINPGDRIGLVGRNGAGKS----TLLKLI--------AGELE--------PDEGI 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 86 LRGIRGNKIAMIfqepmvslnplhslekqlyevlslhrgmrkeaargeildclertgirnaakrlndfpHQLSGGERQRV 165
Cdd:cd03221 57 VTWGSTVKIGYF---------------------------------------------------------EQLSGGEKMRL 79
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1278835479 166 MIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDelnmSLLFITHNLSIVRKLADSVAVMQNGR 234
Cdd:cd03221 80 ALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPG----TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
300-505 |
4.17e-16 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 81.15 E-value: 4.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 300 PVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIAsqGEILFD-GmplhRWNRRQMLPVrPRMQvvfQDPnsslnPR 378
Cdd:PRK11147 17 PLLDNAELHIEDNERVCLVGRNGAGKST----LMKILN--GEVLLDdG----RIIYEQDLIV-ARLQ---QDP-----PR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 379 L---SVLQIVEEGL--------RVHQ-----------PGLSAQQREQEVM-------------RVMVEVGLDPETRHryp 423
Cdd:PRK11147 78 NvegTVYDFVAEGIeeqaeylkRYHDishlvetdpseKNLNELAKLQEQLdhhnlwqlenrinEVLAQLGLDPDAAL--- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 424 AEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEkhrlAYIFISHDLQVVRALCHQVIVLRQGE 503
Cdd:PRK11147 155 SSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG----SIIFISHDRSFIRNMATRIVDLDRGK 230
|
..
gi 1278835479 504 VV 505
Cdd:PRK11147 231 LV 232
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
5-248 |
4.88e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 78.49 E-value: 4.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 5 LLRIDNLSiaFSKQDETrTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLLPsppvsyPQ-GDILFhdRSLLHADE 83
Cdd:PRK13644 1 MIRLENVS--YSYPDGT-PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLR------PQkGKVLV--SGIDTGDF 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 84 QTLRGIRgNKIAMIFQEPmvslnplhslEKQLyevlsLHRGMRKEAARGEILDCLERTGIRNAAKR------LNDF---- 153
Cdd:PRK13644 70 SKLQGIR-KLVGIVFQNP----------ETQF-----VGRTVEEDLAFGPENLCLPPIEIRKRVDRalaeigLEKYrhrs 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 154 PHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRdELNMSLLFITHNLSIVRkLADSVAVMQNG 233
Cdd:PRK13644 134 PKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLH-EKGKTIVYITHNLEELH-DADRIIVMDRG 211
|
250
....*....|....*
gi 1278835479 234 RCVEQNAASTLLSAP 248
Cdd:PRK13644 212 KIVLEGEPENVLSDV 226
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
276-508 |
6.95e-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: 76.03 E-value: 6.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 276 LRVEDLSVSfpirkgilrriVDRNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALL---RLIASQGEILFDG-----M 347
Cdd:cd03217 1 LEIKDLHVS-----------VGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMghpKYEVTEGEILFKGeditdL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 348 PLHRWNRRQMLpvrprmqVVFQDPnsslnPRLsvlqiveEGLRVhqpglsaqqreQEVMRvMVEVGldpetrhrypaeFS 427
Cdd:cd03217 70 PPEERARLGIF-------LAFQYP-----PEI-------PGVKN-----------ADFLR-YVNEG------------FS 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 428 GGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRlAYIFISHDLQVVRALCHQVI-VLRQGEVVE 506
Cdd:cd03217 107 GGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREEGK-SVLIITHYQRLLDYIKPDRVhVLYDGRIVK 185
|
..
gi 1278835479 507 QG 508
Cdd:cd03217 186 SG 187
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
300-508 |
8.70e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 78.72 E-value: 8.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 300 PVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIA-SQGEILFDGMPLHRWNRRqmlpVRPRMQVVFQDPNssLNPR 378
Cdd:PRK13536 55 AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSpDAGKITVLGVPVPARARL----ARARIGVVPQFDN--LDLE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 379 LSVlqivEEGLRVHQP--GLSAQQREQEVMRVMVEVGLDPETRHRYpAEFSGGQRQRIAIARALILKPELIILDEPTSSL 456
Cdd:PRK13536 129 FTV----RENLLVFGRyfGMSTREIEAVIPSLLEFARLESKADARV-SDLSGGMKRRLTLARALINDPQLLILDEPTTGL 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1278835479 457 DRTVQAQILALLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:PRK13536 204 DPHARHLIWERLRSLLARGK-TILLTTHFMEEAERLCDRLCVLEAGRKIAEG 254
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
15-236 |
9.85e-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: 76.54 E-value: 9.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 15 FSKQDETRTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLLPSPPVSYpqGDILFHDRSLlHADEQTLRgirgnkI 94
Cdd:cd03234 13 AKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTS--GQILFNGQPR-KPDQFQKC------V 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 95 AMIFQEPMvsLNPLHSLEKQLY--EVLSLHRGMRKEAARGEILDCLER----TGIRNAAKRlndfphQLSGGERQRVMIA 168
Cdd:cd03234 84 AYVRQDDI--LLPGLTVRETLTytAILRLPRKSSDAIRKKRVEDVLLRdlalTRIGGNLVK------GISGGERRRVSIA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1278835479 169 MALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGRCV 236
Cdd:cd03234 156 VQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIV 223
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
6-237 |
1.01e-15 |
|
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: 75.91 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 6 LRIDNLSIAFSKqdETRTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLlpsppVSYPQGDILFHDRSLLHADEQT 85
Cdd:cd03369 7 IEVENLSVRYAP--DLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRF-----LEAEEGKIEIDGIDISTIPLED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 86 LRgirgNKIAMIFQEPMV-------SLNPL-HSLEKQLYEVLSLHRGmrkeaarGEildclertgirnaakrlndfphQL 157
Cdd:cd03369 80 LR----SSLTIIPQDPTLfsgtirsNLDPFdEYSDEEIYGALRVSEG-------GL----------------------NL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQIltlLRDLRDEL-NMSLLFITHNLSIVRKLaDSVAVMQNGRCV 236
Cdd:cd03369 127 SQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALI---QKTIREEFtNSTILTIAHRLRTIIDY-DKILVMDAGEVK 202
|
.
gi 1278835479 237 E 237
Cdd:cd03369 203 E 203
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
8-246 |
1.01e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 77.74 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 8 IDNLSIAFSKQD--ETRTVvSDLTLQIQRGETLALVGESGSGKSvsalSILRLLPSPPVSyPQGDILFHDRSLlHADEQT 85
Cdd:PRK13645 9 LDNVSYTYAKKTpfEFKAL-NNTSLTFKKNKVTCVIGTTGSGKS----TMIQLTNGLIIS-ETGQTIVGDYAI-PANLKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 86 LRGIRG--NKIAMIFQEPMVSLNPlHSLEKQLyEVLSLHRGMRKEAARGEILDCLERTGI-RNAAKRlndFPHQLSGGER 162
Cdd:PRK13645 82 IKEVKRlrKEIGLVFQFPEYQLFQ-ETIEKDI-AFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKR---SPFELSGGQK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 163 QRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGRCVEQNAAS 242
Cdd:PRK13645 157 RRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPF 236
|
....
gi 1278835479 243 TLLS 246
Cdd:PRK13645 237 EIFS 240
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
301-515 |
1.07e-15 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 76.86 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 301 VLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIA-SQGEILFDG-----MPLHRwnrrqmlpvRPRMQVVFQDPNSS 374
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPrDAGNIIIDDedislLPLHA---------RARRGIGYLPQEAS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 375 LNPRLSVLQIVEEGLRVHQpGLSAQQREQEVMRVMVEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTS 454
Cdd:PRK10895 89 IFRRLSVYDNLMAVLQIRD-DLSAEQREDRANELMEEFHIE-HLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1278835479 455 SLDRTVQAQILALLKGLQEkHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFS 515
Cdd:PRK10895 167 GVDPISVIDIKRIIEHLRD-SGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
156-457 |
1.10e-15 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 79.67 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDElNMSLLFITHNLSIVRKLADSVAVMQNGRC 235
Cdd:PRK10938 135 YLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTL 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 236 VEQNAASTLLS---APQHPYTQRLLNS------EPSGDPvPLDADsTPLLRVEDLSVSFpirkgilrrivDRNPVLKNIR 306
Cdd:PRK10938 214 AETGEREEILQqalVAQLAHSEQLEGVqlpepdEPSARH-ALPAN-EPRIVLNNGVVSY-----------NDRPILHNLS 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 307 FSLRPGESLGLVGESGSGKSTtglaLLRLIAS---QGE----ILFD---GMPLHRWN-RRQMLPVRPRMQVVFQDPNSSL 375
Cdd:PRK10938 281 WQVNPGEHWQIVGPNGAGKST----LLSLITGdhpQGYsndlTLFGrrrGSGETIWDiKKHIGYVSSSLHLDYRVSTSVR 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 376 NPRLS-------VLQIVeeglrvhqpglSAQQReQEVMRVMVEVGLDPETRHRYPAEFSGGQrQRIA-IARALILKPELI 447
Cdd:PRK10938 357 NVILSgffdsigIYQAV-----------SDRQQ-KLAQQWLDILGIDKRTADAPFHSLSWGQ-QRLAlIVRALVKHPTLL 423
|
330
....*....|
gi 1278835479 448 ILDEPTSSLD 457
Cdd:PRK10938 424 ILDEPLQGLD 433
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
30-277 |
1.13e-15 |
|
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: 76.04 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 30 LQIQRGETLALVGESGSGKSVSALSILRLLPSPpvsypQGDILFHDRSllhadeqtlRGIRGNKIAMIFQEPMVSLNPLH 109
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPA-----KGTVKVAGAS---------PGKGWRHIGYVPQRHEFAWDFPI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 110 SLEKQLYEVLSLHRGMRKEAARGE---ILDCLERTGIRNAAKRLNDfphQLSGGERQRVMIAMALLTRPELLIADEPTTA 186
Cdd:TIGR03771 67 SVAHTVMSGRTGHIGWLRRPCVADfaaVRDALRRVGLTELADRPVG---ELSGGQRQRVLVARALATRPSVLLLDEPFTG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 187 LDVTVQAQILTLLRDLRDElNMSLLFITHNLSIVRKLADSVaVMQNGRCVEQNAASTLLSApqHPYTQRLLNSepsgdpv 266
Cdd:TIGR03771 144 LDMPTQELLTELFIELAGA-GTAILMTTHDLAQAMATCDRV-VLLNGRVIADGTPQQLQDP--APWMTTFGVS------- 212
|
250
....*....|.
gi 1278835479 267 pldaDSTPLLR 277
Cdd:TIGR03771 213 ----DSSPLLR 219
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-248 |
1.33e-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: 76.04 E-value: 1.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 6 LRIDNLSiafsKQDETRTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLlpsppVSYPQGDILF--HDRSLLHADE 83
Cdd:cd03218 1 LRAENLS----KRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGL-----VKPDSGKILLdgQDITKLPMHK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 84 QTLRGIrgnkiAMIFQEPMV--SLnplhSLEKQLYEVLSLHRGMRKEAARgEILDCLERTGIRNAAKRLNDfphQLSGGE 161
Cdd:cd03218 72 RARLGI-----GYLPQEASIfrKL----TVEENILAVLEIRGLSKKEREE-KLEELLEEFHITHLRKSKAS---SLSGGE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 162 RQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDeLNMSLLFITHNLSIVRKLADSVAVMQNGRCVEQNAA 241
Cdd:cd03218 139 RRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKD-RGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTP 217
|
....*..
gi 1278835479 242 STLLSAP 248
Cdd:cd03218 218 EEIAANE 224
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
5-489 |
1.34e-15 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 79.61 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 5 LLRIDNLSIAFSKQ---DETrtvvsDLTlqIQRGETLALVGESGSGKSvSALSIL--------------------RLLPS 61
Cdd:PRK11147 3 LISIHGAWLSFSDApllDNA-----ELH--IEDNERVCLVGRNGAGKS-TLMKILngevllddgriiyeqdlivaRLQQD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 62 PP-------VSY------PQGDIL--FHDRSLLHADEQTLRGIrgNKIAmifqepmvslnplhslekQLYEVLSLHRGMR 126
Cdd:PRK11147 75 PPrnvegtvYDFvaegieEQAEYLkrYHDISHLVETDPSEKNL--NELA------------------KLQEQLDHHNLWQ 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 127 KEAargEILDCLERTGIrNAAKRLNDfphqLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDel 206
Cdd:PRK11147 135 LEN---RINEVLAQLGL-DPDAALSS----LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG-- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 207 nmSLLFITHNLSIVRKLADSVAVMQNGRcveqnaastLLSAPQHpYTQRLLNSEPSgdpvpldadstplLRVEDL-SVSF 285
Cdd:PRK11147 205 --SIIFISHDRSFIRNMATRIVDLDRGK---------LVSYPGN-YDQYLLEKEEA-------------LRVEELqNAEF 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 286 P---------IRKGI----------------LRR------------------------IV-----------DRNpVLKNI 305
Cdd:PRK11147 260 DrklaqeevwIRQGIkarrtrnegrvralkaLRRerserrevmgtakmqveeasrsgkIVfemenvnyqidGKQ-LVKDF 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 306 RFSLRPGESLGLVGESGSGKSTtglaLLRLIAsqGEILFDGMPLHrwnrrqmlpVRPRMQVVFQDP-NSSLNPRLSVLQI 384
Cdd:PRK11147 339 SAQVQRGDKIALIGPNGCGKTT----LLKLML--GQLQADSGRIH---------CGTKLEVAYFDQhRAELDPEKTVMDN 403
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 385 VEEGlrvhqpglsaqqrEQEVMrvmveVG-------------LDPETRHRYPAE-FSGGQRQRIAIARaLILKP-ELIIL 449
Cdd:PRK11147 404 LAEG-------------KQEVM-----VNgrprhvlgylqdfLFHPKRAMTPVKaLSGGERNRLLLAR-LFLKPsNLLIL 464
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1278835479 450 DEPTSSLDrtvqAQILALLKGLQEKHRLAYIFISHDLQVV 489
Cdd:PRK11147 465 DEPTNDLD----VETLELLEELLDSYQGTVLLVSHDRQFV 500
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
273-501 |
1.66e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 76.31 E-value: 1.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 273 TPLLRVEDLSVSFPIRKgilrrivdrnpVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIA-SQGEILfdgmplhr 351
Cdd:PRK09544 2 TSLVSLENVSVSFGQRR-----------VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVApDEGVIK-------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 352 wnRRQMLPVRPRMQVVFQDPNSSLNprlsvlqiVEEGLRVHqPGLSAQQREQEVMRVMVEVGLDPETRhrypaEFSGGQR 431
Cdd:PRK09544 63 --RNGKLRIGYVPQKLYLDTTLPLT--------VNRFLRLR-PGTKKEDILPALKRVQAGHLIDAPMQ-----KLSGGET 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 432 QRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQ 501
Cdd:PRK09544 127 QRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-247 |
1.77e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 76.85 E-value: 1.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 1 MTQPLLRIDNLSIAFSKqdeTRTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLlpsppVSYPQGDIlfhdrSLLH 80
Cdd:PRK15056 2 MQQAGIVVNDVTVTWRN---GHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGF-----VRLASGKI-----SILG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 81 adEQTLRGIRGNKIAMIFQEPMVSLNPLHSLEKQLYEVLSLHRGMRKEAA---RGEILDCLERTGirnaakrLNDFPH-- 155
Cdd:PRK15056 69 --QPTRQALQKNLVAYVPQSEEVDWSFPVLVEDVVMMGRYGHMGWLRRAKkrdRQIVTAALARVD-------MVEFRHrq 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 156 --QLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDElNMSLLFITHNLSIVRKLADsVAVMQNG 233
Cdd:PRK15056 140 igELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCD-YTVMVKG 217
|
250
....*....|....
gi 1278835479 234 RCVEQNAASTLLSA 247
Cdd:PRK15056 218 TVLASGPTETTFTA 231
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
13-254 |
1.82e-15 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 79.29 E-value: 1.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 13 IAFSKQDETRTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLlpsppvsYP--QGDILFHDRSLlhaDEQTLRGIR 90
Cdd:PRK11176 347 VTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRF-------YDidEGEILLDGHDL---RDYTLASLR 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 91 gNKIAMIFQEpmVSL------NPLHSLEKQLYEvlslhRGMRKEAARG----EILDCLER---TGI-RNAAkrlndfphQ 156
Cdd:PRK11176 417 -NQVALVSQN--VHLfndtiaNNIAYARTEQYS-----REQIEEAARMayamDFINKMDNgldTVIgENGV--------L 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLrdlrDEL--NMSLLFITHNLSIVRKlADSVAVMQNGR 234
Cdd:PRK11176 481 LSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAAL----DELqkNRTSLVIAHRLSTIEK-ADEILVVEDGE 555
|
250 260
....*....|....*....|
gi 1278835479 235 CVEQNAASTLLsAPQHPYTQ 254
Cdd:PRK11176 556 IVERGTHAELL-AQNGVYAQ 574
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
28-249 |
2.38e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 75.74 E-value: 2.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 28 LTLQIQRGETLALVGESGSGKSVSALSILRLLPSPpvsypqGDILFHDRSLLHADEQTLRGIRgnkiAMIFQepmvSLNP 107
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGS------GSIQFAGQPLEAWSAAELARHR----AYLSQ----QQTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 108 LHSLEKQLYEVLSLHRGMRKEAARGEILDCLERTGIrnaAKRLNDFPHQLSGGERQRVMIAMALL-----TRPE--LLIA 180
Cdd:PRK03695 81 PFAMPVFQYLTLHQPDKTRTEAVASALNEVAEALGL---DDKLGRSVNQLSGGEWQRVRLAAVVLqvwpdINPAgqLLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1278835479 181 DEPTTALDVTVQAQILTLLRDLRdELNMSLLFITHNLSIVRKLADSVAVMQNGRCVEQNAASTLLSAPQ 249
Cdd:PRK03695 158 DEPMNSLDVAQQAALDRLLSELC-QQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPEN 225
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
223-506 |
2.93e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 79.40 E-value: 2.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 223 LADSVAVMQNGRCVEQNA-AST-------------LLSApqhpyTQRL-------LNS-EPSGDPVPLDADSTPLlrVED 280
Cdd:PLN03130 1153 LTASFAVMQNGRAENQAAfASTmglllsyalnitsLLTA-----VLRLaslaensLNAvERVGTYIDLPSEAPLV--IEN 1225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 281 --------LSVSFPIRKGILRRIVDRNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIA-SQGEILFDGMPLHR 351
Cdd:PLN03130 1226 nrpppgwpSSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVElERGRILIDGCDISK 1305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 352 ---WNRRQMLPVRPRMQVVFQ-------DPNSSLNPrlsvLQIVEEGLRVHQpglsaqqreQEVMRvMVEVGLDPETrhr 421
Cdd:PLN03130 1306 fglMDLRKVLGIIPQAPVLFSgtvrfnlDPFNEHND----ADLWESLERAHL---------KDVIR-RNSLGLDAEV--- 1368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 422 ypAE----FSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQIlalLKGLQEKHR-LAYIFISHDLQVVRAlCHQV 496
Cdd:PLN03130 1369 --SEagenFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALI---QKTIREEFKsCTMLIIAHRLNTIID-CDRI 1442
|
330
....*....|
gi 1278835479 497 IVLRQGEVVE 506
Cdd:PLN03130 1443 LVLDAGRVVE 1452
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
22-201 |
3.33e-15 |
|
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: 74.32 E-value: 3.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 22 RTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLLP--SPPVSypqGDILFHDRSLlhadeQTLRGIRGNKIAMIFQ 99
Cdd:TIGR01189 13 RMLFEGLSFTLNAGEALQVTGPNGIGKT----TLLRILAglLRPDS---GEVRWNGTPL-----AEQRDEPHENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 100 EPmvSLNPLHSLEKQLYEVLSLHRGmrkeaARGEILDCLERTGIRNAAKRLndfPHQLSGGERQRVMIAMALLTRPELLI 179
Cdd:TIGR01189 81 LP--GLKPELSALENLHFWAAIHGG-----AQRTIEDALAAVGLTGFEDLP---AAQLSAGQQRRLALARLWLSRRPLWI 150
|
170 180
....*....|....*....|..
gi 1278835479 180 ADEPTTALDVTVQAQILTLLRD 201
Cdd:TIGR01189 151 LDEPTTALDKAGVALLAGLLRA 172
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
272-508 |
3.44e-15 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 75.45 E-value: 3.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 272 STPLLRVEDLSVSfpirkgilrriVDRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIAS-------QGEILF 344
Cdd:CHL00131 4 NKPILEIKNLHAS-----------VNENEILKGLNLSINKGEIHAIMGPNGSGKST----LSKVIAGhpaykilEGDILF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 345 DGmplhrwnrRQMLPVRPRMQ------VVFQDP----------------NS--------SLNPrLSVLQIVEEGLRVhqp 394
Cdd:CHL00131 69 KG--------ESILDLEPEERahlgifLAFQYPieipgvsnadflrlayNSkrkfqglpELDP-LEFLEIINEKLKL--- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 395 glsaqqreqevmrvmveVGLDPETRHRYPAE-FSGGQRQRIAIARALILKPELIILDEPTSSLD----RTVQAQILALLK 469
Cdd:CHL00131 137 -----------------VGMDPSFLSRNVNEgFSGGEKKRNEILQMALLDSELAILDETDSGLDidalKIIAEGINKLMT 199
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1278835479 470 glQEKhrlAYIFISHdLQvvRALCH----QVIVLRQGEVVEQG 508
Cdd:CHL00131 200 --SEN---SIILITH-YQ--RLLDYikpdYVHVMQNGKIIKTG 234
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
15-234 |
5.43e-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: 74.68 E-value: 5.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 15 FSKQDETRTVVSDLTLQIQRGETLALVGESGSGKSvSALSILRLLPSPPvsypQGDILFHDRSLLHADEQTLRgirgnKI 94
Cdd:cd03267 27 FKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKT-TTLKILSGLLQPT----SGEVRVAGLVPWKRRKKFLR-----RI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 95 AMIF-QEPMVS--LNPLHSLE--KQLYEVLSLHRGMRKEaargEILDCLERTGIRNAAKRlndfphQLSGGERQRVMIAM 169
Cdd:cd03267 97 GVVFgQKTQLWwdLPVIDSFYllAAIYDLPPARFKKRLD----ELSELLDLEELLDTPVR------QLSLGQRMRAEIAA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1278835479 170 ALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGR 234
Cdd:cd03267 167 ALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGR 231
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
8-267 |
5.51e-15 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 75.19 E-value: 5.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 8 IDNLSIAFSKQDetRTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLLPS--PPVSypqGDILFHDRSLLHADEQT 85
Cdd:PRK11831 8 VDMRGVSFTRGN--RCIFDNISLTVPRGKITAIMGPSGIGKT----TLLRLIGGqiAPDH---GEILFDGENIPAMSRSR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 86 LRGIRgNKIAMIFQEP--MVSLNPLHSLEKQLYEvlslHRGMRKEAARGEILDCLERTGIRNAAKRLndfPHQLSGGERQ 163
Cdd:PRK11831 79 LYTVR-KRMSMLFQSGalFTDMNVFDNVAYPLRE----HTQLPAPLLHSTVMMKLEAVGLRGAAKLM---PSELSGGMAR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 164 RVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGRCVEQNAAST 243
Cdd:PRK11831 151 RAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQA 230
|
250 260
....*....|....*....|....
gi 1278835479 244 lLSAPQHPYTQRLLNSEPSGdPVP 267
Cdd:PRK11831 231 -LQANPDPRVRQFLDGIADG-PVP 252
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
6-215 |
6.11e-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: 72.57 E-value: 6.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 6 LRIDNLSIAfskQDETRTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLL----PsppvsYPQGDILFHdrsllha 81
Cdd:cd03223 1 IELENLSLA---TPDGRVLLKDLSFEIKPGDRLLITGPSGTGKS----SLFRALaglwP-----WGSGRIGMP------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 82 deqtlrgiRGNKIAMIFQEPMVslnPLHSLEKQLYevlslhrgmrkeaargeildclertgirnaakrlndFP--HQLSG 159
Cdd:cd03223 62 --------EGEDLLFLPQRPYL---PLGTLREQLI------------------------------------YPwdDVLSG 94
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1278835479 160 GERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRdelnMSLLFITH 215
Cdd:cd03223 95 GEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELG----ITVISVGH 146
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-237 |
6.71e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 77.03 E-value: 6.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 4 PLLRIDNLSIAFskqdETRTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLLpsppvsypQGDilfhdrslLHADE 83
Cdd:COG0488 314 KVLELEGLSKSY----GDKTLLDDLSLRIDRGDRIGLIGPNGAGKS----TLLKLL--------AGE--------LEPDS 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 84 QTLRgiRGN--KIAMIFQEPMvSLNPlhslEKQLYEVLS-LHRGMRKEAARGeildCLERTGIRNAakRLNDFPHQLSGG 160
Cdd:COG0488 370 GTVK--LGEtvKIGYFDQHQE-ELDP----DKTVLDELRdGAPGGTEQEVRG----YLGRFLFSGD--DAFKPVGVLSGG 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 161 ERQRVMIAMALLTRPELLIADEPTTALDVtvqaqiltllrDLRDELNMSL-------LFITHNLSIVRKLADSVAVMQNG 233
Cdd:COG0488 437 EKARLALAKLLLSPPNVLLLDEPTNHLDI-----------ETLEALEEALddfpgtvLLVSHDRYFLDRVATRILEFEDG 505
|
....
gi 1278835479 234 RCVE 237
Cdd:COG0488 506 GVRE 509
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
22-248 |
6.98e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 74.82 E-value: 6.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 22 RTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLLP--SPPVSypqGDILFHDRSLLHADEQTLrgirGNKIAMIFQ 99
Cdd:PRK10575 24 RTLLHPLSLTFPAGKVTGLIGHNGSGKS----TLLKMLGrhQPPSE---GEILLDAQPLESWSSKAF----ARKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 100 EpmvsLNPLHSLekQLYEVLSLHR-------GMRKEAARGEILDCLERTGIRNAAKRLNDfphQLSGGERQRVMIAMALL 172
Cdd:PRK10575 93 Q----LPAAEGM--TVRELVAIGRypwhgalGRFGAADREKVEEAISLVGLKPLAHRLVD---SLSGGERQRAWIAMLVA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1278835479 173 TRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGRCVEQNAASTLLSAP 248
Cdd:PRK10575 164 QDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-246 |
7.72e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 74.15 E-value: 7.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 1 MTQPLLRIDNLSIAFSKQDetrtVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLLPSPPVSyPQGDILFHDRSLlh 80
Cdd:PRK11614 1 MEKVMLSFDKVSAHYGKIQ----ALHEVSLHINQGEIVTLIGANGAGKT----TLLGTLCGDPRA-TSGRIVFDGKDI-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 81 ADEQTLRGIRgNKIAM------IFQEPMVSLNPLHS---LEKQLYEvlslhrgMRKEAARGEILDCLERTGIRNAAkrln 151
Cdd:PRK11614 70 TDWQTAKIMR-EAVAIvpegrrVFSRMTVEENLAMGgffAERDQFQ-------ERIKWVYELFPRLHERRIQRAGT---- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 152 dfphqLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDElNMSLLFITHNLSIVRKLADSVAVMQ 231
Cdd:PRK11614 138 -----MSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLE 211
|
250
....*....|....*
gi 1278835479 232 NGRCVEQNAASTLLS 246
Cdd:PRK11614 212 NGHVVLEDTGDALLA 226
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
8-245 |
1.04e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 74.39 E-value: 1.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 8 IDNLSiaFSKQDETRTVvSDLTLQIQRGETLALVGESGSGKSVSALSILRL-LPSppvsypQGDILFHDRSLLHADEQTL 86
Cdd:PRK13647 7 VEDLH--FRYKDGTKAL-KGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIyLPQ------RGRVKVMGREVNAENEKWV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 87 RgirgNKIAMIFQEPMVSLNPLHSLEKQLYEVLSLhrGMRKEaargEILdclERTGIRNAAKRLNDF----PHQLSGGER 162
Cdd:PRK13647 78 R----SKVGLVFQDPDDQVFSSTVWDDVAFGPVNM--GLDKD----EVE---RRVEEALKAVRMWDFrdkpPYHLSYGQK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 163 QRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDElNMSLLFITHNLSIVRKLADSVAVMQNGRCVEQNAAS 242
Cdd:PRK13647 145 KRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKS 223
|
...
gi 1278835479 243 TLL 245
Cdd:PRK13647 224 LLT 226
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
302-506 |
1.09e-14 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 76.37 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 302 LKNIRFSLRPGESLGLVGESGSGKSTtglalLRLIAS--------QGEILFDGMPLHrwnrrqmlpvrprmqvvFQDPNS 373
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKST-----LMKVLSgvyphgsyEGEILFDGEVCR-----------------FKDIRD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 374 S-------------LNPRLSVLQIVEEGLRVHQPGL----SAQQREQEVMRvmvEVGLD--PETRhryPAEFSGGQRQRI 434
Cdd:NF040905 75 SealgiviihqelaLIPYLSIAENIFLGNERAKRGVidwnETNRRARELLA---KVGLDesPDTL---VTDIGVGKQQLV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1278835479 435 AIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEkHRLAYIFISHDLQVVRALCHQVIVLRQGEVVE 506
Cdd:NF040905 149 EIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKA-QGITSIIISHKLNEIRRVADSITVLRDGRTIE 219
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
300-506 |
1.11e-14 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 74.17 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 300 PVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEILFDG-----MPLHrwnrrqmlPVRPRMQVVFQDP-- 371
Cdd:cd03288 35 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVdIFDGKIVIDGidiskLPLH--------TLRSRLSIILQDPil 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 372 -----NSSLNPRLSVL-QIVEEGLRVHQPGLSAQQREQEVMRVMVEVGldpetrhrypAEFSGGQRQRIAIARALILKPE 445
Cdd:cd03288 107 fsgsiRFNLDPECKCTdDRLWEALEIAQLKNMVKSLPGGLDAVVTEGG----------ENFSVGQRQLFCLARAFVRKSS 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1278835479 446 LIILDEPTSSLDrtvqaqiLALLKGLQEKHRLAY-----IFISHDLQVVRAlCHQVIVLRQGEVVE 506
Cdd:cd03288 177 ILIMDEATASID-------MATENILQKVVMTAFadrtvVTIAHRVSTILD-ADLVLVLSRGILVE 234
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
292-485 |
1.56e-14 |
|
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: 76.13 E-value: 1.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 292 LRRIVDRN-PVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILF-DGMplhrwnRRQMLPvrprm 364
Cdd:TIGR03719 10 VSKVVPPKkEILKDISLSFFPGAKIGVLGLNGAGKST----LLRIMAgvdkdFNGEARPqPGI------KVGYLP----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 365 qvvfQDPnsSLNPRLSVLQIVEEGLrvhQPGLSAQQREQEVMRVMVEV----------------------GLDPETR--- 419
Cdd:TIGR03719 75 ----QEP--QLDPTKTVRENVEEGV---AEIKDALDRFNEISAKYAEPdadfdklaaeqaelqeiidaadAWDLDSQlei 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 420 ----HRYP------AEFSGGQRQRIAIARALILKPELIILDEPTSSLDrtvqAQILALLkglqEKHRLAY----IFISHD 485
Cdd:TIGR03719 146 amdaLRCPpwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD----AESVAWL----ERHLQEYpgtvVAVTHD 217
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
28-248 |
2.48e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 75.65 E-value: 2.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 28 LTLQIQRGETLALVGESGSGKS--VSALsiLRLLPsppvsYpQGDILFHDRSLLHADEQTLRgirgNKIAMIFQEPmvsl 105
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTslLNAL--LGFLP-----Y-QGSLKINGIELRELDPESWR----KHLSWVGQNP---- 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 106 nplHSLEKQLYEVLSLHRgmrKEAARGEILDCLERTGIRNAAKRLN---DFPHQ-----LSGGERQRVMIAMALLTRPEL 177
Cdd:PRK11174 433 ---QLPHGTLRDNVLLGN---PDASDEQLQQALENAWVSEFLPLLPqglDTPIGdqaagLSVGQAQRLALARALLQPCQL 506
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1278835479 178 LIADEPTTALDVTVQAQILTLLRDLRdeLNMSLLFITHNLSIVRKLaDSVAVMQNGRCVEQNAASTLLSAP 248
Cdd:PRK11174 507 LLLDEPTASLDAHSEQLVMQALNAAS--RRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
301-509 |
2.53e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 75.69 E-value: 2.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 301 VLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIASQGeilFDGMPLHRwNRRQMLPVRPRMQVVFQDpnSSLNPRLS 380
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNN---FTGTILAN-NRKPTKQILKRTGFVTQD--DILYPHLT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 381 VLQ--IVEEGLRVHQpGLSAQQREQEVMRVMVEVGL----DPETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTS 454
Cdd:PLN03211 157 VREtlVFCSLLRLPK-SLTKQEKILVAESVISELGLtkceNTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTS 235
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1278835479 455 SLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGE 509
Cdd:PLN03211 236 GLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGK 290
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
301-508 |
3.95e-14 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 75.59 E-value: 3.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 301 VLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEILFDGMPLH----RWNRRQ--MLPVRPrmqVVFQDpns 373
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVeVCGGEIRVNGREIGayglRELRRQfsMIPQDP---VLFDG--- 1398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 374 slnprlSVLQIVEeglrvhqPGLSAQqrEQEVMRVMVEVGLdpetRHRYPAE--------------FSGGQRQRIAIARA 439
Cdd:PTZ00243 1399 ------TVRQNVD-------PFLEAS--SAEVWAALELVGL----RERVASEsegidsrvleggsnYSVGQRQLMCMARA 1459
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1278835479 440 LILKPE-LIILDEPTSS----LDRTVQAQILALLKglqekhrlAY--IFISHDLQVVrALCHQVIVLRQGEVVEQG 508
Cdd:PTZ00243 1460 LLKKGSgFILMDEATANidpaLDRQIQATVMSAFS--------AYtvITIAHRLHTV-AQYDKIIVMDHGAVAEMG 1526
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-238 |
4.15e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 72.04 E-value: 4.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 1 MTQpLLRIDNLSIAF------------------SKQDETRTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLL--- 59
Cdd:COG1134 1 MSS-MIEVENVSKSYrlyhepsrslkelllrrrRTRREEFWALKDVSFEVERGESVGIIGRNGAGKS----TLLKLIagi 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 60 --PSppvsypQGDILfhdrsllhadeqtlrgIRGnKIAMIFqEPMVSLNPLHSLEKQLYEVLSLHrGMRKEAARGEILDC 137
Cdd:COG1134 76 lePT------SGRVE----------------VNG-RVSALL-ELGAGFHPELTGRENIYLNGRLL-GLSRKEIDEKFDEI 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 138 LERTGIRnaakrlnDFPHQ----LSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDElNMSLLFI 213
Cdd:COG1134 131 VEFAELG-------DFIDQpvktYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFV 202
|
250 260
....*....|....*....|....*
gi 1278835479 214 THNLSIVRKLADSVAVMQNGRCVEQ 238
Cdd:COG1134 203 SHSMGAVRRLCDRAIWLEKGRLVMD 227
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-234 |
4.50e-14 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 72.33 E-value: 4.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 1 MTQPLLRIDNLSIAFSKQdetrTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLL-----PSppvsypQGDILFhd 75
Cdd:PRK11300 1 MSQPLLSVSGLMMRFGGL----LAVNNVNLEVREQEIVSLIGPNGAGKT----TVFNCLtgfykPT------GGTILL-- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 76 rsllhaDEQTLRGIRGNKIAM-----------IFQEPMVSLNPLHSLEKQLYEvlSLHRGMRKEAA----RGEILD---- 136
Cdd:PRK11300 65 ------RGQHIEGLPGHQIARmgvvrtfqhvrLFREMTVIENLLVAQHQQLKT--GLFSGLLKTPAfrraESEALDraat 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 137 CLERTGIRNAAKRLNDfphQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHN 216
Cdd:PRK11300 137 WLERVGLLEHANRQAG---NLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHD 213
|
250
....*....|....*...
gi 1278835479 217 LSIVRKLADSVAVMQNGR 234
Cdd:PRK11300 214 MKLVMGISDRIYVVNQGT 231
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
16-236 |
8.02e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 74.15 E-value: 8.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 16 SKQDETRTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLLPSPPVSypqGDILFHDRSLlhaDEQTLRgirgnKIA 95
Cdd:PLN03211 75 TRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFT---GTILANNRKP---TKQILK-----RTG 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 96 MIFQEPMvsLNPLHSLEKQLY--EVLSLHRGMRKEAARGEILDCLERTGIRNAAKRL--NDFPHQLSGGERQRVMIAMAL 171
Cdd:PLN03211 144 FVTQDDI--LYPHLTVRETLVfcSLLRLPKSLTKQEKILVAESVISELGLTKCENTIigNSFIRGISGGERKRVSIAHEM 221
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1278835479 172 LTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGRCV 236
Cdd:PLN03211 222 LINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCL 286
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
301-491 |
9.35e-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: 70.21 E-value: 9.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 301 VLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLHRwnrrqmlpVRPRMQ--VVFQDPNS 373
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTT----LLRILAglsppLAGRVLLNGGPLDF--------QRDSIArgLLYLGHAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 374 SLNPRLSVLqiveEGLRVHQPGLSAQQREQevmrVMVEVGLDPeTRHRYPAEFSGGQRQRIAIARALILKPELIILDEPT 453
Cdd:cd03231 83 GIKTTLSVL----ENLRFWHADHSDEQVEE----ALARVGLNG-FEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPT 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 1278835479 454 SSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRA 491
Cdd:cd03231 154 TALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEA 191
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
300-508 |
9.88e-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: 69.98 E-value: 9.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 300 PVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIASQ--------GEILFDGMPLHRWNRRqmlpvrPRMQVVFQDP 371
Cdd:cd03233 21 PILKDFSGVVKPGEMVLVLGRPGSGCST----LLKALANRtegnvsveGDIHYNGIPYKEFAEK------YPGEIIYVSE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 372 NSSLNPRLSVLQIVEeglrvhqpgLSAQQREQEVMRVmvevgldpetrhrypaeFSGGQRQRIAIARALILKPELIILDE 451
Cdd:cd03233 91 EDVHFPTLTVRETLD---------FALRCKGNEFVRG-----------------ISGGERKRVSIAEALVSRASVLCWDN 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1278835479 452 PTSSLDRTVQAQILALLKGLQEKHRLAYIF-ISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:cd03233 145 STRGLDSSTALEILKCIRTMADVLKTTTFVsLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
301-505 |
1.00e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 70.68 E-value: 1.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 301 VLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEILFDGMPLHRWNR----RQMLPVRPRMQVVFQdp 371
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTT----LLGTLcgdprATSGRIVFDGKDITDWQTakimREAVAIVPEGRRVFS-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 372 nsslnpRLSVlqivEEGLRVHQPGLSAQQREQEVMRVMvevGLDP---ETRHRYPAEFSGGQRQRIAIARALILKPELII 448
Cdd:PRK11614 94 ------RMTV----EENLAMGGFFAERDQFQERIKWVY---ELFPrlhERRIQRAGTMSGGEQQMLAIGRALMSQPRLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1278835479 449 LDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRaLCHQVIVLRQGEVV 505
Cdd:PRK11614 161 LDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALK-LADRGYVLENGHVV 216
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
288-508 |
1.31e-13 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 73.83 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 288 RKGILRRIVDRNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEILFDGMPLHRWNRRQMlpvRPRMQV 366
Cdd:TIGR00957 1288 RNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINeSAEGEIIIDGLNIAKIGLHDL---RFKITI 1364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 367 VFQDPnsslnprlsvlqIVEEG-LRVHQPGLSAQQREQ-----EVMRVMVEVGLDPETRHRYPAE----FSGGQRQRIAI 436
Cdd:TIGR00957 1365 IPQDP------------VLFSGsLRMNLDPFSQYSDEEvwwalELAHLKTFVSALPDKLDHECAEggenLSVGQRQLVCL 1432
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1278835479 437 ARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKhrLAYIFISHDLQVVRALChQVIVLRQGEVVEQG 508
Cdd:TIGR00957 1433 ARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFED--CTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFG 1501
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
273-510 |
1.39e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 73.11 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 273 TPLLRVEDLSVSFPIRKGilrrivdrnpvLKNIRFSLRPGESLGLVGESGSGKST-----TGLallrLIASQGEILFDGM 347
Cdd:PRK10762 2 QALLQLKGIDKAFPGVKA-----------LSGAALNVYPGRVMALVGENGAGKSTmmkvlTGI----YTRDAGSILYLGK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 348 PlhrwnrrqmlpvrprmqVVFQDPNSSLNPRLSVlqiveeglrVHQ-----PGLSAQQ-----RE--------------Q 403
Cdd:PRK10762 67 E-----------------VTFNGPKSSQEAGIGI---------IHQelnliPQLTIAEniflgREfvnrfgridwkkmyA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 404 EVMRVMVEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRlAYIFIS 483
Cdd:PRK10762 121 EADKLLARLNL-RFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGR-GIVYIS 198
|
250 260
....*....|....*....|....*..
gi 1278835479 484 HDLQVVRALCHQVIVLRQGEVVeqGEC 510
Cdd:PRK10762 199 HRLKEIFEICDDVTVFRDGQFI--AER 223
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
4-249 |
1.42e-13 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 70.44 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 4 PLLRIDNLSIAFSKqdetRTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLLPsppvsyP-QGDILFHDRSL---- 78
Cdd:COG1137 2 MTLEAENLVKSYGK----RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVK------PdSGRIFLDGEDIthlp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 79 LHadeqtLRGIRGnkIAMIFQEPMV--SLnplhSLEKQLYEVLSLhRGMRKEAARGEILDCLERTGIRNAAKRLNDfphQ 156
Cdd:COG1137 72 MH-----KRARLG--IGYLPQEASIfrKL----TVEDNILAVLEL-RKLSKKEREERLEELLEEFGITHLRKSKAY---S 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 157 LSGGERQRVMIAMALLTRPELLIADEPTTALD-VTVqAQILTLLRDLRDElNMSLLfIT-HN----LSIVrklaDSVAVM 230
Cdd:COG1137 137 LSGGERRRVEIARALATNPKFILLDEPFAGVDpIAV-ADIQKIIRHLKER-GIGVL-ITdHNvretLGIC----DRAYII 209
|
250
....*....|....*....
gi 1278835479 231 QNGRCVEQNAASTLLSAPQ 249
Cdd:COG1137 210 SEGKVLAEGTPEEILNNPL 228
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
295-468 |
1.61e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 69.45 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 295 IVDRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIAS-----QGEILFDGMPLHRwnrrqmlpVRPrmqvvfq 369
Cdd:PRK13538 10 ERDERILFSGLSFTLNAGELVQIEGPNGAGKTS----LLRILAGlarpdAGEVLWQGEPIRR--------QRD------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 370 DPNSSL---------NPRLSVlqivEEGLRVHQPgLSAQQREQEVMRVMVEVGLdpETRHRYPAE-FSGGQRQRIAIARA 439
Cdd:PRK13538 71 EYHQDLlylghqpgiKTELTA----LENLRFYQR-LHGPGDDEALWEALAQVGL--AGFEDVPVRqLSAGQQRRVALARL 143
|
170 180
....*....|....*....|....*....
gi 1278835479 440 LILKPELIILDEPTSSLDRTVQAQILALL 468
Cdd:PRK13538 144 WLTRAPLWILDEPFTAIDKQGVARLEALL 172
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
24-232 |
1.66e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 73.52 E-value: 1.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 24 VVSDLTLQIQRGETLALVGESGSGKSvSALSILRLLPSPPvsypQGDILFHDRSLLhaDEQTLRGIRgNKIAMIFQEPMV 103
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKS-TILKLIERLYDPT----EGDIIINDSHNL--KDINLKWWR-SKIGVVSQDPLL 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 104 --------------SLNPLHSLEKQL-------YEVLSLHRGMRKEAAR--GEILDCLERTGIRNAAKRLN--------- 151
Cdd:PTZ00265 472 fsnsiknnikyslySLKDLEALSNYYnedgndsQENKNKRNSCRAKCAGdlNDMSNTTDSNELIEMRKNYQtikdsevvd 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 152 --------DF---------------PHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNM 208
Cdd:PTZ00265 552 vskkvlihDFvsalpdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENR 631
|
250 260
....*....|....*....|....
gi 1278835479 209 SLLFITHNLSIVRkLADSVAVMQN 232
Cdd:PTZ00265 632 ITIIIAHRLSTIR-YANTIFVLSN 654
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-242 |
2.29e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 70.06 E-value: 2.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 1 MTQPLLRIDNLSIAFSkqdeTRTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLLPSPPvSYP--QGDILFHDRSL 78
Cdd:CHL00131 3 KNKPILEIKNLHASVN----ENEILKGLNLSINKGEIHAIMGPNGSGKS----TLSKVIAGHP-AYKilEGDILFKGESI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 79 LHAdEQTLRGIRGnkIAMIFQEPM----VS--------------------LNPLhslekQLYEVLSlhrgmrkeaargEI 134
Cdd:CHL00131 74 LDL-EPEERAHLG--IFLAFQYPIeipgVSnadflrlaynskrkfqglpeLDPL-----EFLEIIN------------EK 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 135 LDCLERTGI---RNaakrLNDfphQLSGGERQRVMI-AMALLtRPELLIADEPTTALDVTVQAQILTLLRDLRDELNmSL 210
Cdd:CHL00131 134 LKLVGMDPSflsRN----VNE---GFSGGEKKRNEIlQMALL-DSELAILDETDSGLDIDALKIIAEGINKLMTSEN-SI 204
|
250 260 270
....*....|....*....|....*....|....*.
gi 1278835479 211 LFITHnlsIVRKL----ADSVAVMQNGRCVEQNAAS 242
Cdd:CHL00131 205 ILITH---YQRLLdyikPDYVHVMQNGKIIKTGDAE 237
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
15-240 |
2.39e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 70.42 E-value: 2.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 15 FSKQDETrtVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLL-PSppvsypQGDILFHDRSLLHAdEQTLRGIRgNK 93
Cdd:PRK13638 9 FRYQDEP--VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLrPQ------KGAVLWQGKPLDYS-KRGLLALR-QQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 94 IAMIFQEPmvslnplhslEKQLYEVlslhrgmrkeAARGEILDCLERTGIRNA--AKRLND---------FPHQ----LS 158
Cdd:PRK13638 79 VATVFQDP----------EQQIFYT----------DIDSDIAFSLRNLGVPEAeiTRRVDEaltlvdaqhFRHQpiqcLS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 159 GGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNmSLLFITHNLSIVRKLADSVAVMQNGRCVEQ 238
Cdd:PRK13638 139 HGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGN-HVIISSHDIDLIYEISDAVYVLRQGQILTH 217
|
..
gi 1278835479 239 NA 240
Cdd:PRK13638 218 GA 219
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
5-250 |
2.60e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 70.24 E-value: 2.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 5 LLRIDNLSIAfskqDETRTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLLPSPPVSYP---QGDILFHDRSLLHA 81
Cdd:PRK13547 1 MLTADHLHVA----RRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAPRGarvTGDVTLNGEPLAAI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 82 DEQTLRGIRgnkiAMIFQ--EPMVSLNplhslekqLYEVLSL------HRGMRKEAARGEILDC-LERTGIRNAAKRlnD 152
Cdd:PRK13547 77 DAPRLARLR----AVLPQaaQPAFAFS--------AREIVLLgryphaRRAGALTHRDGEIAWQaLALAGATALVGR--D 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 153 FPhQLSGGERQRVMIAMAL---------LTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKL 223
Cdd:PRK13547 143 VT-TLSGGELARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARH 221
|
250 260
....*....|....*....|....*..
gi 1278835479 224 ADSVAVMQNGRCVEQNAASTLLSaPQH 250
Cdd:PRK13547 222 ADRIAMLADGAIVAHGAPADVLT-PAH 247
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
276-503 |
2.71e-13 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 68.65 E-value: 2.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 276 LRVEDLSVSFPirkgilRRIVDRNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALL-RLIASQGEILfdgmplhrwnr 354
Cdd:cd03250 1 ISVEDASFTWD------SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLgELEKLSGSVS----------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 355 rqmlpVRPRMQVVFQDP---NSSlnprlsvlqiVEEGLRVHQPglSAQQREQEVMRV--------------MVEVG---- 413
Cdd:cd03250 64 -----VPGSIAYVSQEPwiqNGT----------IRENILFGKP--FDEERYEKVIKAcalepdleilpdgdLTEIGekgi 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 414 -LdpetrhrypaefSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILA-LLKGLQEKHRlAYIFISHDLQVVRA 491
Cdd:cd03250 127 nL------------SGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEnCILGLLLNNK-TRILVTHQLQLLPH 193
|
250
....*....|..
gi 1278835479 492 lCHQVIVLRQGE 503
Cdd:cd03250 194 -ADQIVVLDNGR 204
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
292-485 |
3.28e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 72.07 E-value: 3.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 292 LRRIVDRN-PVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGE-ILFDGMplhrwnRRQMLPvrprm 364
Cdd:PRK11819 12 VSKVVPPKkQILKDISLSFFPGAKIGVLGLNGAGKST----LLRIMAgvdkeFEGEaRPAPGI------KVGYLP----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 365 qvvfQDPnsSLNPRLSVLQIVEEGLrvhQPGLSAQQREQEVMRVMVEV----------------------GLDPETR--- 419
Cdd:PRK11819 77 ----QEP--QLDPEKTVRENVEEGV---AEVKAALDRFNEIYAAYAEPdadfdalaaeqgelqeiidaadAWDLDSQlei 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 420 ----HRYP------AEFSGGQRQRIAIARALILKPELIILDEPTSSLDrtvqAQILALLkglqEKHRLAY----IFISHD 485
Cdd:PRK11819 148 amdaLRCPpwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWL----EQFLHDYpgtvVAVTHD 219
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-249 |
4.38e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 69.15 E-value: 4.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 5 LLRIDNLSIAFskqdETRTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLLPSPpvsypQGDILFHDR--SLLHAD 82
Cdd:PRK10895 3 TLTAKNLAKAY----KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRD-----AGNIIIDDEdiSLLPLH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 83 EQTLRGIrgnkiAMIFQEPmvSLNPLHSLEKQLYEVLSLHRGMRKEAARGEILDCLERTGIRNAAKRLNdfpHQLSGGER 162
Cdd:PRK10895 74 ARARRGI-----GYLPQEA--SIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMG---QSLSGGER 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 163 QRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDElNMSLLFITHNLSIVRKLADSVAVMQNGRCVEQNAAS 242
Cdd:PRK10895 144 RRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDS-GLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPT 222
|
....*..
gi 1278835479 243 TLLSAPQ 249
Cdd:PRK10895 223 EILQDEH 229
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
22-200 |
5.39e-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: 67.90 E-value: 5.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 22 RTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLLP--SPPVSypqGDILFHDRSLlhaDEQtlRGIRGNKIAMIFQ 99
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKT----TLLRILAglSPPLA---GRVLLNGGPL---DFQ--RDSIARGLLYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 100 EPMVslnplhsleKQLYEVLSLHRGMRKEAARGEILDCLERTGIRNaakrLNDFP-HQLSGGERQRVMIAMALLTRPELL 178
Cdd:cd03231 81 APGI---------KTTLSVLENLRFWHADHSDEQVEEALARVGLNG----FEDRPvAQLSAGQQRRVALARLLLSGRPLW 147
|
170 180
....*....|....*....|..
gi 1278835479 179 IADEPTTALDVTVQAQILTLLR 200
Cdd:cd03231 148 ILDEPTTALDKAGVARFAEAMA 169
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-234 |
6.14e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 70.85 E-value: 6.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 3 QPLLRIDNLS-IAFSkqdetrtvvsDLTLQIQRGETLALVGESGSGKSVSALSILRLlpSPPVSypqGDILFHDRSllha 81
Cdd:PRK15439 266 APVLTVEDLTgEGFR----------NISLEVRAGEILGLAGVVGAGRTELAETLYGL--RPARG---GRIMLNGKE---- 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 82 deqtlrgIRGNKIAMIFQEPMVSL------NPLHsLEKQLY-EVLSLHRGMR-------KEAARgeildcLER------- 140
Cdd:PRK15439 327 -------INALSTAQRLARGLVYLpedrqsSGLY-LDAPLAwNVCALTHNRRgfwikpaRENAV------LERyrralni 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 141 --TGIRNAAKRLndfphqlSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDElNMSLLFITHNLS 218
Cdd:PRK15439 393 kfNHAEQAARTL-------SGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQ-NVAVLFISSDLE 464
|
250
....*....|....*.
gi 1278835479 219 IVRKLADSVAVMQNGR 234
Cdd:PRK15439 465 EIEQMADRVLVMHQGE 480
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
279-505 |
7.12e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 70.91 E-value: 7.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 279 EDLSVSFPIRKGilrrivdrnpvLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIA-SQGEILFDGMPLHRWNRRQM 357
Cdd:PRK10982 2 SNISKSFPGVKA-----------LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQkDSGSILFQGKEIDFKSSKEA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 358 LPVRPRMqvVFQDPNSSLnpRLSVLQIVEEGlRVHQPGLSAQQRE--QEVMRVMVEVGLDPETRHRYpAEFSGGQRQRIA 435
Cdd:PRK10982 71 LENGISM--VHQELNLVL--QRSVMDNMWLG-RYPTKGMFVDQDKmyRDTKAIFDELDIDIDPRAKV-ATLSVSQMQMIE 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 436 IARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHrLAYIFISHDLQVVRALCHQVIVLRQGEVV 505
Cdd:PRK10982 145 IAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERG-CGIVYISHKMEEIFQLCDEITILRDGQWI 213
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
10-236 |
1.03e-12 |
|
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: 66.90 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 10 NLSIAFSKQDETRTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLLPSPPVSY--PQGDILFHDRSLLHADEQTLR 87
Cdd:cd03233 8 NISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCS----TLLKALANRTEGNvsVEGDIHYNGIPYKEFAEKYPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 88 GIrgnkiamIFqepmVSLNPLHSLEKQLYEVLslhrgmrkEAArgeiLDClertgirnaakRLNDFPHQLSGGERQRVMI 167
Cdd:cd03233 84 EI-------IY----VSEEDVHFPTLTVRETL--------DFA----LRC-----------KGNEFVRGISGGERKRVSI 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 168 AMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLS-IVRKLADSVAVMQNGRCV 236
Cdd:cd03233 130 AEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASdEIYDLFDKVLVLYEGRQI 199
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
6-234 |
1.28e-12 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 66.72 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 6 LRIDNLSIAF-SKQDETRTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLLP--------SPPVSY-PQGDILFHD 75
Cdd:cd03250 1 ISVEDASFTWdSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEklsgsvsvPGSIAYvSQEPWIQNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 76 rsllhadeqTlrgIRGNkiaMIFQEPMvslnplhslEKQLYE-VL---SLHRGMrkeaargEILDCLERTGIrnAAKRLN 151
Cdd:cd03250 81 ---------T---IREN---ILFGKPF---------DEERYEkVIkacALEPDL-------EILPDGDLTEI--GEKGIN 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 152 dfphqLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILT--LLRDLRDelNMSLLFITHNLSIVRKlADSVAV 229
Cdd:cd03250 128 -----LSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEncILGLLLN--NKTRILVTHQLQLLPH-ADQIVV 199
|
....*
gi 1278835479 230 MQNGR 234
Cdd:cd03250 200 LDNGR 204
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-247 |
1.55e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 68.29 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 1 MTQPLLRIDNLSiafsKQDETRTVVSDLTLQIQRGETLALVGESGSGKSVSalsiLRLLPSppVSYPQGDilfhdrSLLH 80
Cdd:PRK13537 3 MSVAPIDFRNVE----KRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTT----LRMLLG--LTHPDAG------SISL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 81 ADEQTLRGIRGNKIAMIFQEPMVSLNPLHSLEKQLyEVLSLHRGMRKEAARGEILDCLERTGIRNAAkrlnDFP-HQLSG 159
Cdd:PRK13537 67 CGEPVPSRARHARQRVGVVPQFDNLDPDFTVRENL-LVFGRYFGLSAAAARALVPPLLEFAKLENKA----DAKvGELSG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 160 GERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDElNMSLLFITHNLSIVRKLADSVAVMQNGRCVEQN 239
Cdd:PRK13537 142 GMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEG 220
|
....*...
gi 1278835479 240 AASTLLSA 247
Cdd:PRK13537 221 APHALIES 228
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
14-248 |
1.81e-12 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 69.74 E-value: 1.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 14 AFSKQDETRTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLLpsppvSYPQGDILFHDRSLLHADEQTLRGirgnK 93
Cdd:PRK10789 320 QFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHF-----DVSEGDIRFHDIPLTKLQLDSWRS----R 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 94 IAMIFQEPM---------VSLNPLHSLEKQLYEV----------LSLHRGMRKEAArgeildclERtGIrnaakrlndfp 154
Cdd:PRK10789 391 LAVVSQTPFlfsdtvannIALGRPDATQQEIEHVarlasvhddiLRLPQGYDTEVG--------ER-GV----------- 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 155 hQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDElnMSLLFITHNLSIVRKlADSVAVMQNGR 234
Cdd:PRK10789 451 -MLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEG--RTVIISAHRLSALTE-ASEILVMQHGH 526
|
250
....*....|....
gi 1278835479 235 CVEQNAASTLLSAP 248
Cdd:PRK10789 527 IAQRGNHDQLAQQS 540
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-233 |
1.84e-12 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 67.73 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 3 QPLLRIDNLSIAFSKQDETRTVvsDLTlqIQRGETLALVGESGSGKSVSALSILRLLPSPPVSYPQGDILFHDrslLHAD 82
Cdd:PRK09984 2 QTIIRVEKLAKTFNQHQALHAV--DLN--IHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGSHIELLGRT---VQRE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 83 EQTLRGIRGNK--IAMIFQEPMVsLNPLHSLEKQLYEVLSLHRGMR------KEAARGEILDCLERTGIRNaakrlndFP 154
Cdd:PRK09984 75 GRLARDIRKSRanTGYIFQQFNL-VNRLSVLENVLIGALGSTPFWRtcfswfTREQKQRALQALTRVGMVH-------FA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 155 HQ----LSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVM 230
Cdd:PRK09984 147 HQrvstLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVAL 226
|
...
gi 1278835479 231 QNG 233
Cdd:PRK09984 227 RQG 229
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
297-508 |
2.41e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 67.16 E-value: 2.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 297 DRNPVLKNIRFSLRPGESLGLVGESGSGKST---------TGLALLRLIASQGEILFDGMPLHRWNRRQMlpvrPRMQVV 367
Cdd:PRK13547 12 RHRAILRDLSLRIEPGRVTALLGRNGAGKSTllkalagdlTGGGAPRGARVTGDVTLNGEPLAAIDAPRL----ARLRAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 368 FQDPNSSLNPrLSVLQIVEEGLRVH-QPGLSAQQREQEVM-RVMVEVGLDPETRhRYPAEFSGGQRQRIAIARAL----- 440
Cdd:PRK13547 88 LPQAAQPAFA-FSAREIVLLGRYPHaRRAGALTHRDGEIAwQALALAGATALVG-RDVTTLSGGELARVQFARVLaqlwp 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1278835479 441 ----ILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:PRK13547 166 phdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHG 237
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
157-504 |
4.41e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 68.22 E-value: 4.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDElNMSLLFITHNLSIVRKLADSVAVMQNGRCV 236
Cdd:PRK10982 135 LSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQWI 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 237 EQNAASTLlSAPQ-------HPYTQRLlnsePSGDPVPLDAdstpLLRVEDLSVSfpirkgilrrivdRNPVLKNIRFSL 309
Cdd:PRK10982 214 ATQPLAGL-TMDKiiammvgRSLTQRF----PDKENKPGEV----ILEVRNLTSL-------------RQPSIRDVSFDL 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 310 RPGESLGLVGESGSgKSTTGLALLRLI--ASQGEILFDGMPLHrwNRRQMLPVRPRMQVVFQDPNSS---------LNPR 378
Cdd:PRK10982 272 HKGEILGIAGLVGA-KRTDIVETLFGIreKSAGTITLHGKKIN--NHNANEAINHGFALVTEERRSTgiyayldigFNSL 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 379 LSVLQIVEEGLRVhqpgLSAQQREQEVMRVMVEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDR 458
Cdd:PRK10982 349 ISNIRNYKNKVGL----LDNSRMKSDTQWVIDSMRVKTPGHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDV 424
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1278835479 459 TVQAQILALLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRQGEV 504
Cdd:PRK10982 425 GAKFEIYQLIAELAKKDK-GIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-234 |
4.48e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 68.31 E-value: 4.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 5 LLRIDNLSiAFSKQDETRTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRllpsppvSYP---QGDILFHDRSLlhA 81
Cdd:TIGR02633 257 ILEARNLT-CWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFG-------AYPgkfEGNVFINGKPV--D 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 82 DEQTLRGIRgNKIAMIFQE-PMVSLNPLHSLEKQLyeVLSLhrgMRKEAARGEILDCLERTGIRNAAKRLN------DFP 154
Cdd:TIGR02633 327 IRNPAQAIR-AGIAMVPEDrKRHGIVPILGVGKNI--TLSV---LKSFCFKMRIDAAAELQIIGSAIQRLKvktaspFLP 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 155 -HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDElNMSLLFITHNLSIVRKLADSVAVMQNG 233
Cdd:TIGR02633 401 iGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEG 479
|
.
gi 1278835479 234 R 234
Cdd:TIGR02633 480 K 480
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
24-238 |
5.07e-12 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 67.18 E-value: 5.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 24 VVSDLTLQIQRGETLALVGESGSGKSvsalSILRL---LPSppVSypQGDILFHDRSLLHAdEQTLRGIrgnkiAMIFQE 100
Cdd:PRK11650 19 VIKGIDLDVADGEFIVLVGPSGCGKS----TLLRMvagLER--IT--SGEIWIGGRVVNEL-EPADRDI-----AMVFQN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 101 pmVSLNPLHSLEKQLYEVLSLhRGMRKEaargEIldcleRTGIRNAAK--RLNDF----PHQLSGGERQRVMIAMALLTR 174
Cdd:PRK11650 85 --YALYPHMSVRENMAYGLKI-RGMPKA----EI-----EERVAEAARilELEPLldrkPRELSGGQRQRVAMGRAIVRE 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1278835479 175 PELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGRcVEQ 238
Cdd:PRK11650 153 PAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGV-AEQ 215
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
301-490 |
6.58e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 68.52 E-value: 6.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 301 VLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEILF-DGMPLHRWNRRQMlpvRPRMQVVFQDP--- 371
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKST----ILKLIerlydPTEGDIIInDSHNLKDINLKWW---RSKIGVVSQDPllf 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 372 -NS----------SLNPRLSVLQIVEEGLRVHQPGLSAQQREQ--------EVMRVMVEVGLdPETRHRY---------- 422
Cdd:PTZ00265 473 sNSiknnikyslySLKDLEALSNYYNEDGNDSQENKNKRNSCRakcagdlnDMSNTTDSNEL-IEMRKNYqtikdsevvd 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 423 -------------------------PAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRL 477
Cdd:PTZ00265 552 vskkvlihdfvsalpdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENR 631
|
250
....*....|...
gi 1278835479 478 AYIFISHDLQVVR 490
Cdd:PTZ00265 632 ITIIIAHRLSTIR 644
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
22-485 |
7.20e-12 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 67.65 E-value: 7.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 22 RTVVSDLTLQIQRGETLALVGESGSGKSvSALSIL-----------RLLPSPPVSY-PQGDILFHDRSLLHADEQTLRGI 89
Cdd:TIGR03719 18 KEILKDISLSFFPGAKIGVLGLNGAGKS-TLLRIMagvdkdfngeaRPQPGIKVGYlPQEPQLDPTKTVRENVEEGVAEI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 90 RG-----NKIAMIFQEPMVSLNPLhsLEKQ--LYEVLslhrgmrkEAARGEILDclERTGIRNAAKRL--NDFP-HQLSG 159
Cdd:TIGR03719 97 KDaldrfNEISAKYAEPDADFDKL--AAEQaeLQEII--------DAADAWDLD--SQLEIAMDALRCppWDADvTKLSG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 160 GERQRVMIAMALLTRPELLIADEPTTALDvtvqAQILTLLRDLRDELNMSLLFITHNlsivRKLADSVA----VMQNGRC 235
Cdd:TIGR03719 165 GERRRVALCRLLLSKPDMLLLDEPTNHLD----AESVAWLERHLQEYPGTVVAVTHD----RYFLDNVAgwilELDRGRG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 236 V----------EQNAASTLLSAPQHPYTQRLLNSE-------PSGDpvplDADSTPLL-------------RVEDLSVSF 285
Cdd:TIGR03719 237 IpwegnysswlEQKQKRLEQEEKEESARQKTLKRElewvrqsPKGR----QAKSKARLaryeellsqefqkRNETAEIYI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 286 PI--R--------KGILRRIVDRnPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIASQ-----GEIlfdgmplh 350
Cdd:TIGR03719 313 PPgpRlgdkvieaENLTKAFGDK-LLIDDLSFKLPPGGIVGVIGPNGAGKST----LFRMITGQeqpdsGTI-------- 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 351 rwnrrqmlPVRPRMQVVFQDPN-SSLNPRLSVLQIVEEGLRVHQPGLSAQQREQEVMRVMVEvGLDPETRhryPAEFSGG 429
Cdd:TIGR03719 380 --------EIGETVKLAYVDQSrDALDPNKTVWEEISGGLDIIKLGKREIPSRAYVGRFNFK-GSDQQKK---VGQLSGG 447
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1278835479 430 QRQRIAIARALILKPELIILDEPTSSLD-RTVQaqilALLKGLQEKHRLAYIfISHD 485
Cdd:TIGR03719 448 ERNRVHLAKTLKSGGNVLLLDEPTNDLDvETLR----ALEEALLNFAGCAVV-ISHD 499
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
23-234 |
9.80e-12 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 66.59 E-value: 9.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 23 TVVS-DLTLQIQRGETLALVGESGSGKSvsalSILRLLPSPPvsypqgDILFHDrslLHADEQTLRGI----RGnkIAMI 97
Cdd:PRK11000 16 VVISkDINLDIHEGEFVVFVGPSGCGKS----TLLRMIAGLE------DITSGD---LFIGEKRMNDVppaeRG--VGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 98 FQEpmvslnplhsleKQLYEVLSLHRGMR-----KEAARGEILDCLERTG-IRNAAKRLNDFPHQLSGGERQRVMIAMAL 171
Cdd:PRK11000 81 FQS------------YALYPHLSVAENMSfglklAGAKKEEINQRVNQVAeVLQLAHLLDRKPKALSGGQRQRVAIGRTL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1278835479 172 LTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNGR 234
Cdd:PRK11000 149 VAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGR 211
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
6-236 |
1.05e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 65.88 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 6 LRIDNLSIAFSKQDETR-TVVSDLTLQIQRGETLALVGESGSGKS--VSALSILrLLPSppvsypQGDI--LFHDRSLLH 80
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTElKALDNVSVEINQGEFIAIIGQTGSGKTtfIEHLNAL-LLPD------TGTIewIFKDEKNKK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 81 ADEQT-------------------LRGIRgNKIAMIFQepmvslnplhSLEKQLYEV----------LSLhrGMRKEAAR 131
Cdd:PRK13651 76 KTKEKekvleklviqktrfkkikkIKEIR-RRVGVVFQ----------FAEYQLFEQtiekdiifgpVSM--GVSKEEAK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 132 GEILDCLERTGIrnAAKRLNDFPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDElNMSLL 211
Cdd:PRK13651 143 KRAAKYIELVGL--DESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTII 219
|
250 260
....*....|....*....|....*
gi 1278835479 212 FITHNLSIVRKLADSVAVMQNGRCV 236
Cdd:PRK13651 220 LVTHDLDNVLEWTKRTIFFKDGKII 244
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
300-523 |
1.53e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 67.36 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 300 PVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLR--------------------------------------------- 334
Cdd:PTZ00265 1182 PIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRfydlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefslt 1261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 335 ----------LIASQGEILFDGMPLHRWNRRQMlpvRPRMQVVFQDP---NSSL--NPRLSVLQIVEEGLRvHQPGLSAQ 399
Cdd:PTZ00265 1262 keggsgedstVFKNSGKILLDGVDICDYNLKDL---RNLFSIVSQEPmlfNMSIyeNIKFGKEDATREDVK-RACKFAAI 1337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 400 QREQEVMRVMVEVGLDPetrhrYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAY 479
Cdd:PTZ00265 1338 DEFIESLPNKYDTNVGP-----YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTI 1412
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1278835479 480 IFISHDLQVVRAlCHQVIVL----RQGEVVE-QGECQRVFSAPTQRYTR 523
Cdd:PTZ00265 1413 ITIAHRIASIKR-SDKIVVFnnpdRTGSFVQaHGTHEELLSVQDGVYKK 1460
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
6-234 |
2.04e-11 |
|
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: 66.31 E-value: 2.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 6 LRIDNLSIAFSKQDetRTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLLP--SPPVSypqGDILFHDRSLLHADE 83
Cdd:COG4618 331 LSVENLTVVPPGSK--RPILRGVSFSLEPGEVLGVIGPSGSGKS----TLARLLVgvWPPTA---GSVRLDGADLSQWDR 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 84 QTLRG---------------IRGNkIAMiFQEPmvslNPlhslEKqlyeVLslhrgmrkEAARgeildcleRTGIRNAAK 148
Cdd:COG4618 402 EELGRhigylpqdvelfdgtIAEN-IAR-FGDA----DP----EK----VV--------AAAK--------LAGVHEMIL 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 149 RLND--------FPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDElNMSLLFITHNLSIV 220
Cdd:COG4618 452 RLPDgydtrigeGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRPSLL 530
|
250
....*....|....
gi 1278835479 221 RkLADSVAVMQNGR 234
Cdd:COG4618 531 A-AVDKLLVLRDGR 543
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
5-201 |
5.56e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 62.13 E-value: 5.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 5 LLRIDNLsiAFSKQDetRTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLLP--SPPVSypqGDILFHDRSLLHAD 82
Cdd:PRK13538 1 MLEARNL--ACERDE--RILFSGLSFTLNAGELVQIEGPNGAGKT----SLLRILAglARPDA---GEVLWQGEPIRRQR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 83 EQTLR---------GIRGnkiamifqepmvSLNPLhslekqlyEVLSLHRGMRKEAARGEILDCLERTGIRnaakRLNDF 153
Cdd:PRK13538 70 DEYHQdllylghqpGIKT------------ELTAL--------ENLRFYQRLHGPGDDEALWEALAQVGLA----GFEDV 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1278835479 154 P-HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRD 201
Cdd:PRK13538 126 PvRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQ 174
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-234 |
5.69e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 64.08 E-value: 5.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 1 MTQPLLRIDNLSIAFSKQDetRTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLLpSPPVsypqGDIlfhdrSLLH 80
Cdd:PRK13536 35 GSMSTVAIDLAGVSKSYGD--KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMT-SPDA----GKI-----TVLG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 81 ADEQTLRGIRGNKIAMIFQepMVSLNPLHSLEKQLYeVLSLHRGMRKEAARGEILDCLERTGIRNAAK-RLNDfphqLSG 159
Cdd:PRK13536 103 VPVPARARLARARIGVVPQ--FDNLDLEFTVRENLL-VFGRYFGMSTREIEAVIPSLLEFARLESKADaRVSD----LSG 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1278835479 160 GERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRdELNMSLLFITHNLSIVRKLADSVAVMQNGR 234
Cdd:PRK13536 176 GMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLL-ARGKTILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
19-230 |
5.93e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 62.28 E-value: 5.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 19 DETRTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLLpsppvsypqgdilfhdrsllhadeqtLRGIRGNKIAMIF 98
Cdd:COG2401 40 VVERYVLRDLNLEIEPGEIVLIVGASGSGKS----TLLRLL--------------------------AGALKGTPVAGCV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 99 QEPmvslnplhslEKQLYEVLSlhrgmrkeaargeILDCLERTGIRNAAKR------LNDF------PHQLSGGERQRVM 166
Cdd:COG2401 90 DVP----------DNQFGREAS-------------LIDAIGRKGDFKDAVEllnavgLSDAvlwlrrFKELSTGQKFRFR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1278835479 167 IAMALLTRPELLIADEPTTALDVTVqAQILTL-LRDLRDELNMSLLFITHNLSIVRKLADSVAVM 230
Cdd:COG2401 147 LALLLAERPKLLVIDEFCSHLDRQT-AKRVARnLQKLARRAGITLVVATHHYDVIDDLQPDLLIF 210
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
4-216 |
6.12e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 62.42 E-value: 6.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 4 PLLRIDNlsIAFskQDETRTVVSDLTLQIQRGETLALVGESGSGKSvSALSILRLLPSPPVsypqGDILFHDRSLLHADE 83
Cdd:PRK10247 6 PLLQLQN--VGY--LAGDAKILNNISFSLRAGEFKLITGPSGCGKS-TLLKIVASLISPTS----GTLLFEGEDISTLKP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 84 QTLRgirgNKIAMIFQEPMVslnplhsLEKQLYEVLSLHRGMRKEAA-RGEILDCLERTGIRNAA--KRLNDfphqLSGG 160
Cdd:PRK10247 77 EIYR----QQVSYCAQTPTL-------FGDTVYDNLIFPWQIRNQQPdPAIFLDDLERFALPDTIltKNIAE----LSGG 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1278835479 161 ERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHN 216
Cdd:PRK10247 142 EKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHD 197
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
297-471 |
6.89e-11 |
|
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: 61.49 E-value: 6.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 297 DRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIASQ-------GEILFDGMPLHRWNRRQMLPVRprmQVVFQ 369
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTT----LLDVLAGRktagvitGEILINGRPLDKNFQRSTGYVE---QQDVH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 370 DPNSSlnprlsvlqiVEEGLRvhqpgLSAQQReqevmrvmvevGLDPEtrhrypaefsggQRQRIAIARALILKPELIIL 449
Cdd:cd03232 91 SPNLT----------VREALR-----FSALLR-----------GLSVE------------QRKRLTIGVELAAKPSILFL 132
|
170 180
....*....|....*....|..
gi 1278835479 450 DEPTSSLDRTVQAQILALLKGL 471
Cdd:cd03232 133 DEPTSGLDSQAAYNIVRFLKKL 154
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
287-513 |
1.33e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 64.36 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 287 IRKGILRRIVDRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIASQ---------GEILFDGMPLHRWNRRQm 357
Cdd:TIGR00956 62 FRKLKKFRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCST----LLKTIASNtdgfhigveGVITYDGITPEEIKKHY- 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 358 lpvrpRMQVVFQDPNSSLNPRLSVLQIVEEGLRVHQP-----GLSAQQR-EQEVMRVMVEVGLDPETRHRYPAEF----S 427
Cdd:TIGR00956 137 -----RGDVVYNAETDVHFPHLTVGETLDFAARCKTPqnrpdGVSREEYaKHIADVYMATYGLSHTRNTKVGNDFvrgvS 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 428 GGQRQRIAIARALILKPELIILDEPTSSLDrtvQAQILALLKGLQEKHRL----AYIFISHDLQVVRALCHQVIVLRQGE 503
Cdd:TIGR00956 212 GGERKRVSIAEASLGGAKIQCWDNATRGLD---SATALEFIRALKTSANIldttPLVAIYQCSQDAYELFDKVIVLYEGY 288
|
250
....*....|
gi 1278835479 504 VVEQGECQRV 513
Cdd:TIGR00956 289 QIYFGPADKA 298
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
35-230 |
1.67e-10 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 61.61 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 35 GETLALVGESGSGKSvSALSIL--RLLP------SPPvSYPqgDILFHDR-SLLHadeQTLRGIRGNKIAMIFQEPMVSL 105
Cdd:cd03236 26 GQVLGLVGPNGIGKS-TALKILagKLKPnlgkfdDPP-DWD--EILDEFRgSELQ---NYFTKLLEGDVKVIVKPQYVDL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 106 NPlHSLEKQLYEVLSlhrgmrKEAARGEILDCLERTGIRNAAKRLNDfphQLSGGERQRVMIAMALLTRPELLIADEPTT 185
Cdd:cd03236 99 IP-KAVKGKVGELLK------KKDERGKLDELVDQLELRHVLDRNID---QLSGGELQRVAIAAALARDADFYFFDEPSS 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1278835479 186 ALDVTVQAQILTLLRDLRDELNmSLLFITHNLSIVRKLADSVAVM 230
Cdd:cd03236 169 YLDIKQRLNAARLIRELAEDDN-YVLVVEHDLAVLDYLSDYIHCL 212
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
158-504 |
1.80e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 63.65 E-value: 1.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVTVqaqILTLLRDLRDeLNMSLLFITHNLSIVRKLADSVAVMQ------ 231
Cdd:PRK10636 151 SGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDA---VIWLEKWLKS-YQGTLILISHDRDFLDPIVDKIIHIEqqslfe 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 232 ---NGRCVEQNAASTL---------------------------------------------LSAPQH---PYtqRLLNSE 260
Cdd:PRK10636 227 ytgNYSSFEVQRATRLaqqqamyesqqervahlqsyidrfrakatkakqaqsrikmlermeLIAPAHvdnPF--HFSFRA 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 261 PSGDPvpldadsTPLLRVEDLSVSFPIRKgilrrivdrnpVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIAS-- 338
Cdd:PRK10636 305 PESLP-------NPLLKMEKVSAGYGDRI-----------ILDSIKLNLVPGSRIGLLGRNGAGKST----LIKLLAGel 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 339 ---QGEI-LFDGMPLHRWNRRQMlpvrprmqvvfqdpnSSLNPRLSVLQiveeglrvHQPGLSAQQREQEVMRVMVEVGL 414
Cdd:PRK10636 363 apvSGEIgLAKGIKLGYFAQHQL---------------EFLRADESPLQ--------HLARLAPQELEQKLRDYLGGFGF 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 415 DPETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTV-QAQILALLkglqeKHRLAYIFISHDLQVVRALC 493
Cdd:PRK10636 420 QGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMrQALTEALI-----DFEGALVVVSHDRHLLRSTT 494
|
410
....*....|.
gi 1278835479 494 HQVIVLRQGEV 504
Cdd:PRK10636 495 DDLYLVHDGKV 505
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
24-247 |
2.08e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 63.81 E-value: 2.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 24 VVSDLTLQIQRGETLALVGESGSGKSVSALSILRLLPSPpvsypQGDILFHDRSLLHADEQTLRgirgNKIAMIFQEPMV 103
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESA-----EGEIIIDGLNIAKIGLHDLR----FKITIIPQDPVL 1371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 104 -------SLNPLHSL-EKQLYEVLSLHRGMRKEAARGEILD--CLErtGIRNaakrlndfphqLSGGERQRVMIAMALLT 173
Cdd:TIGR00957 1372 fsgslrmNLDPFSQYsDEEVWWALELAHLKTFVSALPDKLDheCAE--GGEN-----------LSVGQRQLVCLARALLR 1438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1278835479 174 RPELLIADEPTTALDVT----VQAQILTLLRDLrdelnmSLLFITHNLSIVRKLAdSVAVMQNGRCVEQNAASTLLSA 247
Cdd:TIGR00957 1439 KTKILVLDEATAAVDLEtdnlIQSTIRTQFEDC------TVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQQ 1509
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
24-232 |
5.11e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 62.35 E-value: 5.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 24 VVSDLTLQIQRGETLALVGESGSGKSVSALSILRLL-----------------------------------------PSP 62
Cdd:PTZ00265 1183 IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYdlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsLTK 1262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 63 PVSYPQGDILFHDRSLLHAD-----EQTLRGIRgNKIAMIFQEPMVSLNPLHSLEKQLYEVLSLHRGMR--KEAARGEIL 135
Cdd:PTZ00265 1263 EGGSGEDSTVFKNSGKILLDgvdicDYNLKDLR-NLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRacKFAAIDEFI 1341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 136 DCLERTGIRNAAKrlndFPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITH 215
Cdd:PTZ00265 1342 ESLPNKYDTNVGP----YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH 1417
|
250
....*....|....*..
gi 1278835479 216 NLSIVRKlADSVAVMQN 232
Cdd:PTZ00265 1418 RIASIKR-SDKIVVFNN 1433
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
302-513 |
5.23e-10 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 61.83 E-value: 5.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 302 LKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGmplhrwnRRQMLPVrprmqvvfqdpNSSLN 376
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKST----LSNLIAgvtmpNKGTVDIKG-------SAALIAI-----------SSGLN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 377 PRLSVLQIVE-EGLRVhqpGLSAQQReQEVMRVMVEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSS 455
Cdd:PRK13545 98 GQLTGIENIElKGLMM---GLTKEKI-KEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1278835479 456 LDRTVQAQILALLKGLQEKHRLAYiFISHDLQVVRALCHQVIVLRQGEVVEQGECQRV 513
Cdd:PRK13545 174 GDQTFTKKCLDKMNEFKEQGKTIF-FISHSLSQVKSFCTKALWLHYGQVKEYGDIKEV 230
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
262-457 |
6.31e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 61.80 E-value: 6.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 262 SGDPVPLDadstplLRVEDLSVSFPIRKGILRRIVdrnpvlknirfSLRPGESLGLVGESGSGKSTtglaLLRLIASQGe 341
Cdd:PLN03073 170 GGGPAIKD------IHMENFSISVGGRDLIVDASV-----------TLAFGRHYGLVGRNGTGKTT----FLRYMAMHA- 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 342 ilFDGMPlhrwNRRQMLPVRprmQVVFQDPNSSL----NPRLSVLQIVEEGLRVHQ-------PGLSAQ----------- 399
Cdd:PLN03073 228 --IDGIP----KNCQILHVE---QEVVGDDTTALqcvlNTDIERTQLLEEEAQLVAqqrelefETETGKgkgankdgvdk 298
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1278835479 400 ----QREQEVMR----------------VMVEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLD 457
Cdd:PLN03073 299 davsQRLEEIYKrlelidaytaearaasILAGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
6-504 |
6.70e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 61.80 E-value: 6.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 6 LRIDNLSIAFSKQDetrtVVSDLTLQIQRGETLALVGESGSGKSV----------------------------SALSILR 57
Cdd:PLN03073 178 IHMENFSISVGGRD----LIVDASVTLAFGRHYGLVGRNGTGKTTflrymamhaidgipkncqilhveqevvgDDTTALQ 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 58 LLPSPPVSYPQgdiLFHDRSLLHADEQTLRGIRGNKIAMIFQEPMVSLNPLHSLEKQLYEVLSLHRGMRKEAARGEILDC 137
Cdd:PLN03073 254 CVLNTDIERTQ---LLEEEAQLVAQQRELEFETETGKGKGANKDGVDKDAVSQRLEEIYKRLELIDAYTAEARAASILAG 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 138 LERTGiRNAAKRLNDFphqlSGGERQRVMIAMALLTRPELLIADEPTTALDV----------TVQAQILTLLRDLRDELN 207
Cdd:PLN03073 331 LSFTP-EMQVKATKTF----SGGWRMRIALARALFIEPDLLLLDEPTNHLDLhavlwletylLKWPKTFIVVSHAREFLN 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 208 MSLLFITH----NLSIVRKLADSVAVMQNGRCVEQ-----------------------NAASTLLSAPQHPYTQRL---- 256
Cdd:PLN03073 406 TVVTDILHlhgqKLVTYKGDYDTFERTREEQLKNQqkafesnersrshmqafidkfryNAKRASLVQSRIKALDRLghvd 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 257 -LNSEPSGD---PVPLDADSTPLLRVEDLSVSFPirkgilrrivdRNPVL-KNIRFSLRPGESLGLVGESGSGKSTtgla 331
Cdd:PLN03073 486 aVVNDPDYKfefPTPDDRPGPPIISFSDASFGYP-----------GGPLLfKNLNFGIDLDSRIAMVGPNGIGKST---- 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 332 LLRLIAsqGEILFDGMPLHRwnrrqmlPVRPRMQVVFQDP----NSSLNPRLSVLQ----IVEEGLRVHQPGLSaqqreq 403
Cdd:PLN03073 551 ILKLIS--GELQPSSGTVFR-------SAKVRMAVFSQHHvdglDLSSNPLLYMMRcfpgVPEQKLRAHLGSFG------ 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 404 evmrVMVEVGLDPETrhrypaEFSGGQRQRIAIARALILKPELIILDEPTSSLD-RTVQAQI--LALLKGlqekhrlAYI 480
Cdd:PLN03073 616 ----VTGNLALQPMY------TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDlDAVEALIqgLVLFQG-------GVL 678
|
570 580
....*....|....*....|....
gi 1278835479 481 FISHDLQVVRALCHQVIVLRQGEV 504
Cdd:PLN03073 679 MVSHDEHLISGSVDELWVVSEGKV 702
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
6-234 |
8.30e-10 |
|
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: 61.21 E-value: 8.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 6 LRIDNLSIAfsKQDETRTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLLPS--PPVSypqGDILFHDRSLLHADE 83
Cdd:TIGR01842 317 LSVENVTIV--PPGGKKPTLRGISFSLQAGEALAIIGPSGSGKS----TLARLIVGiwPPTS---GSVRLDGADLKQWDR 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 84 QTLrgirGNKIAMIFQEpmvslnplhslekqlyevLSLHRGMRKE-AARGEilDCLERTGIRNAAK------RLNDFPH- 155
Cdd:TIGR01842 388 ETF----GKHIGYLPQD------------------VELFPGTVAEnIARFG--ENADPEKIIEAAKlagvheLILRLPDg 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 156 ----------QLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDElNMSLLFITHNLSIVrKLAD 225
Cdd:TIGR01842 444 ydtvigpggaTLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKAR-GITVVVITHRPSLL-GCVD 521
|
....*....
gi 1278835479 226 SVAVMQNGR 234
Cdd:TIGR01842 522 KILVLQDGR 530
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
22-234 |
9.65e-10 |
|
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: 61.57 E-value: 9.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 22 RTVVSDLTLQIQRGETLALVGESGSGKSVSaLSILRLLpSPPVSypqGDILFHDRSLlhadEQTLRGIRgNKIAMIFQEP 101
Cdd:TIGR01257 943 RPAVDRLNITFYENQITAFLGHNGAGKTTT-LSILTGL-LPPTS---GTVLVGGKDI----ETNLDAVR-QSLGMCPQHN 1012
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 102 MVsLNPLHSLEKQLYevLSLHRGMRKEAARGEILDCLERTGIRNaaKRlNDFPHQLSGGERQRVMIAMALLTRPELLIAD 181
Cdd:TIGR01257 1013 IL-FHHLTVAEHILF--YAQLKGRSWEEAQLEMEAMLEDTGLHH--KR-NEEAQDLSGGMQRKLSVAIAFVGDAKVVVLD 1086
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1278835479 182 EPTTALDVTVQAQILTLLRDLRDelNMSLLFITHNLSIVRKLADSVAVMQNGR 234
Cdd:TIGR01257 1087 EPTSGVDPYSRRSIWDLLLKYRS--GRTIIMSTHHMDEADLLGDRIAIISQGR 1137
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
300-487 |
2.30e-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: 57.73 E-value: 2.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 300 PVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIASQGEILFDGMPLHRWNRRQMLPVRPRMQVVFqdpnSSLNPRL 379
Cdd:cd03290 15 ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAY----AAQKPWL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 380 sVLQIVEEGLRVHQPglSAQQREQEVM---RVMVEVGLDPETRHRYPAE----FSGGQRQRIAIARALILKPELIILDEP 452
Cdd:cd03290 91 -LNATVEENITFGSP--FNKQRYKAVTdacSLQPDIDLLPFGDQTEIGErginLSGGQRQRICVARALYQNTNIVFLDDP 167
|
170 180 190
....*....|....*....|....*....|....*..
gi 1278835479 453 TSSLDRTVQAQIL--ALLKGLQEKHRlAYIFISHDLQ 487
Cdd:cd03290 168 FSALDIHLSDHLMqeGILKFLQDDKR-TLVLVTHKLQ 203
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
299-503 |
3.16e-09 |
|
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: 57.94 E-value: 3.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 299 NPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALL-RLIASQGEILFDGM----PLHRWnrrqMLPVRPRMQVVFQDPNS 373
Cdd:cd03291 50 APVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILgELEPSEGKIKHSGRisfsSQFSW----IMPGTIKENIIFGVSYD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 374 SLNPRlSVLQiveeglrvhqpglsAQQREQEVMR-------VMVEVGLDpetrhrypaeFSGGQRQRIAIARALILKPEL 446
Cdd:cd03291 126 EYRYK-SVVK--------------ACQLEEDITKfpekdntVLGEGGIT----------LSGGQRARISLARAVYKDADL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1278835479 447 IILDEPTSSLDRTVQAQIL--ALLKGLQEKHRlayIFISHDLQVVRAlCHQVIVLRQGE 503
Cdd:cd03291 181 YLLDSPFGYLDVFTEKEIFesCVCKLMANKTR---ILVTSKMEHLKK-ADKILILHEGS 235
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
24-246 |
3.50e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 59.60 E-value: 3.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 24 VVSDLTLQIQRGETLALVGESGSGKSVSALSILRLlpsppVSYPQGDILFHDRSLLHADEQTLRGIrgnkIAMIFQEPMV 103
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRI-----VELEKGRIMIDDCDVAKFGLTDLRRV----LSIIPQSPVL 1321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 104 -------SLNPLhslekqlyevlslhrgmrKEAARGEILDCLERTGIRNAAKRlNDFP---------HQLSGGERQRVMI 167
Cdd:PLN03232 1322 fsgtvrfNIDPF------------------SEHNDADLWEALERAHIKDVIDR-NPFGldaevseggENFSVGQRQLLSL 1382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 168 AMALLTRPELLIADEPTTALDVTVQAQIltlLRDLRDEL-NMSLLFITHNLSIVRKlADSVAVMQNGRCVEQNAASTLLS 246
Cdd:PLN03232 1383 ARALLRRSKILVLDEATASVDVRTDSLI---QRTIREEFkSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLS 1458
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
259-502 |
5.61e-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: 59.26 E-value: 5.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 259 SEPSGDPVPLDAD--------------STPLLRVEDLSVSFPirkGILRRIVDRNPVlknirfSLRPGESLGLVGESGSG 324
Cdd:TIGR01257 1907 AEPAKEPIFDEDDdvaeerqriisggnKTDILRLNELTKVYS---GTSSPAVDRLCV------GVRPGECFGLLGVNGAG 1977
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 325 KSTTGLALL-RLIASQGEILFDGMPlhrwnrrqmlpVRPRMQVVFQdpNSSLNPRLSVLQIVEEG-----LRVHQPGLSA 398
Cdd:TIGR01257 1978 KTTTFKMLTgDTTVTSGDATVAGKS-----------ILTNISDVHQ--NMGYCPQFDAIDDLLTGrehlyLYARLRGVPA 2044
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 399 QQREQEVMRVMVEVGLDPETrHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRlA 478
Cdd:TIGR01257 2045 EEIEKVANWSIQSLGLSLYA-DRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGR-A 2122
|
250 260
....*....|....*....|....
gi 1278835479 479 YIFISHDLQVVRALCHQVIVLRQG 502
Cdd:TIGR01257 2123 VVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
302-490 |
8.51e-09 |
|
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: 55.02 E-value: 8.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 302 LKNIRFSLRPGESLGLVGESGSGKSTTglaLLRLIASQGEILFDGMplhrwnrrqmLPVRPRMQVVFQDPnsslnprlsv 381
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTL---VNEGLYASGKARLISF----------LPKFSRNKLIFIDQ---------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 382 lqiveeglrvhqpglsaqqreqevMRVMVEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPE--LIILDEPTSSLDRT 459
Cdd:cd03238 68 ------------------------LQFLIDVGLGYLTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQ 123
|
170 180 190
....*....|....*....|....*....|..
gi 1278835479 460 VQAQILALLKGL-QEKHRLayIFISHDLQVVR 490
Cdd:cd03238 124 DINQLLEVIKGLiDLGNTV--ILIEHNLDVLS 153
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
311-492 |
1.35e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 53.92 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 311 PGESLGLVGESGSGKSTTGLALLRLIASQGEilfdgmplhrwnrrqmlpvrprmQVVFQDPNSSLNPRLSVLQIVEeglr 390
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGG-----------------------GVIYIDGEDILEEVLDQLLLII---- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 391 vhqpglsaqqreqevmrvmvevgldpetRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILAL--- 467
Cdd:smart00382 54 ----------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeel 105
|
170 180
....*....|....*....|....*..
gi 1278835479 468 --LKGLQEKHRLAYIFISHDLQVVRAL 492
Cdd:smart00382 106 rlLLLLKSEKNLTVILTTNDEKDLGPA 132
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
25-233 |
2.48e-08 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 54.64 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 25 VSDLTLQIQRGETLALVGESGSGKSVSALSILRLLPSPpvsypQGDILFHDRSLLHADEQTLRGIRGNKIAMIFQEPMVs 104
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTL-----EGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWL- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 105 LNPL--------HSLEKQLYEVLSLHRGMRKEAargEILDCLERTGIrnAAKRLNdfphqLSGGERQRVMIAMALLTRPE 176
Cdd:cd03290 91 LNATveenitfgSPFNKQRYKAVTDACSLQPDI---DLLPFGDQTEI--GERGIN-----LSGGQRQRICVARALYQNTN 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1278835479 177 LLIADEPTTALDV-----TVQAQILTLLRDLRdelnMSLLFITHNLSIVRKlADSVAVMQNG 233
Cdd:cd03290 161 IVFLDDPFSALDIhlsdhLMQEGILKFLQDDK----RTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
300-477 |
2.85e-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: 56.84 E-value: 2.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 300 PVLKNIRFSLRPGESLGLVGESGSGKSTTGLALL-RLIASQGEILFDGM----PLHRWnrrqMLPVRPRMQVVFQDPNSS 374
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMgELEPSEGKIKHSGRisfsPQTSW----IMPGTIKDNIIFGLSYDE 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 375 LNPRlSVLQiveeglrvhqpglsAQQREQEVMR-------VMVEVGLdpetrhrypaEFSGGQRQRIAIARALILKPELI 447
Cdd:TIGR01271 516 YRYT-SVIK--------------ACQLEEDIALfpekdktVLGEGGI----------TLSGGQRARISLARAVYKDADLY 570
|
170 180 190
....*....|....*....|....*....|..
gi 1278835479 448 ILDEPTSSLDRTVQAQIL--ALLKGLQEKHRL 477
Cdd:TIGR01271 571 LLDSPFTHLDVVTEKEIFesCLCKLMSNKTRI 602
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
307-515 |
4.39e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.79 E-value: 4.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 307 FSLRPGESLGLVGESGSGKSTTGLALlrliasQGE-ILFDGMPLHRWNRRQMLPVRPRMQVV---FQDPNSSL------N 376
Cdd:PRK10938 24 LTLNAGDSWAFVGANGSGKSALARAL------AGElPLLSGERQSQFSHITRLSFEQLQKLVsdeWQRNNTDMlspgedD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 377 PRLSVLQIVEEGlrVHQPGLSAQQREQevmrvmveVGLDP--ETRHRYpaeFSGGQRQRIAIARALILKPELIILDEPTS 454
Cdd:PRK10938 98 TGRTTAEIIQDE--VKDPARCEQLAQQ--------FGITAllDRRFKY---LSTGETRKTLLCQALMSEPDLLILDEPFD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1278835479 455 SLDRTVQAQILALLKGLQeKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFS 515
Cdd:PRK10938 165 GLDVASRQQLAELLASLH-QSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQ 224
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
22-200 |
6.44e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 52.95 E-value: 6.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 22 RTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLLP--SPPVSypqGDILFHDrsllhaDEQTLRGIR------GNK 93
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKT----TLLRLIAglLPPAA---GTIKLDG------GDIDDPDVAeachylGHR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 94 IAMifqepmvslNPLHSLEkqlyEVLSLHRGMRKeAARGEILDCLERTGIRNAAkrlnDFPHQ-LSGGERQRVMIAMALL 172
Cdd:PRK13539 82 NAM---------KPALTVA----ENLEFWAAFLG-GEELDIAAALEAVGLAPLA----HLPFGyLSAGQKRRVALARLLV 143
|
170 180
....*....|....*....|....*...
gi 1278835479 173 TRPELLIADEPTTALDVTVQAQILTLLR 200
Cdd:PRK13539 144 SNRPIWILDEPTAALDAAAVALFAELIR 171
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
275-509 |
7.64e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 53.64 E-value: 7.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 275 LLRVEDLSVSfpirkgilrriVDRNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALL---RLIASQGEILFDGmplhr 351
Cdd:PRK09580 1 MLSIKDLHVS-----------VEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgreDYEVTGGTVEFKG----- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 352 wnrRQMLPVRPRMQ------VVFQDP------------NSSLNP-----------RLSVLQIVEEGLRVhqpglsaQQRE 402
Cdd:PRK09580 65 ---KDLLELSPEDRagegifMAFQYPveipgvsnqfflQTALNAvrsyrgqepldRFDFQDLMEEKIAL-------LKMP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 403 QEVMRVMVEVGldpetrhrypaeFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRlAYIFI 482
Cdd:PRK09580 135 EDLLTRSVNVG------------FSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKR-SFIIV 201
|
250 260
....*....|....*....|....*...
gi 1278835479 483 SHDLQVVRALCHQ-VIVLRQGEVVEQGE 509
Cdd:PRK09580 202 THYQRILDYIKPDyVHVLYQGRIVKSGD 229
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
308-509 |
9.14e-08 |
|
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: 53.18 E-value: 9.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 308 SLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLHRwnRRQMlpVRPRMQVVFQDPNSSLNPRLsvl 382
Cdd:cd03237 21 SISESEVIGILGPNGIGKTT----FIKMLAgvlkpDEGDIEIELDTVSY--KPQY--IKADYEGTVRDLLSSITKDF--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 383 qiveeglrvhqpgLSAQQREQEVMR-VMVEVGLDPETRhrypaEFSGGQRQRIAIARALILKPELIILDEPTSSLDrtVQ 461
Cdd:cd03237 90 -------------YTHPYFKTEIAKpLQIEQILDREVP-----ELSGGELQRVAIAACLSKDADIYLLDEPSAYLD--VE 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1278835479 462 AQILA--LLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLrQGEVVEQGE 509
Cdd:cd03237 150 QRLMAskVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVF-EGEPSVNGV 198
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
6-253 |
1.01e-07 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 53.37 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 6 LRIDNLSIAFskQDETRTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLlpsppVSYPQGDILFHDRSLLHADEQT 85
Cdd:cd03288 20 IKIHDLCVRY--ENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRM-----VDIFDGKIVIDGIDISKLPLHT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 86 LRgirgNKIAMIFQEPMV-------SLNP-LHSLEKQLYEVLSLH--RGMRKEAARGeiLDCLERTGIRNaakrlndfph 155
Cdd:cd03288 93 LR----SRLSIILQDPILfsgsirfNLDPeCKCTDDRLWEALEIAqlKNMVKSLPGG--LDAVVTEGGEN---------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 156 qLSGGERQRVMIAMALLTRPELLIADEPTTALDVT----VQAQILTLLRDlrdelnMSLLFITHNLSIVRKlADSVAVMQ 231
Cdd:cd03288 157 -FSVGQRQLFCLARAFVRKSSILIMDEATASIDMAteniLQKVVMTAFAD------RTVVTIAHRVSTILD-ADLVLVLS 228
|
250 260
....*....|....*....|..
gi 1278835479 232 NGRCVEQNAASTLLSAPQHPYT 253
Cdd:cd03288 229 RGILVECDTPENLLAQEDGVFA 250
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
300-491 |
1.07e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 52.26 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 300 PVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLHRwNRRQMlpvrpRMQVVFQDPNSS 374
Cdd:PRK13540 15 PLLQQISFHLPAGGLLHLKGSNGAGKTT----LLKLIAgllnpEKGEILFERQSIKK-DLCTY-----QKQLCFVGHRSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 375 LNPRLSVLQIVEEGLRVHQPGLSAqqreQEVMRVM-VEVGLDpetrhrYPAE-FSGGQRQRIAIARALILKPELIILDEP 452
Cdd:PRK13540 85 INPYLTLRENCLYDIHFSPGAVGI----TELCRLFsLEHLID------YPCGlLSSGQKRQVALLRLWMSKAKLWLLDEP 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1278835479 453 TSSLDrtvQAQILALLKGLQEkHRL---AYIFISH-DLQVVRA 491
Cdd:PRK13540 155 LVALD---ELSLLTIITKIQE-HRAkggAVLLTSHqDLPLNKA 193
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
125-244 |
1.18e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 53.97 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 125 MRKEAARGEILDCLERTGIRNAAKRLndfPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDL-R 203
Cdd:NF000106 116 LSRKDARARADELLERFSLTEAAGRA---AAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMvR 192
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1278835479 204 DelNMSLLFITHNLSIVRKLADSVAVMQNGRCVEQNAASTL 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 |
1.86e-07 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 53.86 E-value: 1.86e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1278835479 157 LSGGERQRVMIAMALLTR---PELLIADEPTTAL---DVtvqAQILTLLRDLRDELNmSLLFITHNLSIVrKLAD 225
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLhfdDI---KKLLEVLQRLVDKGN-TVVVIEHNLDVI-KTAD 899
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
5-237 |
2.06e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 52.10 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 5 LLRIDNLSIAFskqdETRTVVSDLTLQIQRGETLALVGESGSGKSVSALSilrLLPSPPVSYPQGDILFHDRSLLHADEQ 84
Cdd:PRK09580 1 MLSIKDLHVSV----EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSAT---LAGREDYEVTGGTVEFKGKDLLELSPE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 85 TLRGirgNKIAMIFQEPMvslnPLHSLEKQLYEVLSLH--RGMRKEAArgeiLDCLERTGIRNAAKRLNDFPHQL----- 157
Cdd:PRK09580 74 DRAG---EGIFMAFQYPV----EIPGVSNQFFLQTALNavRSYRGQEP----LDRFDFQDLMEEKIALLKMPEDLltrsv 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 158 ----SGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDElNMSLLFITHNLSIVRKLA-DSVAVMQN 232
Cdd:PRK09580 143 nvgfSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDG-KRSFIIVTHYQRILDYIKpDYVHVLYQ 221
|
....*
gi 1278835479 233 GRCVE 237
Cdd:PRK09580 222 GRIVK 226
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
310-488 |
2.09e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 52.37 E-value: 2.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 310 RPGESLGLVGESGSGKSTTglalLRLIASQ--------------GEIL--FDGMPLHRWNRR----QMLPVRpRMQVVFQ 369
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTA----LKILAGKlkpnlgkfddppdwDEILdeFRGSELQNYFTKllegDVKVIV-KPQYVDL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 370 DPNSSlnpRLSVLQIVEeglRVHQPGlsaqqREQEVMRVMvevGLDPeTRHRYPAEFSGGQRQRIAIARALILKPELIIL 449
Cdd:cd03236 99 IPKAV---KGKVGELLK---KKDERG-----KLDELVDQL---ELRH-VLDRNIDQLSGGELQRVAIAAALARDADFYFF 163
|
170 180 190
....*....|....*....|....*....|....*....
gi 1278835479 450 DEPTSSLDRTVQAQILALLKGLQEKHRlAYIFISHDLQV 488
Cdd:cd03236 164 DEPSSYLDIKQRLNAARLIRELAEDDN-YVLVVEHDLAV 201
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
155-217 |
2.57e-07 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 50.44 E-value: 2.57e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1278835479 155 HQLSGGERQRVMIAMAL----LTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMsLLFITHNL 217
Cdd:cd03227 76 LQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQ-VIVITHLP 141
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
259-370 |
2.61e-07 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 53.26 E-value: 2.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 259 SEPSGDPVPLDADSTPL------LRVEDLSVSFPIRKGilrrivDRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaL 332
Cdd:COG4615 305 ALAAAEPAAADAAAPPApadfqtLELRGVTYRYPGEDG------DEGFTLGPIDLTIRRGELVFIVGGNGSGKST----L 374
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1278835479 333 LRLI-----ASQGEILFDGMPLHRWNR---RQMlpvrprMQVVFQD 370
Cdd:COG4615 375 AKLLtglyrPESGEILLDGQPVTADNReayRQL------FSAVFSD 414
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
284-506 |
3.04e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 53.25 E-value: 3.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 284 SFPIRKGIlrRIVdrnpvLKNIRFSLRPGESLGLVGESGSGKSTTgLALLR--LIASQGEILFDGMPLHRW-NRRQMLPV 360
Cdd:PRK10636 6 SLQIRRGV--RVL-----LDNATATINPGQKVGLVGKNGCGKSTL-LALLKneISADGGSYTFPGNWQLAWvNQETPALP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 361 RPRMQVV-------------FQDPN--------SSLNPRLSVLQIVEEGLR----VHQPGLSAQQREQEVmrvmvevgld 415
Cdd:PRK10636 78 QPALEYVidgdreyrqleaqLHDANerndghaiATIHGKLDAIDAWTIRSRaaslLHGLGFSNEQLERPV---------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 416 petrhrypAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEkhrlAYIFISHDLQVVRALCHQ 495
Cdd:PRK10636 148 --------SDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQG----TLILISHDRDFLDPIVDK 215
|
250
....*....|.
gi 1278835479 496 VIVLRQGEVVE 506
Cdd:PRK10636 216 IIHIEQQSLFE 226
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
302-513 |
3.17e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 51.74 E-value: 3.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 302 LKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGmplhrwnrrqmlpvrprmQVVFQDPNSSLN 376
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKST----LSNIIGgslspTVGKVDRNG------------------EVSVIAISAGLS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 377 PRLSVLQIVEegLRVHQPGLSaQQREQEVMRVMVEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSL 456
Cdd:PRK13546 98 GQLTGIENIE--FKMLCMGFK-RKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1278835479 457 DRTVQAQILALLKGLQEKHRLAYiFISHDLQVVRALCHQVIVLRQGEVVEQGECQRV 513
Cdd:PRK13546 175 DQTFAQKCLDKIYEFKEQNKTIF-FVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDV 230
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
157-225 |
4.38e-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: 4.38e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1278835479 157 LSGGERQRVMIA--MALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNmSLLFITHNLSIVrKLAD 225
Cdd:cd03238 88 LSGGELQRVKLAseLFSEPPGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGN-TVILIEHNLDVL-SSAD 156
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
299-518 |
4.95e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 52.67 E-value: 4.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 299 NPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLrliasqGEIlfDGMPLHRWNRRQMLPVRPRMQVVFqdpNSSLNPR 378
Cdd:PLN03232 630 KPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAML------GEL--SHAETSSVVIRGSVAYVPQVSWIF---NATVREN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 379 LSVLQIVEEGLRVHQPGLSAQQREQEVM--RVMVEVGldpetrhRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSL 456
Cdd:PLN03232 699 ILFGSDFESERYWRAIDVTALQHDLDLLpgRDLTEIG-------ERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSAL 771
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1278835479 457 DRTVQAQIL--ALLKGLQEKHRlayIFISHDLQVVrALCHQVIVLRQGEVVEQGECQRVFSAPT 518
Cdd:PLN03232 772 DAHVAHQVFdsCMKDELKGKTR---VLVTNQLHFL-PLMDRIILVSEGMIKEEGTFAELSKSGS 831
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
284-511 |
4.98e-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: 52.64 E-value: 4.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 284 SFPIRKGILRRIVDRNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALL-RLIASQGEILFDG----MPLHRWNRRQML 358
Cdd:TIGR00957 636 SITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLaEMDKVEGHVHMKGsvayVPQQAWIQNDSL 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 359 pvrpRMQVVFQDPnssLNPR-----------LSVLQIVEEGLRVHqpglsaqqreqevmrvMVEVGLDpetrhrypaeFS 427
Cdd:TIGR00957 716 ----RENILFGKA---LNEKyyqqvleacalLPDLEILPSGDRTE----------------IGEKGVN----------LS 762
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 428 GGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKG----LQEKHRlayIFISHDLQVVRALcHQVIVLRQGE 503
Cdd:TIGR00957 763 GGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGpegvLKNKTR---ILVTHGISYLPQV-DVIIVMSGGK 838
|
....*...
gi 1278835479 504 VVEQGECQ 511
Cdd:TIGR00957 839 ISEMGSYQ 846
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
427-503 |
5.09e-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: 5.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 427 SGGQRQ------RIAIARALILKPELIILDEPTSSLDR-TVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVL 499
Cdd:cd03240 117 SGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEeNIEESLAEIIEERKSQKNFQLIVITHDEELVDAADHIYRVE 196
|
....
gi 1278835479 500 RQGE 503
Cdd:cd03240 197 KDGR 200
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
148-229 |
5.90e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.12 E-value: 5.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 148 KRLNDfphqLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSV 227
Cdd:PRK13409 449 KNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRL 524
|
..
gi 1278835479 228 AV 229
Cdd:PRK13409 525 MV 526
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
307-484 |
6.00e-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: 52.06 E-value: 6.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 307 FSLRPGESLGLVGESGSGKSTtglaLLRLIasqGEI--LFDG-MPLHRWNRRQMLPVRPRM-------QVVFQDpnssln 376
Cdd:TIGR00954 473 FEVPSGNNLLICGPNGCGKSS----LFRIL---GELwpVYGGrLTKPAKGKLFYVPQRPYMtlgtlrdQIIYPD------ 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 377 prlSVLQIVEEGLRvhqpglsaqqrEQEVMRVMVEVGLDP--------ETRHRYPAEFSGGQRQRIAIARALILKPELII 448
Cdd:TIGR00954 540 ---SSEDMKRRGLS-----------DKDLEQILDNVQLTHilereggwSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAI 605
|
170 180 190
....*....|....*....|....*....|....*.
gi 1278835479 449 LDEPTSSLDRTVQAQILALLKglqeKHRLAYIFISH 484
Cdd:TIGR00954 606 LDECTSAVSVDVEGYMYRLCR----EFGITLFSVSH 637
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
300-508 |
6.73e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 52.32 E-value: 6.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 300 PVLKNIRFSLRPGESLGLVGESGSGKSTTgLALLR--LIASQGEILFDGMPLHRW--NRRQMLPVRPRMQVVFQDpnssl 375
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTT-LSILTglLPPTSGTVLVGGKDIETNldAVRQSLGMCPQHNILFHH----- 1017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 376 nprlsvLQIVEEGLRVHQPGLSAQQREQEVMRVMVE-VGLDpETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTS 454
Cdd:TIGR01257 1018 ------LTVAEHILFYAQLKGRSWEEAQLEMEAMLEdTGLH-HKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTS 1090
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1278835479 455 SLDRTVQAQILALLkgLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:TIGR01257 1091 GVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
3-242 |
7.29e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.42 E-value: 7.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 3 QPLLRIDNLSIAFsKQDETRTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLLPSPPVSYPQGDilfhdRSLLHAD 82
Cdd:TIGR00956 56 KILTRGFRKLKKF-RDTKTFDILKPMDGLIKPGELTVVLGRPGSGCS----TLLKTIASNTDGFHIGV-----EGVITYD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 83 eqtlrGIRGNKIAMIFQEPMV--SLNPLHSLEKQLYEVLSLHRGMRKEAARGEILDCLERTG-IRNAAKRL--------- 150
Cdd:TIGR00956 126 -----GITPEEIKKHYRGDVVynAETDVHFPHLTVGETLDFAARCKTPQNRPDGVSREEYAKhIADVYMATyglshtrnt 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 151 ---NDFPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSI-VRKLADS 226
Cdd:TIGR00956 201 kvgNDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCSQdAYELFDK 280
|
250
....*....|....*.
gi 1278835479 227 VAVMQNGRCVEQNAAS 242
Cdd:TIGR00956 281 VIVLYEGYQIYFGPAD 296
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
24-246 |
7.64e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 52.05 E-value: 7.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 24 VVSDLTLQIQRGETLALVGESGSGKSVSALSILRLlpsppVSYPQGDILFHDRSLLHADEQTLRGIRGnkiaMIFQEPMV 103
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRI-----VELERGRILIDGCDISKFGLMDLRKVLG----IIPQAPVL 1324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 104 -------SLNPL--HSlEKQLYEvlSLHRGMRKEAargeildclertgIRNAAKRLN----DFPHQLSGGERQRVMIAMA 170
Cdd:PLN03130 1325 fsgtvrfNLDPFneHN-DADLWE--SLERAHLKDV-------------IRRNSLGLDaevsEAGENFSVGQRQLLSLARA 1388
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1278835479 171 LLTRPELLIADEPTTALDVTVQAQIltlLRDLRDEL-NMSLLFITHNLSIVRKlADSVAVMQNGRCVEQNAASTLLS 246
Cdd:PLN03130 1389 LLRRSKILVLDEATAAVDVRTDALI---QKTIREEFkSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLLS 1461
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
280-471 |
9.76e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 51.65 E-value: 9.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 280 DLSVSFPIRKGILRrivdrnpVLKNIRFSLRPGESLGLVGESGSGKsTTGLALL--RL---IASQGEILFDGMPLHRWNR 354
Cdd:TIGR00956 764 NLTYEVKIKKEKRV-------ILNNVDGWVKPGTLTALMGASGAGK-TTLLNVLaeRVttgVITGGDRLVNGRPLDSSFQ 835
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 355 RQMLPVRPrmqvvfQDPNSslnPRLSVLQIVEEGLRVHQPG-LSAQQREQEVMRVM--VE--------VGLdpetrhryP 423
Cdd:TIGR00956 836 RSIGYVQQ------QDLHL---PTSTVRESLRFSAYLRQPKsVSKSEKMEYVEEVIklLEmesyadavVGV--------P 898
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1278835479 424 AE-FSGGQRQRIAIARALILKPELII-LDEPTSSLDRTVQAQILALLKGL 471
Cdd:TIGR00956 899 GEgLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKL 948
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
157-231 |
1.02e-06 |
|
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: 49.11 E-value: 1.02e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1278835479 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQ 231
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
157-225 |
1.18e-06 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 49.92 E-value: 1.18e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1278835479 157 LSGGERQRVMIAMALL---TRPELLIADEPTTALDVTVQAQILTLLRDLRDELNmSLLFITHNLSIVrKLAD 225
Cdd:cd03271 170 LSGGEAQRIKLAKELSkrsTGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGN-TVVVIEHNLDVI-KCAD 239
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
302-508 |
1.62e-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: 49.18 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 302 LKNIRFSLRPGESLGLVGESGSGKSTtgLALlRLIASQGEilfdgmplHRWNR------RQMLPVRPRMQVVF------- 368
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSS--LAF-DTIYAEGQ--------RRYVEslsayaRQFLGQMDKPDVDSieglspa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 369 ---QDPNSSLNPRLSVLQIVE--EGLRVhqpgLSAQQREQEVMRVMVEVGLDPETRHRYPAEFSGGQRQRIAIARAL--I 441
Cdd:cd03270 80 iaiDQKTTSRNPRSTVGTVTEiyDYLRL----LFARVGIRERLGFLVDVGLGYLTLSRSAPTLSGGEAQRIRLATQIgsG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1278835479 442 LKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRlAYIFISHDLQVVRALCHQVIV-----LRQGEVVEQG 508
Cdd:cd03270 156 LTGVLYVLDEPSIGLHPRDNDRLIETLKRLRDLGN-TVLVVEHDEDTIRAADHVIDIgpgagVHGGEIVAQG 226
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
417-509 |
1.77e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 50.12 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 417 ETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQeKHRLAYIFISHDLQVVRALCHQV 496
Cdd:NF000106 136 EAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMV-RDGATVLLTTQYMEEAEQLAHEL 214
|
90
....*....|...
gi 1278835479 497 IVLRQGEVVEQGE 509
Cdd:NF000106 215 TVIDRGRVIADGK 227
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
157-225 |
1.91e-06 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 50.80 E-value: 1.91e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1278835479 157 LSGGERQRVMIAMALL---TRPELLIADEPTTAL---DVtvqAQILTLLRDLRDELNmSLLFITHNLSIVrKLAD 225
Cdd:COG0178 827 LSGGEAQRVKLASELSkrsTGKTLYILDEPTTGLhfhDI---RKLLEVLHRLVDKGN-TVVVIEHNLDVI-KTAD 896
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
24-219 |
2.79e-06 |
|
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: 50.13 E-value: 2.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 24 VVSDLTLQIQRGETLALVGESGSGKSvsalSILRLLPSP-PVSYPqgdilfhdrsllhadeqTLRGIRGNKIAMIFQEPM 102
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKS----SLFRILGELwPVYGG-----------------RLTKPAKGKLFYVPQRPY 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 103 VSLNPLHslEKQLYEVLSLH---RGMRkEAARGEILD------CLERTGIRNAakrLNDFPHQLSGGERQRVMIAMALLT 173
Cdd:TIGR00954 526 MTLGTLR--DQIIYPDSSEDmkrRGLS-DKDLEQILDnvqlthILEREGGWSA---VQDWMDVLSGGEKQRIAMARLFYH 599
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1278835479 174 RPELLIADEPTTALDVTVQAQILTLLRdlrdELNMSLLFITHNLSI 219
Cdd:TIGR00954 600 KPQFAILDECTSAVSVDVEGYMYRLCR----EFGITLFSVSHRKSL 641
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-295 |
3.06e-06 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 50.33 E-value: 3.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 18 QDETRTVVSdLTLQIQRGETLALVGESGSGKSvsalSILrllpsppvsypqgdilfhdrSLLHADEQTLRG---IRGNkI 94
Cdd:TIGR00957 648 RDLPPTLNG-ITFSIPEGALVAVVGQVGCGKS----SLL--------------------SALLAEMDKVEGhvhMKGS-V 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 95 AMIFQEPMVSLNPL-------HSLEKQLYEVLslhrgMRKEA--ARGEILDCLERTGIrnAAKRLNdfphqLSGGERQRV 165
Cdd:TIGR00957 702 AYVPQQAWIQNDSLrenilfgKALNEKYYQQV-----LEACAllPDLEILPSGDRTEI--GEKGVN-----LSGGQKQRV 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 166 MIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDEL-NMSLLFITHNLSIVRKLaDSVAVMQNGRCVEQNAASTL 244
Cdd:TIGR00957 770 SLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGPEGVLkNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQEL 848
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 245 LsAPQHPYTQRLLNSEPSGDPVPLDADSTPL--------LRVED-LSVSFPIRKGILRRI 295
Cdd:TIGR00957 849 L-QRDGAFAEFLRTYAPDEQQGHLEDSWTALvsgegkeaKLIENgMLVTDVVGKQLQRQL 907
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
22-188 |
6.71e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.58 E-value: 6.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 22 RTVVSDLTLQIQRGETLALVGESGSGKSvSALSIL-----------RLLPSPPVSY----PQGDilfhdrsllhaDEQTL 86
Cdd:PRK11819 20 KQILKDISLSFFPGAKIGVLGLNGAGKS-TLLRIMagvdkefegeaRPAPGIKVGYlpqePQLD-----------PEKTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 87 RGI-------------RGNKIAMIFQEPMVSLNPLhsLEKQ--LYEVLslhrgmrkEAARGEILDC-LERtgirnAAKRL 150
Cdd:PRK11819 88 RENveegvaevkaaldRFNEIYAAYAEPDADFDAL--AAEQgeLQEII--------DAADAWDLDSqLEI-----AMDAL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1278835479 151 N----DFP-HQLSGGERQRVMIAMALLTRPELLIADEPTTALD 188
Cdd:PRK11819 153 RcppwDAKvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
276-505 |
7.04e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 48.73 E-value: 7.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 276 LRVEDLSVSFpirkgilrrivDRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIAS-----QGEIlfdgmplh 350
Cdd:PRK15064 320 LEVENLTKGF-----------DNGPLFKNLNLLLEAGERLAIIGENGVGKTT----LLRTLVGelepdSGTV-------- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 351 RWNRRQMLPVRPrmqvvfQDPNSSLNPRLSVLQIVEEglrVHQPGlsaqQREQeVMRVMVEVGLDPETRHRYPAE-FSGG 429
Cdd:PRK15064 377 KWSENANIGYYA------QDHAYDFENDLTLFDWMSQ---WRQEG----DDEQ-AVRGTLGRLLFSQDDIKKSVKvLSGG 442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1278835479 430 QRQRIAIARALILKPELIILDEPTSSLD-RTVQAQILALlkglqEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVV 505
Cdd:PRK15064 443 EKGRMLFGKLMMQKPNVLVMDEPTNHMDmESIESLNMAL-----EKYEGTLIFVSHDREFVSSLATRIIEITPDGVV 514
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
157-225 |
7.08e-06 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 48.92 E-value: 7.08e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1278835479 157 LSGGERQRVMIAMALLTRP---ELLIADEPTTAL---DVtvqAQILTLLRDLRDELNmSLLFITHNLSIVrKLAD 225
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRStgkTLYILDEPTTGLhfeDI---RKLLEVLHRLVDKGN-TVVVIEHNLDVI-KTAD 900
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
427-501 |
7.40e-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: 46.20 E-value: 7.40e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1278835479 427 SGGQRQRIAIARALIL---KPE-LIILDEPTSSLDRTVQAQILALLKGLQeKHRLAYIFISHDLQVVRALCHQVIVLRQ 501
Cdd:cd03227 79 SGGEKELSALALILALaslKPRpLYILDEIDRGLDPRDGQALAEAILEHL-VKGAQVIVITHLPELAELADKLIHIKKV 156
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
272-457 |
7.76e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 47.15 E-value: 7.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 272 STPLLRVEDLSVSfpirkgilrriVDRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDG 346
Cdd:PRK13543 8 APPLLAAHALAFS-----------RNEEPVFGPLDFHVDAGEALLVQGDNGAGKTT----LLRVLAgllhvESGQIQIDG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 347 MPLHRWNRRQMLPVRPRMqvvfqdpnSSLNPRLSVLQIVEEGLRVHqpGLSAQQREQEVMRVmveVGL----DPETRHry 422
Cdd:PRK13543 73 KTATRGDRSRFMAYLGHL--------PGLKADLSTLENLHFLCGLH--GRRAKQMPGSALAI---VGLagyeDTLVRQ-- 137
|
170 180 190
....*....|....*....|....*....|....*
gi 1278835479 423 paeFSGGQRQRIAIARALILKPELIILDEPTSSLD 457
Cdd:PRK13543 138 ---LSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
427-508 |
9.64e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 48.58 E-value: 9.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 427 SGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQIL-ALLKG-LQEKHRLAYIFISHDLQVVralcHQVIVLRQGEV 504
Cdd:PLN03130 742 SGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFdKCIKDeLRGKTRVLVTNQLHFLSQV----DRIILVHEGMI 817
|
....
gi 1278835479 505 VEQG 508
Cdd:PLN03130 818 KEEG 821
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
34-224 |
1.42e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 45.06 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 34 RGETLALVGESGSGKSVSALSILRLLPsppvsYPQGDILFHDrsllhadeqtlrgirgnkiamifqepmvslnplhslek 113
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELG-----PPGGGVIYID-------------------------------------- 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 114 qlyevlslhrgmrkeaarGEILdcLERTGIRNAAKRLNDFPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQA 193
Cdd:smart00382 38 ------------------GEDI--LEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEA 97
|
170 180 190
....*....|....*....|....*....|....*.
gi 1278835479 194 QILTLLRDLRD-----ELNMSLLFITHNLSIVRKLA 224
Cdd:smart00382 98 LLLLLEELRLLlllksEKNLTVILTTNDEKDLGPAL 133
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
236-265 |
2.01e-05 |
|
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found towards the C-terminus of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid.
Pssm-ID: 400588 [Multi-domain] Cd Length: 65 Bit Score: 42.39 E-value: 2.01e-05
10 20 30
....*....|....*....|....*....|
gi 1278835479 236 VEQNAASTLLSAPQHPYTQRLLNSEPSGDP 265
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPRLDP 30
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
157-249 |
2.05e-05 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 46.25 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITHNLSIVRKLADSVAVMQNgrcv 236
Cdd:cd03237 116 LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVFEG---- 191
|
90
....*....|...
gi 1278835479 237 eQNAASTLLSAPQ 249
Cdd:cd03237 192 -EPSVNGVANPPQ 203
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
297-457 |
2.36e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 47.53 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 297 DRNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIAS-------QGEILFDGMPlhrwnRRQMLPVRPRMQVVFQ 369
Cdd:PLN03140 891 DRLQLLREVTGAFRPGVLTALMGVSGAGKTT----LMDVLAGrktggyiEGDIRISGFP-----KKQETFARISGYCEQN 961
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 370 DPNSslnPRLSVLQ--IVEEGLRvhqpgLSAQQREQEVMR----VM--VE--------VGLDPETrhrypaEFSGGQRQR 433
Cdd:PLN03140 962 DIHS---PQVTVREslIYSAFLR-----LPKEVSKEEKMMfvdeVMelVEldnlkdaiVGLPGVT------GLSTEQRKR 1027
|
170 180
....*....|....*....|....
gi 1278835479 434 IAIARALILKPELIILDEPTSSLD 457
Cdd:PLN03140 1028 LTIAVELVANPSIIFMDEPTSGLD 1051
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
157-227 |
3.14e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.13 E-value: 3.14e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1278835479 157 LSGGERQRVMIAMALLT---RPELLIADEPTTALDVTVQAQILTLLRDLRDeLNMSLLFITHNLSIVrKLADSV 227
Cdd:PRK00635 810 LSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTH-QGHTVVIIEHNMHVV-KVADYV 881
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
4-234 |
4.15e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 46.32 E-value: 4.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 4 PLLRIDNLSIAFSKqdetRTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLLpSPPVSYPQGDILF---------- 73
Cdd:PRK10636 311 PLLKMEKVSAGYGD----RIILDSIKLNLVPGSRIGLLGRNGAGKS----TLIKLL-AGELAPVSGEIGLakgiklgyfa 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 74 -HDRSLLHADEQTLrgirgnkiamifqEPMVSLNPlHSLEKQLYEVLSlhrgmrkeaargeildclertGIRNAAKRLND 152
Cdd:PRK10636 382 qHQLEFLRADESPL-------------QHLARLAP-QELEQKLRDYLG---------------------GFGFQGDKVTE 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 153 FPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDelnmSLLFITHNLSIVRKLADSVAVMQN 232
Cdd:PRK10636 427 ETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEG----ALVVVSHDRHLLRSTTDDLYLVHD 502
|
..
gi 1278835479 233 GR 234
Cdd:PRK10636 503 GK 504
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
425-499 |
5.16e-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: 5.16e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1278835479 425 EFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVL 499
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVF 145
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
24-249 |
9.55e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 45.54 E-value: 9.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 24 VVSDLTLQIQRGETLALVGESGSGKSVSALSILRLlpsppVSYPQGDILFHDRSLlhaDEQTLRGIRgNKIAMIFQEPM- 102
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRM-----VEVCGGEIRVNGREI---GAYGLRELR-RQFSMIPQDPVl 1395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 103 ----VSLNPLHSLEKQLYEV---LSLhRGMRKEAARgeildclERTGIRNaakRLNDFPHQLSGGERQRVMIAMALLTRP 175
Cdd:PTZ00243 1396 fdgtVRQNVDPFLEASSAEVwaaLEL-VGLRERVAS-------ESEGIDS---RVLEGGSNYSVGQRQLMCMARALLKKG 1464
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1278835479 176 ELLI-ADEPTT----ALDVTVQAQILTLLRdlrdelNMSLLFITHNLSIVRKLaDSVAVMQNGRCVEQNAASTLLSAPQ 249
Cdd:PTZ00243 1465 SGFIlMDEATAnidpALDRQIQATVMSAFS------AYTVITIAHRLHTVAQY-DKIIVMDHGAVAEMGSPRELVMNRQ 1536
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
5-236 |
1.28e-04 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 45.00 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 5 LLRIDNLSIAFSkqDETRTVVSDLTLQIQRGETLALVGESGSGKSVSalsiLRLLpsppvsypQGDILFHDRSLLHADEQ 84
Cdd:TIGR01257 1937 ILRLNELTKVYS--GTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTT----FKML--------TGDTTVTSGDATVAGKS 2002
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 85 TLRGIRGNKIAMIFQEPMVSLNPLHSLEKQLYEVLSLhRGMRKEAARGEILDCLERTGIRNAAKRLNDfphQLSGGERQR 164
Cdd:TIGR01257 2003 ILTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARL-RGVPAEEIEKVANWSIQSLGLSLYADRLAG---TYSGGNKRK 2078
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1278835479 165 VMIAMALLTRPELLIADEPTTALDVTVQAQ----ILTLLRDLRdelnmSLLFITHNLSIVRKLADSVAVMQNG--RCV 236
Cdd:TIGR01257 2079 LSTAIALIGCPPLVLLDEPTTGMDPQARRMlwntIVSIIREGR-----AVVLTSHSMEECEALCTRLAIMVKGafQCL 2151
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
425-499 |
1.28e-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: 1.28e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1278835479 425 EFSGGQRQRIAIARALILKPELIILDEPTSSLD---RTVQAQilaLLKGLQEKHRlAYIFISHDLQVVRALCHQVIVL 499
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDiyqRLNVAR---LIRELAEEGK-YVLVVEHDLAILDYLADYVHIL 285
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
302-485 |
1.45e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 44.58 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 302 LKNIRFSLRPGESLGLVGESGSGKSTTGLALLRL-IASQGEILFDGMPLHRWNRRQMlpvRPRMQVVFQDPNssLNPRLs 380
Cdd:PRK10522 339 VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLyQPQSGEILLDGKPVTAEQPEDY---RKLFSAVFTDFH--LFDQL- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 381 vlqIVEEGLRVhQPGLSAQQREQEVMRVMVEVgldpETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLD--- 457
Cdd:PRK10522 413 ---LGPEGKPA-NPALVEKWLERLKMAHKLEL----EDGRISNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDphf 484
|
170 180
....*....|....*....|....*....
gi 1278835479 458 RTVQAQIlaLLKGLQEKHRLayIF-ISHD 485
Cdd:PRK10522 485 RREFYQV--LLPLLQEMGKT--IFaISHD 509
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
156-227 |
1.58e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 42.98 E-value: 1.58e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1278835479 156 QLSGGERQ------RVMIAMALLTRPELLIADEPTTALDV-TVQAQILTLLRDLRDELNMSLLFITHNLSIVRkLADSV 227
Cdd:cd03240 115 RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEeNIEESLAEIIEERKSQKNFQLIVITHDEELVD-AADHI 192
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
7-237 |
1.94e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 43.27 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 7 RIDNLSIAFSKqDETRTVVSDLTLQIQRGETLALVGESGSGKSVSALSILRLLPspPVSypqGDILFH-DRSLLHADEqt 85
Cdd:PRK13546 23 RMKDALIPKHK-NKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLS--PTV---GKVDRNgEVSVIAISA-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 86 lrGIRGNkiamifqepmvslnpLHSLEKQLYEVLSLhrGM-RKE--AARGEILDCLErtgirnaakrLNDFPHQ----LS 158
Cdd:PRK13546 95 --GLSGQ---------------LTGIENIEFKMLCM--GFkRKEikAMTPKIIEFSE----------LGEFIYQpvkkYS 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1278835479 159 GGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRdELNMSLLFITHNLSIVRKLADSVAVMQNGRCVE 237
Cdd:PRK13546 146 SGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFK-EQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKD 223
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
404-508 |
1.97e-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: 43.37 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 404 EVMRVMVEVGLDPETRHRYPAEFSGGQRQRIAIARALiLKPE----LIILDEPTSSLDRTVQAQILALLKGLQEKHRLAy 479
Cdd:cd03271 148 RKLQTLCDVGLGYIKLGQPATTLSGGEAQRIKLAKEL-SKRStgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTV- 225
|
90 100 110
....*....|....*....|....*....|....*
gi 1278835479 480 IFISHDLQVVRAlCHQVIVL------RQGEVVEQG 508
Cdd:cd03271 226 VVIEHNLDVIKC-ADWIIDLgpeggdGGGQVVASG 259
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
425-499 |
2.81e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 43.64 E-value: 2.81e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1278835479 425 EFSGGQRQRIAIARALILKPELIILDEPTSSLD---RTVQAQilaLLKGLQEKHrlAYIFISHDLQVVRALCHQVIVL 499
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLDirqRLNVAR---LIRELAEGK--YVLVVEHDLAVLDYLADNVHIA 284
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
24-260 |
3.43e-04 |
|
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: 43.75 E-value: 3.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 24 VVSDLTLQIQRGETLALVGESGSGKSVSALSIL-RLLPSPPVSYPQGDILFhdrsllhaDEQTLRGIRGNkiamifqepm 102
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMgELEPSEGKIKHSGRISF--------SPQTSWIMPGT---------- 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 103 VSLNPLHSLEKQLYEVLSLHRGMRKEAargEILDCLERTGIRnaakrLNDFPHQLSGGERQRVMIAMALLTRPELLIADE 182
Cdd:TIGR01271 503 IKDNIIFGLSYDEYRYTSVIKACQLEE---DIALFPEKDKTV-----LGEGGITLSGGQRARISLARAVYKDADLYLLDS 574
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1278835479 183 PTTALDVTVQAQIL-TLLRDLRdeLNMSLLFITHNLSIVRKlADSVAVMQNGRCVEQNAASTlLSAPQHPYTQRLLNSE 260
Cdd:TIGR01271 575 PFTHLDVVTEKEIFeSCLCKLM--SNKTRILVTSKLEHLKK-ADKILLLHEGVCYFYGTFSE-LQAKRPDFSSLLLGLE 649
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
138-215 |
4.92e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 42.69 E-value: 4.92e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1278835479 138 LERTGIrnaAKRLNDFP-HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRDLRDELNMSLLFITH 215
Cdd:PRK10938 385 LDILGI---DKRTADAPfHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSH 460
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
427-509 |
5.02e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 43.23 E-value: 5.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 427 SGGQRQRIAIARALILKPELIILDEPTSSLD-----RTVQAQILALLKGlqeKHRlayIFISHDLQVVrALCHQVIVLRQ 501
Cdd:PTZ00243 784 SGGQKARVSLARAVYANRDVYLLDDPLSALDahvgeRVVEECFLGALAG---KTR---VLATHQVHVV-PRADYVVALGD 856
|
....*...
gi 1278835479 502 GEVVEQGE 509
Cdd:PTZ00243 857 GRVEFSGS 864
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
6-224 |
5.79e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 42.57 E-value: 5.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 6 LRIDNLSIAFskqdETRTVVSDLTLQIQRGETLALVGESGSGKSvsalSILRLLpsppvsypQGDilfhdrslLHADEQT 85
Cdd:PRK15064 320 LEVENLTKGF----DNGPLFKNLNLLLEAGERLAIIGENGVGKT----TLLRTL--------VGE--------LEPDSGT 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 86 LRGIRGNKIAMIFQEPmvslnplhslEKQLYEVLSLHRGMRKEAARGEildclERTGIRNAAKRL----NDFPHQ---LS 158
Cdd:PRK15064 376 VKWSENANIGYYAQDH----------AYDFENDLTLFDWMSQWRQEGD-----DEQAVRGTLGRLlfsqDDIKKSvkvLS 440
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1278835479 159 GGERQRVMIAMALLTRPELLIADEPTTALDV-TVQAqiltllrdlrdeLNM-------SLLFITHNLSIVRKLA 224
Cdd:PRK15064 441 GGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMeSIES------------LNMalekyegTLIFVSHDREFVSSLA 502
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
156-193 |
6.25e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.41 E-value: 6.25e-04
10 20 30
....*....|....*....|....*....|....*....
gi 1278835479 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDV-TVQA 193
Cdd:PRK11819 445 VLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVeTLRA 483
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
404-499 |
1.49e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.74 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 404 EVMRVMVEVGLDPETRHRYPAEFSGGQRQRIAIARALIL---KPELIILDEPTSSL-DRTVQAQILALLKGLQEKHRLay 479
Cdd:PRK00635 788 EKIHALCSLGLDYLPLGRPLSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLhTHDIKALIYVLQSLTHQGHTV-- 865
|
90 100
....*....|....*....|
gi 1278835479 480 IFISHDLQVVRaLCHQVIVL 499
Cdd:PRK00635 866 VIIEHNMHVVK-VADYVLEL 884
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
406-508 |
2.76e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.38 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 406 MRVMVEVGLDPETRHRYPAEFSGGQRQRIAIARALILK---PELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAyIFI 482
Cdd:TIGR00630 810 LQTLCDVGLGYIRLGQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTV-VVI 888
|
90 100 110
....*....|....*....|....*....|..
gi 1278835479 483 SHDLQVVRALCHqVIVL------RQGEVVEQG 508
Cdd:TIGR00630 889 EHNLDVIKTADY-IIDLgpeggdGGGTVVASG 919
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
157-206 |
3.60e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 40.11 E-value: 3.60e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1278835479 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTllRDLRDEL 206
Cdd:PLN03130 741 ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFD--KCIKDEL 788
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
282-529 |
3.85e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.20 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 282 SVSFPIRKGILRRIVDRnpvlknIRFSLRPGESL--GLVGESGSGKSTTGLALLRLIAS-QGE--ILFDGMPLHRWnrrq 356
Cdd:PRK00635 363 TLTHKVWRGVLNEIGEK------VRYSNKPSRYLpkGTSATSCPRCQGTGLGDYANAATwHGKtfAEFQQMSLQEL---- 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 357 mlpvrprmqVVFqdpNSSLNPRLSVLQIVEEGLRvhqpglsaqQReqevMRVMVEVGLDPETRHRYPAEFSGGQRQRIAI 436
Cdd:PRK00635 433 ---------FIF---LSQLPSKSLSIEEVLQGLK---------SR----LSILIDLGLPYLTPERALATLSGGEQERTAL 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835479 437 ARAliLKPELI----ILDEPTSSLDRTVQAQILALLKGLQEKHRlAYIFISHDLQVVrALCHQVIVLRQ------GEVVE 506
Cdd:PRK00635 488 AKH--LGAELIgityILDEPSIGLHPQDTHKLINVIKKLRDQGN-TVLLVEHDEQMI-SLADRIIDIGPgagifgGEVLF 563
|
250 260
....*....|....*....|....*.
gi 1278835479 507 QGECQRVF---SAPTQRYTRQLLSSD 529
Cdd:PRK00635 564 NGSPREFLaksDSLTAKYLRQELTIP 589
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
157-204 |
5.08e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 39.71 E-value: 5.08e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1278835479 157 LSGGERQRVMIAMALLTRPELLI-ADEPTTALDVTVQAQILTLLRDLRD 204
Cdd:TIGR00956 902 LNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLAD 950
|
|
| |
