|
Name |
Accession |
Description |
Interval |
E-value |
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
8-552 |
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: 718.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 8 SAAPILTLKDVCIGFptttasgRRSKSLTDVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGDGEVTGGTITFD 87
Cdd:COG4172 2 MSMPLLSVEDLSVAF-------GQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAAHPSGSILFD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 88 GRDITHLTDREFVSIRGNGIGLVPQDPMTNLNPVWTVGSQIKEALRANNIATGSEAHKKAIELLEQAGLPNAKKRIDQYP 167
Cdd:COG4172 75 GQDLLGLSERELRRIRGNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPERRLDAYP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 168 HEFSGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGR 247
Cdd:COG4172 155 HQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 248 VVETGPALQVLTRPQHPYTKQLIAAAPSLAARRgdrvvaapttSDADQKEILVAKNLVRDFAIRGDRPWR-KDSFRAVDD 326
Cdd:COG4172 235 IVEQGPTAELFAAPQHPYTRKLLAAEPRGDPRP----------VPPDAPPLLEARDLKVWFPIKRGLFRRtVGHVKAVDG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 327 ISFTLRRGRTIGIVGESGSGKSTVANMALGLLdPTEGEVLFDGKRVQGRNRKEELELRRRIQPIFQNPYATLDPMRTVHS 406
Cdd:COG4172 305 VSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRALRPLRRRMQVVFQDPFGSLSPRMTVGQ 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 407 SIEEPLRIHKIG-TKKEREQRVFELLDRVALPAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVSALDVVVQAQ 485
Cdd:COG4172 384 IIAEGLRVHGPGlSAAERRARVAEALEEVGLDPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQ 463
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2524658687 486 VLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDLFDHPEKEYTQRLLDAIP 552
Cdd:COG4172 464 ILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQHPYTRALLAAAP 530
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
10-557 |
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: 663.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 10 APILTLKDVCIGFPTTTasgrrskslTDVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGDGEVtGGTITFDGR 89
Cdd:COG1123 2 TPLLEVRDLSVRYPGGD---------VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRI-SGEVLLDGR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 90 DITHLTDRefvsIRGNGIGLVPQDPMTNLNPVwTVGSQIKEALRANNIaTGSEAHKKAIELLEQAGLPnakKRIDQYPHE 169
Cdd:COG1123 72 DLLELSEA----LRGRRIGMVFQDPMTQLNPV-TVGDQIAEALENLGL-SRAEARARVLELLEAVGLE---RRLDRYPHQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 170 FSGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVV 249
Cdd:COG1123 143 LSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 250 ETGPALQVLTRPQhpytkqLIAAAPSLAARRGDRVVAAPTTsdadqKEILVAKNLVRDFAIRgdrpwRKDSFRAVDDISF 329
Cdd:COG1123 223 EDGPPEEILAAPQ------ALAAVPRLGAARGRAAPAAAAA-----EPLLEVRNLSKRYPVR-----GKGGVRAVDDVSL 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 330 TLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEELELRRRIQPIFQNPYATLDPMRTVHSSIE 409
Cdd:COG1123 287 TLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRELRRRVQMVFQDPYSSLNPRMTVGDIIA 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 410 EPLRIHKIGTKKEREQRVFELLDRVALPAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVSALDVVVQAQVLEL 489
Cdd:COG1123 367 EPLRLHGLLSRAERRERVAELLERVGLPPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNL 446
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2524658687 490 LAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDLFDHPEKEYTQRLLDAIPGASLD 557
Cdd:COG1123 447 LRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQHPYTRALLAAVPSLDPA 514
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
8-548 |
7.19e-165 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 479.20 E-value: 7.19e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 8 SAAPILTLKDVCIGFptttasgRRSKSLTDVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGDGEV-TGGTITF 86
Cdd:PRK15134 1 MTQPLLAIENLSVAF-------RQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVVyPSGDIRF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 87 DGRDITHLTDREFVSIRGNGIGLVPQDPMTNLNPVWTVGSQIKEALRANNIATGSEAHKKAIELLEQAGLPNAKKRIDQY 166
Cdd:PRK15134 74 HGESLLHASEQTLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTDY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 167 PHEFSGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAG 246
Cdd:PRK15134 154 PHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 247 RVVETGPALQVLTRPQHPYTKQLIAAAPSlaarrGDrvvaaPTTSDADQKEILVAKNLVRDFAIRGDRPWRK-DSFRAVD 325
Cdd:PRK15134 234 RCVEQNRAATLFSAPTHPYTQKLLNSEPS-----GD-----PVPLPEPASPLLDVEQLQVAFPIRKGILKRTvDHNVVVK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 326 DISFTLRRGRTIGIVGESGSGKSTVAnMALGLLDPTEGEVLFDGKRVQGRNRKEELELRRRIQPIFQNPYATLDPMRTVH 405
Cdd:PRK15134 304 NISFTLRPGETLGLVGESGSGKSTTG-LALLRLINSQGEIWFDGQPLHNLNRRQLLPVRHRIQVVFQDPNSSLNPRLNVL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 406 SSIEEPLRIH-KIGTKKEREQRVFELLDRVALPAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVSALDVVVQA 484
Cdd:PRK15134 383 QIIEEGLRVHqPTLSAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQA 462
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2524658687 485 QVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDLFDHPEKEYTQRLL 548
Cdd:PRK15134 463 QILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQLL 526
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
36-554 |
9.37e-150 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 443.91 E-value: 9.37e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 36 TDVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLpgdgEVTGGTITFDGR----------DITHLTDREFVSIRGN 105
Cdd:PRK10261 29 IAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLL----EQAGGLVQCDKMllrrrsrqviELSEQSAAQMRHVRGA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 106 GIGLVPQDPMTNLNPVWTVGSQIKEALRANNIATGSEAHKKAIELLEQAGLPNAKKRIDQYPHEFSGGMRQRALIAMGLA 185
Cdd:PRK10261 105 DMAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALS 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 186 AHPKLLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVLTRPQHPY 265
Cdd:PRK10261 185 CRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQHPY 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 266 TKQLIAAAPSLAARRGD---RVVAAPTTSDADQKE-------------ILVAKNLVRDFAIRGDRPWR-KDSFRAVDDIS 328
Cdd:PRK10261 265 TRALLAAVPQLGAMKGLdypRRFPLISLEHPAKQEppieqdtvvdgepILQVRNLVTRFPLRSGLLNRvTREVHAVEKVS 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 329 FTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEELELRRRIQPIFQNPYATLDPMRTVHSSI 408
Cdd:PRK10261 345 FDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFIFQDPYASLDPRQTVGDSI 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 409 EEPLRIHKIGTKKEREQRVFELLDRVALPAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVSALDVVVQAQVLE 488
Cdd:PRK10261 425 MEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIIN 504
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2524658687 489 LLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDLFDHPEKEYTQRLLDAIPGA 554
Cdd:PRK10261 505 LLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAVPVA 570
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
12-283 |
3.37e-135 |
|
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: 395.58 E-value: 3.37e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 12 ILTLKDVCIGFPTttasgrrSKSLTDVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGDGeVTGGTITFDGRDI 91
Cdd:COG0444 1 LLEVRNLKVYFPT-------RRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPG-ITSGEILFDGEDL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 92 THLTDREFVSIRGNGIGLVPQDPMTNLNPVWTVGSQIKEALRANNIATGSEAHKKAIELLEQAGLPNAKKRIDQYPHEFS 171
Cdd:COG0444 73 LKLSEKELRKIRGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRLDRYPHELS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 172 GGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVVET 251
Cdd:COG0444 153 GGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEE 232
|
250 260 270
....*....|....*....|....*....|..
gi 2524658687 252 GPALQVLTRPQHPYTKQLIAAAPSLAARRGDR 283
Cdd:COG0444 233 GPVEELFENPRHPYTRALLSSIPRLDPDGRRL 264
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
293-552 |
4.22e-126 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 372.53 E-value: 4.22e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 293 ADQKEILVAKNLVRDFAIRGDRPWRKDSF-RAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKR 371
Cdd:COG4608 2 AMAEPLLEVRDLKKHFPVRGGLFGRTVGVvKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 372 VQGRNRKEELELRRRIQPIFQNPYATLDPMRTVHSSIEEPLRIHKIGTKKEREQRVFELLDRVALPAEMGRRFPGELSGG 451
Cdd:COG4608 82 ITGLSGRELRPLRRRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLRPEHADRYPHEFSGG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 452 QRQRVAIARALALNPEVVVCDEAVSALDVVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRP 531
Cdd:COG4608 162 QRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAP 241
|
250 260
....*....|....*....|.
gi 2524658687 532 TDDLFDHPEKEYTQRLLDAIP 552
Cdd:COG4608 242 RDELYARPLHPYTQALLSAVP 262
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
298-552 |
2.43e-109 |
|
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: 329.32 E-value: 2.43e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 298 ILVAKNLVRDFAIRgdrpwrKDSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDP---TEGEVLFDGKRVQG 374
Cdd:COG0444 1 LLEVRNLKVYFPTR------RGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 375 RNRKEELELR-RRIQPIFQNPYATLDPMRTVHSSIEEPLRIHKIGTKKEREQRVFELLDRVAL--PAEMGRRFPGELSGG 451
Cdd:COG0444 75 LSEKELRKIRgREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLpdPERRLDRYPHELSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 452 QRQRVAIARALALNPEVVVCDEAVSALDVVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRP 531
Cdd:COG0444 155 MRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGP 234
|
250 260
....*....|....*....|.
gi 2524658687 532 TDDLFDHPEKEYTQRLLDAIP 552
Cdd:COG0444 235 VEELFENPRHPYTRALLSSIP 255
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-279 |
1.56e-102 |
|
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: 318.77 E-value: 1.56e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 2 STDTNTSAAPILTLKDVCIGFPTTTASGRRsksltdVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPgdgeVTG 81
Cdd:COG1123 250 AAPAAAAAEPLLEVRNLSKRYPVRGKGGVR------AVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLR----PTS 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 82 GTITFDGRDITHLTDREFVSIRGNgIGLVPQDPMTNLNPVWTVGSQIKEALRANNIATGSEAHKKAIELLEQAGLPnaKK 161
Cdd:COG1123 320 GSILFDGKDLTKLSRRSLRELRRR-VQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLP--PD 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 162 RIDQYPHEFSGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLV 241
Cdd:COG1123 397 LADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVA 476
|
250 260 270
....*....|....*....|....*....|....*...
gi 2524658687 242 VMQAGRVVETGPALQVLTRPQHPYTKQLIAAAPSLAAR 279
Cdd:COG1123 477 VMYDGRIVEDGPTEEVFANPQHPYTRALLAAVPSLDPA 514
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
12-252 |
5.68e-102 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 307.12 E-value: 5.68e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 12 ILTLKDVCIGFPTttasgrrSKSLTDVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLpgdgEVTGGTITFDGRDI 91
Cdd:cd03257 1 LLEVKNLSVSFPT-------GGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLL----KPTSGSIIFDGKDL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 92 THLtDREFVSIRGNGIGLVPQDPMTNLNPVWTVGSQIKEALRANNIATGSEAhKKAIELLEQAGLPNAKKRIDQYPHEFS 171
Cdd:cd03257 70 LKL-SRRLRKIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEA-RKEAVLLLLVGVGLPEEVLNRYPHELS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 172 GGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVVET 251
Cdd:cd03257 148 GGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEE 227
|
.
gi 2524658687 252 G 252
Cdd:cd03257 228 G 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
299-553 |
4.20e-101 |
|
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: 305.57 E-value: 4.20e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 299 LVAKNLVRDFAIRGDRPwrkdsfRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRK 378
Cdd:COG1124 2 LEVRNLSVSYGQGGRRV------PVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 379 EeleLRRRIQPIFQNPYATLDPMRTVHSSIEEPLRIHKIGtkkEREQRVFELLDRVALPAEMGRRFPGELSGGQRQRVAI 458
Cdd:COG1124 76 A---FRRRVQMVFQDPYASLHPRHTVDRILAEPLRIHGLP---DREERIAELLEQVGLPPSFLDRYPHQLSGGQRQRVAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 459 ARALALNPEVVVCDEAVSALDVVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDLFDH 538
Cdd:COG1124 150 ARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAG 229
|
250
....*....|....*
gi 2524658687 539 PEKEYTQRLLDAIPG 553
Cdd:COG1124 230 PKHPYTRELLAASLA 244
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
298-529 |
5.69e-98 |
|
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: 296.72 E-value: 5.69e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 298 ILVAKNLVRDFAIRGDrpwrkdSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNR 377
Cdd:cd03257 1 LLEVKNLSVSFPTGGG------SVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 378 KEELELRRRIQPIFQNPYATLDPMRTVHSSIEEPLRIHKIGTKKEREQR-VFELLDRVALPAEMGRRFPGELSGGQRQRV 456
Cdd:cd03257 75 RLRKIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEaVLLLLVGVGLPEEVLNRYPHELSGGQRQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2524658687 457 AIARALALNPEVVVCDEAVSALDVVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEH 529
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEE 227
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-278 |
2.42e-91 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 283.54 E-value: 2.42e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 1 MSTDTNTSAAPILTLKDVCIGFptTTASGrrsksltDV--VHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGDGE 78
Cdd:PRK09473 1 TVPLAQQQADALLDVKDLRVTF--STPDG-------DVtaVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 79 VtGGTITFDGRDITHLTDREFVSIRGNGIGLVPQDPMTNLNPVWTVGSQIKEALRANNIATGSEAHKKAIELLEQAGLPN 158
Cdd:PRK09473 72 I-GGSATFNGREILNLPEKELNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 159 AKKRIDQYPHEFSGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERAD 238
Cdd:PRK09473 151 ARKRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICD 230
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2524658687 239 RLVVMQAGRVVETGPALQVLTRPQHPYTKQLIAAAPSLAA 278
Cdd:PRK09473 231 KVLVMYAGRTMEYGNARDVFYQPSHPYSIGLLNAVPRLDA 270
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
294-558 |
1.96e-89 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 278.39 E-value: 1.96e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 294 DQKEILVAKNLVRDFAIRGDRPWRKDSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQ 373
Cdd:PRK11308 1 SQQPLLQAIDLKKHYPVKRGLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 374 GRNRKEELELRRRIQPIFQNPYATLDPMRTVHSSIEEPLRIHKIGTKKEREQRVFELLDRVALPAEMGRRFPGELSGGQR 453
Cdd:PRK11308 81 KADPEAQKLLRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLRPEHYDRYPHMFSGGQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 454 QRVAIARALALNPEVVVCDEAVSALDVVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTD 533
Cdd:PRK11308 161 QRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKE 240
|
250 260
....*....|....*....|....*
gi 2524658687 534 DLFDHPEKEYTQRLLDAIPGASLDL 558
Cdd:PRK11308 241 QIFNNPRHPYTQALLSATPRLNPDD 265
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
7-277 |
6.37e-86 |
|
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: 276.18 E-value: 6.37e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 7 TSAAPILTLKDVCIGFPTTTASGRRSKSLTDVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPgdgevTGGTITF 86
Cdd:COG4172 270 PDAPPLLEARDLKVWFPIKRGLFRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-----SEGEIRF 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 87 DGRDITHLTDREFVSIRGNgIGLVPQDPMTNLNPVWTVGSQIKEALRANNIA-TGSEAHKKAIELLEQAGL-PNAKKRid 164
Cdd:COG4172 345 DGQDLDGLSRRALRPLRRR-MQVVFQDPFGSLSPRMTVGQIIAEGLRVHGPGlSAAERRARVAEALEEVGLdPAARHR-- 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 165 qYPHEFSGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQ 244
Cdd:COG4172 422 -YPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMK 500
|
250 260 270
....*....|....*....|....*....|...
gi 2524658687 245 AGRVVETGPALQVLTRPQHPYTKQLIAAAPSLA 277
Cdd:COG4172 501 DGKVVEQGPTEQVFDAPQHPYTRALLAAAPLLE 533
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
6-285 |
3.57e-84 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 265.06 E-value: 3.57e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 6 NTSAAPILTLKDVCIGFPTTTASGRRSKSLTDVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLpgdgEVTGGTIT 85
Cdd:COG4608 1 AAMAEPLLEVRDLKKHFPVRGGLFGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLE----EPTSGEIL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 86 FDGRDITHLTDREFVSIRGNgIGLVPQDPMTNLNPVWTVGSQIKEALRANNIATGSEAHKKAIELLEQAGLPNAkkRIDQ 165
Cdd:COG4608 77 FDGQDITGLSGRELRPLRRR-MQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLRPE--HADR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 166 YPHEFSGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQA 245
Cdd:COG4608 154 YPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYL 233
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2524658687 246 GRVVETGPALQVLTRPQHPYTKQLIAAAPSL-AARRGDRVV 285
Cdd:COG4608 234 GKIVEIAPRDELYARPLHPYTQALLSAVPVPdPERRRERIV 274
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
13-279 |
1.32e-80 |
|
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: 252.80 E-value: 1.32e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 13 LTLKDVCIGFPTttasGRRSKsltDVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGDGevtgGTITFDGRDIT 92
Cdd:COG1124 2 LEVRNLSVSYGQ----GGRRV---PVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWS----GEVTFDGRPVT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 93 HLTDREFvsiRGNgIGLVPQDPMTNLNPVWTVGSQIKEALRANNIAtgsEAHKKAIELLEQAGLPNAKKriDQYPHEFSG 172
Cdd:COG1124 71 RRRRKAF---RRR-VQMVFQDPYASLHPRHTVDRILAEPLRIHGLP---DREERIAELLEQVGLPPSFL--DRYPHQLSG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 173 GMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETG 252
Cdd:COG1124 142 GQRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEEL 221
|
250 260
....*....|....*....|....*..
gi 2524658687 253 PALQVLTRPQHPYTKQLIAAAPSLAAR 279
Cdd:COG1124 222 TVADLLAGPKHPYTRELLAASLAFERA 248
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
298-548 |
2.33e-78 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 247.44 E-value: 2.33e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 298 ILVAKNLVRDFAIRGdRPWRKDSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNR 377
Cdd:COG4167 4 LLEVRNLSKTFKYRT-GLFRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 378 KeeleLR-RRIQPIFQNPYATLDPMRTVHSSIEEPLRIHKIGTKKEREQRVFELLDRVALPAEMGRRFPGELSGGQRQRV 456
Cdd:COG4167 83 K----YRcKHIRMIFQDPNTSLNPRLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGLLPEHANFYPHMLSSGQKQRV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 457 AIARALALNPEVVVCDEAVSALDVVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDLF 536
Cdd:COG4167 159 ALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVF 238
|
250
....*....|..
gi 2524658687 537 DHPEKEYTQRLL 548
Cdd:COG4167 239 ANPQHEVTKRLI 250
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
39-278 |
3.55e-78 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 249.27 E-value: 3.55e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 39 VHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGDGEVTGGTITFDGRDITHLTDREFVSIRGNGIGLVPQDPMTNL 118
Cdd:PRK11022 23 VDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVMAEKLEFNGQDLQRISEKERRNLVGAEVAMIFQDPMTSL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 119 NPVWTVGSQIKEALRANNIATGSEAHKKAIELLEQAGLPNAKKRIDQYPHEFSGGMRQRALIAMGLAAHPKLLIADEPTS 198
Cdd:PRK11022 103 NPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 199 ALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVLTRPQHPYTKQLIAAAPSLAA 278
Cdd:PRK11022 183 ALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQALLRALPEFAQ 262
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
293-552 |
4.43e-78 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 249.24 E-value: 4.43e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 293 ADQKEILVAKNLVRDFAIRGDR--PWRK-DSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDG 369
Cdd:PRK15079 3 EGKKVLLEVADLKVHFDIKDGKqwFWQPpKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 370 KRVQGRNRKEELELRRRIQPIFQNPYATLDPMRTVHSSIEEPLRIHKIG-TKKEREQRVFELLDRVALPAEMGRRFPGEL 448
Cdd:PRK15079 83 KDLLGMKDDEWRAVRSDIQMIFQDPLASLNPRMTIGEIIAEPLRTYHPKlSRQEVKDRVKAMMLKVGLLPNLINRYPHEF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 449 SGGQRQRVAIARALALNPEVVVCDEAVSALDVVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVE 528
Cdd:PRK15079 163 SGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVE 242
|
250 260
....*....|....*....|....
gi 2524658687 529 HRPTDDLFDHPEKEYTQRLLDAIP 552
Cdd:PRK15079 243 LGTYDEVYHNPLHPYTKALMSAVP 266
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
39-273 |
6.76e-77 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 242.66 E-value: 6.76e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 39 VHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGDGEVTGGTITFDGRDITHLtdrefvSIRGNGIGLVPQDPMTNL 118
Cdd:TIGR02770 2 VQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPGLTQTSGEILLDGRPLLPL------SIRGRHIATIMQNPRTAF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 119 NPVWTVGSQIKEALRANNIATgSEAHKKAIELLEQAGLPNAKKRIDQYPHEFSGGMRQRALIAMGLAAHPKLLIADEPTS 198
Cdd:TIGR02770 76 NPLFTMGNHAIETLRSLGKLS-KQARALILEALEAVGLPDPEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTT 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2524658687 199 ALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVLTRPQHPYTKQLIAAA 273
Cdd:TIGR02770 155 DLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHETTRKLLSAH 229
|
|
| PhnK |
COG4107 |
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and ... |
39-273 |
1.68e-67 |
|
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and metabolism];
Pssm-ID: 443283 [Multi-domain] Cd Length: 262 Bit Score: 219.30 E-value: 1.68e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 39 VHDVNLEVFPGETVAIVGESGSGKSTTahaaLGLLPGDGEVTGGTITFDGR-----DITHLTDREFVSIRGNGIGLVPQD 113
Cdd:COG4107 28 CRDVSFDLYPGEVLGIVGESGSGKSTL----LKCLYFDLAPTSGSVYYRDRdggprDLFALSEAERRRLRRTDWGMVYQN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 114 PMTNLNPVWTVGSQIKEALRANNIATGSEAHKKAIELLEQAGLPNAkkRIDQYPHEFSGGMRQRALIAMGLAAHPKLLIA 193
Cdd:COG4107 104 PRDGLRMDVSAGGNIAERLMAAGERHYGDIRARALEWLERVEIPLE--RIDDLPRTFSGGMQQRVQIARALVTNPRLLFL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 194 DEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVLTRPQHPYTKQLIAAA 273
Cdd:COG4107 182 DEPTTGLDVSVQARLLDLIRRLQRELGLSMIVVTHDLGVIRLLADRTMVMKNGRVVESGLTDQVLEDPQHPYTQLLVSSV 261
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
317-560 |
4.20e-65 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 215.71 E-value: 4.20e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 317 RKDSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEELELRRRIQPIFQNPYa 396
Cdd:COG1135 14 KGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAARRKIGMIFQHFN- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 397 tLDPMRTVHSSIEEPLRIHKIgTKKEREQRVFELLDRVALpAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVS 476
Cdd:COG1135 93 -LLSSRTVAENVALPLEIAGV-PKAEIRKRVAELLELVGL-SDKADAYPSQLSGGQKQRVGIARALANNPKVLLCDEATS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 477 ALDVVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDLFDHPEKEYTQRLLDAIPGASL 556
Cdd:COG1135 170 ALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELTRRFLPTVLNDEL 249
|
....
gi 2524658687 557 DLDL 560
Cdd:COG1135 250 PEEL 253
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
317-540 |
7.13e-64 |
|
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: 208.59 E-value: 7.13e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 317 RKDSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEELELRRRIQPIFQNpYA 396
Cdd:cd03258 14 TGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKARRRIGMIFQH-FN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 397 TLDPmRTVHSSIEEPLRIHKIGtKKEREQRVFELLDRVALpAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVS 476
Cdd:cd03258 93 LLSS-RTVFENVALPLEIAGVP-KAEIEERVLELLELVGL-EDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2524658687 477 ALDVVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDLFDHPE 540
Cdd:cd03258 170 ALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
298-539 |
5.13e-63 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 207.62 E-value: 5.13e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 298 ILVAKNLVRDFA---IRGDRPWRkdsfRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQG 374
Cdd:PRK10419 3 LLNVSGLSHHYAhggLSGKHQHQ----TVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 375 RNRKEELELRRRIQPIFQNPYATLDPMRTVHSSIEEPLRiHKIGTKK-EREQRVFELLDRVALPAEMGRRFPGELSGGQR 453
Cdd:PRK10419 79 LNRAQRKAFRRDIQMVFQDSISAVNPRKTVREIIREPLR-HLLSLDKaERLARASEMLRAVDLDDSVLDKRPPQLSGGQL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 454 QRVAIARALALNPEVVVCDEAVSALDVVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTD 533
Cdd:PRK10419 158 QRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVG 237
|
....*...
gi 2524658687 534 DL--FDHP 539
Cdd:PRK10419 238 DKltFSSP 245
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
316-539 |
5.50e-63 |
|
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: 207.74 E-value: 5.50e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 316 WRKDSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEELELRRRIQPIFQNPY 395
Cdd:TIGR02769 19 GAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAFRRDVQLVFQDSP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 396 ATLDPMRTVHSSIEEPLRIHKIGTKKEREQRVFELLDRVALPAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAV 475
Cdd:TIGR02769 99 SAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAV 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2524658687 476 SALDVVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDL--FDHP 539
Cdd:TIGR02769 179 SNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLlsFKHP 244
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
11-275 |
1.56e-62 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 208.61 E-value: 1.56e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 11 PILTLKDVCIGFptTTASGRrskslTDVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGDGEVTGGTITFDGRD 90
Cdd:COG4170 2 PLLDIRNLTIEI--DTPQGR-----VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNWHVTADRFRWNGID 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 91 ITHLTDREFVSIRGNGIGLVPQDPMTNLNPVWTVGSQIKEALrANNIATGS------EAHKKAIELLEQAGLPNAKKRID 164
Cdd:COG4170 75 LLKLSPRERRKIIGREIAMIFQEPSSCLDPSAKIGDQLIEAI-PSWTFKGKwwqrfkWRKKRAIELLHRVGIKDHKDIMN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 165 QYPHEFSGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQ 244
Cdd:COG4170 154 SYPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLY 233
|
250 260 270
....*....|....*....|....*....|.
gi 2524658687 245 AGRVVETGPALQVLTRPQHPYTKQLIAAAPS 275
Cdd:COG4170 234 CGQTVESGPTEQILKSPHHPYTKALLRSMPD 264
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
10-250 |
1.33e-60 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 199.88 E-value: 1.33e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 10 APILTLKDVCIGFPTTTASgrrskslTDVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPgdgeVTGGTITFDGR 89
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGE-------VTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDR----PTSGEVLIDGQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 90 DITHLTDREFVSIRGNGIGLVPQDPmtNLNPVWTVGSQIKEALRANNIaTGSEAHKKAIELLEQAGLpnaKKRIDQYPHE 169
Cdd:COG1136 71 DISSLSERELARLRRRHIGFVFQFF--NLLPELTALENVALPLLLAGV-SRKERRERARELLERVGL---GDRLDHRPSQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 170 FSGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAeRADRLVVMQAGRVV 249
Cdd:COG1136 145 LSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAA-RADRVIRLRDGRIV 223
|
.
gi 2524658687 250 E 250
Cdd:COG1136 224 S 224
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
5-274 |
1.65e-60 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 203.40 E-value: 1.65e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 5 TNTSAAPILTLKDVCIGFPTTTASG---RRSKSLTdVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLpgdgEVTG 81
Cdd:PRK15079 1 VTEGKKVLLEVADLKVHFDIKDGKQwfwQPPKTLK-AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLV----KATD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 82 GTITFDGRDITHLTDREFVSIRgNGIGLVPQDPMTNLNPVWTVGSQIKEALRANNIA-TGSEAHKKAIELLEQAGL-PNA 159
Cdd:PRK15079 76 GEVAWLGKDLLGMKDDEWRAVR-SDIQMIFQDPLASLNPRMTIGEIIAEPLRTYHPKlSRQEVKDRVKAMMLKVGLlPNL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 160 kkrIDQYPHEFSGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADR 239
Cdd:PRK15079 155 ---INRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDR 231
|
250 260 270
....*....|....*....|....*....|....*
gi 2524658687 240 LVVMQAGRVVETGPALQVLTRPQHPYTKQLIAAAP 274
Cdd:PRK15079 232 VLVMYLGHAVELGTYDEVYHNPLHPYTKALMSAVP 266
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
4-285 |
3.06e-60 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 210.48 E-value: 3.06e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 4 DTNTSAAPILTLKDVCIGFPTTTASGRRSKSLTDVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLpgdgEVTGGT 83
Cdd:PRK10261 305 DTVVDGEPILQVRNLVTRFPLRSGLLNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLV----ESQGGE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 84 ITFDGRDITHLTDREFVSIRGNgIGLVPQDPMTNLNPVWTVGSQIKEALRANNIATGSEAHKKAIELLEQAGL-PNAKKR 162
Cdd:PRK10261 381 IIFNGQRIDTLSPGKLQALRRD-IQFIFQDPYASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLlPEHAWR 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 163 idqYPHEFSGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVV 242
Cdd:PRK10261 460 ---YPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAV 536
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2524658687 243 MQAGRVVETGPALQVLTRPQHPYTKQLIAAAP--SLAARRGDRVV 285
Cdd:PRK10261 537 MYLGQIVEIGPRRAVFENPQHPYTRKLMAAVPvaDPSRQRPQRVL 581
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
39-285 |
1.37e-59 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 200.58 E-value: 1.37e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 39 VHDVNLEVFPGETVAIVGESGSGKSTTAHAaLGLLPgdgEVTGGTITFDGRDITHlTDREFVSIRGNGIGLVPQDPMTNL 118
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARL-LTMIE---TPTGGELYYQGQDLLK-ADPEAQKLLRQKIQIVFQNPYGSL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 119 NPVWTVGSQIKEALRANNIATGSEAHKKAIELLEQAGL-PNAKKRidqYPHEFSGGMRQRALIAMGLAAHPKLLIADEPT 197
Cdd:PRK11308 106 NPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLrPEHYDR---YPHMFSGGQRQRIAIARALMLDPDVVVADEPV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 198 SALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVLTRPQHPYTKQLIAAAPSL- 276
Cdd:PRK11308 183 SALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPYTQALLSATPRLn 262
|
....*....
gi 2524658687 277 AARRGDRVV 285
Cdd:PRK11308 263 PDDRRERIK 271
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
36-248 |
9.57e-57 |
|
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: 189.62 E-value: 9.57e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 36 TDVVHDVNLEVFPGETVAIVGESGSGKSTTahaaLGLLPGDGEVTGGTITFDGRDITHLTDREFVSIRGNGIGLVPQDPm 115
Cdd:cd03255 17 VQALKGVSLSIEKGEFVAIVGPSGSGKSTL----LNILGGLDRPTSGEVRVDGTDISKLSEKELAAFRRRHIGFVFQSF- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 116 tNLNPVWTVGSQIKEALRANNIAtGSEAHKKAIELLEQAGLpnaKKRIDQYPHEFSGGMRQRALIAMGLAAHPKLLIADE 195
Cdd:cd03255 92 -NLLPDLTALENVELPLLLAGVP-KKERRERAEELLERVGL---GDRLNHYPSELSGGQQQRVAIARALANDPKIILADE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2524658687 196 PTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLaAERADRLVVMQAGRV 248
Cdd:cd03255 167 PTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPEL-AEYADRIIELRDGKI 218
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
39-276 |
2.45e-56 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 189.53 E-value: 2.45e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 39 VHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGDGEVTGGTITFDGRDIthltdrEFVSIRGNGIGLVPQDPMTNL 118
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGVRQTAGRVLLDGKPV------APCALRGRKIATIMQNPRSAF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 119 NPVWTVGSQIKEALRANNIaTGSEAhkKAIELLEQAGLPNAKKRIDQYPHEFSGGMRQRALIAMGLAAHPKLLIADEPTS 198
Cdd:PRK10418 93 NPLHTMHTHARETCLALGK-PADDA--TLTAALEAVGLENAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTT 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2524658687 199 ALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVLTRPQHPYTKQLIAAAPSL 276
Cdd:PRK10418 170 DLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSAHLAL 247
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
40-272 |
6.11e-56 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 188.60 E-value: 6.11e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 40 HDVNLEVFPGETVAIVGESGSGKSTTahaaLGLLPGDGEVTGGTITFDGR-----DITHLTDREFVSIRGNGIGLVPQDP 114
Cdd:PRK11701 23 RDVSFDLYPGEVLGIVGESGSGKTTL----LNALSARLAPDAGEVHYRMRdgqlrDLYALSEAERRRLLRTEWGFVHQHP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 115 MTNLNPVWTVGSQIKEALRANNIATGSEAHKKAIELLEQAGLPNAkkRIDQYPHEFSGGMRQRALIAMGLAAHPKLLIAD 194
Cdd:PRK11701 99 RDGLRMQVSAGGNIGERLMAVGARHYGDIRATAGDWLERVEIDAA--RIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMD 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2524658687 195 EPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVLTRPQHPYTKQLIAA 272
Cdd:PRK11701 177 EPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVLDDPQHPYTQLLVSS 254
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
323-560 |
1.43e-54 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 187.70 E-value: 1.43e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 323 AVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEELELRRRIQPIFQNPYatLDPMR 402
Cdd:PRK11153 20 ALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKARRQIGMIFQHFN--LLSSR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 403 TVHSSIEEPLRIHKIgTKKEREQRVFELLDRVALpAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVSALDVVV 482
Cdd:PRK11153 98 TVFDNVALPLELAGT-PKAEIKARVTELLELVGL-SDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDPAT 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2524658687 483 QAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDLFDHPEKEYTQRLLDAIPGASLDLDL 560
Cdd:PRK11153 176 TRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREFIQSTLHLDLPEDY 253
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
323-552 |
3.54e-54 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 186.47 E-value: 3.54e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 323 AVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDP---TEGEVLFDGKRVQGRNRKEELELR-RRIQPIFQNPYATL 398
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLPEKELNKLRaEQISMIFQDPMTSL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 399 DPMRTVHSSIEEPLRIHKIGTKKEREQRVFELLDRVALPaEMGRR---FPGELSGGQRQRVAIARALALNPEVVVCDEAV 475
Cdd:PRK09473 111 NPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMP-EARKRmkmYPHEFSGGMRQRVMIAMALLCRPKLLIADEPT 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2524658687 476 SALDVVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDLFDHPEKEYTQRLLDAIP 552
Cdd:PRK09473 190 TALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSHPYSIGLLNAVP 266
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
318-552 |
4.47e-54 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 186.10 E-value: 4.47e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 318 KDSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDpTEGEVLFDGKRVQGRNRKEELELRRR------IQPIF 391
Cdd:PRK11022 17 SAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLID-YPGRVMAEKLEFNGQDLQRISEKERRnlvgaeVAMIF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 392 QNPYATLDPMRTVHSSIEEPLRIHKIGTKKEREQRVFELLDRVALPAEMGRR--FPGELSGGQRQRVAIARALALNPEVV 469
Cdd:PRK11022 96 QDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLdvYPHQLSGGMSQRVMIAMAIACRPKLL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 470 VCDEAVSALDVVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDLFDHPEKEYTQRLLD 549
Cdd:PRK11022 176 IADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQALLR 255
|
...
gi 2524658687 550 AIP 552
Cdd:PRK11022 256 ALP 258
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
9-535 |
6.62e-54 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 190.23 E-value: 6.62e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 9 AAPILTLKDVCIGFPTTTAsgrrsksltdvVHDVNLEVFPGETVAIVGESGSGKSTtahaaL-----GLLPGDGevtgGT 83
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKA-----------LDGVSLELRPGEVHALLGENGAGKST-----LmkilsGVYQPDS----GE 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 84 ITFDGRDITHLTDREfvSIRgNGIGLVPQDPmtNLNPVWTVgsqikealrANNIATGSE-----------AHKKAIELLE 152
Cdd:COG1129 61 ILLDGEPVRFRSPRD--AQA-AGIAIIHQEL--NLVPNLSV---------AENIFLGREprrgglidwraMRRRARELLA 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 153 QAGLPnakkrIDqyPH----EFSGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSElGTSVVLITH 228
Cdd:COG1129 127 RLGLD-----ID--PDtpvgDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISH 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 229 DLGLAAERADRLVVMQAGRVVETGPAlQVLTRPQhpytkqLIAAapsLAARRGDRVvaAPTTSDADQKEILVAKNLVRDf 308
Cdd:COG1129 199 RLDEVFEIADRVTVLRDGRLVGTGPV-AELTEDE------LVRL---MVGRELEDL--FPKRAAAPGEVVLEVEGLSVG- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 309 airgdrpwrkdsfRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEELEL----- 383
Cdd:COG1129 266 -------------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRAgiayv 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 384 ---RRR-----IQPIFQNpyATLdpmrtvhSSIEEPLRIHKIGTKKERE--QRVFELLD----RVALPAemgrrfpGELS 449
Cdd:COG1129 333 pedRKGeglvlDLSIREN--ITL-------ASLDRLSRGGLLDRRRERAlaEEYIKRLRiktpSPEQPV-------GNLS 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 450 GGQRQRVAIARALALNPEVVVCDEAVSALDVVVQAQVlellaelQEEMD------LAYLFITHDLAVVRQVADEVIVMEH 523
Cdd:COG1129 397 GGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEI-------YRLIRelaaegKAVIVISSELPELLGLSDRILVMRE 469
|
570
....*....|..
gi 2524658687 524 GKMVEHRPTDDL 535
Cdd:COG1129 470 GRIVGELDREEA 481
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
325-539 |
1.94e-53 |
|
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: 181.33 E-value: 1.94e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 325 DDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEELELRRRIQPIFQNPyATLDPMrTV 404
Cdd:COG1127 22 DGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELRRRIGMLFQGG-ALFDSL-TV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 405 HSSIEEPLRIHKIGTKKEREQRVFELLDRVALPaEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVSALDVVVQA 484
Cdd:COG1127 100 FENVAFPLREHTDLSEAEIRELVLEKLELVGLP-GAADKMPSELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2524658687 485 QVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDLF--DHP 539
Cdd:COG1127 179 VIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLasDDP 235
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
319-551 |
1.27e-52 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 179.42 E-value: 1.27e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 319 DSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVqGRNRKEELELRRRIQPIFQNpyATL 398
Cdd:COG1126 12 GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL-TDSKKDINKLRRKVGMVFQQ--FNL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 399 DPMRTVHSSIEEPLRIHKIGTKKEREQRVFELLDRVALpAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVSAL 478
Cdd:COG1126 89 FPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGL-ADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSAL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 479 D-----VVVQAqvlellaelqeeM-DLAY-----LFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDLFDHPEKEYTQRL 547
Cdd:COG1126 168 DpelvgEVLDV------------MrDLAKegmtmVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRAF 235
|
....
gi 2524658687 548 LDAI 551
Cdd:COG1126 236 LSKV 239
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
325-539 |
8.58e-52 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 176.92 E-value: 8.58e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 325 DDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEELELRRRIQPIFQNPyATLDPMrTV 404
Cdd:cd03261 17 KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRRMGMLFQSG-ALFDSL-TV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 405 HSSIEEPLRIHKIGTKKEREQRVFELLDRVALPAEmGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVSALDVVVQA 484
Cdd:cd03261 95 FENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGA-EDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2524658687 485 QVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDLF--DHP 539
Cdd:cd03261 174 VIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRasDDP 230
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
298-551 |
9.99e-52 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 177.59 E-value: 9.99e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 298 ILVAKNLVRDFAIRGDRpwrkdsFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNR 377
Cdd:COG1116 7 ALELRGVSKRFPTGGGG------VTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 378 keelelRRRIqpIFQNPyaTLDPMRTVHSSIEEPLRIHKIGtKKEREQRVFELLDRVALpAEMGRRFPGELSGGQRQRVA 457
Cdd:COG1116 81 ------DRGV--VFQEP--ALLPWLTVLDNVALGLELRGVP-KAERRERARELLELVGL-AGFEDAYPHQLSGGMRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 458 IARALALNPEVVVCDEAVSALDVVVQAQVLELLAELQEEMDLAYLFITHDL--AVVrqVADEVIVMEH--GKMVEH---- 529
Cdd:COG1116 149 IARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVdeAVF--LADRVVVLSArpGRIVEEidvd 226
|
250 260
....*....|....*....|....*.
gi 2524658687 530 --RP-TDDLFDHPE-KEYTQRLLDAI 551
Cdd:COG1116 227 lpRPrDRELRTSPEfAALRAEILDLL 252
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
12-274 |
1.37e-51 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 179.89 E-value: 1.37e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 12 ILTLKDVCIGFPTTTASgrrskslTDVVHDVNLEVFPGETVAIVGESGSGKSTtahaalgLL--------PgdgevTGGT 83
Cdd:COG1135 1 MIELENLSKTFPTKGGP-------VTALDDVSLTIEKGEIFGIIGYSGAGKST-------LIrcinllerP-----TSGS 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 84 ITFDGRDITHLTDREFVSIRGNgIGLVPQDPmtNLNPVWTVgsqikealrANNIA--------TGSEAHKKAIELLEQAG 155
Cdd:COG1135 62 VLVDGVDLTALSERELRAARRK-IGMIFQHF--NLLSSRTV---------AENVAlpleiagvPKAEIRKRVAELLELVG 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 156 LpnaKKRIDQYPHEFSGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAE 235
Cdd:COG1135 130 L---SDKADAYPSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRR 206
|
250 260 270
....*....|....*....|....*....|....*....
gi 2524658687 236 RADRLVVMQAGRVVETGPALQVLTRPQHPYTKQLIAAAP 274
Cdd:COG1135 207 ICDRVAVLENGRIVEQGPVLDVFANPQSELTRRFLPTVL 245
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
322-552 |
2.46e-51 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 184.14 E-value: 2.46e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 322 RAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLdPT------EGEVLFDGKRVQgrnRKEELELRR----RIQPIF 391
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLL-PSppvvypSGDIRFHGESLL---HASEQTLRGvrgnKIAMIF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 392 QNPYATLDPMRTVHSSIEEPLRIHKiGTKKEREQ-RVFELLDRVAL--PAEMGRRFPGELSGGQRQRVAIARALALNPEV 468
Cdd:PRK15134 99 QEPMVSLNPLHTLEKQLYEVLSLHR-GMRREAARgEILNCLDRVGIrqAAKRLTDYPHQLSGGERQRVMIAMALLTRPEL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 469 VVCDEAVSALDVVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDLFDHPEKEYTQRLL 548
Cdd:PRK15134 178 LIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPYTQKLL 257
|
....
gi 2524658687 549 DAIP 552
Cdd:PRK15134 258 NSEP 261
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
296-528 |
3.78e-51 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 174.85 E-value: 3.78e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 296 KEILVAKNLVRDFAiRGDRPwrkdsFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGR 375
Cdd:COG1136 2 SPLLELRNLTKSYG-TGEGE-----VTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 376 NRKEELELRRR-IQPIFQNPYatLDPMRTVHSSIEEPLRIHKIGtKKEREQRVFELLDRVALpAEMGRRFPGELSGGQRQ 454
Cdd:COG1136 76 SERELARLRRRhIGFVFQFFN--LLPELTALENVALPLLLAGVS-RKERRERARELLERVGL-GDRLDHRPSQLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2524658687 455 RVAIARALALNPEVVVCDEAVSALDVVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQvADEVIVMEHGKMVE 528
Cdd:COG1136 152 RVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAAR-ADRVIRLRDGRIVS 224
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
319-541 |
1.06e-50 |
|
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: 173.67 E-value: 1.06e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 319 DSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEeleLRRRIQPIFQNPYATL 398
Cdd:COG1122 12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRE---LRRKVGLVFQNPDDQL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 399 dpmrtVHSSIEE----PLRIHKIgTKKEREQRVFELLDRVALpAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEA 474
Cdd:COG1122 89 -----FAPTVEEdvafGPENLGL-PREEIRERVEEALELVGL-EHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2524658687 475 VSALDVVVQAQVlellaelqeeMDLAY---------LFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDLFDHPEK 541
Cdd:COG1122 162 TAGLDPRGRREL----------LELLKrlnkegktvIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYEL 227
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
298-559 |
3.33e-50 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 173.82 E-value: 3.33e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 298 ILVAKNLVRDFAIRGDRpWRKDSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQ-GRN 376
Cdd:PRK15112 4 LLEVRNLSKTFRYRTGW-FRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfGDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 377 RKEElelrRRIQPIFQNPYATLDPMRTVHSSIEEPLRIHKIGTKKEREQRVFELLDRVALPAEMGRRFPGELSGGQRQRV 456
Cdd:PRK15112 83 SYRS----QRIRMIFQDPSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 457 AIARALALNPEVVVCDEAVSALDVVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDLF 536
Cdd:PRK15112 159 GLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVL 238
|
250 260
....*....|....*....|...
gi 2524658687 537 DHPEKEYTQRLLDAIPGASLDLD 559
Cdd:PRK15112 239 ASPLHELTKRLIAGHFGEALTAD 261
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
298-539 |
4.53e-50 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 176.06 E-value: 4.53e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 298 ILVAKNLVRDFairgdrpwrkDSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGrnr 377
Cdd:COG3842 5 ALELENVSKRY----------GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTG--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 378 keeleL---RRRIQPIFQNpYAtLDPMRTVHSSIEEPLRIHKIGtKKEREQRVFELLDRVALpAEMGRRFPGELSGGQRQ 454
Cdd:COG3842 72 -----LppeKRNVGMVFQD-YA-LFPHLTVAENVAFGLRMRGVP-KAEIRARVAELLELVGL-EGLADRYPHQLSGGQQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 455 RVAIARALALNPEVVVCDEAVSALDVVVQAQVLELLAELQEEMDLAYLFITHD----LAvvrqVADEVIVMEHGKMVEHR 530
Cdd:COG3842 143 RVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDqeeaLA----LADRIAVMNDGRIEQVG 218
|
....*....
gi 2524658687 531 PTDDLFDHP 539
Cdd:COG3842 219 TPEEIYERP 227
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
30-250 |
4.90e-50 |
|
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: 171.77 E-value: 4.90e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 30 RRSKSLTDVVHDVNLEVFPGETVAIVGESGSGKSTTAHaalgLLPGDGEVTGGTITFDGRDITHLTDREFVSIRGNGIGL 109
Cdd:TIGR02211 12 QEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLH----LLGGLDNPTSGEVLFNGQSLSKLSSNERAKLRNKKLGF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 110 VPQdpMTNLNPVWTVGSQIKEALRANNIATGsEAHKKAIELLEQAGLpnaKKRIDQYPHEFSGGMRQRALIAMGLAAHPK 189
Cdd:TIGR02211 88 IYQ--FHHLLPDFTALENVAMPLLIGKKSVK-EAKERAYEMLEKVGL---EHRINHRPSELSGGERQRVAIARALVNQPS 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2524658687 190 LLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLaAERADRLVVMQAGRVVE 250
Cdd:TIGR02211 162 LVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLEL-AKKLDRVLEMKDGQLFN 221
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
9-273 |
5.15e-50 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 180.67 E-value: 5.15e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 9 AAPILTLKDVCIGFPTTTASGRRSKSLTDVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGDGEvtggtITFDG 88
Cdd:PRK15134 272 ASPLLDVEQLQVAFPIRKGILKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQGE-----IWFDG 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 89 RDITHLTDREFVSIRgNGIGLVPQDPMTNLNPVWTVGSQIKEALRANNIA-TGSEAHKKAIELLEQAGL-PNAKKRidqY 166
Cdd:PRK15134 347 QPLHNLNRRQLLPVR-HRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHQPTlSAAQREQQVIAVMEEVGLdPETRHR---Y 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 167 PHEFSGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAG 246
Cdd:PRK15134 423 PAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQG 502
|
250 260
....*....|....*....|....*..
gi 2524658687 247 RVVETGPALQVLTRPQHPYTKQLIAAA 273
Cdd:PRK15134 503 EVVEQGDCERVFAAPQQEYTRQLLALS 529
|
|
| PhnK |
COG4107 |
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and ... |
298-547 |
5.62e-50 |
|
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and metabolism];
Pssm-ID: 443283 [Multi-domain] Cd Length: 262 Bit Score: 173.08 E-value: 5.62e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 298 ILVAKNLVRDFAIRGDRPWrkdsfrAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRN- 376
Cdd:COG4107 8 LLSVRGLSKRYGPGCGTVV------ACRDVSFDLYPGEVLGIVGESGSGKSTLLKCLYFDLAPTSGSVYYRDRDGGPRDl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 377 RKEELELRRRIQP-----IFQNPYATLDPMRTVHSSIEEPL------RIHKIgtkkerEQRVFELLDRVALPAEMGRRFP 445
Cdd:COG4107 82 FALSEAERRRLRRtdwgmVYQNPRDGLRMDVSAGGNIAERLmaagerHYGDI------RARALEWLERVEIPLERIDDLP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 446 GELSGGQRQRVAIARALALNPEVVVCDEAVSALDVVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGK 525
Cdd:COG4107 156 RTFSGGMQQRVQIARALVTNPRLLFLDEPTTGLDVSVQARLLDLIRRLQRELGLSMIVVTHDLGVIRLLADRTMVMKNGR 235
|
250 260
....*....|....*....|..
gi 2524658687 526 MVEHRPTDDLFDHPEKEYTQRL 547
Cdd:COG4107 236 VVESGLTDQVLEDPQHPYTQLL 257
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
38-268 |
1.59e-49 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 170.95 E-value: 1.59e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETVAIVGESGSGKSTtahaALGLLPGDGEVTGGTITFDGRDITHlTDREFVSIRGNgIGLVPQDPmtN 117
Cdd:COG1126 16 VLKGISLDVEKGEVVVIIGPSGSGKST----LLRCINLLEEPDSGTITVDGEDLTD-SKKDINKLRRK-VGMVFQQF--N 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 118 LNPVWTVGSQIKEALRANNIATGSEAHKKAIELLEQAGLPNakkRIDQYPHEFSGGMRQRALIAMGLAAHPKLLIADEPT 197
Cdd:COG1126 88 LFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLAD---KADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPT 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2524658687 198 SALDVTVAKKILDHLDKLTSElGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVLTRPQHPYTKQ 268
Cdd:COG1126 165 SALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRA 234
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
299-525 |
2.40e-49 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 169.98 E-value: 2.40e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 299 LVAKNLVRDFAIRGDRpwrkdsFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRK 378
Cdd:cd03255 1 IELKNLSKTYGGGGEK------VQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 379 EELELRRR-IQPIFQNPYatLDPMRTVHSSIEEPLRIHKIGtKKEREQRVFELLDRVALPAEMgRRFPGELSGGQRQRVA 457
Cdd:cd03255 75 ELAAFRRRhIGFVFQSFN--LLPDLTALENVELPLLLAGVP-KKERRERAEELLERVGLGDRL-NHYPSELSGGQQQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2524658687 458 IARALALNPEVVVCDEAVSALDVVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQvADEVIVMEHGK 525
Cdd:cd03255 151 IARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELRDGK 217
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
8-270 |
2.70e-49 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 170.55 E-value: 2.70e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 8 SAAPILTLKDVCIGFptttasGRRsksltdVVH-DVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGDGevtgGTITF 86
Cdd:COG1127 1 MSEPMIEVRNLTKSF------GDR------VVLdGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDS----GEILV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 87 DGRDITHLTDREFVSIRGNgIGLVPQ-----DPMTnlnpvwtVGSQIKEALRANNIATGSEAHKKAIELLEQAGLPNAkk 161
Cdd:COG1127 65 DGQDITGLSEKELYELRRR-IGMLFQggalfDSLT-------VFENVAFPLREHTDLSEAEIRELVLEKLELVGLPGA-- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 162 rIDQYPHEFSGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLV 241
Cdd:COG1127 135 -ADKMPSELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVA 213
|
250 260
....*....|....*....|....*....
gi 2524658687 242 VMQAGRVVETGPaLQVLTRPQHPYTKQLI 270
Cdd:COG1127 214 VLADGKIIAEGT-PEELLASDDPWVRQFL 241
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
32-272 |
2.95e-49 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 171.17 E-value: 2.95e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 32 SKSLTDVVHDVNLEVFPGETVAIVGESGSGKSTTAHaalgLLPGDGEVTGGTITFDGRditHLTDREFvSIRGNGIGLVP 111
Cdd:COG4167 22 RRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAK----MLAGIIEPTSGEILINGH---KLEYGDY-KYRCKHIRMIF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 112 QDPMTNLNPVWTVGSQIKEALRANNIATGSEAHKKAIELLEQAGL-PNakkRIDQYPHEFSGGMRQRALIAMGLAAHPKL 190
Cdd:COG4167 94 QDPNTSLNPRLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGLlPE---HANFYPHMLSSGQKQRVALARALILQPKI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 191 LIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVLTRPQHPYTKQLI 270
Cdd:COG4167 171 IIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFANPQHEVTKRLI 250
|
..
gi 2524658687 271 AA 272
Cdd:COG4167 251 ES 252
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
41-273 |
4.44e-49 |
|
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: 170.40 E-value: 4.44e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 41 DVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGDGevtgGTITFDGRD-----ITHLTDREFVSIRGNGIGLVPQDPM 115
Cdd:TIGR02323 21 DVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDH----GTATYIMRSgaeleLYQLSEAERRRLMRTEWGFVHQNPR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 116 TNLNPVWTVGSQIKEALRANNIATGSEAHKKAIELLEQAGLPNAkkRIDQYPHEFSGGMRQRALIAMGLAAHPKLLIADE 195
Cdd:TIGR02323 97 DGLRMRVSAGANIGERLMAIGARHYGNIRATAQDWLEEVEIDPT--RIDDLPRAFSGGMQQRLQIARNLVTRPRLVFMDE 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2524658687 196 PTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVLTRPQHPYTKQLIAAA 273
Cdd:TIGR02323 175 PTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDPQHPYTQLLVSSI 252
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
319-548 |
5.64e-49 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 173.02 E-value: 5.64e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 319 DSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRnrkeeLELR-RRIQPIFQNpYAt 397
Cdd:COG1118 13 GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTN-----LPPReRRVGFVFQH-YA- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 398 LDPMRTVHSSIEEPLRIHKIGtKKEREQRVFELLDRVALpAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVSA 477
Cdd:COG1118 86 LFPHMTVAENIAFGLRVRPPS-KAEIRARVEELLELVQL-EGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2524658687 478 LDVVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDLFDHPEKEYTQRLL 548
Cdd:COG1118 164 LDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFL 234
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
12-259 |
1.11e-48 |
|
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: 169.45 E-value: 1.11e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 12 ILTLKDVCIGFPTTTasgrrsksltdVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPgdgeVTGGTITFDGRDI 91
Cdd:COG1120 1 MLEAENLSVGYGGRP-----------VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLK----PSSGEVLLDGRDL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 92 THLTDREFVSIrgngIGLVPQDPMTNLNpvWTVgsqiKEALR------ANNIATGSEAHKKAI-ELLEQAGLPN-AKKRI 163
Cdd:COG1120 66 ASLSRRELARR----IAYVPQEPPAPFG--LTV----RELVAlgryphLGLFGRPSAEDREAVeEALERTGLEHlADRPV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 164 DqyphEFSGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVM 243
Cdd:COG1120 136 D----ELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLL 211
|
250
....*....|....*.
gi 2524658687 244 QAGRVVETGPALQVLT 259
Cdd:COG1120 212 KDGRIVAQGPPEEVLT 227
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
13-251 |
1.31e-48 |
|
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: 168.03 E-value: 1.31e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 13 LTLKDVCIGFPTTTASgrrskslTDVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPgdgeVTGGTITFDGRDIT 92
Cdd:cd03293 1 LEVRNVSKTYGGGGGA-------VTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLER----PTSGEVLVDGEPVT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 93 HltdrefvsiRGNGIGLVPQDPmtNLNPvW-TVGSQIKEALRANNIATgSEAHKKAIELLEQAGLPNAKKRidqYPHEFS 171
Cdd:cd03293 70 G---------PGPDRGYVFQQD--ALLP-WlTVLDNVALGLELQGVPK-AEARERAEELLELVGLSGFENA---YPHQLS 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 172 GGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQA--GRVV 249
Cdd:cd03293 134 GGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIV 213
|
..
gi 2524658687 250 ET 251
Cdd:cd03293 214 AE 215
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
321-521 |
2.44e-48 |
|
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: 167.26 E-value: 2.44e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 321 FRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRkeelelRRRIqpIFQNPyaTLDP 400
Cdd:cd03293 17 VTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP------DRGY--VFQQD--ALLP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 401 MRTVHSSIEEPLRIHKIGtKKEREQRVFELLDRVALpAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVSALDV 480
Cdd:cd03293 87 WLTVLDNVALGLELQGVP-KAEARERAEELLELVGL-SGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2524658687 481 VVQAQVLELLAELQEEMDLAYLFITHDL--AVVrqVADEVIVM 521
Cdd:cd03293 165 LTREQLQEELLDIWRETGKTVLLVTHDIdeAVF--LADRVVVL 205
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
319-529 |
3.64e-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: 166.54 E-value: 3.64e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 319 DSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNrkeelELRRRIQPIFQNPyaTL 398
Cdd:cd03259 11 GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVP-----PERRNIGMVFQDY--AL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 399 DPMRTVHSSIEEPLRIHKIGtKKEREQRVFELLDRVALPAEMGRRfPGELSGGQRQRVAIARALALNPEVVVCDEAVSAL 478
Cdd:cd03259 84 FPHLTVAENIAFGLKLRGVP-KAEIRARVRELLELVGLEGLLNRY-PHELSGGQQQRVALARALAREPSLLLLDEPLSAL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2524658687 479 DVVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEH 529
Cdd:cd03259 162 DAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQV 212
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
38-260 |
4.90e-48 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 166.78 E-value: 4.90e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPgdgeVTGGTITFDGRDIThltdREFVSIRGNgIGLVPQDPmtN 117
Cdd:COG1131 15 ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLR----PTSGEVRVLGEDVA----RDPAEVRRR-IGYVPQEP--A 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 118 LNPVWTVGSQIKEALRANNIaTGSEAHKKAIELLEQAGLPN-AKKRIDQYphefSGGMRQRALIAMGLAAHPKLLIADEP 196
Cdd:COG1131 84 LYPDLTVRENLRFFARLYGL-PRKEARERIDELLELFGLTDaADRKVGTL----SGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2524658687 197 TSALDVTVAKKILDHLDKLTSElGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVLTR 260
Cdd:COG1131 159 TSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
308-535 |
5.08e-48 |
|
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: 166.59 E-value: 5.08e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 308 FAIRGDRPWRKDsFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLD-----PTEGEVLFDGKRVQGRNrKEELE 382
Cdd:cd03260 1 IELRDLNVYYGD-KHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLD-VDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 383 LRRRIQPIFQNPyaTLDPMrTVHSSIEEPLRIHKIGTKKEREQRVFELLDRVALPAEMGRR-FPGELSGGQRQRVAIARA 461
Cdd:cd03260 79 LRRRVGMVFQKP--NPFPG-SIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKDRlHALGLSGGQQQRLCLARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2524658687 462 LALNPEVVVCDEAVSALDVVVQAQVleLLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDL 535
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPISTAKI--EELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
8-254 |
1.24e-47 |
|
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: 165.68 E-value: 1.24e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 8 SAAPILTLKDVCIGFPTttasgrRSKSLTdVVHDVNLEVFPGETVAIVGESGSGKSTtahaALGLLPGDGEVTGGTITFD 87
Cdd:COG4181 4 SSAPIIELRGLTKTVGT------GAGELT-ILKGISLEVEAGESVAIVGASGSGKST----LLGLLAGLDRPTSGTVRLA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 88 GRDITHLTDREFVSIRGNGIGLVPQD----P-MTNLNPVwtvgsqikeALRANnIATGSEAHKKAIELLEQAGLpnaKKR 162
Cdd:COG4181 73 GQDLFALDEDARARLRARHVGFVFQSfqllPtLTALENV---------MLPLE-LAGRRDARARARALLERVGL---GHR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 163 IDQYPHEFSGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAeRADRLVV 242
Cdd:COG4181 140 LDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAA-RCDRVLR 218
|
250
....*....|..
gi 2524658687 243 MQAGRVVETGPA 254
Cdd:COG4181 219 LRAGRLVEDTAA 230
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
8-535 |
4.01e-47 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 171.75 E-value: 4.01e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 8 SAAPILTLKDVCIGFPTTTAsgrrsksltdvVHDVNLEVFPGETVAIVGESGSGKSTtahaaL-----GLLPGDGevtgG 82
Cdd:COG3845 1 MMPPALELRGITKRFGGVVA-----------NDDVSLTVRPGEIHALLGENGAGKST-----LmkilyGLYQPDS----G 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 83 TITFDGRDithltdrefVSIRG------NGIGLVPQDPMtnLNPVWTVgsqikealrANNIATGSE-----------AHK 145
Cdd:COG3845 61 EILIDGKP---------VRIRSprdaiaLGIGMVHQHFM--LVPNLTV---------AENIVLGLEptkggrldrkaARA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 146 KAIELLEQAGL---PNAKkridqyPHEFSGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSElGTS 222
Cdd:COG3845 121 RIRELSERYGLdvdPDAK------VEDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAE-GKS 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 223 VVLITHDLGLAAERADRLVVMQAGRVVETGPALQVltrpqhpyTKQLIAA-----APSLAARRGDRVVAAPttsdadqke 297
Cdd:COG3845 194 IIFITHKLREVMAIADRVTVLRRGKVVGTVDTAET--------SEEELAElmvgrEVLLRVEKAPAEPGEV--------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 298 ILVAKNLVrdfaIRGDRPwrkdsFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNR 377
Cdd:COG3845 257 VLEVENLS----VRDDRG-----VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSP 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 378 KEELELR-RRIqpifqnPYatlDPMRT--VHS-SIEEPL---RIHKIGT-------KKEREQRVFELLDR-------VAL 436
Cdd:COG3845 328 RERRRLGvAYI------PE---DRLGRglVPDmSVAENLilgRYRRPPFsrggfldRKAIRAFAEELIEEfdvrtpgPDT 398
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 437 PAemgrrfpGELSGGQRQRVAIARALALNPEVVVCDEAVSALDVVVQAQVlellaeLQEEMDL-----AYLFITHDLAVV 511
Cdd:COG3845 399 PA-------RSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFI------HQRLLELrdagaAVLLISEDLDEI 465
|
570 580
....*....|....*....|....
gi 2524658687 512 RQVADEVIVMEHGKMVEHRPTDDL 535
Cdd:COG3845 466 LALSDRIAVMYEGRIVGEVPAAEA 489
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
38-535 |
4.40e-47 |
|
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: 172.29 E-value: 4.40e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGL---LPGDGEVT-------------------------GGTITFDGR 89
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqyEPTSGRIIyhvalcekcgyverpskvgepcpvcGGTLEPEEV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 90 DITHLTDREFVSIRGNgIGLVPQDPMTnLNPVWTVGSQIKEALraNNIA-TGSEAHKKAIELLEQAGLPNakkRIDQYPH 168
Cdd:TIGR03269 95 DFWNLSDKLRRRIRKR-IAIMLQRTFA-LYGDDTVLDNVLEAL--EEIGyEGKEAVGRAVDLIEMVQLSH---RITHIAR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 169 EFSGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRV 248
Cdd:TIGR03269 168 DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLENGEI 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 249 VETGPALQVLTRpqhpytkqLIAAAPSLaarRGDRVVAApttsdadQKEILVAKNLVRDFaIRGDRpwrkDSFRAVDDIS 328
Cdd:TIGR03269 248 KEEGTPDEVVAV--------FMEGVSEV---EKECEVEV-------GEPIIKVRNVSKRY-ISVDR----GVVKAVDNVS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 329 FTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLF---------DGKRVQGRNRkeeleLRRRIQPIFQNpyATLD 399
Cdd:TIGR03269 305 LEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdewvdmTKPGPDGRGR-----AKRYIGILHQE--YDLY 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 400 PMRTVHSSIEEPL------------RIHKIGTKKEREQRVFELLDRvalpaemgrrFPGELSGGQRQRVAIARALALNPE 467
Cdd:TIGR03269 378 PHRTVLDNLTEAIglelpdelarmkAVITLKMVGFDEEKAEEILDK----------YPDELSEGERHRVALAQVLIKEPR 447
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2524658687 468 VVVCDEAVSALDVVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDL 535
Cdd:TIGR03269 448 IVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
317-550 |
6.71e-47 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 164.01 E-value: 6.71e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 317 RKDSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVqgrNRKEELELRRRIQPIFQNpyA 396
Cdd:cd03295 10 YGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDI---REQDPVELRRKIGYVIQQ--I 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 397 TLDPMRTVHSSIEEPLRIHKIGtKKEREQRVFELLDRVAL-PAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAV 475
Cdd:cd03295 85 GLFPHMTVEENIALVPKLLKWP-KEKIRERADELLALVGLdPAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPF 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2524658687 476 SALDVVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDLFDHPEKEYTQRLLDA 550
Cdd:cd03295 164 GALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGA 238
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
36-262 |
9.65e-47 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 163.27 E-value: 9.65e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 36 TDVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGdgevTGGTITFDGRDITHLTDREfvsIRGNgIGLVPQDPM 115
Cdd:COG1122 14 TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKP----TSGEVLVDGKDITKKNLRE---LRRK-VGLVFQNPD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 116 TNL-NPvwTVGSQIKEALRANNIaTGSEAHKKAIELLEQAGLPNAKKRidqYPHEFSGGMRQRALIAMGLAAHPKLLIAD 194
Cdd:COG1122 86 DQLfAP--TVEEDVAFGPENLGL-PREEIRERVEEALELVGLEHLADR---PPHELSGGQKQRVAIAGVLAMEPEVLVLD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2524658687 195 EPTSALDVTVAKKILDHLDKLTSElGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVLTRPQ 262
Cdd:COG1122 160 EPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
7-264 |
1.75e-46 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 163.72 E-value: 1.75e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 7 TSAAPILTLKDVCIGFPTTTASgrrskslTDVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPgdgeVTGGTITF 86
Cdd:COG1116 2 SAAAPALELRGVSKRFPTGGGG-------VTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEK----PTSGEVLV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 87 DGRDITHLTDRefvsirgngIGLVPQDPmtNLNPvW-TVGSQIKEALRANNIATgSEAHKKAIELLEQAGLpnaKKRIDQ 165
Cdd:COG1116 71 DGKPVTGPGPD---------RGVVFQEP--ALLP-WlTVLDNVALGLELRGVPK-AERRERARELLELVGL---AGFEDA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 166 YPHEFSGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQA 245
Cdd:COG1116 135 YPHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSA 214
|
250 260
....*....|....*....|..
gi 2524658687 246 --GRVVETgpaLQV-LTRPQHP 264
Cdd:COG1116 215 rpGRIVEE---IDVdLPRPRDR 233
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
11-274 |
3.91e-46 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 164.98 E-value: 3.91e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 11 PILTLKDVCIGFPTttasgrrSKSLTDVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGDGEVTGGTITFDGRD 90
Cdd:PRK15093 2 PLLDIRNLTIEFKT-------SDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRVTADRMRFDDID 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 91 ITHLTDREFVSIRGNGIGLVPQDPMTNLNPVWTVGSQIKEAL-----------RANniatgsEAHKKAIELLEQAGLPNA 159
Cdd:PRK15093 75 LLRLSPRERRKLVGHNVSMIFQEPQSCLDPSERVGRQLMQNIpgwtykgrwwqRFG------WRKRRAIELLHRVGIKDH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 160 KKRIDQYPHEFSGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADR 239
Cdd:PRK15093 149 KDAMRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADK 228
|
250 260 270
....*....|....*....|....*....|....*
gi 2524658687 240 LVVMQAGRVVETGPALQVLTRPQHPYTKQLIAAAP 274
Cdd:PRK15093 229 INVLYCGQTVETAPSKELVTTPHHPYTQALIRAIP 263
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
9-364 |
4.48e-46 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 165.27 E-value: 4.48e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 9 AAPILTLKDVCIGFPTTTAsgrrsksltdvVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPgdgeVTGGTITFDG 88
Cdd:COG3842 2 AMPALELENVSKRYGDVTA-----------LDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFET----PDSGRILLDG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 89 RDITHLT--DRefvsirgnGIGLVPQD----PmtNLnpvwTVgsqikealrANNIATG--------SEAHKKAIELLEQA 154
Cdd:COG3842 67 RDVTGLPpeKR--------NVGMVFQDyalfP--HL----TV---------AENVAFGlrmrgvpkAEIRARVAELLELV 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 155 GLPNAKKRidqYPHEFSGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAA 234
Cdd:COG3842 124 GLEGLADR---YPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEAL 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 235 ERADRLVVMQAGRVVETGPALQVLTRPQHPY-----------TKQLIAAAPSLAARRGDRVVAAPTTSDADQKEILVAkn 303
Cdd:COG3842 201 ALADRIAVMNDGRIEQVGTPEEIYERPATRFvadfigeanllPGTVLGDEGGGVRTGGRTLEVPADAGLAAGGPVTVA-- 278
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2524658687 304 lVR--DFAIRGDRPwrKDSFRA-VDDISFtlrRGRTIGIVGESGSGKSTVANMAL-GLLDPTEGE 364
Cdd:COG3842 279 -IRpeDIRLSPEGP--ENGLPGtVEDVVF---LGSHVRYRVRLGDGQELVVRVPNrAALPLEPGD 337
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
299-535 |
5.27e-46 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 161.38 E-value: 5.27e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 299 LVAKNLVRDFairgdrpwrkDSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVqgrnRK 378
Cdd:COG1131 1 IEVRGLTKRY----------GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDV----AR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 379 EELELRRRIQPIFQNPYatLDPMRTVHSSIEEPLRIHKIgTKKEREQRVFELLDRVALPAEMGRRFpGELSGGQRQRVAI 458
Cdd:COG1131 67 DPAEVRRRIGYVPQEPA--LYPDLTVRENLRFFARLYGL-PRKEARERIDELLELFGLTDAADRKV-GTLSGGMKQRLGL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 459 ARALALNPEVVVCDEAVSALDVVVQAQVlellaelqeeMDL---------AYLFITHDLAVVRQVADEVIVMEHGKMVEH 529
Cdd:COG1131 143 ALALLHDPELLILDEPTSGLDPEARREL----------WELlrelaaegkTVLLSTHYLEEAERLCDRVAIIDKGRIVAD 212
|
....*.
gi 2524658687 530 RPTDDL 535
Cdd:COG1131 213 GTPDEL 218
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
317-552 |
6.47e-46 |
|
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: 162.43 E-value: 6.47e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 317 RKDSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEELELRR-RIQPIFQNpY 395
Cdd:cd03294 33 KTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRkKISMVFQS-F 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 396 ATLdPMRTVHSSIEEPLRIHKIGtKKEREQRVFELLDRVALpAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAV 475
Cdd:cd03294 112 ALL-PHRTVLENVAFGLEVQGVP-RAEREERAAEALELVGL-EGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2524658687 476 SALDVVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDLFDHPEKEYTQRLLDAIP 552
Cdd:cd03294 189 SALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFRGVD 265
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
12-262 |
3.61e-45 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 159.28 E-value: 3.61e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 12 ILTLKDVCIGFPTTtasgrrsKSLTDVVHDVNLEVFPGETVAIVGESGSGKSTTahaaLGLLPGDGEVTGGTITFDGRDI 91
Cdd:cd03258 1 MIELKNVSKVFGDT-------GGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTL----IRCINGLERPTSGSVLVDGTDL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 92 THLTDREFVSIRGNgIGLVPQdpmtNLNPVW--TVGSQIKEALRANNIAtGSEAHKKAIELLEQAGLPNakkRIDQYPHE 169
Cdd:cd03258 70 TLLSGKELRKARRR-IGMIFQ----HFNLLSsrTVFENVALPLEIAGVP-KAEIEERVLELLELVGLED---KADAYPAQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 170 FSGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVV 249
Cdd:cd03258 141 LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVV 220
|
250
....*....|...
gi 2524658687 250 ETGPALQVLTRPQ 262
Cdd:cd03258 221 EEGTVEEVFANPQ 233
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
13-252 |
7.65e-45 |
|
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: 157.68 E-value: 7.65e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 13 LTLKDVCIGFPTTTAsgrrsksltdvVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPgdgeVTGGTITFDGRDIT 92
Cdd:cd03259 1 LELKGLSKTYGSVRA-----------LDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLER----PDSGEILIDGRDVT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 93 HLTDREfvsirgNGIGLVPQDPmtNLNPVWTVGSQIKEALRANNIATGsEAHKKAIELLEQAGLPNAKKRidqYPHEFSG 172
Cdd:cd03259 66 GVPPER------RNIGMVFQDY--ALFPHLTVAENIAFGLKLRGVPKA-EIRARVRELLELVGLEGLLNR---YPHELSG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 173 GMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETG 252
Cdd:cd03259 134 GQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
38-280 |
1.01e-44 |
|
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: 159.20 E-value: 1.01e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLlpgdGEVTGGTITFDGRDITHLTDREFVSIRGNgIGLVPQDPMTN 117
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGL----EKPAQGTVSFRGQDLYQLDRKQRRAFRRD-VQLVFQDSPSA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 118 LNPVWTVGSQIKEALRANNIATGSEAHKKAIELLEQAGLPNakKRIDQYPHEFSGGMRQRALIAMGLAAHPKLLIADEPT 197
Cdd:TIGR02769 101 VNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRS--EDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 198 SALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVLTRpQHPYTKQLIAAA-PSL 276
Cdd:TIGR02769 179 SNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLLSF-KHPAGRNLQSAVlPEH 257
|
....
gi 2524658687 277 AARR 280
Cdd:TIGR02769 258 PVRR 261
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
15-268 |
1.11e-44 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 158.05 E-value: 1.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 15 LKDVCIGFPTTTasgrrsksltdVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGDGevtgGTITFDGRDITHL 94
Cdd:cd03261 3 LRGLTKSFGGRT-----------VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDS----GEVLIDGEDISGL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 95 TDREFVSIRgNGIGLVPQDP--MTNLnpvwTVGSQIKEALRANNIATGSEAHKKAIELLEQAGLPNAKkriDQYPHEFSG 172
Cdd:cd03261 68 SEAELYRLR-RRMGMLFQSGalFDSL----TVFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAE---DLYPAELSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 173 GMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETG 252
Cdd:cd03261 140 GMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEG 219
|
250
....*....|....*.
gi 2524658687 253 PaLQVLTRPQHPYTKQ 268
Cdd:cd03261 220 T-PEELRASDDPLVRQ 234
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
36-316 |
2.06e-44 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 160.70 E-value: 2.06e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 36 TDVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGDGevtgGTITFDGRDI-THLTDREfvsiRGngIGLVPQDP 114
Cdd:COG1118 15 FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDS----GRIVLNGRDLfTNLPPRE----RR--VGFVFQHY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 115 MtnLNPVWTVgsqikealrANNIATG--------SEAHKKAIELLEQAGLPNAKKRidqYPHEFSGGMRQRALIAMGLAA 186
Cdd:COG1118 85 A--LFPHMTV---------AENIAFGlrvrppskAEIRARVEELLELVQLEGLADR---YPSQLSGGQRQRVALARALAV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 187 HPKLLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVLTRPQHPYT 266
Cdd:COG1118 151 EPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFV 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2524658687 267 KQLIAAAPSLAARRGDRVVAapttsdADQKEILVAKNLVRDFAIRGDRPW 316
Cdd:COG1118 231 ARFLGCVNVLRGRVIGGQLE------ADGLTLPVAEPLPDGPAVAGVRPH 274
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
39-270 |
2.57e-44 |
|
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: 158.19 E-value: 2.57e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 39 VHDVNLEVFPGETVAIVGESGSGKSTTahaaLGLLPGDGEVTGGTITFDGRDITHLTDREFVSIRGNGIGLVPQDpmTNL 118
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTL----LRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKKISMVFQS--FAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 119 NPVWTVGSQIKEALRANNIATgSEAHKKAIELLEQAGLpnaKKRIDQYPHEFSGGMRQRALIAMGLAAHPKLLIADEPTS 198
Cdd:cd03294 114 LPHRTVLENVAFGLEVQGVPR-AEREERAAEALELVGL---EGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFS 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2524658687 199 ALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVLTRPQHPYTKQLI 270
Cdd:cd03294 190 ALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFF 261
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
15-247 |
3.30e-44 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 155.70 E-value: 3.30e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 15 LKDVCIGFPTTTasgrrskslTDVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPgdgeVTGGTITFDGRDITHL 94
Cdd:cd03225 2 LKNLSFSYPDGA---------RPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLG----PTSGEVLVDGKDLTKL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 95 TDREFvsirGNGIGLVPQDPMTNL-NPvwTVGSQIKEALRANNIAtGSEAHKKAIELLEQAGLPNAKKRidqYPHEFSGG 173
Cdd:cd03225 69 SLKEL----RRKVGLVFQNPDDQFfGP--TVEEEVAFGLENLGLP-EEEIEERVEEALELVGLEGLRDR---SPFTLSGG 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2524658687 174 MRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSElGTSVVLITHDLGLAAERADRLVVMQAGR 247
Cdd:cd03225 139 QKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
319-540 |
4.77e-44 |
|
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: 156.24 E-value: 4.77e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 319 DSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRnrkeeLELRRRIQPIFQNpYAtL 398
Cdd:cd03300 11 GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNL-----PPHKRPVNTVFQN-YA-L 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 399 DPMRTVHSSIEEPLRIHKIGtKKEREQRVFELLDRVALpAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVSAL 478
Cdd:cd03300 84 FPHLTVFENIAFGLRLKKLP-KAEIKERVAEALDLVQL-EGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGAL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2524658687 479 DVVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDLFDHPE 540
Cdd:cd03300 162 DLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
317-539 |
9.74e-44 |
|
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: 155.57 E-value: 9.74e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 317 RKDSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEelelrRRIQPIFQNpYA 396
Cdd:cd03296 11 RFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE-----RNVGFVFQH-YA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 397 TLDPMrTVHSSIEEPLRIHKIGT---KKEREQRVFELLDRVALPAeMGRRFPGELSGGQRQRVAIARALALNPEVVVCDE 473
Cdd:cd03296 85 LFRHM-TVFDNVAFGLRVKPRSErppEAEIRAKVHELLKLVQLDW-LADRYPAQLSGGQRQRVALARALAVEPKVLLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2524658687 474 AVSALDVVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDLFDHP 539
Cdd:cd03296 163 PFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHP 228
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
8-259 |
5.67e-43 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 153.71 E-value: 5.67e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 8 SAAPILTLKDVCIGFPTTTasgrrsksltdVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPgdgeVTGGTITFD 87
Cdd:COG1121 2 MMMPAIELENLTVSYGGRP-----------VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLP----PTSGTVRLF 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 88 GRDITHltdrefvsiRGNGIGLVPQD-------PMTnlnpVW-TVGSQIKEALRANNIAtGSEAHKKAIELLEQAGLPN- 158
Cdd:COG1121 67 GKPPRR---------ARRRIGYVPQRaevdwdfPIT----VRdVVLMGRYGRRGLFRRP-SRADREAVDEALERVGLEDl 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 159 AKKRIDqyphEFSGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSElGTSVVLITHDLGLAAERAD 238
Cdd:COG1121 133 ADRPIG----ELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFD 207
|
250 260
....*....|....*....|.
gi 2524658687 239 RLVVMqAGRVVETGPALQVLT 259
Cdd:COG1121 208 RVLLL-NRGLVAHGPPEEVLT 227
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
319-557 |
5.85e-43 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 153.67 E-value: 5.85e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 319 DSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEELELRRRIQPIFQNPYatL 398
Cdd:COG3638 14 GGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLRRRIGMIFQQFN--L 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 399 DPMRTVHSSIeepL--RIHKIGT---------KKEReQRVFELLDRVALPAEMGRRfPGELSGGQRQRVAIARALALNPE 467
Cdd:COG3638 92 VPRLSVLTNV---LagRLGRTSTwrsllglfpPEDR-ERALEALERVGLADKAYQR-ADQLSGGQQQRVAIARALVQEPK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 468 VVVCDEAVSALDVVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDLfdhpekeyTQRL 547
Cdd:COG3638 167 LILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL--------TDAV 238
|
250
....*....|
gi 2524658687 548 LDAIPGASLD 557
Cdd:COG3638 239 LREIYGGEAE 248
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
324-550 |
6.58e-43 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 153.70 E-value: 6.58e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 324 VDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDP----TEGEVLFDGKRVQGRnrkeelELR-RRIQPIFQNPYATL 398
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPC------ALRgRKIATIMQNPRSAF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 399 DPMRTVHSSIEEPLRihKIGtKKEREQRVFELLDRVAL--PAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVS 476
Cdd:PRK10418 93 NPLHTMHTHARETCL--ALG-KPADDATLTAALEAVGLenAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTT 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2524658687 477 ALDVVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDLFDHPEKEYTQRLLDA 550
Cdd:PRK10418 170 DLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSA 243
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
36-252 |
7.92e-43 |
|
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: 151.05 E-value: 7.92e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 36 TDVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGDGevtgGTITFDGRDITHLTDREFVSIrgngIGLVPQdpm 115
Cdd:cd03214 12 RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSS----GEILLDGKDLASLSPKELARK----IAYVPQ--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 116 tnlnpvwtvgsqikealranniatgseahkkAIELLEQAGLpnAKKRIDqyphEFSGGMRQRALIAMGLAAHPKLLIADE 195
Cdd:cd03214 81 -------------------------------ALELLGLAHL--ADRPFN----ELSGGERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2524658687 196 PTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETG 252
Cdd:cd03214 124 PTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
323-525 |
1.42e-42 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 150.42 E-value: 1.42e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 323 AVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQgRNRKEELELRRRIQPIFQNPyaTLDPMR 402
Cdd:cd03229 15 VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLT-DLEDELPPLRRRIGMVFQDF--ALFPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 403 TVhssieeplrihkigtkkereqrvfelLDRVALPaemgrrfpgeLSGGQRQRVAIARALALNPEVVVCDEAVSALDVVV 482
Cdd:cd03229 92 TV--------------------------LENIALG----------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPIT 135
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2524658687 483 QAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGK 525
Cdd:cd03229 136 RREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
323-525 |
1.53e-42 |
|
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: 151.47 E-value: 1.53e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 323 AVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEeleLRRRIQPIFQNPYATLdPMR 402
Cdd:cd03225 16 ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKE---LRRKVGLVFQNPDDQF-FGP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 403 TVHSSIEEPLRIHKIgTKKEREQRVFELLDRVALpAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVSALDVVV 482
Cdd:cd03225 92 TVEEEVAFGLENLGL-PEEEIEERVEEALELVGL-EGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAG 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2524658687 483 QAQVlellaelqeeMDL---------AYLFITHDLAVVRQVADEVIVMEHGK 525
Cdd:cd03225 170 RREL----------LELlkklkaegkTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
38-248 |
1.55e-42 |
|
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: 151.53 E-value: 1.55e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLlpgdGEVTGGTITFDGRDITHlTDREFVSIRGNgIGLVPQDpmTN 117
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLL----EEPDSGTIIIDGLKLTD-DKKNINELRQK-VGMVFQQ--FN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 118 LNPVWTVGSQIKEALRANNIATGSEAHKKAIELLEQAGLPNakkRIDQYPHEFSGGMRQRALIAMGLAAHPKLLIADEPT 197
Cdd:cd03262 87 LFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLAD---KADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPT 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2524658687 198 SALDVTVAKKILDHLDKLTSElGTSVVLITHDLGLAAERADRLVVMQAGRV 248
Cdd:cd03262 164 SALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
39-290 |
2.34e-42 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 154.96 E-value: 2.34e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 39 VHDVNLEVFPGETVAIVGESGSGKSTTahaaLGLLPGDGEVTGGTITFDGRDITHLTDREFVSIRGNgIGLVPQDpmTNL 118
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTL----IRCINLLERPTSGRVLVDGQDLTALSEKELRKARRQ-IGMIFQH--FNL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 119 NPVWTVGSQIKEALRANNIATgSEAHKKAIELLEQAGLpnAKKRiDQYPHEFSGGMRQRALIAMGLAAHPKLLIADEPTS 198
Cdd:PRK11153 94 LSSRTVFDNVALPLELAGTPK-AEIKARVTELLELVGL--SDKA-DRYPAQLSGGQKQRVAIARALASNPKVLLCDEATS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 199 ALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVLTRPQHPYTKQLIAAA--PSL 276
Cdd:PRK11153 170 ALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREFIQSTlhLDL 249
|
250
....*....|....
gi 2524658687 277 AARRGDRVVAAPTT 290
Cdd:PRK11153 250 PEDYLARLQAEPTT 263
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
324-474 |
3.58e-42 |
|
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: 148.18 E-value: 3.58e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 324 VDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKeelELRRRIQPIFQNPyaTLDPMRT 403
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERK---SLRKEIGYVFQDP--QLFPRLT 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2524658687 404 VHSSIEEPLRIHKIgTKKEREQRVFELLDRVALPAEMGRR---FPGELSGGQRQRVAIARALALNPEVVVCDEA 474
Cdd:pfam00005 76 VRENLRLGLLLKGL-SKREKDARAEEALEKLGLGDLADRPvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
12-250 |
3.94e-42 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 150.59 E-value: 3.94e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 12 ILTLKDVCIGFPTTTasgrrsksltDVVHDVNLEVFPGETVAIVGESGSGKSTTahaaLGLLPGDGEVTGGTITFDGRDI 91
Cdd:COG2884 1 MIRFENVSKRYPGGR----------EALSDVSLEIEKGEFVFLTGPSGAGKSTL----LKLLYGEERPTSGQVLVNGQDL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 92 THLTDREFVSIRGNgIGLVPQDpmTNLNPVWTVGSQIKEALRANNiATGSEAHKKAIELLEQAGLpnaKKRIDQYPHEFS 171
Cdd:COG2884 67 SRLKRREIPYLRRR-IGVVFQD--FRLLPDRTVYENVALPLRVTG-KSRKEIRRRVREVLDLVGL---SDKAKALPHELS 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2524658687 172 GGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLtSELGTSVVLITHDLGLAAERADRLVVMQAGRVVE 250
Cdd:COG2884 140 GGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEI-NRRGTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
30-280 |
8.22e-42 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 151.38 E-value: 8.22e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 30 RRSKSLTdVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLlpgdGEVTGGTITFDGRDITHLTDREFVSIRGNgIGL 109
Cdd:PRK10419 20 GKHQHQT-VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGL----ESPSQGNVSWRGEPLAKLNRAQRKAFRRD-IQM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 110 VPQDPMTNLNPVWTVGSQIKEALRanNIATGSEAHKKA--IELLEQAGLPNAKkrIDQYPHEFSGGMRQRALIAMGLAAH 187
Cdd:PRK10419 94 VFQDSISAVNPRKTVREIIREPLR--HLLSLDKAERLAraSEMLRAVDLDDSV--LDKRPPQLSGGQLQRVCLARALAVE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 188 PKLLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVLTRpQHPYTK 267
Cdd:PRK10419 170 PKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKLTF-SSPAGR 248
|
250
....*....|....
gi 2524658687 268 QLIAAA-PSLAARR 280
Cdd:PRK10419 249 VLQNAVlPAFPVRR 262
|
|
| ABC_MetN |
TIGR02314 |
D-methionine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding ... |
323-560 |
8.93e-42 |
|
D-methionine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of the D-methionine ABC transporter complex. Known members belong to the Proteobacteria.
Pssm-ID: 131367 [Multi-domain] Cd Length: 343 Bit Score: 153.50 E-value: 8.93e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 323 AVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEELELRRRIQPIFQnpYATLDPMR 402
Cdd:TIGR02314 20 ALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTSGSVIVDGQDLTTLSNSELTKARRQIGMIFQ--HFNLLSSR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 403 TVHSSIEEPLRIHkiGTKKER-EQRVFELLDRVALpAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVSALDVV 481
Cdd:TIGR02314 98 TVFGNVALPLELD--NTPKDEiKRKVTELLALVGL-GDKHDSYPSNLSGGQKQRVAIARALASNPKVLLCDEATSALDPA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2524658687 482 VQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDLFDHPEKEYTQRLLDaipgASLDLDL 560
Cdd:TIGR02314 175 TTQSILELLKEINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQGTVSEIFSHPKTPLAQKFIR----STLHLSI 249
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
320-525 |
1.66e-41 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 148.83 E-value: 1.66e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 320 SFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRnRKEELELRRRIQPIFQNpyATLD 399
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDD-KKNINELRQKVGMVFQQ--FNLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 400 PMRTVHSSIEEPLRIHKIGTKKEREQRVFELLDRVALpAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVSALD 479
Cdd:cd03262 89 PHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGL-ADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2524658687 480 VVVQAQVLELLAelqeemDLAY-----LFITHDLAVVRQVADEVIVMEHGK 525
Cdd:cd03262 168 PELVGEVLDVMK------DLAEegmtmVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
13-265 |
1.82e-41 |
|
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: 159.23 E-value: 1.82e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 13 LTLKDVCIGFPtttasgrrsKSLTDVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLpgdgEVTGGTITFDGRDIT 92
Cdd:COG2274 474 IELENVSFRYP---------GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLY----EPTSGRILIDGIDLR 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 93 HLtDREfvSIRGNgIGLVPQDPMtnlnpVWTvGSqIKEalranNIATGSEA--HKKAIELLEQAGLpnakkridqypHEF 170
Cdd:COG2274 541 QI-DPA--SLRRQ-IGVVLQDVF-----LFS-GT-IRE-----NITLGDPDatDEEIIEAARLAGL-----------HDF 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 171 -------------------SGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSelGTSVVLITHDLG 231
Cdd:COG2274 594 iealpmgydtvvgeggsnlSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLS 671
|
250 260 270
....*....|....*....|....*....|....
gi 2524658687 232 LAAeRADRLVVMQAGRVVETGPALQVLTRPQHPY 265
Cdd:COG2274 672 TIR-LADRIIVLDKGRIVEDGTHEELLARKGLYA 704
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
319-539 |
2.07e-41 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 152.53 E-value: 2.07e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 319 DSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEelelrRRIQPIFQNpYATL 398
Cdd:COG3839 14 GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD-----RNIAMVFQS-YALY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 399 DPMrTVHSSIEEPLRIHKIgTKKEREQRVFELLDRVALPAEMGRRfPGELSGGQRQRVAIARALALNPEVVVCDEAVSAL 478
Cdd:COG3839 88 PHM-TVYENIAFPLKLRKV-PKAEIDRRVREAAELLGLEDLLDRK-PKQLSGGQRQRVALGRALVREPKVFLLDEPLSNL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2524658687 479 DVVVQAQVLEllaelqeemDLAYL---------FITHDlavvrQV-----ADEVIVMEHGKMVEHRPTDDLFDHP 539
Cdd:COG3839 165 DAKLRVEMRA---------EIKRLhrrlgtttiYVTHD-----QVeamtlADRIAVMNDGRIQQVGTPEELYDRP 225
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
323-531 |
2.84e-41 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 148.28 E-value: 2.84e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 323 AVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEELELRRRIQPIFQnpyatlD--- 399
Cdd:COG2884 17 ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRRRIGVVFQ------Dfrl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 400 -PMRTVHSSIEEPLRIHKIgTKKEREQRVFELLDRVALpAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVSAL 478
Cdd:COG2884 91 lPDRTVYENVALPLRVTGK-SRKEIRRRVREVLDLVGL-SDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2524658687 479 DvvvqaqvlellaeLQEEMDLAYLFI------------THDLAVVRQVADEVIVMEHGKMVEHRP 531
Cdd:COG2884 169 D-------------PETSWEIMELLEeinrrgttvliaTHDLELVDRMPKRVLELEDGRLVRDEA 220
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
268-543 |
1.20e-40 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 156.53 E-value: 1.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 268 QLIAAAPSL-----AARRGDRVVAAPTTSDADQKEI--------LVAKNLVrdFAIRGDRPWrkdsfrAVDDISFTLRRG 334
Cdd:COG2274 430 QLIGLLQRFqdakiALERLDDILDLPPEREEGRSKLslprlkgdIELENVS--FRYPGDSPP------VLDNISLTIKPG 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 335 RTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEeleLRRRIQPIFQNPYatldpmrTVHSSIEEPLRI 414
Cdd:COG2274 502 ERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPAS---LRRQIGVVLQDVF-------LFSGTIRENITL 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 415 HKIGTkkeREQRVFELLDRV-------ALP-------AEMGRRfpgeLSGGQRQRVAIARALALNPEVVVCDEAVSALDV 480
Cdd:COG2274 572 GDPDA---TDEEIIEAARLAglhdfieALPmgydtvvGEGGSN----LSGGQRQRLAIARALLRNPRILILDEATSALDA 644
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2524658687 481 VVQAQVLELLAELQEEMDLayLFITHDLAVVRQvADEVIVMEHGKMVEHRPTDDLFDHPEKEY 543
Cdd:COG2274 645 ETEAIILENLRRLLKGRTV--IIIAHRLSTIRL-ADRIIVLDKGRIVEDGTHEELLARKGLYA 704
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
318-551 |
2.50e-40 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 146.56 E-value: 2.50e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 318 KDSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEELELRRRIQPIFQNpYAT 397
Cdd:cd03256 11 PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQIGMIFQQ-FNL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 398 LDPMrtvhSSIEEPL-----RIHKIGT-----KKEREQRVFELLDRVALpAEMGRRFPGELSGGQRQRVAIARALALNPE 467
Cdd:cd03256 90 IERL----SVLENVLsgrlgRRSTWRSlfglfPKEEKQRALAALERVGL-LDKAYQRADQLSGGQQQRVAIARALMQQPK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 468 VVVCDEAVSALDVVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVehrptddlFDHPEKEYTQRL 547
Cdd:cd03256 165 LILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIV--------FDGPPAELTDEV 236
|
....
gi 2524658687 548 LDAI 551
Cdd:cd03256 237 LDEI 240
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
323-525 |
2.62e-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: 144.06 E-value: 2.62e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 323 AVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEeleLRRRIQPIFQNPYatLdpmr 402
Cdd:cd03228 17 VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLES---LRKNIAYVPQDPF--L---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 403 tVHSSIEEPLrihkigtkkereqrvfelldrvalpaemgrrfpgeLSGGQRQRVAIARALALNPEVVVCDEAVSALDVVV 482
Cdd:cd03228 88 -FSGTIRENI-----------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPET 131
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2524658687 483 QAQVLELLAELQEemDLAYLFITHDLAVVRQvADEVIVMEHGK 525
Cdd:cd03228 132 EALILEALRALAK--GKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
29-254 |
3.10e-40 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 146.17 E-value: 3.10e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 29 GRRSKSLTDVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLpgdgEVTGGTITFDGRDITHLTDREFVSIRGNgIG 108
Cdd:cd03256 7 SKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLV----EPTSGSVLIDGTDINKLKGKALRQLRRQ-IG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 109 LVPQDPmtNLNPVWTVgsqIKEAL--RANNIATG-------SEAHK-KAIELLEQAGL-PNAKKRIDQypheFSGGMRQR 177
Cdd:cd03256 82 MIFQQF--NLIERLSV---LENVLsgRLGRRSTWrslfglfPKEEKqRALAALERVGLlDKAYQRADQ----LSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2524658687 178 ALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPA 254
Cdd:cd03256 153 VAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPP 229
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
325-526 |
6.09e-40 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 144.19 E-value: 6.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 325 DDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRkeeLELRRRIQPIFQNPYATLDpmrTV 404
Cdd:COG4619 17 SPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPP---PEWRRQVAYVPQEPALWGG---TV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 405 HSSIEEPLRIHKigtKKEREQRVFELLDRVALPAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVSALDVVVQA 484
Cdd:COG4619 91 RDNLPFPFQLRE---RKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2524658687 485 QVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKM 526
Cdd:COG4619 168 RVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
36-258 |
9.96e-40 |
|
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: 144.11 E-value: 9.96e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 36 TDVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPgdgeVTGGTITFDGRDITHLTDREFVSIrgnGIGLVPQDPm 115
Cdd:cd03224 13 SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLP----PRSGSIRFDGRDITGLPPHERARA---GIGYVPEGR- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 116 tNLNPVWTVGSQIKEALRANNIATGSEAHKKAIELleqagLPNAKKRIDQYPHEFSGGMRQRALIAMGLAAHPKLLIADE 195
Cdd:cd03224 85 -RIFPELTVEENLLLGAYARRRAKRKARLERVYEL-----FPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2524658687 196 PTSALDVTVAKKILDHLDKLtSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVL 258
Cdd:cd03224 159 PSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELL 220
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
38-272 |
1.41e-39 |
|
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: 144.37 E-value: 1.41e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLpgdgEVTGGTITFDGRDITHLtdrEFVSIRGNgIGLVPQDpmTN 117
Cdd:cd03295 16 AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLI----EPTSGEIFIDGEDIREQ---DPVELRRK-IGYVIQQ--IG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 118 LNPVWTVgsqikealrANNIAT--------GSEAHKKAIELLEQAGLPNAKKRiDQYPHEFSGGMRQRALIAMGLAAHPK 189
Cdd:cd03295 86 LFPHMTV---------EENIALvpkllkwpKEKIRERADELLALVGLDPAEFA-DRYPHELSGGQQQRVGVARALAADPP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 190 LLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVLTRPQHPYTKQL 269
Cdd:cd03295 156 LLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEF 235
|
...
gi 2524658687 270 IAA 272
Cdd:cd03295 236 VGA 238
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
38-249 |
1.32e-38 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 140.92 E-value: 1.32e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETVAIVGESGSGKSTTahaaLGLLPGDGEVTGGTITFDGRDITHLTDREFVSIRGNgIGLVPQDpmTN 117
Cdd:TIGR02982 20 VLFDINLEINPGEIVILTGPSGSGKTTL----LTLIGGLRSVQEGSLKVLGQELHGASKKQLVQLRRR-IGYIFQA--HN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 118 LNPVWTVGSQIKEALRANNIATGSEAHKKAIELLEQAGLpnaKKRIDQYPHEFSGGMRQRALIAMGLAAHPKLLIADEPT 197
Cdd:TIGR02982 93 LLGFLTARQNVQMALELQPNLSYQEARERARAMLEAVGL---GDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2524658687 198 SALDVTVAKKILDHLDKLTSELGTSVVLITHD---LGLaaerADRLVVMQAGRVV 249
Cdd:TIGR02982 170 AALDSKSGRDVVELMQKLAKEQGCTILMVTHDnriLDV----ADRILQMEDGKLL 220
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
289-545 |
1.52e-38 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 142.10 E-value: 1.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 289 TTSDADQKEILVAKNLvrDFAIrgdrpwrkDSFRAVDDISFTLRRGRTIGIVGESGSGKSTVanmalgL--------LDP 360
Cdd:COG1117 2 TAPASTLEPKIEVRNL--NVYY--------GDKQALKDINLDIPENKVTALIGPSGCGKSTL------LrclnrmndLIP 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 361 ---TEGEVLFDGKRVqgRNRKEEL-ELRRRIQPIFQ--NPYatldPMrtvhsSIEE----PLRIHKIGTKKEREQRVFEL 430
Cdd:COG1117 66 garVEGEILLDGEDI--YDPDVDVvELRRRVGMVFQkpNPF----PK-----SIYDnvayGLRLHGIKSKSELDEIVEES 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 431 LDRVALPAEMGRRF--PG-ELSGGQRQRVAIARALALNPEVVVCDEAVSALDVVVQAQVLellaelqeemDLAY------ 501
Cdd:COG1117 135 LRKAALWDEVKDRLkkSAlGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIE----------ELILelkkdy 204
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2524658687 502 --LFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDLFDHPEKEYTQ 545
Cdd:COG1117 205 tiVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKDKRTE 250
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
321-558 |
1.83e-38 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 143.89 E-value: 1.83e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 321 FRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDP----TEGEVLFDGK---RVQGRNRKEELelRRRIQPIFQN 393
Cdd:COG4170 20 VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIdllKLSPRERRKII--GREIAMIFQE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 394 PYATLDPMRTVHSSIEE-----PLRIHKIGTKKEREQRVFELLDRVAL--PAEMGRRFPGELSGGQRQRVAIARALALNP 466
Cdd:COG4170 98 PSSCLDPSAKIGDQLIEaipswTFKGKWWQRFKWRKKRAIELLHRVGIkdHKDIMNSYPHELTEGECQKVMIAMAIANQP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 467 EVVVCDEAVSALDVVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDLFDHPEKEYTQR 546
Cdd:COG4170 178 RLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSPHHPYTKA 257
|
250
....*....|..
gi 2524658687 547 LLDAIPGASLDL 558
Cdd:COG4170 258 LLRSMPDFRQPL 269
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
277-528 |
2.06e-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: 2.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 277 AARRGDRVVAAPT--TSDADQKEILVAKNLVR----DFAIRGDRPwrkdsfrAVDDISFTLRRGRTIGIVGESGSGKSTV 350
Cdd:COG1132 310 SAERIFELLDEPPeiPDPPGAVPLPPVRGEIEfenvSFSYPGDRP-------VLKDISLTIPPGETVALVGPSGSGKSTL 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 351 ANMALGLLDPTEGEVLFDGKRVQGRNRKEeleLRRRIQPIFQNPYatLdpmrtVHSSIEEPLRIhkiGTKKEREQRVFEL 430
Cdd:COG1132 383 VNLLLRFYDPTSGRILIDGVDIRDLTLES---LRRQIGVVPQDTF--L-----FSGTIRENIRY---GRPDATDEEVEEA 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 431 LDRVALpAEMGRRFP-------GE----LSGGQRQRVAIARALALNPEVVVCDEAVSALDVVVQAQVLELlaelqeemdL 499
Cdd:COG1132 450 AKAAQA-HEFIEALPdgydtvvGErgvnLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEA---------L 519
|
250 260 270
....*....|....*....|....*....|....*.
gi 2524658687 500 AYL-------FITHDLAVVRQvADEVIVMEHGKMVE 528
Cdd:COG1132 520 ERLmkgrttiVIAHRLSTIRN-ADRILVLDDGRIVE 554
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
299-535 |
2.87e-38 |
|
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: 140.76 E-value: 2.87e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 299 LVAKNLVRDFairgdrpwrkDSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVqgrnRK 378
Cdd:COG4555 2 IEVENLSKKY----------GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDV----RK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 379 EELELRRRIQPIFQNPYatLDPMRTVHSSIEEPLRIHKIgTKKEREQRVFELLDRVALPAEMGRRFpGELSGGQRQRVAI 458
Cdd:COG4555 68 EPREARRQIGVLPDERG--LYDRLTVRENIRYFAELYGL-FDEELKKRIEELIELLGLEEFLDRRV-GELSTGMKKKVAL 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2524658687 459 ARALALNPEVVVCDEAVSALDVVVQAQVLELLAELQEEmDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDL 535
Cdd:COG4555 144 ARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
38-270 |
3.60e-38 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 142.54 E-value: 3.60e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETVAIVGESGSGKSTTahaaL----GLLpgdgEVTGGTITFDGRDIThltDREFVSIRGNgIGLVPQD 113
Cdd:COG1125 17 AVDDLSLTIPAGEFTVLVGPSGCGKTTT----LrminRLI----EPTSGRILIDGEDIR---DLDPVELRRR-IGYVIQQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 114 pmTNLNPVWTVgsqikealrANNIAT-----G---SEAHKKAIELLEQAGLPNAKKRiDQYPHEFSGGMRQRALIAMGLA 185
Cdd:COG1125 85 --IGLFPHMTV---------AENIATvprllGwdkERIRARVDELLELVGLDPEEYR-DRYPHELSGGQQQRVGVARALA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 186 AHPKLLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVLTRPQHPY 265
Cdd:COG1125 153 ADPPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDF 232
|
....*
gi 2524658687 266 TKQLI 270
Cdd:COG1125 233 VADFV 237
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
36-253 |
4.38e-38 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 148.00 E-value: 4.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 36 TDVVHDVNLEVFPGETVAIVGESGSGKSTTAHaalgLLPGDGEVTGGTITFDGRDITHLTDRefvSIRGNgIGLVPQDPm 115
Cdd:COG1132 353 RPVLKDISLTIPPGETVALVGPSGSGKSTLVN----LLLRFYDPTSGRILIDGVDIRDLTLE---SLRRQ-IGVVPQDT- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 116 tnlnpvW----TVgsqikealrANNIATGS-EAHKKAIEL-LEQAglpNAKKRIDQYPH-----------EFSGGMRQRA 178
Cdd:COG1132 424 ------FlfsgTI---------RENIRYGRpDATDEEVEEaAKAA---QAHEFIEALPDgydtvvgergvNLSGGQRQRI 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2524658687 179 LIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSelGTSVVLITHDLGlAAERADRLVVMQAGRVVETGP 253
Cdd:COG1132 486 AIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLS-TIRNADRILVLDDGRIVEQGT 557
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
13-247 |
4.92e-38 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 137.90 E-value: 4.92e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 13 LTLKDVCIGFPTTTAsgrrsksltDVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLpgdgEVTGGTITFDGRDIT 92
Cdd:cd03228 1 IEFKNVSFSYPGRPK---------PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLY----DPTSGEILIDGVDLR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 93 HLTDRefvSIRGNgIGLVPQDP----MTnlnpvwtvgsqIKEalranNIatgseahkkaielleqaglpnakkridqyph 168
Cdd:cd03228 68 DLDLE---SLRKN-IAYVPQDPflfsGT-----------IRE-----NI------------------------------- 96
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2524658687 169 eFSGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSelGTSVVLITHDLGLaAERADRLVVMQAGR 247
Cdd:cd03228 97 -LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLST-IRDADRIIVLDDGR 171
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
38-248 |
9.42e-38 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 137.14 E-value: 9.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPgdgeVTGGTITFDGRDIThltdREFVSIRGNgIGLVPQDPMtn 117
Cdd:cd03230 15 ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLK----PDSGEIKVLGKDIK----KEPEEVKRR-IGYLPEEPS-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 118 LNPVWTVgsqikealranniatgseahkkaIELLEqaglpnakkridqypheFSGGMRQRALIAMGLAAHPKLLIADEPT 197
Cdd:cd03230 84 LYENLTV-----------------------RENLK-----------------LSGGMKQRLALAQALLHDPELLILDEPT 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2524658687 198 SALDVTVAKKILDHLDKLTSElGTSVVLITHDLGLAAERADRLVVMQAGRV 248
Cdd:cd03230 124 SGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
270-538 |
1.05e-37 |
|
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: 146.44 E-value: 1.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 270 IAAAPSLAA---RRGDRVVAAPTTSDADQKEILVAKNLVrdFAIRGDRPwrkdsfrAVDDISFTLRRGRTIGIVGESGSG 346
Cdd:COG4988 305 IAAAEKIFAlldAPEPAAPAGTAPLPAAGPPSIELEDVS--FSYPGGRP-------ALDGLSLTIPPGERVALVGPSGAG 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 347 KSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEeleLRRRIQPIFQNPYatldpmrTVHSSIEEPLRIhkiGTKKEREQR 426
Cdd:COG4988 376 KSTLLNLLLGFLPPYSGSILINGVDLSDLDPAS---WRRQIAWVPQNPY-------LFAGTIRENLRL---GRPDASDEE 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 427 VFELLDRVALpAEMGRRFP-------GE----LSGGQRQRVAIARALALNPEVVVCDEAVSALDVVVQAQVLELLAELQE 495
Cdd:COG4988 443 LEAALEAAGL-DEFVAALPdgldtplGEggrgLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK 521
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2524658687 496 emDLAYLFITHDLAVVRQvADEVIVMEHGKMVEHRPTDDLFDH 538
Cdd:COG4988 522 --GRTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEELLAK 561
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
323-541 |
2.57e-37 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 139.10 E-value: 2.57e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 323 AVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVqgRNRKEELELRRRIQPIFQNPYATLdpmr 402
Cdd:TIGR04520 17 ALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDT--LDEENLWEIRKKVGMVFQNPDNQF---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 403 tVHSSIE-------EPLRIhkigTKKEREQRVFELLDRVALpAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAV 475
Cdd:TIGR04520 91 -VGATVEddvafglENLGV----PREEMRKRVDEALKLVGM-EDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEAT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2524658687 476 SALDVVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQvADEVIVMEHGKMVEHRPTDDLFDHPEK 541
Cdd:TIGR04520 165 SMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIFSQVEL 229
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
294-543 |
2.61e-37 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 141.40 E-value: 2.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 294 DQKEILVAKNLVRDFAirgdrpwrkdSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQ 373
Cdd:PRK11432 2 TQKNFVVLKNITKRFG----------SNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 374 GRNRKEelelrRRIQPIFQNpYAtLDPMRTVHSSIEEPLRIHKIGtKKEREQRVFELLDRVALpAEMGRRFPGELSGGQR 453
Cdd:PRK11432 72 HRSIQQ-----RDICMVFQS-YA-LFPHMSLGENVGYGLKMLGVP-KEERKQRVKEALELVDL-AGFEDRYVDQISGGQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 454 QRVAIARALALNPEVVVCDEAVSALDVVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTD 533
Cdd:PRK11432 143 QRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQ 222
|
250
....*....|
gi 2524658687 534 DLFDHPEKEY 543
Cdd:PRK11432 223 ELYRQPASRF 232
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
8-265 |
3.41e-37 |
|
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: 145.29 E-value: 3.41e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 8 SAAPILTLKDVCIGFPTTTAsgrrsksltDVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPgdgeVTGGTITFD 87
Cdd:COG4987 329 PGGPSLELEDVSFRYPGAGR---------PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLD----PQSGSITLG 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 88 GRDITHLTDREfvsIRGNgIGLVPQDP----MTnlnpvwtvgsqIKEALR-ANNIATGSEahkkAIELLEQAGLpnaKKR 162
Cdd:COG4987 396 GVDLRDLDEDD---LRRR-IAVVPQRPhlfdTT-----------LRENLRlARPDATDEE----LWAALERVGL---GDW 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 163 IDQYPH-----------EFSGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSelGTSVVLITHDLg 231
Cdd:COG4987 454 LAALPDgldtwlgeggrRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRL- 530
|
250 260 270
....*....|....*....|....*....|....
gi 2524658687 232 LAAERADRLVVMQAGRVVETGPALQVLTRPQHPY 265
Cdd:COG4987 531 AGLERMDRILVLEDGRIVEQGTHEELLAQNGRYR 564
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
298-551 |
3.73e-37 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 138.14 E-value: 3.73e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 298 ILVAKNLVRDFAIRgdrpwrkdsfRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNR 377
Cdd:PRK11701 6 LLSVRGLTKLYGPR----------KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 378 KEELELRRRIQP------IFQNPYATLDPMRTVHSSIEEPLRihKIGTKKEREQR--VFELLDRVALPAEMGRRFPGELS 449
Cdd:PRK11701 76 YALSEAERRRLLrtewgfVHQHPRDGLRMQVSAGGNIGERLM--AVGARHYGDIRatAGDWLERVEIDAARIDDLPTTFS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 450 GGQRQRVAIARALALNPEVVVCDEAVSALDVVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEH 529
Cdd:PRK11701 154 GGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVES 233
|
250 260
....*....|....*....|..
gi 2524658687 530 RPTDDLFDHPEKEYTQRLLDAI 551
Cdd:PRK11701 234 GLTDQVLDDPQHPYTQLLVSSV 255
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
30-248 |
4.25e-37 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 136.48 E-value: 4.25e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 30 RRSKSLTDVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGdgevTGGTITFDGRDITHLTDREFVSIrgngIGL 109
Cdd:COG4619 7 SFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPP----TSGEIYLDGKPLSAMPPPEWRRQ----VAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 110 VPQDPmtnlnpVW---TVGSQIKEALRANNIATGSEahkKAIELLEQAGLPNA--KKRIdqypHEFSGGMRQRALIAMGL 184
Cdd:COG4619 79 VPQEP------ALwggTVRDNLPFPFQLRERKFDRE---RALELLERLGLPPDilDKPV----ERLSGGERQRLALIRAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2524658687 185 AAHPKLLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRV 248
Cdd:COG4619 146 LLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
326-527 |
4.80e-37 |
|
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: 136.66 E-value: 4.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 326 DISFTLRRGRTiGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEELEL-RRRIQPIFQNpyATLDPMRTV 404
Cdd:cd03297 16 KIDFDLNEEVT-GIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPqQRKIGLVFQQ--YALFPHLNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 405 HSSIEEPLRIHKigtKKEREQRVFELLDRVALpAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVSALDVVVQA 484
Cdd:cd03297 93 RENLAFGLKRKR---NREDRISVDELLDLLGL-DHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2524658687 485 QVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMV 527
Cdd:cd03297 169 QLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
323-539 |
5.62e-37 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 137.53 E-value: 5.62e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 323 AVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRnrkeelelRRRI----QpifqnpYATL 398
Cdd:COG1121 21 VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA--------RRRIgyvpQ------RAEV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 399 D---PMR---TVHSSIEEPLRIHKIGTKKEREqRVFELLDRVALPAEMGRRFpGELSGGQRQRVAIARALALNPEVVVCD 472
Cdd:COG1121 87 DwdfPITvrdVVLMGRYGRRGLFRRPSRADRE-AVDEALERVGLEDLADRPI-GELSGGQQQRVLLARALAQDPDLLLLD 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2524658687 473 EAVSALDVVVQAQVlellaelqeeMDL---------AYLFITHDLAVVRQVADEVIVMEHGkMVEHRPTDDLFDHP 539
Cdd:COG1121 165 EPFAGVDAATEEAL----------YELlrelrregkTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPEEVLTPE 229
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
37-272 |
1.21e-36 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 137.23 E-value: 1.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 37 DVVHDVNLEVFPGETVAIVGESGSGKSTTAHaalgLLPGDGEVTGGTITFDGRDItHLTDREFVSIRgngIGLVPQDPMT 116
Cdd:PRK15112 27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAK----MLAGMIEPTSGELLIDDHPL-HFGDYSYRSQR---IRMIFQDPST 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 117 NLNPVWTVGSQIKEALRANNIATGSEAHKKAIELLEQAGLpnAKKRIDQYPHEFSGGMRQRALIAMGLAAHPKLLIADEP 196
Cdd:PRK15112 99 SLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGL--LPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEA 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2524658687 197 TSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVLTRPQHPYTKQLIAA 272
Cdd:PRK15112 177 LASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPLHELTKRLIAG 252
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
36-264 |
1.31e-36 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 136.38 E-value: 1.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 36 TDVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLlpgdGEVTGGTITFDGRDIT--HLTDREfvsIRGNGiGLV--- 110
Cdd:PRK09493 14 TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKL----EEITSGDLIVDGLKVNdpKVDERL---IRQEA-GMVfqq 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 111 ----PQdpMTNLNPVWTVGSQIKEALRAnniatgsEAHKKAIELLEQAGLpnaKKRIDQYPHEFSGGMRQRALIAMGLAA 186
Cdd:PRK09493 86 fylfPH--LTALENVMFGPLRVRGASKE-------EAEKQARELLAKVGL---AERAHHYPSELSGGQQQRVAIARALAV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2524658687 187 HPKLLIADEPTSALDVTVAKKILDHLDKLTSElGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVLTRPQHP 264
Cdd:PRK09493 154 KPKLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQ 230
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
320-542 |
1.79e-36 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 135.91 E-value: 1.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 320 SFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMaLGLLD-PTEGEVLFDGKRV---QGRNRKEELELRRRIQPIFQNpY 395
Cdd:COG4161 14 SHQALFDINLECPSGETLVLLGPSGAGKSSLLRV-LNLLEtPDSGQLNIAGHQFdfsQKPSEKAIRLLRQKVGMVFQQ-Y 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 396 aTLDPMRTVHSS-IEEPLRIHKIgTKKEREQRVFELLDRVALpAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEA 474
Cdd:COG4161 92 -NLWPHLTVMENlIEAPCKVLGL-SKEQAREKAMKLLARLRL-TDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2524658687 475 VSALDVVVQAQVlELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHrPTDDLFDHPEKE 542
Cdd:COG4161 169 TAALDPEITAQV-VEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQ-GDASHFTQPQTE 234
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
39-198 |
1.90e-36 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 132.77 E-value: 1.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 39 VHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGdgevTGGTITFDGRDITHLTDRefvsIRGNGIGLVPQDPmtNL 118
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSP----TEGTILLDGQDLTDDERK----SLRKEIGYVFQDP--QL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 119 NPVWTVGSQIKEALRANNIATgSEAHKKAIELLEQAGLPN-AKKRIDQYPHEFSGGMRQRALIAMGLAAHPKLLIADEPT 197
Cdd:pfam00005 71 FPRLTVRENLRLGLLLKGLSK-REKDARAEEALEKLGLGDlADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
.
gi 2524658687 198 S 198
Cdd:pfam00005 150 A 150
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
324-548 |
4.21e-36 |
|
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: 134.77 E-value: 4.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 324 VDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQgrNRKEElelRRRIQPIFQNpYAtLDPMRT 403
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT--NLPPE---KRDISYVPQN-YA-LFPHMT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 404 VHSSIEEPLRiHKIGTKKEREQRVFELLDRVALpAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVSALDVVVQ 483
Cdd:cd03299 88 VYKNIAYGLK-KRKVDKKEIERKVLEIAEMLGI-DHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTK 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2524658687 484 AQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDLFDHPEKEYTQRLL 548
Cdd:cd03299 166 EKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFL 230
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
10-295 |
4.42e-36 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 137.86 E-value: 4.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 10 APILTLKDVCIGFPTTTAsgrrsksltdvVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLlpgdGEVTGGTITFDGR 89
Cdd:TIGR03265 2 SPYLSIDNIRKRFGAFTA-----------LKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGL----ERQTAGTIYQGGR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 90 DITHLTdrefVSIRGNGIglVPQDpmTNLNPVWTVgsqikealrANNIATG--------SEAHKKAIELLEQAGLPNAKk 161
Cdd:TIGR03265 67 DITRLP----PQKRDYGI--VFQS--YALFPNLTV---------ADNIAYGlknrgmgrAEVAERVAELLDLVGLPGSE- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 162 riDQYPHEFSGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLV 241
Cdd:TIGR03265 129 --RKYPGQLSGGQQQRVALARALATSPGLLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIV 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2524658687 242 VMQAGRVVETGPALQVLTRPQHPYTKQLIAAAPSLAARRGD--RVVAAPTTSDADQ 295
Cdd:TIGR03265 207 VMNHGVIEQVGTPQEIYRHPATPFVADFVGEVNWLPGTRGGgsRARVGGLTLACAP 262
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
13-247 |
1.22e-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: 131.54 E-value: 1.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 13 LTLKDVCIGFPTTTasgrrsksltdVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLpgdgEVTGGTITFDGRDIT 92
Cdd:cd03229 1 LELKNVSKRYGQKT-----------VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLE----EPDSGSILIDGEDLT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 93 hlTDREFVSIRGNGIGLVPQDPmtNLNPVWTVGSQIKEALranniatgseahkkaielleqaglpnakkridqyphefSG 172
Cdd:cd03229 66 --DLEDELPPLRRRIGMVFQDF--ALFPHLTVLENIALGL--------------------------------------SG 103
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2524658687 173 GMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGR 247
Cdd:cd03229 104 GQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
36-276 |
1.41e-35 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 133.39 E-value: 1.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 36 TDVVHDVNLEVFPGETVAIVGESGSGKSTTahaaLGLLPGDGEVTGGTITFDGRDITHltdrefVSIRGNGIGLVPQDpm 115
Cdd:TIGR00968 13 FQALDDVNLEVPTGSLVALLGPSGSGKSTL----LRIIAGLEQPDSGRIRLNGQDATR------VHARDRKIGFVFQH-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 116 TNLNPVWTVGSQIKEALRANNIaTGSEAHKKAIELLEQAGLpnaKKRIDQYPHEFSGGMRQRALIAMGLAAHPKLLIADE 195
Cdd:TIGR00968 81 YALFKHLTVRDNIAFGLEIRKH-PKAKIKARVEELLELVQL---EGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 196 PTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVLTRPQHPYTKQLIAAAPS 275
Cdd:TIGR00968 157 PFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLGEVNV 236
|
.
gi 2524658687 276 L 276
Cdd:TIGR00968 237 L 237
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
39-272 |
1.73e-35 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 133.23 E-value: 1.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 39 VHDVNLEVFPGETVAIVGESGSGKSTTahaaLGLLPGDGEVTGGTITFDGRDITHLTDREfvsirgNGIGLVPQDpmTNL 118
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTL----LRLIAGLERPDSGTILFGGEDATDVPVQE------RNVGFVFQH--YAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 119 NPVWTVGSQIKEALRANNIATG---SEAHKKAIELLEQAGLPNAKKRidqYPHEFSGGMRQRALIAMGLAAHPKLLIADE 195
Cdd:cd03296 86 FRHMTVFDNVAFGLRVKPRSERppeAEIRAKVHELLKLVQLDWLADR---YPAQLSGGQRQRVALARALAVEPKVLLLDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2524658687 196 PTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVLTRPQHPYTKQLIAA 272
Cdd:cd03296 163 PFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLGE 239
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
323-551 |
2.53e-35 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 132.81 E-value: 2.53e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 323 AVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEELELRRRIQPIFQNpYATLDPMr 402
Cdd:TIGR02315 17 ALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLRRRIGMIFQH-YNLIERL- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 403 tvhsSIEEPLRIHKIGTK-----------KEREQRVFELLDRVALpAEMGRRFPGELSGGQRQRVAIARALALNPEVVVC 471
Cdd:TIGR02315 95 ----TVLENVLHGRLGYKptwrsllgrfsEEDKERALSALERVGL-ADKAYQRADQLSGGQQQRVAIARALAQQPDLILA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 472 DEAVSALDVVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVehrptddlFDHPEKEYTQRLLDAI 551
Cdd:TIGR02315 170 DEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIV--------FDGAPSELDDEVLRHI 241
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
38-252 |
2.97e-35 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 131.50 E-value: 2.97e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPgdgeVTGGTITFDGRDITHLTDRefvsirgngIGLVPQD---- 113
Cdd:cd03235 14 VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLK----PTSGSIRVFGKPLEKERKR---------IGYVPQRrsid 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 114 ---PMTnlnpVWTVgsqikealrannIATGSEAH------------KKAIELLEQAGLPN-AKKRIDqyphEFSGGMRQR 177
Cdd:cd03235 81 rdfPIS----VRDV------------VLMGLYGHkglfrrlskadkAKVDEALERVGLSElADRQIG----ELSGGQQQR 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2524658687 178 ALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSElGTSVVLITHDLGLAAERADRlVVMQAGRVVETG 252
Cdd:cd03235 141 VLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDR-VLLLNRTVVASG 213
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
32-262 |
3.12e-35 |
|
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: 132.46 E-value: 3.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 32 SKSLTD-VVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGDGevtgGTITFDGRDITHLTDREfvsirgNGIGLV 110
Cdd:cd03299 7 SKDWKEfKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDS----GKILLNGKDITNLPPEK------RDISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 111 PQDpmTNLNPVWTVGSQIKEALRaNNIATGSEAHKKAIELLEQAGLPNAkkrIDQYPHEFSGGMRQRALIAMGLAAHPKL 190
Cdd:cd03299 77 PQN--YALFPHMTVYKNIAYGLK-KRKVDKKEIERKVLEIAEMLGIDHL---LNRKPETLSGGEQQRVAIARALVVNPKI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2524658687 191 LIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVLTRPQ 262
Cdd:cd03299 151 LLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPK 222
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
38-260 |
4.61e-35 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 132.94 E-value: 4.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLL-PgdgevTGGTITFDG---RDITHLTDrefvsIRGNgIGLVPQD 113
Cdd:TIGR04520 17 ALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLlP-----TSGKVTVDGldtLDEENLWE-----IRKK-VGMVFQN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 114 PMTNLnpvwtVGSQIKEalranNIATGseahkkaielLEQAGLPNA--KKRIDQY-------------PHEFSGGMRQRA 178
Cdd:TIGR04520 86 PDNQF-----VGATVED-----DVAFG----------LENLGVPREemRKRVDEAlklvgmedfrdrePHLLSGGQKQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 179 LIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAErADRLVVMQAGRVVETGPALQVL 258
Cdd:TIGR04520 146 AIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIF 224
|
..
gi 2524658687 259 TR 260
Cdd:TIGR04520 225 SQ 226
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
38-262 |
6.07e-35 |
|
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: 131.26 E-value: 6.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPgdgeVTGGTITFDGRDITHL-TDRefvsIRGNGIGLVPQD--- 113
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLP----PRSGSIRFDGEDITGLpPHR----IARLGIGYVPEGrri 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 114 --PMT---NLnpvwTVGsqikeALRANNIATGSEAHKKAIELLeqaglPNAKKRIDQYPHEFSGGMRQRALIAMGLAAHP 188
Cdd:COG0410 90 fpSLTveeNL----LLG-----AYARRDRAEVRADLERVYELF-----PRLKERRRQRAGTLSGGEQQMLAIGRALMSRP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2524658687 189 KLLIADEPTSALDVTVAKKILDHLDKLTSElGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVLTRPQ 262
Cdd:COG0410 156 KLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
33-248 |
7.54e-35 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 131.09 E-value: 7.54e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 33 KSLTDVVHDVNLEVFPGETVAIVGESGSGKSTTAHaalgLLPGDGEVTGGTITFDGRDITHLTDREFVSIRGNGIGLVPQ 112
Cdd:PRK11629 19 SVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLH----LLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQKLGFIYQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 113 dpMTNLNPVWTVGSQIKEALRANNIATgSEAHKKAIELLEQAGLpnaKKRIDQYPHEFSGGMRQRALIAMGLAAHPKLLI 192
Cdd:PRK11629 95 --FHHLLPDFTALENVAMPLLIGKKKP-AEINSRALEMLAAVGL---EHRANHRPSELSGGERQRVAIARALVNNPRLVL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2524658687 193 ADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLaAERADRLVVMQAGRV 248
Cdd:PRK11629 169 ADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQL-AKRMSRQLEMRDGRL 223
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
38-270 |
1.05e-34 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 131.41 E-value: 1.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETVAIVGESGSGKsTTAHAALGLL--PGDGEVTGGTITFDGRDITHLTDREFVSIRGNgIGLVPQDpm 115
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGK-TTLLRCINLLeqPEAGTIRVGDITIDTARSLSQQKGLIRQLRQH-VGFVFQN-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 116 TNLNPVWTVGSQIKEALRANNIATGSEAHKKAIELLEQAGLPNAKkriDQYPHEFSGGMRQRALIAMGLAAHPKLLIADE 195
Cdd:PRK11264 94 FNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKE---TSYPRRLSGGQQQRVAIARALAMRPEVILFDE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2524658687 196 PTSALDVTVAKKILDHLDKLTSELGTsVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVLTRPQHPYTKQLI 270
Cdd:PRK11264 171 PTSALDPELVGEVLNTIRQLAQEKRT-MVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQFL 244
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
324-537 |
1.05e-34 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 131.32 E-value: 1.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 324 VDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEeleLRRRIQPIFQNPYATlDPM-- 401
Cdd:COG1120 17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRE---LARRIAYVPQEPPAP-FGLtv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 402 -------RTVHSSIEEPLRihkigtkKEREQRVFELLDRVALpAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEA 474
Cdd:COG1120 93 relvalgRYPHLGLFGRPS-------AEDREAVEEALERTGL-EHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2524658687 475 VSALDVVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDLFD 537
Cdd:COG1120 165 TSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLT 227
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-252 |
1.14e-34 |
|
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: 137.97 E-value: 1.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 2 STDTNTSAAPILTLKDVCIGFPTTTAsgrrsksltdVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPgdgeVTG 81
Cdd:COG4988 326 TAPLPAAGPPSIELEDVSFSYPGGRP----------ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLP----PYS 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 82 GTITFDGRDITHLTDRefvSIRGNgIGLVPQdpmtnlNPVWTVGSqIKEALR-ANNIATGSEAHkkaiELLEQAGLpnaK 160
Cdd:COG4988 392 GSILINGVDLSDLDPA---SWRRQ-IAWVPQ------NPYLFAGT-IRENLRlGRPDASDEELE----AALEAAGL---D 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 161 KRIDQYPHEF-----------SGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSelGTSVVLITHD 229
Cdd:COG4988 454 EFVAALPDGLdtplgeggrglSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHR 531
|
250 260
....*....|....*....|...
gi 2524658687 230 LGLAAeRADRLVVMQAGRVVETG 252
Cdd:COG4988 532 LALLA-QADRILVLDDGRIVEQG 553
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
38-260 |
1.27e-34 |
|
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: 130.75 E-value: 1.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGDGevtgGTITFDGRDITHLTDRefvsIRGNgIGLVPQDPmtN 117
Cdd:COG4555 16 ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDS----GSILIDGEDVRKEPRE----ARRQ-IGVLPDER--G 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 118 LNPVWTVGSQIKEALRANNIaTGSEAHKKAIELLEQAGLPN-AKKRIdqypHEFSGGMRQRALIAMGLAAHPKLLIADEP 196
Cdd:COG4555 85 LYDRLTVRENIRYFAELYGL-FDEELKKRIEELIELLGLEEfLDRRV----GELSTGMKKKVALARALVHDPKVLLLDEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2524658687 197 TSALDVTVAKKILDHLDKLTSElGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVLTR 260
Cdd:COG4555 160 TNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREE 222
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
41-261 |
1.37e-34 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 133.69 E-value: 1.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 41 DVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGDGevtgGTITFDGRDITHLTDREFVSIRGNGIGLVPQDPmtNLNP 120
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDS----GRIRLGGEVLQDSARGIFLPPHRRRIGYVFQEA--RLFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 121 VWTVGSQIKEALRANNIATGSEAHKKAIELLEQAGLpnakkrIDQYPHEFSGGMRQRALIAMGLAAHPKLLIADEPTSAL 200
Cdd:COG4148 91 HLSVRGNLLYGRKRAPRAERRISFDEVVELLGIGHL------LDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAAL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2524658687 201 DVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVLTRP 261
Cdd:COG4148 165 DLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
38-257 |
1.53e-34 |
|
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: 129.99 E-value: 1.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGDGEV-TGGTITFDGRDITHLtDREFVSIRGNgIGLVPQDPmt 116
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGApDEGEVLLDGKDIYDL-DVDVLELRRR-VGMVFQKP-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 117 nlNPVW-TVGSQIKEALRANNIATGSEAHKKAIELLEQAGLPNAKKRiDQYPHEFSGGMRQRALIAMGLAAHPKLLIADE 195
Cdd:cd03260 91 --NPFPgSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKD-RLHALGLSGGQQQRLCLARALANEPEVLLLDE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2524658687 196 PTSALDVTVAKKILDHLDKLTSElgTSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQV 257
Cdd:cd03260 168 PTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
34-479 |
1.54e-34 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 139.10 E-value: 1.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 34 SLTDVVH---------DVNLEVFPGETVAIVGESGSGKSTTahaaLGLLPGDGEVTGGTITFDGRDITHLTDREFVSIRg 104
Cdd:NF033858 3 RLEGVSHrygktvaldDVSLDIPAGCMVGLIGPDGVGKSSL----LSLIAGARKIQQGRVEVLGGDMADARHRRAVCPR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 105 ngIGLVPQDPMTNLNPVWTVgsqikealrANNIA--------TGSEAHKKAIELLEQAGL------PNAKkridqypheF 170
Cdd:NF033858 78 --IAYMPQGLGKNLYPTLSV---------FENLDffgrlfgqDAAERRRRIDELLRATGLapfadrPAGK---------L 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 171 SGGMRQR-----ALIamglaaH-PKLLIADEPTSALDVTVAKKILDHLDKLTSEL-GTSVVLIThdlglA----AERADR 239
Cdd:NF033858 138 SGGMKQKlglccALI------HdPDLLILDEPTTGVDPLSRRQFWELIDRIRAERpGMSVLVAT-----AymeeAERFDW 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 240 LVVMQAGRVVETGPALQVLTRPQhpyTKQLIAAAPSL---AARRGDR-VVAAPTTSDADQKEILVAKNLVRDFairGDrp 315
Cdd:NF033858 207 LVAMDAGRVLATGTPAELLARTG---ADTLEAAFIALlpeEKRRGHQpVVIPPRPADDDDEPAIEARGLTMRF---GD-- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 316 wrkdsFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNrkeeLELRRRIQPIFQ--N 393
Cdd:NF033858 279 -----FTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGD----IATRRRVGYMSQafS 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 394 PYATLdpmrTVHSSIEEPLRIHKIGtKKEREQRVFELLDRVALPAEMGRRfPGELSGGQRQRVAIARALALNPEVVVCDE 473
Cdd:NF033858 350 LYGEL----TVRQNLELHARLFHLP-AAEIAARVAEMLERFDLADVADAL-PDSLPLGIRQRLSLAVAVIHKPELLILDE 423
|
....*.
gi 2524658687 474 AVSALD 479
Cdd:NF033858 424 PTSGVD 429
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
320-542 |
1.75e-34 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 130.52 E-value: 1.75e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 320 SFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMaLGLLD-PTEGEV-----LFDGKrvQGRNRKEELELRRRIQPIFQN 393
Cdd:PRK11124 14 AHQALFDITLDCPQGETLVLLGPSGAGKSSLLRV-LNLLEmPRSGTLniagnHFDFS--KTPSDKAIRELRRNVGMVFQQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 394 pYaTLDPMRTV-HSSIEEPLRIHKIgTKKEREQRVFELLDRVALpAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCD 472
Cdd:PRK11124 91 -Y-NLWPHLTVqQNLIEAPCRVLGL-SKDQALARAEKLLERLRL-KPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFD 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 473 EAVSALDVVVQAQVlELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHrPTDDLFDHPEKE 542
Cdd:PRK11124 167 EPTAALDPEITAQI-VSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQ-GDASCFTQPQTE 234
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
38-262 |
1.81e-34 |
|
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: 130.05 E-value: 1.81e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETVAIVGESGSGKSTTahaaLGLLPGDGEVTGGTITFDGRDITHLTDREfvsirgNGIGLVPQDpmTN 117
Cdd:cd03300 15 ALDGVSLDIKEGEFFTLLGPSGCGKTTL----LRLIAGFETPTSGEILLDGKDITNLPPHK------RPVNTVFQN--YA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 118 LNPVWTVGSQIKEALRANNIaTGSEAHKKAIELLEQAGLPNAKKRidqYPHEFSGGMRQRALIAMGLAAHPKLLIADEPT 197
Cdd:cd03300 83 LFPHLTVFENIAFGLRLKKL-PKAEIKERVAEALDLVQLEGYANR---KPSQLSGGQQQRVAIARALVNEPKVLLLDEPL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2524658687 198 SALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVLTRPQ 262
Cdd:cd03300 159 GALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
317-528 |
3.08e-34 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 128.91 E-value: 3.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 317 RKDSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEelelrRRIQPIFQNpYA 396
Cdd:cd03301 9 RFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD-----RDIAMVFQN-YA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 397 tLDPMRTVHSSIEEPLRIHKIGtKKEREQRVFELLDRVALPAEMGRRfPGELSGGQRQRVAIARALALNPEVVVCDEAVS 476
Cdd:cd03301 83 -LYPHMTVYDNIAFGLKLRKVP-KDEIDERVREVAELLQIEHLLDRK-PKQLSGGQRQRVALGRAIVREPKVFLMDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2524658687 477 ALDVVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVE 528
Cdd:cd03301 160 NLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQ 211
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
325-549 |
3.41e-34 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 129.44 E-value: 3.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 325 DDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEElELRRRIQPIFQNPYatLDPMRTV 404
Cdd:PRK09493 18 HNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDER-LIRQEAGMVFQQFY--LFPHLTA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 405 HSSIE-EPLRIHKIGtKKEREQRVFELLDRVALpAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVSALDVVVQ 483
Cdd:PRK09493 95 LENVMfGPLRVRGAS-KEEAEKQARELLAKVGL-AERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELR 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2524658687 484 AQVLELLAelqeemDLA-----YLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDLFDHPEkeyTQRLLD 549
Cdd:PRK09493 173 HEVLKVMQ------DLAeegmtMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPP---SQRLQE 234
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
299-526 |
4.92e-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: 4.92e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 299 LVAKNLVRDFairgdrpwrkDSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVqgrnRK 378
Cdd:cd03230 1 IEVRNLSKRY----------GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDI----KK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 379 EELELRRRIQPIFQNP--YATLdpmrtvhssieeplrihkigtkkereqRVFELLDrvalpaemgrrfpgeLSGGQRQRV 456
Cdd:cd03230 67 EPEEVKRRIGYLPEEPslYENL---------------------------TVRENLK---------------LSGGMKQRL 104
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 457 AIARALALNPEVVVCDEAVSALDVVVQAQVLELLAELQEEmDLAYLFITHDLAVVRQVADEVIVMEHGKM 526
Cdd:cd03230 105 ALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
316-527 |
5.27e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 130.11 E-value: 5.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 316 WRKDSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEeleLRRRIQPIFQNPy 395
Cdd:PRK13632 17 YPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKE---IRKKIGIIFQNP- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 396 atlDPM---RTVHSSIEEPLRIHKIgTKKEREQRVFELLDRVALpAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCD 472
Cdd:PRK13632 93 ---DNQfigATVEDDIAFGLENKKV-PPKKMKDIIDDLAKKVGM-EDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2524658687 473 EAVSALDVVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQvADEVIVMEHGKMV 527
Cdd:PRK13632 168 ESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFSEGKLI 221
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
323-541 |
5.68e-34 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 130.14 E-value: 5.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 323 AVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVlfdgkRVQGRNRKEEL--ELRRRIQPIFQNPyatlDP 400
Cdd:PRK13635 22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTI-----TVGGMVLSEETvwDVRRQVGMVFQNP----DN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 401 M---RTVHSSIEEPLRIHKIgtkkEREQ---RVFELLDRVALPAEMGRRfPGELSGGQRQRVAIARALALNPEVVVCDEA 474
Cdd:PRK13635 93 QfvgATVQDDVAFGLENIGV----PREEmveRVDQALRQVGMEDFLNRE-PHRLSGGQKQRVAIAGVLALQPDIIILDEA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2524658687 475 VSALDVVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQvADEVIVMEHGKMVEHRPTDDLFDHPEK 541
Cdd:PRK13635 168 TSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFKSGHM 233
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
321-540 |
9.09e-34 |
|
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: 128.32 E-value: 9.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 321 FRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGrnRKEELELRRRIQPIFQNP--YATL 398
Cdd:cd03219 13 LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITG--LPPHEIARLGIGRTFQIPrlFPEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 399 dpmrTV---------HSSIEEPLRIHKIGTKKEREQRVFELLDRVALPAEMGRRfPGELSGGQRQRVAIARALALNPEVV 469
Cdd:cd03219 91 ----TVlenvmvaaqARTGSGLLLARARREEREARERAEELLERVGLADLADRP-AGELSYGQQRRLEIARALATDPKLL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2524658687 470 VCDEAVSALDvVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDLFDHPE 540
Cdd:cd03219 166 LLDEPAAGLN-PEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
317-525 |
1.17e-33 |
|
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: 125.43 E-value: 1.17e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 317 RKDSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVqgrNRKEELELRRRIQPIFQnpya 396
Cdd:cd00267 8 RYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDI---AKLPLEELRRRIGYVPQ---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 397 tldpmrtvhssieeplrihkigtkkereqrvfelldrvalpaemgrrfpgeLSGGQRQRVAIARALALNPEVVVCDEAVS 476
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2524658687 477 ALDVVVQAQVLELLAELQEEmDLAYLFITHDLAVVRQVADEVIVMEHGK 525
Cdd:cd00267 110 GLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
38-261 |
1.29e-33 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 128.31 E-value: 1.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETVAIVGESGSGKSTTahaaLGLLPGDGEVTGGTITFDGRDITHLTDREFVSIRGngigLVPQDpmTN 117
Cdd:COG4559 16 LLDDVSLTLRPGELTAIIGPNGAGKSTL----LKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRA----VLPQH--SS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 118 LNPVWTVgSQIKEALRANNIATGSEAHKKAIELLEQAGLPNAKKRidQYPhEFSGGMRQRALIAMGLA-------AHPKL 190
Cdd:COG4559 86 LAFPFTV-EEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGR--SYQ-TLSGGEQQRVQLARVLAqlwepvdGGPRW 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2524658687 191 LIADEPTSALDVTVAKKILDHLDKLTSElGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVLTRP 261
Cdd:COG4559 162 LFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDE 231
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
41-528 |
3.51e-33 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 132.99 E-value: 3.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 41 DVNLEVFPGETVAIVGESGSGKSTTahaaLGLLPGDGEVTGGTITFDGRDITHLTDREFVSirgNGIGLVPQ-----DPM 115
Cdd:PRK09700 23 SVNLTVYPGEIHALLGENGAGKSTL----MKVLSGIHEPTKGTITINNINYNKLDHKLAAQ---LGIGIIYQelsviDEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 116 TNLNPVWtVGSQIKEALRANNIATGSEAHKKAIELLEQAGLpnaKKRIDQYPHEFSGGMRQRALIAMGLAAHPKLLIADE 195
Cdd:PRK09700 96 TVLENLY-IGRHLTKKVCGVNIIDWREMRVRAAMMLLRVGL---KVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 196 PTSALDVTVAKKILDHLDKLTSElGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVltrpqhpYTKQLIaaapS 275
Cdd:PRK09700 172 PTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV-------SNDDIV----R 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 276 LAARR--GDRVVA-APTTSDADQKEILVAKNLVrdfairgdrpwRKDsFRAVDDISFTLRRGRTIGIVGESGSGKSTVAN 352
Cdd:PRK09700 240 LMVGRelQNRFNAmKENVSNLAHETVFEVRNVT-----------SRD-RKKVRDISFSVCRGEILGFAGLVGSGRTELMN 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 353 MALGLLDPTEGEVLFDGKRVQGRNRKEELEL-------RRRIQPIFQNpyatLDPMRTVhsSIEEPLRIHKIG------T 419
Cdd:PRK09700 308 CLFGVDKRAGGEIRLNGKDISPRSPLDAVKKgmayiteSRRDNGFFPN----FSIAQNM--AISRSLKDGGYKgamglfH 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 420 KKEREQRVFELLDRVALPAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVSALDVVVQAQVLELLAELQEEmDL 499
Cdd:PRK09700 382 EVDEQRTAENQRELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GK 460
|
490 500
....*....|....*....|....*....
gi 2524658687 500 AYLFITHDLAVVRQVADEVIVMEHGKMVE 528
Cdd:PRK09700 461 VILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
38-247 |
3.97e-33 |
|
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: 123.89 E-value: 3.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPgdgeVTGGTITFDGRDITHLTDREfvsiRGNGIGLVPQdpmtn 117
Cdd:cd00267 14 ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLK----PTSGEILIDGKDIAKLPLEE----LRRRIGYVPQ----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 118 lnpvwtvgsqikealranniatgseahkkaielleqaglpnakkridqypheFSGGMRQRALIAMGLAAHPKLLIADEPT 197
Cdd:cd00267 81 ----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPT 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2524658687 198 SALDVTVAKKILDHLDKLTSElGTSVVLITHDLGLAAERADRLVVMQAGR 247
Cdd:cd00267 109 SGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
299-535 |
4.12e-33 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 125.95 E-value: 4.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 299 LVAKNLVRDFairgdrpwrkDSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVqgrnRK 378
Cdd:cd03265 1 IEVENLVKKY----------GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDV----VR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 379 EELELRRRIQPIFQnpYATLDPMRTVHSSIEEPLRIHKIGtKKEREQRVFELLDRVALpAEMGRRFPGELSGGQRQRVAI 458
Cdd:cd03265 67 EPREVRRRIGIVFQ--DLSVDDELTGWENLYIHARLYGVP-GAERRERIDELLDFVGL-LEAADRLVKTYSGGMRRRLEI 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2524658687 459 ARALALNPEVVVCDEAVSALDVVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDL 535
Cdd:cd03265 143 ARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
339-551 |
4.54e-33 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 128.77 E-value: 4.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 339 IVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQgrNRKEElelRRRIQPIFQNpYAtLDPMRTVHSSIEEPLRIHKIG 418
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVT--NVPPH---LRHINMVFQS-YA-LFPHMTVEENVAFGLKMRKVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 419 tKKEREQRVFELLDRVALpAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVSALDVVVQAQVLELLAELQEEMD 498
Cdd:TIGR01187 74 -RAEIKPRVLEALRLVQL-EEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLG 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2524658687 499 LAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDLFDHPEKEYTQRLLDAI 551
Cdd:TIGR01187 152 ITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEI 204
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
38-262 |
6.19e-33 |
|
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: 126.01 E-value: 6.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPgdgeVTGGTITFDGRDITHLTDREfvsIRGNGIGLVPQDP--- 114
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLR----PTSGSVLFDGEDITGLPPHE---IARLGIGRTFQIPrlf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 115 --MTNLNPVwTVGSQIKE---ALRANNIATGSEAHKKAIELLEQAGLPNakkRIDQYPHEFSGGMRQRALIAMGLAAHPK 189
Cdd:cd03219 88 peLTVLENV-MVAAQARTgsgLLLARARREEREARERAEELLERVGLAD---LADRPAGELSYGQQRRLEIARALATDPK 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2524658687 190 LLIADEPTSALDVTVAKKILDHLDKLtSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVLTRPQ 262
Cdd:cd03219 164 LLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
38-259 |
6.54e-33 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 126.42 E-value: 6.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETVAIVGESGSGKSTTahaaLGLLPGDGEVTGGTITFDGRDITHLTDREFVSIRGngigLVPQDpmTN 117
Cdd:PRK13548 17 LLDDVSLTLRPGEVVAILGPNGAGKSTL----LRALSGELSPDSGEVRLNGRPLADWSPAELARRRA----VLPQH--SS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 118 LNPVWTVgSQIKEALRANNiaTGSEAHKKAI--ELLEQAGLPNAKKRidQYPhEFSGGMRQRALIAMGLA------AHPK 189
Cdd:PRK13548 87 LSFPFTV-EEVVAMGRAPH--GLSRAEDDALvaAALAQVDLAHLAGR--DYP-QLSGGEQQRVQLARVLAqlwepdGPPR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 190 LLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVLT 259
Cdd:PRK13548 161 WLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLT 230
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
327-548 |
8.69e-33 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 125.25 E-value: 8.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 327 ISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEelelrRRIQPIFQ--NPYATLDPMRTV 404
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE-----RPVSMLFQenNLFPHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 405 HSSIEEPLRIhkigTKKEReQRVFELLDRVALpAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVSALDVVVQA 484
Cdd:COG3840 93 GLGLRPGLKL----TAEQR-AQVEQALERVGL-AGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQ 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2524658687 485 QVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDLFDHPEKEYTQRLL 548
Cdd:COG3840 167 EMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYL 230
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
326-551 |
1.18e-32 |
|
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: 125.71 E-value: 1.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 326 DISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRN--RKEELELRRRIQP----IFQNPYATLD 399
Cdd:TIGR02323 21 DVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELElyQLSEAERRRLMRTewgfVHQNPRDGLR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 400 PMRTVHSSIEEplRIHKIGTK---KEREQRVfELLDRVALPAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVS 476
Cdd:TIGR02323 101 MRVSAGANIGE--RLMAIGARhygNIRATAQ-DWLEEVEIDPTRIDDLPRAFSGGMQQRLQIARNLVTRPRLVFMDEPTG 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2524658687 477 ALDVVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDLFDHPEKEYTQRLLDAI 551
Cdd:TIGR02323 178 GLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDPQHPYTQLLVSSI 252
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
327-549 |
1.36e-32 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 125.63 E-value: 1.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 327 ISFTLRRGRTIGIVGESGSGKSTVANmALGLLDPTE------GEVLFDGKRVQGRNRKEELELRRRIQPIFQNpyATLDP 400
Cdd:PRK11264 22 IDLEVKPGEVVAIIGPSGSGKTTLLR-CINLLEQPEagtirvGDITIDTARSLSQQKGLIRQLRQHVGFVFQN--FNLFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 401 MRTVHSSIEEPLRIHKIGTKKEREQRVFELLDRVALpAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVSALDV 480
Cdd:PRK11264 99 HRTVLENIIEGPVIVKGEPKEEATARARELLAKVGL-AGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDP 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2524658687 481 VVQAQVLELLAELQEEmDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDLFDHPEKEYTQRLLD 549
Cdd:PRK11264 178 ELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQFLE 245
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
36-270 |
1.53e-32 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 127.88 E-value: 1.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 36 TDVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLpgdgEVTGGTITFDGRDITHLT--DRefvsirgnGIGLVPQD 113
Cdd:COG3839 16 VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLE----DPTSGEILIGGRDVTDLPpkDR--------NIAMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 114 P-----MTnlnpvwtVgsqikealrANNIATGseahkkaielLEQAGLPNA--KKRI-------------DQYPHEFSGG 173
Cdd:COG3839 84 YalyphMT-------V---------YENIAFP----------LKLRKVPKAeiDRRVreaaellgledllDRKPKQLSGG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 174 MRQRalIAMG--LAAHPKLLIADEPTSALDvtvAK---KILDHLDKLTSELGTSVVLITHD----LGLaaerADRLVVMQ 244
Cdd:COG3839 138 QRQR--VALGraLVREPKVFLLDEPLSNLD---AKlrvEMRAEIKRLHRRLGTTTIYVTHDqveaMTL----ADRIAVMN 208
|
250 260
....*....|....*....|....*.
gi 2524658687 245 AGRVVETGPALQVLTRPQHPYTKQLI 270
Cdd:COG3839 209 DGRIQQVGTPEELYDRPANLFVAGFI 234
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
293-540 |
1.81e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 125.63 E-value: 1.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 293 ADQKEILVAKNLvrDFAIRGDRPWrkdsfrAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRV 372
Cdd:PRK13648 2 EDKNSIIVFKNV--SFQYQSDASF------TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 373 QGRNRKEeleLRRRIQPIFQNPYATLdPMRTVHSSIEEPLRIHKIGTKKEREqRVFELLDRVALPAEMGRRfPGELSGGQ 452
Cdd:PRK13648 74 TDDNFEK---LRKHIGIVFQNPDNQF-VGSIVKYDVAFGLENHAVPYDEMHR-RVSEALKQVDMLERADYE-PNALSGGQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 453 RQRVAIARALALNPEVVVCDEAVSALDVVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQvADEVIVMEHGKMVEHRPT 532
Cdd:PRK13648 148 KQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTP 226
|
....*...
gi 2524658687 533 DDLFDHPE 540
Cdd:PRK13648 227 TEIFDHAE 234
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
277-535 |
1.99e-32 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 131.43 E-value: 1.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 277 AARR-------GDRVVAAPTTSDADQKEILVAKNLVrdFAIRGDRPWrkdsfrAVDDISFTLRRGRTIGIVGESGSGKST 349
Cdd:COG4987 305 AARRlnelldaPPAVTEPAEPAPAPGGPSLELEDVS--FRYPGAGRP------VLDGLSLTLPPGERVAIVGPSGSGKST 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 350 VANMALGLLDPTEGEVLFDGKRVQGRNRKeelELRRRIQPIFQNPYAtldpmrtVHSSIEEPLRIHKIGTKkerEQRVFE 429
Cdd:COG4987 377 LLALLLRFLDPQSGSITLGGVDLRDLDED---DLRRRIAVVPQRPHL-------FDTTLRENLRLARPDAT---DEELWA 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 430 LLDRV-------ALPA-------EMGRRfpgeLSGGQRQRVAIARALALNPEVVVCDEAVSALDVVVQAQVLELLAELQE 495
Cdd:COG4987 444 ALERVglgdwlaALPDgldtwlgEGGRR----LSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA 519
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2524658687 496 emDLAYLFITHDLAVVRQvADEVIVMEHGKMVEHRPTDDL 535
Cdd:COG4987 520 --GRTVLLITHRLAGLER-MDRILVLEDGRIVEQGTHEEL 556
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
5-535 |
2.56e-32 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 130.17 E-value: 2.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 5 TNTSAAPILTLKDVCigfptttasgrRSKSLTDVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGDgevtGGTI 84
Cdd:PRK15439 4 SDTTAPPLLCARSIS-----------KQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPD----SGTL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 85 TFDGRDITHLTDrefVSIRGNGIGLVPQDPMtnLNPVWTVgsqiKEalranNIATGSEAHKKAIELLEQAgLPNAKKRID 164
Cdd:PRK15439 69 EIGGNPCARLTP---AKAHQLGIYLVPQEPL--LFPNLSV----KE-----NILFGLPKRQASMQKMKQL-LAALGCQLD 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 165 qyPHEFSGGM----RQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSElGTSVVLITHDLGLAAERADRL 240
Cdd:PRK15439 134 --LDSSAGSLevadRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQ-GVGIVFISHKLPEIRQLADRI 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 241 VVMQAGRVVETGPAlqvltrpqHPYTKQLIAAAPSLAARRGDrvvaapttSDADQKEILVAKNL----VRDFAIRGDRPW 316
Cdd:PRK15439 211 SVMRDGTIALSGKT--------ADLSTDDIIQAITPAAREKS--------LSASQKLWLELPGNrrqqAAGAPVLTVEDL 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 317 RKDSFRavdDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEELEL-------RRRIQP 389
Cdd:PRK15439 275 TGEGFR---NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARglvylpeDRQSSG 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 390 IFqnpyatLD-PMRTVHSSieepLRIHKIG--TKKEREQRVFELLDRValpaeMGRRFPGE------LSGGQRQRVAIAR 460
Cdd:PRK15439 352 LY------LDaPLAWNVCA----LTHNRRGfwIKPARENAVLERYRRA-----LNIKFNHAeqaartLSGGNQQKVLIAK 416
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2524658687 461 ALALNPEVVVCDEAVSALDVVVQAQVLELLAELQEEmDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDL 535
Cdd:PRK15439 417 CLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAI 490
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
323-521 |
2.78e-32 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 124.97 E-value: 2.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 323 AVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGrnrkeelelrrriqP------IFQNpyA 396
Cdd:COG4525 22 ALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG--------------PgadrgvVFQK--D 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 397 TLDPMRTVHSSIEEPLRIHKIGtKKEREQRVFELLDRVALpAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVS 476
Cdd:COG4525 86 ALLPWLNVLDNVAFGLRLRGVP-KAERRARAEELLALVGL-ADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFG 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2524658687 477 ALDVVVQAQVLELLAELQEEMDLAYLFITHDL--AVVrqVADEVIVM 521
Cdd:COG4525 164 ALDALTREQMQELLLDVWQRTGKGVFLITHSVeeALF--LATRLVVM 208
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
38-247 |
2.82e-32 |
|
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: 123.70 E-value: 2.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETVAIVGESGSGKSTTahaaLGLLPGDGEVTGGTITFDGR----DITHLTDREFVSIRGNGIGLVPQd 113
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTL----LKCIYGNYLPDSGSILVRHDggwvDLAQASPREILALRRRTIGYVSQ- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 114 pmtNLNPVWTVGSQ--IKEALRANNIATgSEAHKKAIELLEQAGLPnaKKRIDQYPHEFSGGMRQRALIAMGLAAHPKLL 191
Cdd:COG4778 101 ---FLRVIPRVSALdvVAEPLLERGVDR-EEARARARELLARLNLP--ERLWDLPPATFSGGEQQRVNIARGFIADPPLL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2524658687 192 IADEPTSALDVTVAKKILDHLDKLTSElGTSVVLITHDLGLAAERADRLVVMQAGR 247
Cdd:COG4778 175 LLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
42-250 |
6.85e-32 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 122.97 E-value: 6.85e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 42 VNLEVFPGETVAIVGESGSGKSTTahaaLGLLPGDGEVTGGTITFDGRDITHLTDREFVSIRGNGIGLVPQDPM--TNLN 119
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTL----LAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAKHVGFVFQSFMliPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 120 PVWTVgsQIKEALRANNiatGSEAHKKAIELLEQAGLpnaKKRIDQYPHEFSGGMRQRALIAMGLAAHPKLLIADEPTSA 199
Cdd:PRK10584 105 ALENV--ELPALLRGES---SRQSRNGAKALLEQLGL---GKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGN 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2524658687 200 LDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAeRADRLVVMQAGRVVE 250
Cdd:PRK10584 177 LDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAA-RCDRRLRLVNGQLQE 226
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
39-252 |
6.94e-32 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 122.48 E-value: 6.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 39 VHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPgdgeVTGGTITFDGRDIThltdREFVSIRGNgIGLVPQDPmtNL 118
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLK----PTSGRATVAGHDVV----REPREVRRR-IGIVFQDL--SV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 119 NPVWTVGSQIKEALRANNIAtGSEAHKKAIELLEQAGLPNAKKRIDQYpheFSGGMRQRALIAMGLAAHPKLLIADEPTS 198
Cdd:cd03265 85 DDELTGWENLYIHARLYGVP-GAERRERIDELLDFVGLLEAADRLVKT---YSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2524658687 199 ALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETG 252
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEG 214
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
307-537 |
7.07e-32 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 123.11 E-value: 7.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 307 DFAIRGDRPWrkdsfrAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEeleLRRR 386
Cdd:cd03251 7 TFRYPGDGPP------VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLAS---LRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 387 IQPIFQNPYATLDpmrTVHSSIeeplrihKIGTKKEREQRVFELLdRVALPAEMGRRFP-------GE----LSGGQRQR 455
Cdd:cd03251 78 IGLVSQDVFLFND---TVAENI-------AYGRPGATREEVEEAA-RAANAHEFIMELPegydtviGErgvkLSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 456 VAIARALALNPEVVVCDEAVSALDVVVQAQVLELLAELQEemDLAYLFITHDLAVVRQvADEVIVMEHGKMVEHRPTDDL 535
Cdd:cd03251 147 IAIARALLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEEL 223
|
..
gi 2524658687 536 FD 537
Cdd:cd03251 224 LA 225
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
325-535 |
8.42e-32 |
|
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: 122.65 E-value: 8.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 325 DDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEeleLRRRIQPIFQNP--YATldpmr 402
Cdd:cd03249 20 KGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRW---LRSQIGLVSQEPvlFDG----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 403 tvhsSIEEPLRIHKI-GTKKEREQ--RVFELLDRVA-LP----AEMGRRfPGELSGGQRQRVAIARALALNPEVVVCDEA 474
Cdd:cd03249 92 ----TIAENIRYGKPdATDEEVEEaaKKANIHDFIMsLPdgydTLVGER-GSQLSGGQKQRIAIARALLRNPKILLLDEA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2524658687 475 VSALDVVVQAQVleLLAELQEEMDLAYLFITHDLAVVRQvADEVIVMEHGKMVEHRPTDDL 535
Cdd:cd03249 167 TSALDAESEKLV--QEALDRAMKGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDEL 224
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
322-527 |
1.25e-31 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 120.62 E-value: 1.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 322 RAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEeleLRRRIQPIFQnpyatldpm 401
Cdd:cd03214 13 TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKE---LARKIAYVPQ--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 402 rtvhssieeplrihkigtkkereqrvfeLLDRVALpAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVSALDVV 481
Cdd:cd03214 81 ----------------------------ALELLGL-AHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIA 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2524658687 482 VQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMV 527
Cdd:cd03214 132 HQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
322-540 |
2.47e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 123.02 E-value: 2.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 322 RAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEEL-ELRRRIQPIFQNPYATLDP 400
Cdd:PRK13641 21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLkKLRKKVSLVFQFPEAQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 401 mRTVHSSIE-EPLRIHkiGTKKEREQRVFELLDRVALPAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVSALD 479
Cdd:PRK13641 101 -NTVLKDVEfGPKNFG--FSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 480 VVVQAQVlellaelqeeMDL---------AYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDLFDHPE 540
Cdd:PRK13641 178 PEGRKEM----------MQLfkdyqkaghTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
36-268 |
2.62e-31 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 121.66 E-value: 2.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 36 TDVVHDVNLEVFPGETVAIVGESGSGKSTTAHAaLGLL--PGDGEVTGGTITFDGRdiTHLTDREFVSIRGNgIGLVPQD 113
Cdd:COG4161 15 HQALFDINLECPSGETLVLLGPSGAGKSSLLRV-LNLLetPDSGQLNIAGHQFDFS--QKPSEKAIRLLRQK-VGMVFQQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 114 pmTNLNPVWTVGSQIKEA-LRANNIATgSEAHKKAIELLEQAGLPNakkRIDQYPHEFSGGMRQRALIAMGLAAHPKLLI 192
Cdd:COG4161 91 --YNLWPHLTVMENLIEApCKVLGLSK-EQAREKAMKLLARLRLTD---KADRFPLHLSGGQQQRVAIARALMMEPQVLL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2524658687 193 ADEPTSALDVTVAKKILDHLDKLtSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPAlqvlTRPQHPYTKQ 268
Cdd:COG4161 165 FDEPTAALDPEITAQVVEIIREL-SQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDA----SHFTQPQTEA 235
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
39-257 |
4.96e-31 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 122.05 E-value: 4.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 39 VHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGDGevtgGTITFDGRDithLTDREFVSIRGNgIGLVPQDPMTNL 118
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEA----GTITVGGMV---LSEETVWDVRRQ-VGMVFQNPDNQF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 119 npvwtVGSQIkealrANNIATGSE----AHKKAIELLEQA-GLPNAKKRIDQYPHEFSGGMRQRALIAMGLAAHPKLLIA 193
Cdd:PRK13635 95 -----VGATV-----QDDVAFGLEnigvPREEMVERVDQAlRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2524658687 194 DEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAeRADRLVVMQAGRVVETGPALQV 257
Cdd:PRK13635 165 DEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAA-QADRVIVMNKGEILEEGTPEEI 227
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
322-556 |
9.62e-31 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 122.60 E-value: 9.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 322 RAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGlldptegeVLFDGKRVQG-RNRKEELEL-------RRR-----IQ 388
Cdd:PRK15093 21 KAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICG--------VTKDNWRVTAdRMRFDDIDLlrlspreRRKlvghnVS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 389 PIFQNPYATLDPMRTVHSSIEEPL-----------RIHkigtkkEREQRVFELLDRVAL--PAEMGRRFPGELSGGQRQR 455
Cdd:PRK15093 93 MIFQEPQSCLDPSERVGRQLMQNIpgwtykgrwwqRFG------WRKRRAIELLHRVGIkdHKDAMRSFPYELTEGECQK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 456 VAIARALALNPEVVVCDEAVSALDVVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDL 535
Cdd:PRK15093 167 VMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKEL 246
|
250 260
....*....|....*....|...
gi 2524658687 536 FDHPEKEYTQRLLDAIP--GASL 556
Cdd:PRK15093 247 VTTPHHPYTQALIRAIPdfGSAM 269
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
39-526 |
9.71e-31 |
|
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: 125.71 E-value: 9.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 39 VHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLP-GDGEvtgGTITFDGRDI--THLTDREfvsirGNGIGLVPQDPM 115
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhGTWD---GEIYWSGSPLkaSNIRDTE-----RAGIVIIHQELT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 116 tnLNPVWTVGSQI---KEALRANNIATGSEAHKKAIELLEQAGLP--NAKKRIDQYphefSGGMRQRALIAMGLAAHPKL 190
Cdd:TIGR02633 89 --LVPELSVAENIflgNEITLPGGRMAYNAMYLRAKNLLRELQLDadNVTRPVGDY----GGGQQQLVEIAKALNKQARL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 191 LIADEPTSALDVTVAKKILDHLDKLTSElGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPAlQVLTRPQ---HPYTK 267
Cdd:TIGR02633 163 LILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQHVATKDM-STMSEDDiitMMVGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 268 QLIAAAPSLAARRGDrvvaapttsdadqkEILVAKNLVrdfAIRGDRPWRKdsfrAVDDISFTLRRGRTIGIVGESGSGK 347
Cdd:TIGR02633 241 EITSLYPHEPHEIGD--------------VILEARNLT---CWDVINPHRK----RVDDVSFSLRRGEILGVAGLVGAGR 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 348 STVANMALGLLDPT-EGEVLFDGKRVQGRNRKEELELRRRIQPIFQNPYATLDPMRTVH----SSIEEPLRIHKIGTKKE 422
Cdd:TIGR02633 300 TELVQALFGAYPGKfEGNVFINGKPVDIRNPAQAIRAGIAMVPEDRKRHGIVPILGVGKnitlSVLKSFCFKMRIDAAAE 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 423 rEQRVFELLDRVALPAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVSALDVVVQAQVLELLAELQEEmDLAYL 502
Cdd:TIGR02633 380 -LQIIGSAIQRLKVKTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAII 457
|
490 500
....*....|....*....|....
gi 2524658687 503 FITHDLAVVRQVADEVIVMEHGKM 526
Cdd:TIGR02633 458 VVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
326-540 |
1.56e-30 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 122.50 E-value: 1.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 326 DISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEelelrRRIQPIFQNpYATLDPMrTVH 405
Cdd:PRK10851 20 DISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD-----RKVGFVFQH-YALFRHM-TVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 406 SSIEEPLRI---HKIGTKKEREQRVFELLDRVALpAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVSALDVVV 482
Cdd:PRK10851 93 DNIAFGLTVlprRERPNAAAIKAKVTQLLEMVQL-AHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQV 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2524658687 483 QAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDLFDHPE 540
Cdd:PRK10851 172 RKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPA 229
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
38-252 |
1.62e-30 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 119.18 E-value: 1.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETVAIVGESGSGKSTTahaaLGLLPGDGEVTGGTITFDGRDITHLTDREFVSIrgngIGLVPQDPMTN 117
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTV----VSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQ----IGLVSQEPVLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 118 LNPVwtvgsqikealrANNIATGS-EAHKKAIEllEQAGLPNAKKRIDQYPHEF-----------SGGMRQRALIAMGLA 185
Cdd:cd03249 90 DGTI------------AENIRYGKpDATDEEVE--EAAKKANIHDFIMSLPDGYdtlvgergsqlSGGQKQRIAIARALL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2524658687 186 AHPKLLIADEPTSALDVTVAKKILDHLDKLTseLGTSVVLITHDLgLAAERADRLVVMQAGRVVETG 252
Cdd:cd03249 156 RNPKILLLDEATSALDAESEKLVQEALDRAM--KGRTTIVIAHRL-STIRNADLIAVLQNGQVVEQG 219
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
322-535 |
1.75e-30 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 125.84 E-value: 1.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 322 RAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEeleLRRRIQPIFQnpyatlDPM 401
Cdd:PRK13657 349 QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRAS---LRRNIAVVFQ------DAG 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 402 rTVHSSIEEPLRIHKIGTKKEREQRVFEL-------------LDRVAlpAEMGRRfpgeLSGGQRQRVAIARALALNPEV 468
Cdd:PRK13657 420 -LFNRSIEDNIRVGRPDATDEEMRAAAERaqahdfierkpdgYDTVV--GERGRQ----LSGGERQRLAIARALLKDPPI 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2524658687 469 VVCDEAVSALDVVVQAQVLELLAELQEemDLAYLFITHDLAVVRQvADEVIVMEHGKMVEHRPTDDL 535
Cdd:PRK13657 493 LILDEATSALDVETEAKVKAALDELMK--GRTTFIIAHRLSTVRN-ADRILVFDNGRVVESGSFDEL 556
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
322-541 |
2.31e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 120.12 E-value: 2.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 322 RAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFdGKRV--QGRNRKEELELRRRIQPIFQNPYATLD 399
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVitAGKKNKKLKPLRKKVGIVFQFPEHQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 400 PmRTVHSSIE-EPLrihKIG-TKKEREQRVFELLDRVALPAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVSA 477
Cdd:PRK13634 100 E-ETVEKDICfGPM---NFGvSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAG 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2524658687 478 LDVVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDLFDHPEK 541
Cdd:PRK13634 176 LDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDE 239
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
13-252 |
2.73e-30 |
|
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: 117.74 E-value: 2.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 13 LTLKDVCIGFPTTTAsgrrsksltdvVHDVNLEVFPGETVAIVGESGSGKSTTahaaLGLLPGDGEVTGGTITFDGRDIT 92
Cdd:cd03301 1 VELENVTKRFGNVTA-----------LDDLNLDIADGEFVVLLGPSGCGKTTT----LRMIAGLEEPTSGRIYIGGRDVT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 93 HLTDREfvsirgNGIGLVPQDpmTNLNPVWTVGSQIKEALRANNI--ATGSEAHKKAIELLEQAGLpnakkrIDQYPHEF 170
Cdd:cd03301 66 DLPPKD------RDIAMVFQN--YALYPHMTVYDNIAFGLKLRKVpkDEIDERVREVAELLQIEHL------LDRKPKQL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 171 SGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVVE 250
Cdd:cd03301 132 SGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQ 211
|
..
gi 2524658687 251 TG 252
Cdd:cd03301 212 IG 213
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
320-527 |
3.23e-30 |
|
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: 115.99 E-value: 3.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 320 SFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEELelRRRIQPIFQnpyatld 399
Cdd:cd03216 12 GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDAR--RAGIAMVYQ------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 400 pmrtvhssieeplrihkigtkkereqrvfelldrvalpaemgrrfpgeLSGGQRQRVAIARALALNPEVVVCDEAVSALD 479
Cdd:cd03216 83 ------------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALT 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2524658687 480 vVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMV 527
Cdd:cd03216 115 -PAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
323-537 |
3.48e-30 |
|
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: 118.10 E-value: 3.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 323 AVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKeelELRRRIQPIFQNPYATLDpmr 402
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRK---SLRSMIGVVLQDTFLFSG--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 403 tvhsSIEEPLRIHKIGTKKEREQRVFELLDrvalPAEMGRRFP-----------GELSGGQRQRVAIARALALNPEVVVC 471
Cdd:cd03254 92 ----TIMENIRLGRPNATDEEVIEAAKEAG----AHDFIMKLPngydtvlgengGNLSQGERQLLAIARAMLRDPKILIL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 472 DEAVSALDVV----VQAQVLELLAELQEEMdlaylfITHDLAVVRQvADEVIVMEHGKMVEHRPTDDLFD 537
Cdd:cd03254 164 DEATSNIDTEteklIQEALEKLMKGRTSII------IAHRLSTIKN-ADKILVLDDGKIIEEGTHDELLA 226
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
38-256 |
3.52e-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: 117.61 E-value: 3.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETVAIVGESGSGKSTTahaaLGLLPGDGEVTGGTITFDGRDIthLTDRefVSIRGNgIGLVPQDPM-- 115
Cdd:cd03263 17 AVDDLSLNVYKGEIFGLLGHNGAGKTTT----LKMLTGELRPTSGTAYINGYSI--RTDR--KAARQS-LGYCPQFDAlf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 116 TNLNPvwtvgsqiKEALRANNIATG---SEAHKKAIELLEQAGL-PNAKKRIdqypHEFSGGMRQRALIAMGLAAHPKLL 191
Cdd:cd03263 88 DELTV--------REHLRFYARLKGlpkSEIKEEVELLLRVLGLtDKANKRA----RTLSGGMKRKLSLAIALIGGPSVL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2524658687 192 IADEPTSALDVTVAKKILDHLDKLTSelGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQ 256
Cdd:cd03263 156 LLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQE 218
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
9-526 |
4.52e-30 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 123.50 E-value: 4.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 9 AAPILTLKDVCIGFPTTTAsgrrsksltdvVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLP-GDGEvtgGTITFD 87
Cdd:PRK13549 2 MEYLLEMKNITKTFGGVKA-----------LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhGTYE---GEIIFE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 88 GRDIT--HLTDREfvsirGNGIGLVPQDPMtnLNPVWTVgsqikealrANNIATGSEAHK-----------KAIELLEQA 154
Cdd:PRK13549 68 GEELQasNIRDTE-----RAGIAIIHQELA--LVKELSV---------LENIFLGNEITPggimdydamylRAQKLLAQL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 155 GLP-NAKKRIDQYphefSGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSElGTSVVLITHDLGLA 233
Cdd:PRK13549 132 KLDiNPATPVGNL----GLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEV 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 234 AERADRLVVMQAGRVVETGPALQVLTrpqhpytkqliaaapslaarrgDRVVAA----------PTTSDADQKEILVAKN 303
Cdd:PRK13549 207 KAISDTICVIRDGRHIGTRPAAGMTE----------------------DDIITMmvgreltalyPREPHTIGEVILEVRN 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 304 LVrdfAIRGDRPWRKdsfrAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLD-PTEGEVLFDGKRVQGRNRKEEL- 381
Cdd:PRK13549 265 LT---AWDPVNPHIK----RVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNPQQAIa 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 382 -------ELRRR--IQPIF---QN-PYATLDPMrTVHSSIEEPLRIHKIgtkkerEQRVFELLDRVALP-AEMGRrfpge 447
Cdd:PRK13549 338 qgiamvpEDRKRdgIVPVMgvgKNiTLAALDRF-TGGSRIDDAAELKTI------LESIQRLKVKTASPeLAIAR----- 405
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2524658687 448 LSGGQRQRVAIARALALNPEVVVCDEAVSALDVVVQAQVlELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKM 526
Cdd:PRK13549 406 LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEI-YKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
319-524 |
7.54e-30 |
|
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: 116.48 E-value: 7.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 319 DSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQgrnrkeelELRRRIQPIFQNPYATL 398
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE--------KERKRIGYVPQRRSIDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 399 D-PMR---TVHSSIEEPLRIHKIGTKKEREqRVFELLDRVALpAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEA 474
Cdd:cd03235 82 DfPISvrdVVLMGLYGHKGLFRRLSKADKA-KVDEALERVGL-SELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2524658687 475 VSALDVVVQAQVlELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHG 524
Cdd:cd03235 160 FAGVDPKTQEDI-YELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
43-264 |
9.16e-30 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 116.78 E-value: 9.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 43 NLEVFPGETVAIVGESGSGKSTTAHAALGLLPgdgeVTGGTITFDGRDITHLT--DREfVSIrgngiglVPQDpmTNLNP 120
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLP----PDSGRILWNGQDLTALPpaERP-VSM-------LFQE--NNLFP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 121 VWTVgsqikealrANNIATG--------SEAHKKAIELLEQAGLPNAKKRidqYPHEFSGGMRQRALIAMGLAAHPKLLI 192
Cdd:COG3840 85 HLTV---------AQNIGLGlrpglkltAEQRAQVEQALERVGLAGLLDR---LPGQLSGGQRQRVALARCLVRKRPILL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2524658687 193 ADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVLTRPQHP 264
Cdd:COG3840 153 LDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPP 224
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
13-252 |
9.93e-30 |
|
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: 116.95 E-value: 9.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 13 LTLKDVCIGFPtttasgrrsKSLTDVVHDVNLEVFPGETVAIVGESGSGKSTtahaALGLLPGDGEVTGGTITFDGRDIT 92
Cdd:cd03251 1 VEFKNVTFRYP---------GDGPPVLRDISLDIPAGETVALVGPSGSGKST----LVNLIPRFYDVDSGRILIDGHDVR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 93 hltDREFVSIRgNGIGLVPQDPMTNLNPVwtvgsqikealrANNIATG-SEAHKKAIEllEQAGLPNAKKRIDQYPHEF- 170
Cdd:cd03251 68 ---DYTLASLR-RQIGLVSQDVFLFNDTV------------AENIAYGrPGATREEVE--EAARAANAHEFIMELPEGYd 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 171 ----------SGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSelGTSVVLITHDLGlAAERADRL 240
Cdd:cd03251 130 tvigergvklSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLS-TIENADRI 206
|
250
....*....|..
gi 2524658687 241 VVMQAGRVVETG 252
Cdd:cd03251 207 VVLEDGKIVERG 218
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
326-540 |
9.94e-30 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 120.21 E-value: 9.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 326 DISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQ----GRNRKEElelRRRIQPIFQNpyATLDPM 401
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQdsarGIFLPPH---RRRIGYVFQE--ARLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 402 RTVHSSIEEPLRIHKIGTKKEREQRVFELLDRVALpaeMGRRfPGELSGGQRQRVAIARALALNPEVVVCDEAVSALDVV 481
Cdd:COG4148 92 LSVRGNLLYGRKRAPRAERRISFDEVVELLGIGHL---LDRR-PATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2524658687 482 VQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDLFDHPE 540
Cdd:COG4148 168 RKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPD 226
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
335-546 |
1.02e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 117.32 E-value: 1.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 335 RTI-GIVGESGSGKSTVANMALGLLD-----PTEGEVLFDGKRVqgrNRKEELELRRRIQPIFQ--NPYATLdpmrTVHS 406
Cdd:PRK14247 29 NTItALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDI---FKMDVIELRRRVQMVFQipNPIPNL----SIFE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 407 SIEEPLRIHKI-GTKKEREQRVFELLDRVALPAEMGRRF---PGELSGGQRQRVAIARALALNPEVVVCDEAVSALDVVV 482
Cdd:PRK14247 102 NVALGLKLNRLvKSKKELQERVRWALEKAQLWDEVKDRLdapAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPEN 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2524658687 483 QAQVLELLAELQEemDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDLFDHPEKEYTQR 546
Cdd:PRK14247 182 TAKIESLFLELKK--DMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELTEK 243
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
36-249 |
1.20e-29 |
|
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: 115.82 E-value: 1.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 36 TDVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLpgdgEVTGGTITFDGRDItHLTDRefvsiRGNgIGLVPQDPM 115
Cdd:cd03226 13 TEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLI----KESSGSILLNGKPI-KAKER-----RKS-IGYVMQDVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 116 TNLNPVwTVGSQIKEALRAnniatGSEAHKKAIELLEQAGLPNAKkriDQYPHEFSGGMRQRALIAMGLAAHPKLLIADE 195
Cdd:cd03226 82 YQLFTD-SVREELLLGLKE-----LDAGNEQAETVLKDLDLYALK---ERHPLSLSGGQKQRLAIAAALLSGKDLLIFDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2524658687 196 PTSALDVTVAKKILDHLDKLTSElGTSVVLITHDLGLAAERADRLVVMQAGRVV 249
Cdd:cd03226 153 PTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
318-528 |
1.53e-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: 116.56 E-value: 1.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 318 KDSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVqgrnRKEELE-LRRRIQPIfqnpya 396
Cdd:cd03253 11 DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDI----REVTLDsLRRAIGVV------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 397 tldPMRTV--HSSIEEPLRIhkiGTKKEREQRVFElldrVALPAEMGR---RFP-------GE----LSGGQRQRVAIAR 460
Cdd:cd03253 81 ---PQDTVlfNDTIGYNIRY---GRPDATDEEVIE----AAKAAQIHDkimRFPdgydtivGErglkLSGGEKQRVAIAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2524658687 461 ALALNPEVVVCDEAVSALDVVVQAQVLELLAELQEEMDLayLFITHDLAVVRQvADEVIVMEHGKMVE 528
Cdd:cd03253 151 AILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTT--IVIAHRLSTIVN-ADKIIVLKDGRIVE 215
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
38-270 |
2.28e-29 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 116.67 E-value: 2.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETVAIVGESGSGKSTtahaalgLL----------PGdGEVTGgTITFDGRDITHlTDREFVSIRGNgI 107
Cdd:COG1117 26 ALKDINLDIPENKVTALIGPSGCGKST-------LLrclnrmndliPG-ARVEG-EILLDGEDIYD-PDVDVVELRRR-V 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 108 GLVPQDP----MTnlnpvwtvgsqIKE----ALRANNIATGSEAHKKAIELLEQAGLPN-AKKRIDQYPHEFSGGMRQRA 178
Cdd:COG1117 95 GMVFQKPnpfpKS-----------IYDnvayGLRLHGIKSKSELDEIVEESLRKAALWDeVKDRLKKSALGLSGGQQQRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 179 LIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSELgtSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVL 258
Cdd:COG1117 164 CIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDY--TIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIF 241
|
250
....*....|..
gi 2524658687 259 TRPQHPYTKQLI 270
Cdd:COG1117 242 TNPKDKRTEDYI 253
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
321-541 |
4.87e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 116.42 E-value: 4.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 321 FRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEELE-LRRRIQPIFQNPYATL- 398
Cdd:PRK13646 20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRpVRKRIGMVFQFPESQLf 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 399 -DpmrTVHSSIEeplrihkIGTK------KEREQRVFELLDRVALPAEMGRRFPGELSGGQRQRVAIARALALNPEVVVC 471
Cdd:PRK13646 100 eD---TVEREII-------FGPKnfkmnlDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 472 DEAVSALDVVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDLFDHPEK 541
Cdd:PRK13646 170 DEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKKK 239
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
41-529 |
5.26e-29 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 120.55 E-value: 5.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 41 DVNLEVFPGETVAIVGESGSGKSTTahaaLGLLPGDGEVTGGTITFDgRDIThltdrefvsirgngIGLVPQDP------ 114
Cdd:COG0488 16 DVSLSINPGDRIGLVGRNGAGKSTL----LKILAGELEPDSGEVSIP-KGLR--------------IGYLPQEPpldddl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 115 ------MTNLNPVWTVGSQIKEALRAnnIATGSEAHKKAIEL---LEQAGLPNAKKRI--------------DQYPHEFS 171
Cdd:COG0488 77 tvldtvLDGDAELRALEAELEELEAK--LAEPDEDLERLAELqeeFEALGGWEAEARAeeilsglgfpeedlDRPVSELS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 172 GGMRQRALIAMGLAAHPKLLIADEPTSALDV-TVAKkiL-DHLDKLTselGTsVVLITHDlglaaeRA--DRLVvmqaGR 247
Cdd:COG0488 155 GGWRRRVALARALLSEPDLLLLDEPTNHLDLeSIEW--LeEFLKNYP---GT-VLVVSHD------RYflDRVA----TR 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 248 VVE---------TGP--------ALQvLTRPQHPYTKQ--LIA------AAPSLAARRG-------------DRVVAAPT 289
Cdd:COG0488 219 ILEldrgkltlyPGNysayleqrAER-LEQEAAAYAKQqkKIAkeeefiRRFRAKARKAkqaqsrikaleklEREEPPRR 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 290 TSDAD---------QKEILVAKNLVRDFairGDRPwrkdsfrAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDP 360
Cdd:COG0488 298 DKTVEirfppperlGKKVLELEGLSKSY---GDKT-------LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEP 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 361 TEGEVLFdGKRV------QGRnrkeelelrrriqpifqnpyATLDPMRTVHSSIEEplrihkiGTKKEREQRVFELLDRV 434
Cdd:COG0488 368 DSGTVKL-GETVkigyfdQHQ--------------------EELDPDKTVLDELRD-------GAPGGTEQEVRGYLGRF 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 435 ALPAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDE-----AVSALDVVVQAqvlellaelqeemdL-----AYLFI 504
Cdd:COG0488 420 LFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEptnhlDIETLEALEEA--------------LddfpgTVLLV 485
|
570 580
....*....|....*....|....*
gi 2524658687 505 THDLAVVRQVADEVIVMEHGKMVEH 529
Cdd:COG0488 486 SHDRYFLDRVATRILEFEDGGVREY 510
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
326-546 |
5.58e-29 |
|
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: 117.91 E-value: 5.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 326 DISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEELEL-RRRIQPIFQNpyATLDPMRTV 404
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPeKRRIGYVFQE--ARLFPHLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 405 HSSIEEPLRIHKIGTKKEREQRVFELLDRVALPaemgRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVSALDVVVQA 484
Cdd:TIGR02142 93 RGNLRYGMKRARPSERRISFERVIELLGIGHLL----GRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2524658687 485 QVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDLFDHPEKEYTQR 546
Cdd:TIGR02142 169 EILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWLAR 230
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
323-526 |
6.85e-29 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 114.04 E-value: 6.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 323 AVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEELELRRRIQPIFQNpyATLDPMR 402
Cdd:cd03292 16 ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRKIGVVFQD--FRLLPDR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 403 TVHSSIEEPLRIHKIGtKKEREQRVFELLDRVALpAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVSALDVVV 482
Cdd:cd03292 94 NVYENVAFALEVTGVP-PREIRKRVPAALELVGL-SHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDT 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2524658687 483 QAQVlELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKM 526
Cdd:cd03292 172 TWEI-MNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
39-252 |
6.85e-29 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 116.34 E-value: 6.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 39 VHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGDGevtgGTITFDGRDIThltdREFVSIRgNGIGLVPQDPmtNL 118
Cdd:TIGR01188 9 VDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTS----GTARVAGYDVV----REPRKVR-RSIGIVPQYA--SV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 119 NPVWTVGSQIKEALRANNIaTGSEAHKKAIELLEQAGLPNAKKRIDQYpheFSGGMRQRALIAMGLAAHPKLLIADEPTS 198
Cdd:TIGR01188 78 DEDLTGRENLEMMGRLYGL-PKDEAEERAEELLELFELGEAADRPVGT---YSGGMRRRLDIAASLIHQPDVLFLDEPTT 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2524658687 199 ALDVTVAKKILDHLDKLTSElGTSVVLITHDLGLAAERADRLVVMQAGRVVETG 252
Cdd:TIGR01188 154 GLDPRTRRAIWDYIRALKEE-GVTILLTTHYMEEADKLCDRIAIIDHGRIIAEG 206
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
37-254 |
7.55e-29 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 114.78 E-value: 7.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 37 DVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLlPGDgEVTGGTITFDGRDITHLTdrefVSIRGN-GIGLVPQDP- 114
Cdd:COG0396 14 EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGH-PKY-EVTSGSILLDGEDILELS----PDERARaGIFLAFQYPv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 115 ------MTNLnpvwtvgsqIKEALRANNIATGS--EAHKKAIELLEQAGLPnaKKRIDQYPHE-FSGGMRQRALIAMGLA 185
Cdd:COG0396 88 eipgvsVSNF---------LRTALNARRGEELSarEFLKLLKEKMKELGLD--EDFLDRYVNEgFSGGEKKRNEILQMLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2524658687 186 AHPKLLIADEPTSALDVTVAKKILDHLDKLTSElGTSVVLITH--DLgLAAERADRLVVMQAGRVVETGPA 254
Cdd:COG0396 157 LEPKLAILDETDSGLDIDALRIVAEGVNKLRSP-DRGILIITHyqRI-LDYIKPDFVHVLVDGRIVKSGGK 225
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
34-248 |
7.87e-29 |
|
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: 112.91 E-value: 7.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 34 SLTDVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPgdgeVTGGTITFDGRDITHLTDREFvsiRGNGIGLVPQD 113
Cdd:cd03215 11 SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRP----PASGEITLDGKPVTRRSPRDA---IRAGIAYVPED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 114 PMTN-LNPVWTVgsqikealrANNIATGSeahkkaieLLeqaglpnakkridqyphefSGGMRQRALIAMGLAAHPKLLI 192
Cdd:cd03215 84 RKREgLVLDLSV---------AENIALSS--------LL-------------------SGGNQQKVVLARWLARDPRVLI 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2524658687 193 ADEPTSALDVTVAKKILDHLDKLTSElGTSVVLITHDLGLAAERADRLVVMQAGRV 248
Cdd:cd03215 128 LDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
298-544 |
8.11e-29 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 118.01 E-value: 8.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 298 ILVAKNLVRDFairgdrpwrkDSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQgrnr 377
Cdd:PRK11607 19 LLEIRNLTKSF----------DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 378 kEELELRRRIQPIFQNpYAtLDPMRTVHSSIEEPLRIHKIgTKKEREQRVFELLDRVALpAEMGRRFPGELSGGQRQRVA 457
Cdd:PRK11607 85 -HVPPYQRPINMMFQS-YA-LFPHMTVEQNIAFGLKQDKL-PKAEIASRVNEMLGLVHM-QEFAKRKPHQLSGGQRQRVA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 458 IARALALNPEVVVCDEAVSALDVVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDLFD 537
Cdd:PRK11607 160 LARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYE 239
|
....*..
gi 2524658687 538 HPEKEYT 544
Cdd:PRK11607 240 HPTTRYS 246
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
13-259 |
8.50e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 115.47 E-value: 8.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 13 LTLKDVCIGFPTTTASGRRSKSLtdVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLpgdgEVTGGTITFDGRDIT 92
Cdd:PRK13632 1 IKNKSVMIKVENVSFSYPNSENN--ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLL----KPQSGEIKIDGITIS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 93 HLTDREfvsIRGNgIGLVPQDPMTNLnpvwtVGSQIKEalranNIATGSEAHK------KAI--ELLEQAGLpnaKKRID 164
Cdd:PRK13632 75 KENLKE---IRKK-IGIIFQNPDNQF-----IGATVED-----DIAFGLENKKvppkkmKDIidDLAKKVGM---EDYLD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 165 QYPHEFSGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGlAAERADRLVVMQ 244
Cdd:PRK13632 138 KEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMD-EAILADKVIVFS 216
|
250
....*....|....*
gi 2524658687 245 AGRVVETGPALQVLT 259
Cdd:PRK13632 217 EGKLIAQGKPKEILN 231
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
38-278 |
9.03e-29 |
|
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding component of an ABC transport system is found in Salmonella and Burkholderia lineages in the vicinity of enzymes for the breakdown of 2-aminoethylphosphonate.
Pssm-ID: 132302 [Multi-domain] Cd Length: 362 Bit Score: 117.40 E-value: 9.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGDGEVtgGTITFDGRDITHLTDREfvsirgNGIGLVPQDpmTN 117
Cdd:TIGR03258 20 VLDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKAAGLT--GRIAIADRDLTHAPPHK------RGLALLFQN--YA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 118 LNPVWTVGSQIKEALRANNIATgSEAHKKAIELLEQAGLPNAKKRidqYPHEFSGGMRQRALIAMGLAAHPKLLIADEPT 197
Cdd:TIGR03258 90 LFPHLKVEDNVAFGLRAQKMPK-ADIAERVADALKLVGLGDAAAH---LPAQLSGGMQQRIAIARAIAIEPDVLLLDEPL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 198 SALDVTVAKKILDHLDKLTSEL-GTSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVLTRPQHPYTKQLIAAAPSL 276
Cdd:TIGR03258 166 SALDANIRANMREEIAALHEELpELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDAPADGFAAEFLGAANIL 245
|
..
gi 2524658687 277 AA 278
Cdd:TIGR03258 246 PA 247
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
322-541 |
9.14e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 115.53 E-value: 9.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 322 RAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEElELRRRIQPIFQNP-YATLDp 400
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLS-DIRKKVGLVFQYPeYQLFE- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 401 mRTVHSSIEEPLRihKIG-TKKEREQRVFELLDRVALPAE-MGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVSAL 478
Cdd:PRK13637 99 -ETIEKDIAFGPI--NLGlSEEEIENRVKRAMNIVGLDYEdYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2524658687 479 DVVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDLFDHPEK 541
Cdd:PRK13637 176 DPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEVET 238
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
13-260 |
9.95e-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: 9.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 13 LTLKDVCIGFPTttasGRrsksltDVVHDVNLEVFPGETVAIVGESGSGKSTTahaaLGLLPGDGEVTGGTITFDGRDIT 92
Cdd:cd03253 1 IEFENVTFAYDP----GR------PVLKDVSFTIPAGKKVAIVGPSGSGKSTI----LRLLFRFYDVSSGSILIDGQDIR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 93 HLTdreFVSIRGNgIGLVPQD-PMTNLnpvwTVGsqikealraNNIATGSEAHKKaIELLEQAGLPNAKKRIDQYPHEF- 170
Cdd:cd03253 67 EVT---LDSLRRA-IGVVPQDtVLFND----TIG---------YNIRYGRPDATD-EEVIEAAKAAQIHDKIMRFPDGYd 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 171 ----------SGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSelGTSVVLITHDLGLAAErADRL 240
Cdd:cd03253 129 tivgerglklSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKI 205
|
250 260
....*....|....*....|
gi 2524658687 241 VVMQAGRVVETGPALQVLTR 260
Cdd:cd03253 206 IVLKDGRIVERGTHEELLAK 225
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
319-525 |
1.07e-28 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 117.36 E-value: 1.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 319 DSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKeelelRRRIQPIFQNpYAtL 398
Cdd:PRK09452 25 DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE-----NRHVNTVFQS-YA-L 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 399 DPMRTVHSSIEEPLRIHKIGtKKEREQRVFELLDRVALpAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVSAL 478
Cdd:PRK09452 98 FPHMTVFENVAFGLRMQKTP-AAEITPRVMEALRMVQL-EEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSAL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2524658687 479 DVVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGK 525
Cdd:PRK09452 176 DYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGR 222
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
327-548 |
1.30e-28 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 114.68 E-value: 1.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 327 ISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQ------GRNR---KEELE-LRRRIQPIFQNpYA 396
Cdd:PRK10619 24 VSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdGQLKvadKNQLRlLRTRLTMVFQH-FN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 397 TLDPMRTVHSSIEEPLRIHKIgTKKEREQRVFELLDRVALPAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVS 476
Cdd:PRK10619 103 LWSHMTVLENVMEAPIQVLGL-SKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTS 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2524658687 477 ALDVVVQAQVLELLAELQEEMDlAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDLFDHPEKEYTQRLL 548
Cdd:PRK10619 182 ALDPELVGEVLRIMQQLAEEGK-TMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQFL 252
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
323-551 |
1.32e-28 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 117.83 E-value: 1.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 323 AVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEELELRRR-IQPIFQNpyATLDPM 401
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKkIAMVFQS--FALMPH 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 402 RTVHSSIEEPLRIHKIGTKkEREQRVFELLDRVALpAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVSALDVV 481
Cdd:PRK10070 121 MTVLDNTAFGMELAGINAE-ERREKALDALRQVGL-ENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 482 VQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDLFDHPEKEYTQRLLDAI 551
Cdd:PRK10070 199 IRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGV 268
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
32-261 |
1.37e-28 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 116.72 E-value: 1.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 32 SKSL--TDVVHDVNLEVFPGETVAIVGESGSGKSTTahaaLGLLPGDGEVTGGTITFDGRDITHLTDREfvsirgNGIGL 109
Cdd:PRK10851 9 KKSFgrTQVLNDISLDIPSGQMVALLGPSGSGKTTL----LRIIAGLEHQTSGHIRFHGTDVSRLHARD------RKVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 110 VPQD-----PMTnlnpvwtvgsqikealRANNIATG------------SEAHKKAIELLEQAGLPNAKKRidqYPHEFSG 172
Cdd:PRK10851 79 VFQHyalfrHMT----------------VFDNIAFGltvlprrerpnaAAIKAKVTQLLEMVQLAHLADR---YPAQLSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 173 GMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETG 252
Cdd:PRK10851 140 GQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAG 219
|
....*....
gi 2524658687 253 PALQVLTRP 261
Cdd:PRK10851 220 TPDQVWREP 228
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
38-252 |
1.42e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 115.18 E-value: 1.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETVAIVGESGSGKSTTA-HAALGLLPGDGEVTggTITFDGRDITHLTDrefvsIRgNGIGLVPQDPmt 116
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAkHMNALLIPSEGKVY--VDGLDTSDEENLWD-----IR-NKAGMVFQNP-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 117 nlnpvwtvGSQIKEALRANNIATGSEahKKAIELLE-QAGLPNAKKRIDQY------PHEFSGGMRQRALIAMGLAAHPK 189
Cdd:PRK13633 95 --------DNQIVATIVEEDVAFGPE--NLGIPPEEiRERVDESLKKVGMYeyrrhaPHLLSGGQKQRVAIAGILAMRPE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2524658687 190 LLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAErADRLVVMQAGRVVETG 252
Cdd:PRK13633 165 CIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEG 226
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
40-252 |
1.54e-28 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 113.16 E-value: 1.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 40 HDVNLE-VFPGETVAIVGESGSGKSTTAHAALGLLpgdgEVTGGTITFDGRDITHLTDREFVSIRGNGIGLVPQDpmTNL 118
Cdd:cd03297 13 FTLKIDfDLNEEVTGIFGASGAGKSTLLRCIAGLE----KPDGGTIVLNGTVLFDSRKKINLPPQQRKIGLVFQQ--YAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 119 NPVWTVGSQIKEALRanniatGSEAHKKAIELLEQAGLPNAKKRIDQYPHEFSGGMRQRALIAMGLAAHPKLLIADEPTS 198
Cdd:cd03297 87 FPHLNVRENLAFGLK------RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2524658687 199 ALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETG 252
Cdd:cd03297 161 ALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
39-267 |
1.63e-28 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 117.44 E-value: 1.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 39 VHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLpgdgEVTGGTITFDGRDITHLTDREFVSIRGNGIGLVPQDpmTNL 118
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLI----EPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQS--FAL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 119 NPVWTVGSQIKEALRANNIAtGSEAHKKAIELLEQAGLPNAKKridQYPHEFSGGMRQRALIAMGLAAHPKLLIADEPTS 198
Cdd:PRK10070 118 MPHMTVLDNTAFGMELAGIN-AEERREKALDALRQVGLENYAH---SYPDELSGGMRQRVGLARALAINPDILLMDEAFS 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2524658687 199 ALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVLTRPQHPYTK 267
Cdd:PRK10070 194 ALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVR 262
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
321-540 |
1.65e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 115.11 E-value: 1.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 321 FRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQG--RNRKEELELRRRIQPIFQNPYATL 398
Cdd:PRK13645 24 FKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlKKIKEVKRLRKEIGLVFQFPEYQL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 399 dpmrtVHSSIEEPLR---IHKIGTKKEREQRVFELLDRVALPAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAV 475
Cdd:PRK13645 104 -----FQETIEKDIAfgpVNLGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPT 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2524658687 476 SALDVVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDLFDHPE 540
Cdd:PRK13645 179 GGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQE 243
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
36-252 |
1.69e-28 |
|
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: 113.07 E-value: 1.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 36 TDVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLpgdgEVTGGTITFDGRDITHLTDREfvsIRGNgIGLVPQDPM 115
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLY----KPTSGSVLLDGTDIRQLDPAD---LRRN-IGYVPQDVT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 116 TnlnpvwtvgsqIKEALRaNNIATGSEAHKKAiELLEQAGLPNAKKRIDQYPHEF-----------SGGMRQRALIAMGL 184
Cdd:cd03245 89 L-----------FYGTLR-DNITLGAPLADDE-RILRAAELAGVTDFVNKHPNGLdlqigergrglSGGQRQAVALARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2524658687 185 AAHPKLLIADEPTSALDVTVAKKILDHLDKLTSelGTSVVLITHDLGLaAERADRLVVMQAGRVVETG 252
Cdd:cd03245 156 LNDPPILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPSL-LDLVDRIIVMDSGRIVADG 220
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
37-260 |
1.86e-28 |
|
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: 119.44 E-value: 1.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 37 DVVHDVNLEVFPGETVAIVGESGSGKSTTAHaalgLLPGDGEVTGGTITFDGRDITHLTDRefvSIRgNGIGLVPQDPMT 116
Cdd:TIGR02203 346 PALDSISLVIEPGETVALVGRSGSGKSTLVN----LIPRFYEPDSGQILLDGHDLADYTLA---SLR-RQVALVSQDVVL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 117 NLNPVwtvgsqikealrANNIATGSEAHKKAIELLEQAGLPNAKKRIDQYPHEF-----------SGGMRQRALIAMGLA 185
Cdd:TIGR02203 418 FNDTI------------ANNIAYGRTEQADRAEIERALAAAYAQDFVDKLPLGLdtpigengvllSGGQRQRLAIARALL 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2524658687 186 AHPKLLIADEPTSALDVTVAKKILDHLDKLTSELGTSVvlITHDLGlAAERADRLVVMQAGRVVETGPALQVLTR 260
Cdd:TIGR02203 486 KDAPILILDEATSALDNESERLVQAALERLMQGRTTLV--IAHRLS-TIEKADRIVVMDDGRIVERGTHNELLAR 557
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
32-261 |
2.21e-28 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 113.64 E-value: 2.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 32 SKSLTD--VVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGDGevtgGTITFDGRDITHLTDREF---VSIrgng 106
Cdd:COG4604 8 SKRYGGkvVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDS----GEVLVDGLDVATTPSRELakrLAI---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 107 iglVPQDPMTNLNpvWTVgsqikEALrannIATG----------SEAHKK---AIELLEQAGLpnAKKRIDqyphEFSGG 173
Cdd:COG4604 80 ---LRQENHINSR--LTV-----REL----VAFGrfpyskgrltAEDREIideAIAYLDLEDL--ADRYLD----ELSGG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 174 MRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETGP 253
Cdd:COG4604 140 QRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGT 219
|
....*...
gi 2524658687 254 ALQVLTRP 261
Cdd:COG4604 220 PEEIITPE 227
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
36-268 |
2.51e-28 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 113.19 E-value: 2.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 36 TDVVHDVNLEVFPGETVAIVGESGSGKSTTAHAaLGLL--PGDGEVTGGTITFDGRdiTHLTDREFVSIRGNgIGLVPQD 113
Cdd:PRK11124 15 HQALFDITLDCPQGETLVLLGPSGAGKSSLLRV-LNLLemPRSGTLNIAGNHFDFS--KTPSDKAIRELRRN-VGMVFQQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 114 pmTNLNPVWTVGSQIKEA-LRANNIATgSEAHKKAIELLEQAGLPNakkRIDQYPHEFSGGMRQRALIAMGLAAHPKLLI 192
Cdd:PRK11124 91 --YNLWPHLTVQQNLIEApCRVLGLSK-DQALARAEKLLERLRLKP---YADRFPLHLSGGQQQRVAIARALMMEPQVLL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2524658687 193 ADEPTSALDVTVAKKILDHLDKLtSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPAlqvlTRPQHPYTKQ 268
Cdd:PRK11124 165 FDEPTAALDPEITAQIVSIIREL-AETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDA----SCFTQPQTEA 235
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
38-251 |
3.25e-28 |
|
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: 110.21 E-value: 3.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGDGevtgGTITFDGRDITHLTDREfvSIRgNGIGLVPQdpmtn 117
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDS----GEILVDGKEVSFASPRD--ARR-AGIAMVYQ----- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 118 lnpvwtvgsqikealranniatgseahkkaielleqaglpnakkridqypheFSGGMRQRALIAMGLAAHPKLLIADEPT 197
Cdd:cd03216 83 ----------------------------------------------------LSVGERQMVEIARALARNARLLILDEPT 110
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2524658687 198 SALDVTVAKKILDHLDKLTSElGTSVVLITHDLGLAAERADRLVVMQAGRVVET 251
Cdd:cd03216 111 AALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
13-245 |
3.29e-28 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 111.80 E-value: 3.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 13 LTLKDVCIGfptttasgRRSKSLtdvVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGDGEVTgGTITFDGRDIT 92
Cdd:COG4136 2 LSLENLTIT--------LGGRPL---LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFSAS-GEVLLNGRRLT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 93 HLtdrefvSIRGNGIGLVPQDPMtnLNPVWTVGSQIKEALRANniATGSEAHKKAIELLEQAGLPNAKKRidqYPHEFSG 172
Cdd:COG4136 70 AL------PAEQRRIGILFQDDL--LFPHLSVGENLAFALPPT--IGRAQRRARVEQALEEAGLAGFADR---DPATLSG 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2524658687 173 GMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKI----LDHLDkltsELGTSVVLITHDLGlAAERADRLVVMQA 245
Cdd:COG4136 137 GQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFrefvFEQIR----QRGIPALLVTHDEE-DAPAAGRVLDLGN 208
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
40-248 |
3.38e-28 |
|
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: 112.12 E-value: 3.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 40 HDVNLEVFPGETVAIVGESGSGKSTTahaaLGLLPGDGEVTGGTITFDGRDITHLTDREFVSIRgNGIGLVPQDpmTNLN 119
Cdd:cd03292 18 DGINISISAGEFVFLVGPSGAGKSTL----LKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR-RKIGVVFQD--FRLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 120 PVWTVGSQIKEALRANNiATGSEAHKKAIELLEQAGLpnaKKRIDQYPHEFSGGMRQRALIAMGLAAHPKLLIADEPTSA 199
Cdd:cd03292 91 PDRNVYENVAFALEVTG-VPPREIRKRVPAALELVGL---SHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGN 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2524658687 200 LDVTVAKKILDHLDKLtSELGTSVVLITHDLGLAAERADRLVVMQAGRV 248
Cdd:cd03292 167 LDPDTTWEIMNLLKKI-NKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
324-524 |
4.24e-28 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 112.17 E-value: 4.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 324 VDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQ--GRNRkeelelrrriQPIFQNpYATLdPM 401
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITepGPDR----------MVVFQN-YSLL-PW 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 402 RTVHSSIEEPL-RIHKIGTKKEREQRVFELLDRVALPAEMGRRfPGELSGGQRQRVAIARALALNPEVVVCDEAVSALDV 480
Cdd:TIGR01184 69 LTVRENIALAVdRVLPDLSKSERRAIVEEHIALVGLTEAADKR-PGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2524658687 481 VVQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHG 524
Cdd:TIGR01184 148 LTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
322-533 |
4.30e-28 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 112.87 E-value: 4.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 322 RAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEELelrrriqpIFQNpyATLDPM 401
Cdd:PRK11248 15 PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERGV--------VFQN--EGLLPW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 402 RTVHSSIEEPLRIHKIGtKKEREQRVFELLDRVALpAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVSALDVV 481
Cdd:PRK11248 85 RNVQDNVAFGLQLAGVE-KMQRLEIAHQMLKKVGL-EGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAF 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2524658687 482 VQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVME--HGKMVEHRPTD 533
Cdd:PRK11248 163 TREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSpgPGRVVERLPLN 216
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
38-311 |
5.57e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 113.67 E-value: 5.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGDGevtgGTITFDGRDITHLTdrefvsirGNGIGLVPQDPmtN 117
Cdd:COG4152 16 AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDS----GEVLWDGEPLDPED--------RRRIGYLPEER--G 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 118 LNPVWTVGSQIK--EALRAnniATGSEAHKKAIELLEQAGLP-NAKKRIDqyphEFSGGMRQRALIAMGLAAHPKLLIAD 194
Cdd:COG4152 82 LYPKMKVGEQLVylARLKG---LSKAEAKRRADEWLERLGLGdRANKKVE----ELSKGNQQKVQLIAALLHDPELLILD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 195 EPTSALD---VTVAKK-ILDHLDKltselGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVltRPQHPYTK--- 267
Cdd:COG4152 155 EPFSGLDpvnVELLKDvIRELAAK-----GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI--RRQFGRNTlrl 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2524658687 268 QLIAAAPSLAARRGDRVVAAPT-------TSDADQKEIL---VAKNLVRDFAIR 311
Cdd:COG4152 228 EADGDAGWLRALPGVTVVEEDGdgaelklEDGADAQELLralLARGPVREFEEV 281
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
38-260 |
5.79e-28 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 117.93 E-value: 5.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPgdgeVTGGTITFDGRDITHLTDREFvsirGNGIGLVPQDPmtN 117
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWP----PTAGSVRLDGADLSQWDREEL----GRHIGYLPQDV--E 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 118 LNPvwtvGSqIKEalranNIATGSEAH-KKAIELLEQAG-------LPNA-KKRIDQYPHEFSGGMRQRaliaMGLA--- 185
Cdd:COG4618 417 LFD----GT-IAE-----NIARFGDADpEKVVAAAKLAGvhemilrLPDGyDTRIGEGGARLSGGQRQR----IGLAral 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2524658687 186 -AHPKLLIADEPTSALDVTVAKKILDHLDKLTSElGTSVVLITHDLGLAAErADRLVVMQAGRVVETGPALQVLTR 260
Cdd:COG4618 483 yGDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRPSLLAA-VDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
324-525 |
5.87e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 113.29 E-value: 5.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 324 VDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNrkeELELRRRIQPIFQNPyatldPMRT 403
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEEN---VWDIRHKIGMVFQNP-----DNQF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 404 VHSSIEEPLRI---HKIGTKKEREQRVFELLDRVALpAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVSALDV 480
Cdd:PRK13650 95 VGATVEDDVAFgleNKGIPHEEMKERVNEALELVGM-QDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDP 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2524658687 481 VVQAQVLELLAELQEEMDLAYLFITHDLAVVrQVADEVIVMEHGK 525
Cdd:PRK13650 174 EGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQ 217
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
41-257 |
6.74e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 113.22 E-value: 6.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 41 DVNLEVFPGETVAIVGESGSGKSTTAHAALGLLpgdgEVTGGTITFDGRDIT----HLTDrefvsIRGNgIGLVPQDPMt 116
Cdd:PRK13637 25 NVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLL----KPTSGKIIIDGVDITdkkvKLSD-----IRKK-VGLVFQYPE- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 117 nlnpvwtvgSQIKEALRANNIATG--------SEAHKKAIELLEQAGLPNAKKRiDQYPHEFSGGMRQRALIAMGLAAHP 188
Cdd:PRK13637 94 ---------YQLFEETIEKDIAFGpinlglseEEIENRVKRAMNIVGLDYEDYK-DKSPFELSGGQKRRVAIAGVVAMEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2524658687 189 KLLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQV 257
Cdd:PRK13637 164 KILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREV 232
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
325-533 |
6.79e-28 |
|
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: 111.76 E-value: 6.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 325 DDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEELELRRR-IQPIFQNpyATLDPMRT 403
Cdd:COG4181 29 KGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARLRARhVGFVFQS--FQLLPTLT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 404 VHSSIEEPLrihKIGTKKEREQRVFELLDRVALpaemGRR---FPGELSGGQRQRVAIARALALNPEVVVCDEAVSALDV 480
Cdd:COG4181 107 ALENVMLPL---ELAGRRDARARARALLERVGL----GHRldhYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDA 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2524658687 481 VVQAQVlellaelqeeMDLayLF------------ITHDLAVVRQvADEVIVMEHGKMVEHRPTD 533
Cdd:COG4181 180 ATGEQI----------IDL--LFelnrergttlvlVTHDPALAAR-CDRVLRLRAGRLVEDTAAT 231
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
30-265 |
7.67e-28 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 114.82 E-value: 7.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 30 RRSKSLTDVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGDGevtgGTITFDGRDITHLTDREFVSIRGNGIGL 109
Cdd:TIGR02142 4 RFSKRLGDFSLDADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDE----GEIVLNGRTLFDSRKGIFLPPEKRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 110 VPQDpmTNLNPVWTVGSQIKEALRANNIATGSEAHKKAIELLEQAGLpnakkrIDQYPHEFSGGMRQRALIAMGLAAHPK 189
Cdd:TIGR02142 80 VFQE--ARLFPHLSVRGNLRYGMKRARPSERRISFERVIELLGIGHL------LGRLPGRLSGGEKQRVAIGRALLSSPR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2524658687 190 LLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVLTRPQHPY 265
Cdd:TIGR02142 152 LLLMDEPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPW 227
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
323-527 |
8.27e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 112.87 E-value: 8.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 323 AVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGkrVQGRNRKEELELRRRIQPIFQNPYATLdpmr 402
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG--LDTSDEENLWDIRNKAGMVFQNPDNQI---- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 403 tVHSSIEEPLRI--HKIGTK-KEREQRVFELLDRVALpAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVSALD 479
Cdd:PRK13633 99 -VATIVEEDVAFgpENLGIPpEEIRERVDESLKKVGM-YEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2524658687 480 VVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQvADEVIVMEHGKMV 527
Cdd:PRK13633 177 PSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVV 223
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
41-298 |
1.02e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 112.81 E-value: 1.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 41 DVNLEVFPGETVAIVGESGSGKSTTAHAALGLLpgdgEVTGGTITFDGRDITHLTD-REFVSIRgNGIGLVPQDPMtnln 119
Cdd:PRK13634 25 DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLL----QPTSGTVTIGERVITAGKKnKKLKPLR-KKVGIVFQFPE---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 120 pvwtvgSQIKEALRANNIATG--------SEAHKKAIELLEQAGLPnaKKRIDQYPHEFSGGMRQRALIAMGLAAHPKLL 191
Cdd:PRK13634 96 ------HQLFEETVEKDICFGpmnfgvseEDAKQKAREMIELVGLP--EELLARSPFELSGGQMRRVAIAGVLAMEPEVL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 192 IADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVLTRPQHPYTKQL-- 269
Cdd:PRK13634 168 VLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDELEAIGLdl 247
|
250 260 270
....*....|....*....|....*....|..
gi 2524658687 270 ---IAAAPSLAARRGDRVVAAPTTSDADQKEI 298
Cdd:PRK13634 248 petVKFKRALEEKFGISFPKPCLTLEELAHEV 279
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
199-538 |
1.05e-27 |
|
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: 117.12 E-value: 1.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 199 ALDVTVAKKILDHLDKLTSELGTSVVLIthdLGLAAERADRL-------VVMQAGRVVetgPALQVLTRPQHPYTKQLiA 271
Cdd:TIGR02203 230 AMKMTSAGSISSPITQLIASLALAVVLF---IALFQAQAGSLtagdftaFITAMIALI---RPLKSLTNVNAPMQRGL-A 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 272 AAPSLAArrgdrVVAAPTTSDADQKEILVAKNLVRDFAIrgDRPWRKDSFRAVDDISFTLRRGRTIGIVGESGSGKSTVA 351
Cdd:TIGR02203 303 AAESLFT-----LLDSPPEKDTGTRAIERARGDVEFRNV--TFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLV 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 352 NMALGLLDPTEGEVLFDGKRVQGRNRKEeleLRRRIQPIFQNPYATLDpmrTVHSSIEEPLRIHKIGTKKEREQRVFELL 431
Cdd:TIGR02203 376 NLIPRFYEPDSGQILLDGHDLADYTLAS---LRRQVALVSQDVVLFND---TIANNIAYGRTEQADRAEIERALAAAYAQ 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 432 DRV-ALPaeMGRRFP-----GELSGGQRQRVAIARALALNPEVVVCDEAVSALDV----VVQAQVLELLAELQEemdlay 501
Cdd:TIGR02203 450 DFVdKLP--LGLDTPigengVLLSGGQRQRLAIARALLKDAPILILDEATSALDNeserLVQAALERLMQGRTT------ 521
|
330 340 350
....*....|....*....|....*....|....*..
gi 2524658687 502 LFITHDLAVVrQVADEVIVMEHGKMVEHRPTDDLFDH 538
Cdd:TIGR02203 522 LVIAHRLSTI-EKADRIVVMDDGRIVERGTHNELLAR 557
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
322-528 |
1.09e-27 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 110.38 E-value: 1.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 322 RAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQgrnrkEELELRRRIQPIFQNPyaTLDPM 401
Cdd:cd03268 14 RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ-----KNIEALRRIGALIEAP--GFYPN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 402 RTVHSSIEEPLRIHKIgtkkeREQRVFELLDRVALPAEMGRRFpGELSGGQRQRVAIARALALNPEVVVCDEAVSALDVV 481
Cdd:cd03268 87 LTARENLRLLARLLGI-----RKKRIDEVLDVVGLKDSAKKKV-KGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2524658687 482 VQAQVlellaeLQEEMDLA-----YLFITHDLAVVRQVADEVIVMEHGKMVE 528
Cdd:cd03268 161 GIKEL------RELILSLRdqgitVLISSHLLSEIQKVADRIGIINKGKLIE 206
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
38-258 |
1.38e-27 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 110.78 E-value: 1.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLpgdgEVTGGTITFDGRDIthlTDREFVSIRgNGIGLVPQDPmtn 117
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFY----DPQKGQILIDGIDI---RDISRKSLR-SMIGVVLQDT--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 118 lnpvWTVGSQIKEALR-ANNIATGSEahkkAIELLEQAGLPN-AKKRIDQYPHE-------FSGGMRQRALIAMGLAAHP 188
Cdd:cd03254 87 ----FLFSGTIMENIRlGRPNATDEE----VIEAAKEAGAHDfIMKLPNGYDTVlgenggnLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 189 KLLIADEPTSALDVTVAKKILDHLDKLTSelGTSVVLITHDLGlAAERADRLVVMQAGRVVETGPALQVL 258
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLS-TIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
326-518 |
1.42e-27 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 110.68 E-value: 1.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 326 DISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEELELR-RRIQPIFQnpYATLDPMRTV 404
Cdd:PRK11629 27 NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRnQKLGFIYQ--FHHLLPDFTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 405 HSSIEEPLRIHKIGTKkEREQRVFELLDRVALPAEMGRRfPGELSGGQRQRVAIARALALNPEVVVCDEAVSALDVVVQA 484
Cdd:PRK11629 105 LENVAMPLLIGKKKPA-EINSRALEMLAAVGLEHRANHR-PSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNAD 182
|
170 180 190
....*....|....*....|....*....|....
gi 2524658687 485 QVLELLAELQEEMDLAYLFITHDLAVVRQVADEV 518
Cdd:PRK11629 183 SIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQL 216
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
38-254 |
1.62e-27 |
|
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: 109.54 E-value: 1.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLlpGDGEVTGGTITFDGRDITHLTDREFVsirGNGIGLVPQdpmtn 117
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH--PKYEVTEGEILFKGEDITDLPPEERA---RLGIFLAFQ----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 118 lNPVWTVGSQIKEALRANNIAtgseahkkaielleqaglpnakkridqypheFSGGMRQRALIAMGLAAHPKLLIADEPT 197
Cdd:cd03217 85 -YPPEIPGVKNADFLRYVNEG-------------------------------FSGGEKKRNEILQLLLLEPDLAILDEPD 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2524658687 198 SALDVTVAKKILDHLDKLTSElGTSVVLITHDLGLAAE-RADRLVVMQAGRVVETGPA 254
Cdd:cd03217 133 SGLDIDALRLVAEVINKLREE-GKSVLIITHYQRLLDYiKPDRVHVLYDGRIVKSGDK 189
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
326-539 |
1.82e-27 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 117.13 E-value: 1.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 326 DISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEeleLRRRIQPIFQNP--YAtldpmRT 403
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHY---LHRQVALVGQEPvlFS-----GS 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 404 VHSSIEEPLRihkiGTKKEREQRVFELLDRVALPAEMGRRFPGE-------LSGGQRQRVAIARALALNPEVVVCDEAVS 476
Cdd:TIGR00958 571 VRENIAYGLT----DTPDEEIMAAAKAANAHDFIMEFPNGYDTEvgekgsqLSGGQKQRIAIARALVRKPRVLILDEATS 646
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2524658687 477 ALDVVVQAQVLELLAELqeemDLAYLFITHDLAVVRQvADEVIVMEHGKMVEHRPTDDLFDHP 539
Cdd:TIGR00958 647 ALDAECEQLLQESRSRA----SRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
326-546 |
1.88e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 111.29 E-value: 1.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 326 DISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQ-GRN--RKEELELRRRIQPIFQNPYATldPMR 402
Cdd:PRK14246 28 DITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYfGKDifQIDAIKLRKEVGMVFQQPNPF--PHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 403 TVHSSIEEPLRIHKIGTKKEREQRVFELLDRVALPAEMGRRF---PGELSGGQRQRVAIARALALNPEVVVCDEAVSALD 479
Cdd:PRK14246 106 SIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLnspASQLSGGQQQRLTIARALALKPKVLLMDEPTSMID 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2524658687 480 VVVQAQVLELLAELQEEMdlAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDLFDHPEKEYTQR 546
Cdd:PRK14246 186 IVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEK 250
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
41-284 |
1.90e-27 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 110.25 E-value: 1.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 41 DVNLEVFPGETVAIVGESGSGKSTTahaaLGLLPGDGEVTGGTITFDGRDITHLTDREFVsirgngiglVPQDpmTNLNP 120
Cdd:TIGR01184 3 GVNLTIQQGEFISLIGHSGCGKSTL----LNLISGLAQPTSGGVILEGKQITEPGPDRMV---------VFQN--YSLLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 121 VWTVGSQIKEALRANNiATGSEAHKKAI--ELLEQAGLPNAKkriDQYPHEFSGGMRQRALIAMGLAAHPKLLIADEPTS 198
Cdd:TIGR01184 68 WLTVRENIALAVDRVL-PDLSKSERRAIveEHIALVGLTEAA---DKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 199 ALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQV-LTRPQHpytKQLIAAAPSLA 277
Cdd:TIGR01184 144 ALDALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRPRD---RLEVVEDPSYY 220
|
....*..
gi 2524658687 278 ARRGDRV 284
Cdd:TIGR01184 221 DLRNEAL 227
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
305-522 |
1.99e-27 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 109.88 E-value: 1.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 305 VRDFAI-RGDRPwrkdsfrAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDP---TEGEVLFDGKRVQGRNrkee 380
Cdd:COG4136 4 LENLTItLGGRP-------LLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALP---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 381 lELRRRIQPIFQNPYatLDPmrtvHSSIEEPLRI---HKIGtKKEREQRVFELLDRVALpAEMGRRFPGELSGGQRQRVA 457
Cdd:COG4136 73 -AEQRRIGILFQDDL--LFP----HLSVGENLAFalpPTIG-RAQRRARVEQALEEAGL-AGFADRDPATLSGGQRARVA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2524658687 458 IARALALNPEVVVCDEAVSALDVVVQAQVLELLAELQEEMDLAYLFITHDLAVVrQVADEVIVME 522
Cdd:COG4136 144 LLRALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDA-PAAGRVLDLG 207
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
11-251 |
2.05e-27 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 111.11 E-value: 2.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 11 PILTLKDVCIGFPTTTASgrrskslTDVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPgdgeVTGGTITFDGRD 90
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQP-------QPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLA----PSSGEITLDGVP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 91 ITHL-TDRefvsirgngiGLVPQDpmTNLNPVWTVGSQIKEALRANNIATgSEAHKKAIELLEQAGLPNAKKRidqYPHE 169
Cdd:COG4525 71 VTGPgADR----------GVVFQK--DALLPWLNVLDNVAFGLRLRGVPK-AERRARAEELLALVGLADFARR---RIWQ 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 170 FSGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQA--GR 247
Cdd:COG4525 135 LSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPgpGR 214
|
....
gi 2524658687 248 VVET 251
Cdd:COG4525 215 IVER 218
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
283-540 |
2.58e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 112.25 E-value: 2.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 283 RVVAAPTTSDADqkEILVAKNLVRDFAIRGDRPwrkdsFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTE 362
Cdd:PRK13631 8 KKLKVPNPLSDD--IILRVKNLYCVFDEKQENE-----LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 363 GEVL---------FDGKRVQGRNRKEEL----ELRRRIQPIFQNPYATLdpmrtVHSSIEEPLRIHKI--GTKKER-EQR 426
Cdd:PRK13631 81 GTIQvgdiyigdkKNNHELITNPYSKKIknfkELRRRVSMVFQFPEYQL-----FKDTIEKDIMFGPValGVKKSEaKKL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 427 VFELLDRVALPAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVSALDVVVQAQVlellaelqeeMDL------- 499
Cdd:PRK13631 156 AKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEM----------MQLildakan 225
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2524658687 500 --AYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDLFDHPE 540
Cdd:PRK13631 226 nkTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQH 268
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
318-527 |
3.10e-27 |
|
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: 108.88 E-value: 3.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 318 KDSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRkeelelRRRIQPIFQNPYAT 397
Cdd:cd03226 10 KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKER------RKSIGYVMQDVDYQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 398 LdpmrtVHSSIEEPLRIhKIGTKKEREQRVFELLDRVALpAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVSA 477
Cdd:cd03226 84 L-----FTDSVREELLL-GLKELDAGNEQAETVLKDLDL-YALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2524658687 478 LDVVVQAQVlELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMV 527
Cdd:cd03226 157 LDYKNMERV-GELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
316-537 |
3.61e-27 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 109.88 E-value: 3.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 316 WRKDSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEeleLRRRIQPIFQNpy 395
Cdd:cd03252 10 YKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAW---LRRQVGVVLQE-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 396 ATLdpmrtVHSSIEEPLRIHKIGTKKEREQRVFELLDRVALPAEM--------GRRFPGeLSGGQRQRVAIARALALNPE 467
Cdd:cd03252 85 NVL-----FNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELpegydtivGEQGAG-LSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 468 VVVCDEAVSALDvvVQAQVLELLAELQEEMDLAYLFITHDLAVVRQvADEVIVMEHGKMVEHRPTDDLFD 537
Cdd:cd03252 159 ILIFDEATSALD--YESEHAIMRNMHDICAGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLA 225
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
38-243 |
4.32e-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: 115.08 E-value: 4.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPgdgeVTGGTITFDGRDITHLTdrefVSIRGNGIGLVPQDPmtn 117
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVD----PTEGSIAVNGVPLADAD----ADSWRDQIAWVPQHP--- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 118 lnpvwtvgsQIKEALRANNIATG-SEAHKKAI-ELLEQAGLPNAKK--------RIDQYPHEFSGGMRQRALIAMGLAAH 187
Cdd:TIGR02857 406 ---------FLFAGTIAENIRLArPDASDAEIrEALERAGLDEFVAalpqgldtPIGEGGAGLSGGQAQRLALARAFLRD 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2524658687 188 PKLLIADEPTSALDVTVAKKILDHLDKLTSelGTSVVLITHDLGLaAERADRLVVM 243
Cdd:TIGR02857 477 APLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLAL-AALADRIVVL 529
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
40-252 |
8.28e-27 |
|
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: 114.53 E-value: 8.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 40 HDVNLEVFPGETVAIVGESGSGKSTTAHaalgLLPGDGEVTGGTITFDGRDITHLTDRefvSIRGNgIGLVPQDpmtnln 119
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLAR----LLFRFYDVTSGRILIDGQDIRDVTQA---SLRAA-IGIVPQD------ 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 120 pvwTV--GSQIkealrANNIATG----SEAhkkaiELLEQAGLPNAKKRIDQYPHEF-----------SGGMRQRALIAM 182
Cdd:COG5265 441 ---TVlfNDTI-----AYNIAYGrpdaSEE-----EVEAAARAAQIHDFIESLPDGYdtrvgerglklSGGEKQRVAIAR 507
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 183 GLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSelGTSVVLITHDLGLAAeRADRLVVMQAGRVVETG 252
Cdd:COG5265 508 TLLKNPPILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAHRLSTIV-DADEILVLEAGRIVERG 574
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
321-535 |
1.00e-26 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 107.91 E-value: 1.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 321 FRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRnrKEELELRRRI------QPIFQNp 394
Cdd:cd03224 13 SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGL--PPHERARAGIgyvpegRRIFPE- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 395 yatldpMrTVHSSIEEPLRIHKIGTKKEREQRVFELLDRVAlpaEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEA 474
Cdd:cd03224 90 ------L-TVEENLLLGAYARRRAKRKARLERVYELFPRLK---ERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2524658687 475 VSALDVVVQAQVlELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDL 535
Cdd:cd03224 160 SEGLAPKIVEEI-FEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
7-254 |
1.78e-26 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 112.81 E-value: 1.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 7 TSAAPILTLKDVCIgfptttasgrRSKSLTDVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPgdgeVTGGTITF 86
Cdd:COG3845 252 EPGEVVLEVENLSV----------RDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRP----PASGSIRL 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 87 DGRDITHLTDREfvsIRGNGIGLVPQDPMTN-LNPVWTV------GSQIKEALRANNIATGSEAHKKAIELLEQ----AG 155
Cdd:COG3845 318 DGEDITGLSPRE---RRRLGVAYIPEDRLGRgLVPDMSVaenlilGRYRRPPFSRGGFLDRKAIRAFAEELIEEfdvrTP 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 156 LPNAKKRidqyphEFSGGMRQRALIAMGLAAHPKLLIADEPTSALDV----TVAKKILDHLDKltselGTSVVLITHDLG 231
Cdd:COG3845 395 GPDTPAR------SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVgaieFIHQRLLELRDA-----GAAVLLISEDLD 463
|
250 260
....*....|....*....|...
gi 2524658687 232 LAAERADRLVVMQAGRVVETGPA 254
Cdd:COG3845 464 EILALSDRIAVMYEGRIVGEVPA 486
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
323-527 |
1.87e-26 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 107.29 E-value: 1.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 323 AVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKeelELRRRIQPIFQNP---YATLD 399
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPA---DLRRNIGYVPQDVtlfYGTLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 400 ---PMRTVHSSIEEPLRIHKIGTkkereqrVFELLDRvaLPAEMGRRFpGE----LSGGQRQRVAIARALALNPEVVVCD 472
Cdd:cd03245 96 dniTLGAPLADDERILRAAELAG-------VTDFVNK--HPNGLDLQI-GErgrgLSGGQRQAVALARALLNDPPILLLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2524658687 473 EAVSALDVVVQAQVLELLAELQEEMDLayLFITHDLAVVrQVADEVIVMEHGKMV 527
Cdd:cd03245 166 EPTSAMDMNSEERLKERLRQLLGDKTL--IIITHRPSLL-DLVDRIIVMDSGRIV 217
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
297-540 |
2.09e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 108.64 E-value: 2.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 297 EILVAKNLVRDFAIRGDrpwrkdsFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRN 376
Cdd:PRK13642 3 KILEVENLVFKYEKESD-------VNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAEN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 377 rkeELELRRRIQPIFQNPyatldPMRTVHSSIEEPLRIHKIGTKKEREQRVfELLDRVALPAEM---GRRFPGELSGGQR 453
Cdd:PRK13642 76 ---VWNLRRKIGMVFQNP-----DNQFVGATVEDDVAFGMENQGIPREEMI-KRVDEALLAVNMldfKTREPARLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 454 QRVAIARALALNPEVVVCDEAVSALDVVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQvADEVIVMEHGKMVEHRPTD 533
Cdd:PRK13642 147 QRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPS 225
|
....*..
gi 2524658687 534 DLFDHPE 540
Cdd:PRK13642 226 ELFATSE 232
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
315-526 |
3.20e-26 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 106.79 E-value: 3.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 315 PWRKDSfRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEeleLRRRIQPIFQNP 394
Cdd:cd03248 22 PTRPDT-LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKY---LHSKVSLVGQEP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 395 YATldpMRTVHSSIEEPLRIHKIGTKKEREQRV----FELLDRVALPAEMGRRfPGELSGGQRQRVAIARALALNPEVVV 470
Cdd:cd03248 98 VLF---ARSLQDNIAYGLQSCSFECVKEAAQKAhahsFISELASGYDTEVGEK-GSQLSGGQKQRVAIARALIRNPQVLI 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2524658687 471 CDEAVSALDVVVQAQVLELLAELQEemDLAYLFITHDLAVVRQvADEVIVMEHGKM 526
Cdd:cd03248 174 LDEATSALDAESEQQVQQALYDWPE--RRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
298-535 |
3.90e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 108.27 E-value: 3.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 298 ILVAKNLVRDFAirgdrpwrkdSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNR 377
Cdd:COG4152 1 MLELKGLTKRFG----------DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 378 K------EELELRRRIQPIFQNPY-ATLDPMrtvhssieeplrihkigTKKEREQRVFELLDRVALPAEMGRRFpGELSG 450
Cdd:COG4152 71 RrigylpEERGLYPKMKVGEQLVYlARLKGL-----------------SKAEAKRRADEWLERLGLGDRANKKV-EELSK 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 451 GQRQRVAIARALALNPEVVVCDEAVSALDVVVQAQVlellaeLQEEMDLAY-----LFITHDLAVVRQVADEVIVMEHGK 525
Cdd:COG4152 133 GNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELL------KDVIRELAAkgttvIFSSHQMELVEELCDRIVIINKGR 206
|
250
....*....|
gi 2524658687 526 MVEHRPTDDL 535
Cdd:COG4152 207 KVLSGSVDEI 216
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
12-249 |
3.98e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 107.48 E-value: 3.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 12 ILTLKDVCIGFPTTTASGRRsksltdVVHDVNLEVFPGETVAIVGESGSGKSTTahaaLGLLPGDGEVTGGTITFDGRDI 91
Cdd:COG1101 1 MLELKNLSKTFNPGTVNEKR------ALDGLNLTIEEGDFVTVIGSNGAGKSTL----LNAIAGSLPPDSGSILIDGKDV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 92 THLTDREfvsiRGNGIGLVPQDPMTNlnpvwTVGS-QIKEAL-------RANNIATGSEAHKKAI--ELLEQAGLpNAKK 161
Cdd:COG1101 71 TKLPEYK----RAKYIGRVFQDPMMG-----TAPSmTIEENLalayrrgKRRGLRRGLTKKRRELfrELLATLGL-GLEN 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 162 RIDQYPHEFSGGMRQrAL-IAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRL 240
Cdd:COG1101 141 RLDTKVGLLSGGQRQ-ALsLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRL 219
|
....*....
gi 2524658687 241 VVMQAGRVV 249
Cdd:COG1101 220 IMMHEGRII 228
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
38-248 |
4.00e-26 |
|
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: 104.99 E-value: 4.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPgdgeVTGGTITFDGRDITHLTDREFvsirGNGIGLVPQDpmtn 117
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLR----PTSGRVRLDGADISQWDPNEL----GDHVGYLPQD---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 118 lnpvwtvgsqikealranniatgseahkkaIELLEQAGLPNAkkridqypheFSGGMRQRALIAMGLAAHPKLLIADEPT 197
Cdd:cd03246 85 ------------------------------DELFSGSIAENI----------LSGGQRQRLGLARALYGNPRILVLDEPN 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2524658687 198 SALDVTVAKKILDHLDKLtSELGTSVVLITHDLGLAAeRADRLVVMQAGRV 248
Cdd:cd03246 125 SHLDVEGERALNQAIAAL-KAAGATRIVIAHRPETLA-SADRILVLEDGRV 173
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
324-553 |
6.32e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 106.85 E-value: 6.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 324 VDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLD-----PTEGEVLFDGKRVQGRNrKEELELRRRIQPIFQ--NPYa 396
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPD-VDPIEVRREVGMVFQypNPF- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 397 tldPMRTVHSSIEEPLRIHK-IGTKKEREQRVFELLDRVALPAEMGRR---FPGELSGGQRQRVAIARALALNPEVVVCD 472
Cdd:PRK14267 98 ---PHLTIYDNVAIGVKLNGlVKSKKELDERVEWALKKAALWDEVKDRlndYPSNLSGGQRQRLVIARALAMKPKILLMD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 473 EAVSALDVVVQAQVLELLAELQEemDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDLFDHPEKEYTQRLLDAIP 552
Cdd:PRK14267 175 EPTANIDPVGTAKIEELLFELKK--EYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEKYVTGAL 252
|
.
gi 2524658687 553 G 553
Cdd:PRK14267 253 G 253
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
11-259 |
7.23e-26 |
|
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: 106.32 E-value: 7.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 11 PILTLKDVCIgfptttasgRRSKslTDVVHDVNLEVFPGETVAIVGESGSGKSTtahaALGLLPGD------------GE 78
Cdd:COG1119 2 PLLELRNVTV---------RRGG--KTILDDISWTVKPGEHWAILGPNGAGKST----LLSLITGDlpptygndvrlfGE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 79 VTGGTITFDgrdithltdrefvsIRGNgIGLVPQDpMTNLNPVWTVGSQIkealrannIATGS------------EAHKK 146
Cdd:COG1119 67 RRGGEDVWE--------------LRKR-IGLVSPA-LQLRFPRDETVLDV--------VLSGFfdsiglyreptdEQRER 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 147 AIELLEQAGLpnaKKRIDQYPHEFSGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLI 226
Cdd:COG1119 123 ARELLELLGL---AHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLV 199
|
250 260 270
....*....|....*....|....*....|...
gi 2524658687 227 THDLGLAAERADRLVVMQAGRVVETGPALQVLT 259
Cdd:COG1119 200 THHVEEIPPGITHVLLLKDGRVVAAGPKEEVLT 232
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
38-252 |
9.12e-26 |
|
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: 104.99 E-value: 9.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGDGevtgGTITFDGRDITHLTDREfvsirgNGIGLVPQDPmtN 117
Cdd:cd03268 15 VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDS----GEITFDGKSYQKNIEAL------RRIGALIEAP--G 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 118 LNPVWTVgsqiKEALRANNIATGSEaHKKAIELLEQAGLPN-AKKRIDQYphefSGGMRQRALIAMGLAAHPKLLIADEP 196
Cdd:cd03268 83 FYPNLTA----RENLRLLARLLGIR-KKRIDEVLDVVGLKDsAKKKVKGF----SLGMKQRLGIALALLGNPDLLILDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2524658687 197 TSALDVTVAKKILDHLDKLTSElGTSVVLITHDLGLAAERADRLVVMQAGRVVETG 252
Cdd:cd03268 154 TNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
324-530 |
9.46e-26 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 105.57 E-value: 9.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 324 VDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEeleLRRRIQPIFQNPYATLDpmrT 403
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEI---YRQQVSYCAQTPTLFGD---T 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 404 VHSSIEEPLRIHKigtKKEREQRVFELLDRVALPAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVSALDVVVQ 483
Cdd:PRK10247 97 VYDNLIFPWQIRN---QQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNK 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2524658687 484 AQVLELLAELQEEMDLAYLFITHDLAVVRQvADEVIVMEH--GKMVEHR 530
Cdd:PRK10247 174 HNVNEIIHRYVREQNIAVLWVTHDKDEINH-ADKVITLQPhaGEMQEAR 221
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
38-273 |
1.10e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 106.08 E-value: 1.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGL--LPGDGEVTGGTITFdGRDItHLTDREFVSIRGNgIGLVPQDPm 115
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLleLNEEARVEGEVRLF-GRNI-YSPDVDPIEVRRE-VGMVFQYP- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 116 tNLNPVWTVGSQIKEALRANNIATGSEAHKKAIE-LLEQAGL-PNAKKRIDQYPHEFSGGMRQRALIAMGLAAHPKLLIA 193
Cdd:PRK14267 95 -NPFPHLTIYDNVAIGVKLNGLVKSKKELDERVEwALKKAALwDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLM 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 194 DEPTSALDVTVAKKILDHLDKLTSELgtSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVLTRPQHPYTKQLIAAA 273
Cdd:PRK14267 174 DEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEKYVTGA 251
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
37-252 |
1.48e-25 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 105.26 E-value: 1.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 37 DVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGDgevtGGTITFDGRDIThLTDREFVSIRgngIGLVPQDPMt 116
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPE----NGRVLVDGHDLA-LADPAWLRRQ---VGVVLQENV- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 117 nlnpvwTVGSQIKEalranNIATGSEAHKKAiELLEQAGLPNAKKRIDQYPHEF-----------SGGMRQRALIAMGLA 185
Cdd:cd03252 87 ------LFNRSIRD-----NIALADPGMSME-RVIEAAKLAGAHDFISELPEGYdtivgeqgaglSGGQRQRIAIARALI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2524658687 186 AHPKLLIADEPTSALDVTVAKKILDHLDKLTSelGTSVVLITHDLGlAAERADRLVVMQAGRVVETG 252
Cdd:cd03252 155 HNPRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLS-TVKNADRIIVMEKGRIVEQG 218
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
316-535 |
1.54e-25 |
|
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: 111.20 E-value: 1.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 316 WRKDSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEeleLRRRIQPIFQNPy 395
Cdd:TIGR03797 461 YRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQA---VRRQLGVVLQNG- 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 396 atldpmRTVHSSIEEPLRIHKIGTKKEreqrVFELLDRVALpAEMGRRFP-----------GELSGGQRQRVAIARALAL 464
Cdd:TIGR03797 537 ------RLMSGSIFENIAGGAPLTLDE----AWEAARMAGL-AEDIRAMPmgmhtviseggGTLSGGQRQRLLIARALVR 605
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2524658687 465 NPEVVVCDEAVSALDVVVQAQVlellAELQEEMDLAYLFITHDLAVVRQvADEVIVMEHGKMVEHRPTDDL 535
Cdd:TIGR03797 606 KPRILLFDEATSALDNRTQAIV----SESLERLKVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYDEL 671
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
298-540 |
1.59e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 106.32 E-value: 1.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 298 ILVAKNLVRDFairgdrpwrKDSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQgRNR 377
Cdd:PRK13639 1 ILETRDLKYSY---------PDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK-YDK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 378 KEELELRRRIQPIFQNPYATLDPMRTVHSSIEEPLrihKIGTKKER-EQRVFELLDRVALPAeMGRRFPGELSGGQRQRV 456
Cdd:PRK13639 71 KSLLEVRKTVGIVFQNPDDQLFAPTVEEDVAFGPL---NLGLSKEEvEKRVKEALKAVGMEG-FENKPPHHLSGGQKKRV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 457 AIARALALNPEVVVCDEAVSALDVVVQAQVlellaelqeeMDLAY---------LFITHDLAVVRQVADEVIVMEHGKMV 527
Cdd:PRK13639 147 AIAGILAMKPEIIVLDEPTSGLDPMGASQI----------MKLLYdlnkegitiIISTHDVDLVPVYADKVYVMSDGKII 216
|
250
....*....|...
gi 2524658687 528 EHRPTDDLFDHPE 540
Cdd:PRK13639 217 KEGTPKEVFSDIE 229
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
39-252 |
1.92e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 106.40 E-value: 1.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 39 VHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLpgdgEVTGGTITFDGRDITHLT-DREFVSIRGNgIGLVPQDPMTN 117
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALL----KPTTGTVTVDDITITHKTkDKYIRPVRKR-IGMVFQFPESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 118 LNPVwTVGSQIKEALRANNIATgSEAHKKAIELLEQAGLPnaKKRIDQYPHEFSGG-MRQRALIAMgLAAHPKLLIADEP 196
Cdd:PRK13646 98 LFED-TVEREIIFGPKNFKMNL-DEVKNYAHRLLMDLGFS--RDVMSQSPFQMSGGqMRKIAIVSI-LAMNPDIIVLDEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2524658687 197 TSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETG 252
Cdd:PRK13646 173 TAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQT 228
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
38-252 |
1.92e-25 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 104.20 E-value: 1.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETvAIVGESGSGKSTTAHAALGLLPGDGevtgGTITFDGRDIThltdREFVSIRGNgIGLVPQDPMTN 117
Cdd:cd03264 15 ALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSS----GTIRIDGQDVL----KQPQKLRRR-IGYLPQEFGVY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 118 lnPVWTVGSQIKEALRANNIAtGSEAHKKAIELLEQAGLPNAKKRidqYPHEFSGGMRQRALIAMGLAAHPKLLIADEPT 197
Cdd:cd03264 85 --PNFTVREFLDYIAWLKGIP-SKEVKARVDEVLELVNLGDRAKK---KIGSLSGGMRRRVGIAQALVGDPSILIVDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2524658687 198 SALDvtVAKKIldHLDKLTSELGTS--VVLITHDLGLAAERADRLVVMQAGRVVETG 252
Cdd:cd03264 159 AGLD--PEERI--RFRNLLSELGEDriVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
323-528 |
2.09e-25 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 110.49 E-value: 2.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 323 AVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVqgrnRKEELE-LRRRIQPIFQNPYATLDpm 401
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDL----RDYTLAsLRNQVALVSQNVHLFND-- 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 402 rTVHSSIEeplriHKIGTKKEREQrvFELLDRVALPAEMGRRFP-------GE----LSGGQRQRVAIARALALNPEVVV 470
Cdd:PRK11176 432 -TIANNIA-----YARTEQYSREQ--IEEAARMAYAMDFINKMDngldtviGEngvlLSGGQRQRIAIARALLRDSPILI 503
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2524658687 471 CDEAVSALDV----VVQAQVLELLAelqeemDLAYLFITHDLAVVRQvADEVIVMEHGKMVE 528
Cdd:PRK11176 504 LDEATSALDTeserAIQAALDELQK------NRTSLVIAHRLSTIEK-ADEILVVEDGEIVE 558
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
11-252 |
2.97e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 105.22 E-value: 2.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 11 PILTLKDVCIGFPTTTAsgrrsksLTdvVHDVNLEVFPGETVAIVGESGSGKSTTAHaalgLLPGDGEVTGGTITFDGRD 90
Cdd:PRK13648 6 SIIVFKNVSFQYQSDAS-------FT--LKDVSFNIPKGQWTSIVGHNGSGKSTIAK----LMIGIEKVKSGEIFYNNQA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 91 IThltDREFVSIRGNgIGLVPQDPMTNLnpvwtVGSQIKEALR---ANNIATGSEAHKKAIELLEQAGLPNakkRIDQYP 167
Cdd:PRK13648 73 IT---DDNFEKLRKH-IGIVFQNPDNQF-----VGSIVKYDVAfglENHAVPYDEMHRRVSEALKQVDMLE---RADYEP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 168 HEFSGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAErADRLVVMQAGR 247
Cdd:PRK13648 141 NALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGT 219
|
....*
gi 2524658687 248 VVETG 252
Cdd:PRK13648 220 VYKEG 224
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
39-252 |
3.26e-25 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 109.67 E-value: 3.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 39 VHDVNLEVFPGETVAIVGESGSGKSTTahaaLGLLPGDGEVTGGTITFDGRDITHLTDRefvSIRGNgIGLVPQDPMTnL 118
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTL----INLLQRVFDPQSGRILIDGTDIRTVTRA---SLRRN-IAVVFQDAGL-F 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 119 NpvwtvgSQIKEalranNIATGSEAHKKAiELLEQAGLPNAKKRIDQYPHEF-----------SGGMRQRALIAMGLAAH 187
Cdd:PRK13657 422 N------RSIED-----NIRVGRPDATDE-EMRAAAERAQAHDFIERKPDGYdtvvgergrqlSGGERQRLAIARALLKD 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2524658687 188 PKLLIADEPTSALDVTVAKKILDHLDKLTSelGTSVVLITHDLGLAAErADRLVVMQAGRVVETG 252
Cdd:PRK13657 490 PPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAHRLSTVRN-ADRILVFDNGRVVESG 551
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
326-527 |
5.17e-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: 102.96 E-value: 5.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 326 DISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEelelrRRIQPIFQ--NPYATLDPMRT 403
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD-----RPVSMLFQenNLFAHLTVEQN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 404 VHSSIEEPLRIhkigtKKEREQRVFELLDRVALpAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVSALDVVVQ 483
Cdd:cd03298 91 VGLGLSPGLKL-----TAEDRQAIEVALARVGL-AGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2524658687 484 AQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMV 527
Cdd:cd03298 165 AEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
37-273 |
8.37e-25 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 103.51 E-value: 8.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 37 DVVHDVNLEVFPGETVAIVGESGSGKSTTAHAaLGLLPGDGEvtgGTITFDGRDIT---------HLTDREFVSIRGNGI 107
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRC-INFLEKPSE---GSIVVNGQTINlvrdkdgqlKVADKNQLRLLRTRL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 108 GLVPQDpmTNLNPVWTVGSQIKEALRANNIATGSEAHKKAIELLEQAGLPNAKKriDQYPHEFSGGMRQRALIAMGLAAH 187
Cdd:PRK10619 95 TMVFQH--FNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQ--GKYPVHLSGGQQQRVSIARALAME 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 188 PKLLIADEPTSALDVTVAKKILDHLDKLTSElGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVLTRPQHPYTK 267
Cdd:PRK10619 171 PEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQ 249
|
....*.
gi 2524658687 268 QLIAAA 273
Cdd:PRK10619 250 QFLKGS 255
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
270-521 |
8.48e-25 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 108.14 E-value: 8.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 270 IAAAPSLAA--RRGDRVVAAPTTSDADQKEILVAKNLvrDFAIRGDRPwrkdsfrAVDDISFTLRRGRTIGIVGESGSGK 347
Cdd:TIGR02857 291 VAAAEALFAvlDAAPRPLAGKAPVTAAPASSLEFSGV--SVAYPGRRP-------ALRPVSFTVPPGERVALVGPSGAGK 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 348 STVANMALGLLDPTEGEVLFDGKRVQGRNRKeelELRRRIQPIFQNPYatldpmrTVHSSIEEPLRIHKIGTKKEREQRV 427
Cdd:TIGR02857 362 STLLNLLLGFVDPTEGSIAVNGVPLADADAD---SWRDQIAWVPQHPF-------LFAGTIAENIRLARPDASDAEIREA 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 428 FEL--LDRV--ALPA----EMGRRfPGELSGGQRQRVAIARALALNPEVVVCDEAVSALDVVVQAQVLELLAELQEEMDL 499
Cdd:TIGR02857 432 LERagLDEFvaALPQgldtPIGEG-GAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTV 510
|
250 260
....*....|....*....|..
gi 2524658687 500 ayLFITHDLAVVRqVADEVIVM 521
Cdd:TIGR02857 511 --LLVTHRLALAA-LADRIVVL 529
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
319-527 |
8.51e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 104.16 E-value: 8.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 319 DSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQgRNRKEELELRRRIQPIFQNPYATL 398
Cdd:PRK13636 17 DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPID-YSRKGLMKLRESVGMVFQDPDNQL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 399 dpmrtVHSSIEEPLRIHKIGT---KKEREQRVFELLDRVALpAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAV 475
Cdd:PRK13636 96 -----FSASVYQDVSFGAVNLklpEDEVRKRVDNALKRTGI-EHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2524658687 476 SALDVVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMV 527
Cdd:PRK13636 170 AGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVI 221
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
318-527 |
1.02e-24 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 102.45 E-value: 1.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 318 KDSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQgrnrKEELELRRRIQPIFQNpyAT 397
Cdd:cd03266 15 KKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVV----KEPAEARRRLGFVSDS--TG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 398 LDPMRTVHSSIEEPLRIHkiGTKK-EREQRVFELLDRVALPAEMGRRfPGELSGGQRQRVAIARALALNPEVVVCDEAVS 476
Cdd:cd03266 89 LYDRLTARENLEYFAGLY--GLKGdELTARLEELADRLGMEELLDRR-VGGFSTGMRQKVAIARALVHDPPVLLLDEPTT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2524658687 477 ALDVVVqAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMV 527
Cdd:cd03266 166 GLDVMA-TRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
36-270 |
1.04e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 103.07 E-value: 1.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 36 TDVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGDGEV-TGGTITFDGRDITHLtdrEFVSIRGNgIGLVPQDP 114
Cdd:PRK14247 16 VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEArVSGEVYLDGQDIFKM---DVIELRRR-VQMVFQIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 115 mtNLNPVWTVGSQIKEALRANNIA-TGSEAHKKAIELLEQAGL-PNAKKRIDQYPHEFSGGMRQRALIAMGLAAHPKLLI 192
Cdd:PRK14247 92 --NPIPNLSIFENVALGLKLNRLVkSKKELQERVRWALEKAQLwDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2524658687 193 ADEPTSALDVTVAKKILDHLDKLTSELgtSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVLTRPQHPYTKQLI 270
Cdd:PRK14247 170 ADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELTEKYV 245
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
38-259 |
1.21e-24 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 103.17 E-value: 1.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLL-PgdgevTGGTITFDGRDITHLTDREFvsirGNGIGLVPQDPMT 116
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLtP-----QSGTVFLGDKPISMLSSRQL----ARRLALLPQHHLT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 117 N---------------LNPVWTVGSQIKEALRAnniatgseahkKAIELLEQAGLpnAKKRIDqyphEFSGGMRQRALIA 181
Cdd:PRK11231 88 PegitvrelvaygrspWLSLWGRLSAEDNARVN-----------QAMEQTRINHL--ADRRLT----DLSGGQRQRAFLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2524658687 182 MGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSElGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVLT 259
Cdd:PRK11231 151 MVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMT 227
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
324-528 |
1.45e-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: 108.11 E-value: 1.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 324 VDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQgrnrkeelELRRRI---------QPIFQNP 394
Cdd:TIGR03796 495 IENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPRE--------EIPREVlansvamvdQDIFLFE 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 395 YATLDPMRTVHSSI-EEPLR-------IHKIGTKkereqRVFELLDRVAlpaEMGRRFpgelSGGQRQRVAIARALALNP 466
Cdd:TIGR03796 567 GTVRDNLTLWDPTIpDADLVrackdaaIHDVITS-----RPGGYDAELA---EGGANL----SGGQRQRLEIARALVRNP 634
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2524658687 467 EVVVCDEAVSALDVVVQAQVLEllaelqeemDLAY-----LFITHDLAVVRQvADEVIVMEHGKMVE 528
Cdd:TIGR03796 635 SILILDEATSALDPETEKIIDD---------NLRRrgctcIIVAHRLSTIRD-CDEIIVLERGKVVQ 691
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
38-245 |
1.58e-24 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 101.40 E-value: 1.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPgdgeVTGGTITFDGRDIthltDREFVSIRGNgIGLVPQDPMtn 117
Cdd:COG4133 17 LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLP----PSAGEVLWNGEPI----RDAREDYRRR-LAYLGHADG-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 118 LNPVWTVGsqikEALRANNIATGSEAHKKAI-ELLEQAGLPnakKRIDQYPHEFSGGMRQRALIAMGLAAHPKLLIADEP 196
Cdd:COG4133 86 LKPELTVR----ENLRFWAALYGLRADREAIdEALEAVGLA---GLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2524658687 197 TSALDV----TVAKKILDHLDKltselGTSVVLITHDLgLAAERADRLVVMQA 245
Cdd:COG4133 159 FTALDAagvaLLAELIAAHLAR-----GGAVLLTTHQP-LELAAARVLDLGDF 205
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-282 |
1.76e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 103.25 E-value: 1.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 8 SAAPILTLKDVCIGFPTTTasgrrsksltdVVHDVNLEvFPGETV-AIVGESGSGKST---TAHAALGLLPG---DGEVT 80
Cdd:PRK14271 17 AAAPAMAAVNLTLGFAGKT-----------VLDQVSMG-FPARAVtSLMGPTGSGKTTflrTLNRMNDKVSGyrySGDVL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 81 -GGTITFDGRDITHLTDRefvsirgngIGLVPQDPmtnlNPV-WTVGSQIKEALRANNIATGSEAHKKAIELLEQAGLPN 158
Cdd:PRK14271 85 lGGRSIFNYRDVLEFRRR---------VGMLFQRP----NPFpMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 159 A-KKRIDQYPHEFSGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSELgtSVVLITHDLGLAAERA 237
Cdd:PRK14271 152 AvKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARIS 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2524658687 238 DRLVVMQAGRVVETGPALQVLTRPQHPYTKQLIA--AAPSLAARRGD 282
Cdd:PRK14271 230 DRAALFFDGRLVEEGPTEQLFSSPKHAETARYVAglSGDVKDAKRGN 276
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
38-273 |
1.88e-24 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 105.30 E-value: 1.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETVAIVGESGSGKSTTahaaLGLLPGDGEVTGGTITFDGRDITHltdrefvsirgngiglVP--QDPM 115
Cdd:PRK11607 34 AVDDVSLTIYKGEIFALLGASGCGKSTL----LRMLAGFEQPTAGQIMLDGVDLSH----------------VPpyQRPI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 116 T------NLNPVWTVGSQIKEALRANNIATGsEAHKKAIELLEQAGLPNAKKRidqYPHEFSGGMRQRALIAMGLAAHPK 189
Cdd:PRK11607 94 NmmfqsyALFPHMTVEQNIAFGLKQDKLPKA-EIASRVNEMLGLVHMQEFAKR---KPHQLSGGQRQRVALARSLAKRPK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 190 LLIADEPTSALDvtvaKKILDHLD----KLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVLTRPQHPY 265
Cdd:PRK11607 170 LLLLDEPMGALD----KKLRDRMQlevvDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRY 245
|
....*...
gi 2524658687 266 TKQLIAAA 273
Cdd:PRK11607 246 SAEFIGSV 253
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
38-252 |
2.20e-24 |
|
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: 101.20 E-value: 2.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGDGevtgGTITFDGRDITHLTdrefvsirGNGIGLVPQDpmTN 117
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDS----GEVLFDGKPLDIAA--------RNRIGYLPEE--RG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 118 LNPVWTVGSQIK--EALRANNIatgSEAHKKAIELLEQAGL-PNAKKRIDqyphEFSGGMRQRALIAMGLAAHPKLLIAD 194
Cdd:cd03269 81 LYPKMKVIDQLVylAQLKGLKK---EEARRRIDEWLERLELsEYANKRVE----ELSKGNQQKVQFIAAVIHDPELLILD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2524658687 195 EPTSALDVTVAKKILDHLDKLTSElGTSVVLITHDLGLAAERADRLVVMQAGRVVETG 252
Cdd:cd03269 154 EPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
38-258 |
2.28e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 103.63 E-value: 2.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETVAIVGESGSGKST-TAHAALGLLPGDGEVTggtITFDGRDITHLTDREFVSIRGNGIGLVPQDPMT 116
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTfIEHLNALLLPDTGTIE---WIFKDEKNKKKTKEKEKVLEKLVIQKTRFKKIK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 117 NLNPVWT-VGS-------QIKEALRANNIATG--------SEAHKKAIELLEQAGLPnaKKRIDQYPHEFSGGMRQRALI 180
Cdd:PRK13651 99 KIKEIRRrVGVvfqfaeyQLFEQTIEKDIIFGpvsmgvskEEAKKRAAKYIELVGLD--ESYLQRSPFELSGGQKRRVAL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2524658687 181 AMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSElGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVL 258
Cdd:PRK13651 177 AGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDIL 253
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
30-253 |
2.40e-24 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 101.42 E-value: 2.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 30 RRSKSLTDVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLpgdgEVTGGTITFDGRDITHLTDREfvsIRGNgIGL 109
Cdd:cd03244 11 RYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLV----ELSSGSILIDGVDISKIGLHD---LRSR-ISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 110 VPQDPMT-------NLNP--VWTvGSQIKEALRANNIATGSEAHKKAIELLEQAGLPNakkridqypheFSGGMRQRALI 180
Cdd:cd03244 83 IPQDPVLfsgtirsNLDPfgEYS-DEELWQALERVGLKEFVESLPGGLDTVVEEGGEN-----------LSVGQRQLLCL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2524658687 181 AMGLAAHPKLLIADEPTSALDVTVAKKIldhLDKLTSEL-GTSVVLITHDLGLAAErADRLVVMQAGRVVETGP 253
Cdd:cd03244 151 ARALLRKSKILVLDEATASVDPETDALI---QKTIREAFkDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFDS 220
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
322-527 |
2.51e-24 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 100.82 E-value: 2.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 322 RAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQ--GRNR----KEELELRRRIQPIFQNPY 395
Cdd:cd03269 14 TALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDiaARNRigylPEERGLYPKMKVIDQLVY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 396 -ATLDPMrtvhssieeplrihkigTKKEREQRVFELLDRVALPAEMGRRFPgELSGGQRQRVAIARALALNPEVVVCDEA 474
Cdd:cd03269 94 lAQLKGL-----------------KKEEARRRIDEWLERLELSEYANKRVE-ELSKGNQQKVQFIAAVIHDPELLILDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2524658687 475 VSALDvVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMV 527
Cdd:cd03269 156 FSGLD-PVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
13-261 |
3.05e-24 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 107.12 E-value: 3.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 13 LTLKDVCIGFPTttasgrRSKSLtdVVHDVNLEVFPGETVAIVGESGSGKSTTAhaalGLLPGDGEVTGGTITFDGRDIT 92
Cdd:TIGR00958 479 IEFQDVSFSYPN------RPDVP--VLKGLTFTLHPGEVVALVGPSGSGKSTVA----ALLQNLYQPTGGQVLLDGVPLV 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 93 HLtdrEFVSIRGNgIGLVPQDPMtnlnpVWtvGSQIKEalranNIATGSEAHKKAiELLEQAGLPNAKKRIDQYPHEF-- 170
Cdd:TIGR00958 547 QY---DHHYLHRQ-VALVGQEPV-----LF--SGSVRE-----NIAYGLTDTPDE-EIMAAAKAANAHDFIMEFPNGYdt 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 171 ---------SGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKildhLDKLTSELGTSVVLITHDLGLaAERADRLV 241
Cdd:TIGR00958 610 evgekgsqlSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQL----LQESRSRASRTVLLIAHRLST-VERADQIL 684
|
250 260
....*....|....*....|
gi 2524658687 242 VMQAGRVVETGPALQVLTRP 261
Cdd:TIGR00958 685 VLKKGSVVEMGTHKQLMEDQ 704
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
11-270 |
3.17e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 101.78 E-value: 3.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 11 PILTLKDVCIGFptttasgRRSKSLtdvvHDVNLEVFPGETVAIVGESGSGKSTTAHAA--LG-LLPgdgEVT-GGTITF 86
Cdd:PRK14239 4 PILQVSDLSVYY-------NKKKAL----NSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNdLNP---EVTiTGSIVY 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 87 DGRDI-THLTDRefVSIRGNgIGLVPQDPmtnlNPV-WTVGSQIKEALRANNIATGSEAHKKAIELLEQAGLPN-AKKRI 163
Cdd:PRK14239 70 NGHNIySPRTDT--VDLRKE-IGMVFQQP----NPFpMSIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASIWDeVKDRL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 164 DQYPHEFSGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSELgtSVVLITHDLGLAAERADRLVVM 243
Cdd:PRK14239 143 HDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFF 220
|
250 260
....*....|....*....|....*..
gi 2524658687 244 QAGRVVETGPALQVLTRPQHPYTKQLI 270
Cdd:PRK14239 221 LDGDLIEYNDTKQMFMNPKHKETEDYI 247
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
318-540 |
3.86e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 102.19 E-value: 3.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 318 KDSFR-AVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDP---TEGEVLFDGKRVqgrNRKEELELRRRIQPIFQN 393
Cdd:PRK13640 16 PDSKKpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITL---TAKTVWDIREKVGIVFQN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 394 PyatldPMRTVHSSIEEPLR--IHKIGTKKEREQR-VFELLDRVALpAEMGRRFPGELSGGQRQRVAIARALALNPEVVV 470
Cdd:PRK13640 93 P-----DNQFVGATVGDDVAfgLENRAVPRPEMIKiVRDVLADVGM-LDYIDSEPANLSGGQKQRVAIAGILAVEPKIII 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 471 CDEAVSALDVVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQvADEVIVMEHGKMVEHRPTDDLFDHPE 540
Cdd:PRK13640 167 LDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSPVEIFSKVE 235
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
321-540 |
5.52e-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: 5.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 321 FRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRnRKEEL---------ELRRriqpIF 391
Cdd:COG0410 16 IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGL-PPHRIarlgigyvpEGRR----IF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 392 qnpyATLdpmrtvhsSIEEPLRI-----HKIGTKKEREQRVFELLDRVAlpaEMGRRFPGELSGGQRQRVAIARALALNP 466
Cdd:COG0410 91 ----PSL--------TVEENLLLgayarRDRAEVRADLERVYELFPRLK---ERRRQRAGTLSGGEQQMLAIGRALMSRP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2524658687 467 EVVVCDEAVSALDVVVQAQVlELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDLFDHPE 540
Cdd:COG0410 156 KLLLLDEPSLGLAPLIVEEI-FEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
54-270 |
7.75e-24 |
|
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: 102.57 E-value: 7.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 54 IVGESGSGKSTTahaaLGLLPGDGEVTGGTITFDGRDITHltdrefVSIRGNGIGLVPQDpmTNLNPVWTVGSQIKEALR 133
Cdd:TIGR01187 1 LLGPSGCGKTTL----LRLLAGFEQPDSGSIMLDGEDVTN------VPPHLRHINMVFQS--YALFPHMTVEENVAFGLK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 134 ANniatGSEAHKKAIELLEQAGLPNAKKRIDQYPHEFSGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLD 213
Cdd:TIGR01187 69 MR----KVPRAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELK 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2524658687 214 KLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVLTRPQHPYTKQLI 270
Cdd:TIGR01187 145 TIQEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFI 201
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
38-244 |
1.05e-23 |
|
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated C-P lysase complex. This protein (PhnL) and the adjacent-encoded PhnK (TIGR02323) resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this C-P lyase complex rather than part of a transporter per se.
Pssm-ID: 131377 [Multi-domain] Cd Length: 224 Bit Score: 99.39 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETVAIVGESGSGKSTTAHAALG-LLPGDGEV---TGGTITfdgrDITHLTDREFVSIRGNGIGLVPQd 113
Cdd:TIGR02324 23 VLKNVSLTVNAGECVALSGPSGAGKSTLLKSLYAnYLPDSGRIlvrHEGAWV----DLAQASPREVLEVRRKTIGYVSQ- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 114 pMTNLNPVWTVGSQIKEALRANNIATgSEAHKKAIELLEQAGLPnaKKRIDQYPHEFSGGMRQRALIAMGLAAHPKLLIA 193
Cdd:TIGR02324 98 -FLRVIPRVSALEVVAEPLLERGVPR-EAARARARELLARLNIP--ERLWHLPPATFSGGEQQRVNIARGFIADYPILLL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2524658687 194 DEPTSALDVTVAKKILDHLDKLTSElGTSVVLITHDLGLAAERADRLVVMQ 244
Cdd:TIGR02324 174 DEPTASLDAANRQVVVELIAEAKAR-GAALIGIFHDEEVRELVADRVMDVT 223
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
42-259 |
1.06e-23 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 100.30 E-value: 1.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 42 VNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGDGEvtggtITFDGRDITHLTDREFVSIRGNgigLVPQDPMTNLNPV 121
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQGE-----ILLNGRPLSDWSAAELARHRAY---LSQQQSPPFAMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 122 WTVgsqIKEALRANniaTGSEAHKKAI-ELLEQAGLPnakkriDQYP---HEFSGGMRQRALIAM-------GLAAHPKL 190
Cdd:COG4138 87 FQY---LALHQPAG---ASSEAVEQLLaQLAEALGLE------DKLSrplTQLSGGEWQRVRLAAvllqvwpTINPEGQL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2524658687 191 LIADEPTSALDvtVAKKILdhLDKLTSEL---GTSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVLT 259
Cdd:COG4138 155 LLLDEPMNSLD--VAQQAA--LDRLLRELcqqGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMT 222
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
322-553 |
1.40e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 99.85 E-value: 1.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 322 RAVDDISFTLRRGRTIGIVGESGSGKSTV--ANMALGLLDP---TEGEVLFDGKRVQGRnRKEELELRRRIQPIFQ--NP 394
Cdd:PRK14239 19 KALNSVSLDFYPNEITALIGPSGSGKSTLlrSINRMNDLNPevtITGSIVYNGHNIYSP-RTDTVDLRKEIGMVFQqpNP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 395 YatldPMrTVHSSIEEPLRIHKIGTKKEREQRVFELLDRVALPAEMGRRFPGE---LSGGQRQRVAIARALALNPEVVVC 471
Cdd:PRK14239 98 F----PM-SIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASIWDEVKDRLHDSalgLSGGQQQRVCIARVLATSPKIILL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 472 DEAVSALDVVVQAQVLELLAELQEemDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDLFDHPEKEYTQrllDAI 551
Cdd:PRK14239 173 DEPTSALDPISAGKIEETLLGLKD--DYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKHKETE---DYI 247
|
..
gi 2524658687 552 PG 553
Cdd:PRK14239 248 SG 249
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
299-480 |
1.51e-23 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 98.71 E-value: 1.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 299 LVAKNLVRdfaIRGDRPwrkdsfrAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVqgrnRK 378
Cdd:COG4133 3 LEAENLSC---RRGERL-------LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI----RD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 379 EELELRRRIQPIFqnPYATLDPMRTVhssiEEPLRIH-KIGTKKEREQRVFELLDRVALpAEMGRRFPGELSGGQRQRVA 457
Cdd:COG4133 69 AREDYRRRLAYLG--HADGLKPELTV----RENLRFWaALYGLRADREAIDEALEAVGL-AGLADLPVRQLSAGQKRRVA 141
|
170 180
....*....|....*....|...
gi 2524658687 458 IARALALNPEVVVCDEAVSALDV 480
Cdd:COG4133 142 LARLLLSPAPLWLLDEPFTALDA 164
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
318-540 |
1.94e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 100.26 E-value: 1.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 318 KDSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEeleLRRRIQPIFQNPyat 397
Cdd:PRK13652 14 SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIRE---VRKFVGLVFQNP--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 398 ldPMRTVHSSIEEPLRIHKI--GTKKER-EQRVFELLDRVALpAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEA 474
Cdd:PRK13652 88 --DDQIFSPTVEQDIAFGPInlGLDEETvAHRVSSALHMLGL-EELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2524658687 475 VSALDVVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDLFDHPE 540
Cdd:PRK13652 165 TAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPD 230
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
10-261 |
3.00e-23 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 102.23 E-value: 3.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 10 APILTLKDVCIGFPTTTasgrrsksltdVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLpgdgEVTGGTITFDGR 89
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTT-----------VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTL----TPTAGTVLVAGD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 90 DITHLTDREFvsirGNGIGLVPQDpmTNLNPVWTVgSQIKEALRA---NNIATGSEAHKKAIE-LLEQAGlpnAKKRIDQ 165
Cdd:PRK09536 66 DVEALSARAA----SRRVASVPQD--TSLSFEFDV-RQVVEMGRTphrSRFDTWTETDRAAVErAMERTG---VAQFADR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 166 YPHEFSGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSElGTSVVLITHDLGLAAERADRLVVMQA 245
Cdd:PRK09536 136 PVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLAD 214
|
250
....*....|....*.
gi 2524658687 246 GRVVETGPALQVLTRP 261
Cdd:PRK09536 215 GRVRAAGPPADVLTAD 230
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
41-269 |
3.53e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 99.43 E-value: 3.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 41 DVNLEVFPGETVAIVGESGSGKSTTahaaLGLLPGDGEVTGGTITFDGRDIT-HLTDREFVSIRGNgIGLVPQDPMtnln 119
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTI----MQLLNGLHVPTQGSVRVDDTLITsTSKNKDIKQIRKK-VGLVFQFPE---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 120 pvwtvgSQIKEALRANNIATG--------SEAHKKAIELLEQAGLpnAKKRIDQYPHEFSGGMRQRALIAMGLAAHPKLL 191
Cdd:PRK13649 96 ------SQLFEETVLKDVAFGpqnfgvsqEEAEALAREKLALVGI--SESLFEKNPFELSGGQMRRVAIAGILAMEPKIL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2524658687 192 IADEPTSALDVTVAKKILDHLDKLtSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVLTRPQHPYTKQL 269
Cdd:PRK13649 168 VLDEPTAGLDPKGRKELMTLFKKL-HQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQDVDFLEEKQL 244
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
324-553 |
4.33e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 99.40 E-value: 4.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 324 VDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEG-----EVLFDGKRVqgRNRKEELELRRRIQPIFQ--NPYa 396
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSI--FNYRDVLEFRRRVGMLFQrpNPF- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 397 tldPMrTVHSSIEEPLRIHKIGTKKEREQRVFELLDRVALPAEMGRRF---PGELSGGQRQRVAIARALALNPEVVVCDE 473
Cdd:PRK14271 114 ---PM-SIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLsdsPFRLSGGQQQLLCLARTLAVNPEVLLLDE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 474 AVSALDVVVQAQVLELLAELQEEmdLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDLFDHPEKEYTQRLLDAIPG 553
Cdd:PRK14271 190 PTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVAGLSG 267
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
39-258 |
5.26e-23 |
|
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: 102.57 E-value: 5.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 39 VHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLL-PGDGEVTggtiTFDGRDITHLTDREFVSiRGNG---IGLVPQDp 114
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLePTSGEVN----VRVGDEWVDMTKPGPDG-RGRAkryIGILHQE- 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 115 mTNLNPVWTVGSQIKEALranNIATGSE-AHKKAIELLEQAGLPNAKKR--IDQYPHEFSGGMRQRALIAMGLAAHPKLL 191
Cdd:TIGR03269 374 -YDLYPHRTVLDNLTEAI---GLELPDElARMKAVITLKMVGFDEEKAEeiLDKYPDELSEGERHRVALAQVLIKEPRIV 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2524658687 192 IADEPTSALD----VTVAKKILdhldKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVL 258
Cdd:TIGR03269 450 ILDEPTGTMDpitkVDVTHSIL----KAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIV 516
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
321-524 |
5.61e-23 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 100.30 E-value: 5.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 321 FRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEelelrRRIQPIFQNpYAtLDP 400
Cdd:PRK11650 17 TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD-----RDIAMVFQN-YA-LYP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 401 MRTVHSSIEEPLRIHKIGtKKEREQRVFELLDRVALPAEMGRRfPGELSGGQRQRVAIARALALNPEVVVCDEAVSALDV 480
Cdd:PRK11650 90 HMSVRENMAYGLKIRGMP-KAEIEERVAEAARILELEPLLDRK-PRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2524658687 481 VVQAQVLELLAELQEEMDLAYLFITHDlavvrQV-----ADEVIVMEHG 524
Cdd:PRK11650 168 KLRVQMRLEIQRLHRRLKTTSLYVTHD-----QVeamtlADRVVVMNGG 211
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
13-252 |
6.10e-23 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 102.79 E-value: 6.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 13 LTLKDVcigfpTTTASGRRSKSLtdvvHDVNLEVFPGETVAIVGESGSGKSTTAHaalgLLPGDGEVTGGTITFDGRDit 92
Cdd:PRK11176 342 IEFRNV-----TFTYPGKEVPAL----RNINFKIPAGKTVALVGRSGSGKSTIAN----LLTRFYDIDEGEILLDGHD-- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 93 hLTDREFVSIRgNGIGLVPQDpmtnlnpVWTVGSQIkealrANNIATGSEAHKKAIELLEQAGLPNAKKRIDQYPHEF-- 170
Cdd:PRK11176 407 -LRDYTLASLR-NQVALVSQN-------VHLFNDTI-----ANNIAYARTEQYSREQIEEAARMAYAMDFINKMDNGLdt 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 171 ---------SGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSElGTSVVlITHDLGlAAERADRLV 241
Cdd:PRK11176 473 vigengvllSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKN-RTSLV-IAHRLS-TIEKADEIL 549
|
250
....*....|.
gi 2524658687 242 VMQAGRVVETG 252
Cdd:PRK11176 550 VVEDGEIVERG 560
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
38-251 |
6.51e-23 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 98.23 E-value: 6.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETVAIVGESGSGKSTTahaaLGLLPGDGEVTGGTITFDGRDITHLTDREFVSIRGNGigLVP-QDPMT 116
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTL----LNLIAGFVPYQHGSITLDGKPVEGPGAERGVVFQNEG--LLPwRNVQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 117 NLnpvwTVGSQIKEALRANNIATgseahkkAIELLEQAGLPNAKKRidqYPHEFSGGMRQRALIAMGLAAHPKLLIADEP 196
Cdd:PRK11248 90 NV----AFGLQLAGVEKMQRLEI-------AHQMLKKVGLEGAEKR---YIWQLSGGQRQRVGIARALAANPQLLLLDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2524658687 197 TSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQ--AGRVVET 251
Cdd:PRK11248 156 FGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSpgPGRVVER 212
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
322-536 |
6.58e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 99.04 E-value: 6.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 322 RAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEELE-LRRRIQPIFQNPYATLDP 400
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKpVRKKVGVVFQFPESQLFE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 401 MRTVHSSIEEPlriHKIGTKKEREQRVF-ELLDRVALPAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVSALD 479
Cdd:PRK13643 100 ETVLKDVAFGP---QNFGIPKEKAEKIAaEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2524658687 480 VVVQAQVLELLAELQEEMDLAYLfITHDLAVVRQVADEVIVMEHGKMVEHRPTDDLF 536
Cdd:PRK13643 177 PKARIEMMQLFESIHQSGQTVVL-VTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
326-525 |
6.63e-23 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 100.49 E-value: 6.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 326 DISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVqgrNRKEELElrRRIQPIFQNpYAtLDPMRTVH 405
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRM---NDVPPAE--RGVGMVFQS-YA-LYPHLSVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 406 SSIEEPLRIHKIGtKKEREQRVFELLDRVALPAEMGRRfPGELSGGQRQRVAIARALALNPEVVVCDEAVSALDVVVQAQ 485
Cdd:PRK11000 94 ENMSFGLKLAGAK-KEEINQRVNQVAEVLQLAHLLDRK-PKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQ 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2524658687 486 VLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGK 525
Cdd:PRK11000 172 MRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGR 211
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
301-527 |
1.13e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 98.62 E-value: 1.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 301 AKNLVRDFAIRgdRPWrkdSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLF---DGKRVQGRNR 377
Cdd:PRK13651 5 VKNIVKIFNKK--LPT---ELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkDEKNKKKTKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 378 KEEL------------------ELRRRIQPIFQNPYATLdpmrtVHSSIEEPLRIHKIG---TKKEREQRVFELLDRVAL 436
Cdd:PRK13651 80 KEKVleklviqktrfkkikkikEIRRRVGVVFQFAEYQL-----FEQTIEKDIIFGPVSmgvSKEEAKKRAAKYIELVGL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 437 PAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVSALDVVVQAQVlELLAELQEEMDLAYLFITHDLAVVRQVAD 516
Cdd:PRK13651 155 DESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEI-LEIFDNLNKQGKTIILVTHDLDNVLEWTK 233
|
250
....*....|.
gi 2524658687 517 EVIVMEHGKMV 527
Cdd:PRK13651 234 RTIFFKDGKII 244
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
324-527 |
1.56e-22 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 97.11 E-value: 1.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 324 VDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVqGRNRKEELELRRRIQPifQnpyatldpmrt 403
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPL-AAWSPWELARRRAVLP--Q----------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 404 vHSSIEEPL---------RIHKIGTKKEREQRVFELLDRVALPAEMGRRFPgELSGGQRQRVAIARALA-------LNPE 467
Cdd:COG4559 83 -HSSLAFPFtveevvalgRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQ-TLSGGEQQRVQLARVLAqlwepvdGGPR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2524658687 468 VVVCDEAVSALDVVVQAQVlellaelqeeMDLAYLF---------ITHDLAVVRQVADEVIVMEHGKMV 527
Cdd:COG4559 161 WLFLDEPTSALDLAHQHAV----------LRLARQLarrgggvvaVLHDLNLAAQYADRILLLHQGRLV 219
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
322-527 |
1.64e-22 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 96.10 E-value: 1.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 322 RAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEELELRRRIQPIFQNPYATLDpm 401
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQIGMIFQDHHLLMD-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 402 RTVHSSIEEPLRIHKIGTKKEReQRVFELLDRVALpAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVSALDVV 481
Cdd:PRK10908 94 RTVYDNVAIPLIIAGASGDDIR-RRVSAALDKVGL-LDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2524658687 482 VQAQVlELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMV 527
Cdd:PRK10908 172 LSEGI-LRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
12-262 |
2.02e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 97.56 E-value: 2.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 12 ILTLKDVCIGFPTTTASgrrsksltdVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALG-LLPGDGEVTggTITFDGrd 90
Cdd:PRK13640 5 IVEFKHVSFTYPDSKKP---------ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlLLPDDNPNS--KITVDG-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 91 iTHLTDREFVSIRgNGIGLVPQDPmTNLNPVWTVGSQIKEALRaNNIATGSEAHKKAIELLEQAGLPNAkkrIDQYPHEF 170
Cdd:PRK13640 72 -ITLTAKTVWDIR-EKVGIVFQNP-DNQFVGATVGDDVAFGLE-NRAVPRPEMIKIVRDVLADVGMLDY---IDSEPANL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 171 SGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGlAAERADRLVVMQAGRVVE 250
Cdd:PRK13640 145 SGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDID-EANMADQVLVLDDGKLLA 223
|
250
....*....|..
gi 2524658687 251 TGPALQVLTRPQ 262
Cdd:PRK13640 224 QGSPVEIFSKVE 235
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
11-480 |
2.69e-22 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 100.08 E-value: 2.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 11 PILTLKDVCIGFPTTTAsgrrsksltdvVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGDgevtGGTITFDGRD 90
Cdd:PRK10762 3 ALLQLKGIDKAFPGVKA-----------LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRD----AGSILYLGKE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 91 IThltdreFVSIRGN---GIGLVPQDpmTNLNPVWTVgsqikealrANNIATGSE------------AHKKAIELLEQAG 155
Cdd:PRK10762 68 VT------FNGPKSSqeaGIGIIHQE--LNLIPQLTI---------AENIFLGREfvnrfgridwkkMYAEADKLLARLN 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 156 LPNAKKRIdqyPHEFSGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSElGTSVVLITH------- 228
Cdd:PRK10762 131 LRFSSDKL---VGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQ-GRGIVYISHrlkeife 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 229 ---------DLGLAAERA------DRLVVMQAGRVVETgpalqvltrpQHPYtkqliaaapsLAARRGDRVvaapttsda 293
Cdd:PRK10762 207 icddvtvfrDGQFIAEREvadlteDSLIEMMVGRKLED----------QYPR----------LDKAPGEVR--------- 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 294 dqkeiLVAKNLvrdfairgdrpwrkdSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQ 373
Cdd:PRK10762 258 -----LKVDNL---------------SGPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVV 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 374 GRNRKEEL--------ELRRRIQPI----------------FQNPYATLDPMRTvHSSIEEPLRIHKIGTkKEREQRVfe 429
Cdd:PRK10762 318 TRSPQDGLangivyisEDRKRDGLVlgmsvkenmsltalryFSRAGGSLKHADE-QQAVSDFIRLFNIKT-PSMEQAI-- 393
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 2524658687 430 lldrvalpaemgrrfpGELSGGQRQRVAIARALALNPEVVVCDEAVSALDV 480
Cdd:PRK10762 394 ----------------GLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDV 428
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
317-527 |
4.07e-22 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 94.88 E-value: 4.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 317 RKDSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQgRNRKeelELRRRIQPIFQnpYA 396
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR-TDRK---AARQSLGYCPQ--FD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 397 TLDPMRTVhssiEEPLRIH---KIGTKKEREQRVFELLDRVALPAEMGRRfPGELSGGQRQRVAIARALALNPEVVVCDE 473
Cdd:cd03263 85 ALFDELTV----REHLRFYarlKGLPKSEIKEEVELLLRVLGLTDKANKR-ARTLSGGMKRKLSLAIALIGGPSVLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2524658687 474 AVSALDVVVQAQVLELLAELQEemDLAYLFITHDLAVVRQVADEVIVMEHGKMV 527
Cdd:cd03263 160 PTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
8-230 |
4.62e-22 |
|
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: 99.74 E-value: 4.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 8 SAAPILTLKDVCIGFPTTTAsgrrsksltdVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGDGevtgGTITFD 87
Cdd:TIGR02868 330 LGKPTLELRDLSAGYPGAPP----------VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQ----GEVTLD 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 88 GRDITHLTDREFVSIrgngIGLVPQDPMTnlnpvwtVGSQIKEALR-ANNIATGSEAhkkaIELLEQAGLPNAkkrIDQY 166
Cdd:TIGR02868 396 GVPVSSLDQDEVRRR----VSVCAQDAHL-------FDTTVRENLRlARPDATDEEL----WAALERVGLADW---LRAL 457
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2524658687 167 PH-----------EFSGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSelGTSVVLITHDL 230
Cdd:TIGR02868 458 PDgldtvlgeggaRLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALS--GRTVVLITHHL 530
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
6-284 |
4.85e-22 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 98.10 E-value: 4.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 6 NTSAAPILTLKDVCIGFPTTTasgrrsksltdVVHDVNLEVFPGETVAIVGESGSGKSTtahaALGLLPGDGEVTGGTIT 85
Cdd:PRK09452 8 PSSLSPLVELRGISKSFDGKE-----------VISNLDLTINNGEFLTLLGPSGCGKTT----VLRLIAGFETPDSGRIM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 86 FDGRDITHLTdrefvsirgngiglvPQDPMTN-------LNPVWTVGSQIKEALRANNIATgSEAHKKAIELLEQAGLpn 158
Cdd:PRK09452 73 LDGQDITHVP---------------AENRHVNtvfqsyaLFPHMTVFENVAFGLRMQKTPA-AEITPRVMEALRMVQL-- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 159 aKKRIDQYPHEFSGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERAD 238
Cdd:PRK09452 135 -EEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSD 213
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2524658687 239 RLVVMQAGRVVETGPALQVLTRPQHPYTKQLIAAAPSLAARRGDRV 284
Cdd:PRK09452 214 RIVVMRDGRIEQDGTPREIYEEPKNLFVARFIGEINIFDATVIERL 259
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
24-249 |
5.60e-22 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 93.77 E-value: 5.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 24 TTTASGRRSKSLTDVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGDGevTGGTITFDGRDithLTDREFVSIr 103
Cdd:cd03213 10 TVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLG--VSGEVLINGRP---LDKRSFRKI- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 104 gngIGLVPQDPMtnLNPVWTVgsqiKEALRANniatgseAHKKAIelleqaglpnakkridqyphefSGGMRQRALIAMG 183
Cdd:cd03213 84 ---IGYVPQDDI--LHPTLTV----RETLMFA-------AKLRGL----------------------SGGERKRVSIALE 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2524658687 184 LAAHPKLLIADEPTSALDVTVAKKILDHLDKLtSELGTSVVLITHDL-GLAAERADRLVVMQAGRVV 249
Cdd:cd03213 126 LVSNPSLLFLDEPTSGLDSSSALQVMSLLRRL-ADTGRTIICSIHQPsSEIFELFDKLLLLSQGRVI 191
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
243-528 |
5.88e-22 |
|
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: 100.20 E-value: 5.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 243 MQAGRVveTGPALQvLTRPQHPYTKQLIAAApslaaRRGDrVVAAPTTSDADQKeilvAKNLVRDFAIRGDR---PWRKD 319
Cdd:TIGR01846 402 MLAGRV--TQPVLR-LAQLWQDFQQTGIALE-----RLGD-ILNSPTEPRSAGL----AALPELRGAITFENirfRYAPD 468
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 320 SFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQgrnRKEELELRRRIQPIFQNPYatld 399
Cdd:TIGR01846 469 SPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLA---IADPAWLRRQMGVVLQENV---- 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 400 pmrTVHSSIEEPLRIHKIGTKKEREQRVFELLDRVALPAEMGRRFP-------GELSGGQRQRVAIARALALNPEVVVCD 472
Cdd:TIGR01846 542 ---LFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELPQGYNtevgekgANLSGGQRQRIAIARALVGNPRILIFD 618
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2524658687 473 EAVSALDVVVQAQVLELLAELQEEMDLayLFITHDLAVVRQvADEVIVMEHGKMVE 528
Cdd:TIGR01846 619 EATSALDYESEALIMRNMREICRGRTV--IIIAHRLSTVRA-CDRIIVLEKGQIAE 671
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
10-275 |
6.46e-22 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 99.80 E-value: 6.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 10 APILTLKDVCIGFPtttaSGRRSkslTDVVHDVNLEVFPGETVAIVGESGSGKSTTAHaALGLLpgdGEVTGGTITFDGR 89
Cdd:PRK10535 2 TALLELKDIRRSYP----SGEEQ---VEVLKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCL---DKPTSGTYRVAGQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 90 DITHLTDREFVSIRGNGIGLVPQ--DPMTNLNPVWTVgsqikealRANNIATGSEAHK---KAIELLEQAGLpnaKKRID 164
Cdd:PRK10535 71 DVATLDADALAQLRREHFGFIFQryHLLSHLTAAQNV--------EVPAVYAGLERKQrllRAQELLQRLGL---EDRVE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 165 QYPHEFSGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLtSELGTSVVLITHDLGLAAErADRLVVMQ 244
Cdd:PRK10535 140 YQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAAQ-AERVIEIR 217
|
250 260 270
....*....|....*....|....*....|.
gi 2524658687 245 AGRVVETGPAlqVLTRPQHPYTKQLIAAAPS 275
Cdd:PRK10535 218 DGEIVRNPPA--QEKVNVAGGTEPVVNTASG 246
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
328-526 |
9.18e-22 |
|
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: 93.77 E-value: 9.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 328 SFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGrnrkeELELRRRIQPIFQ--NPYATLDPMRTVH 405
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTG-----LAPYQRPVSMLFQenNLFAHLTVRQNIG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 406 SSIEEPLRIHKigtkkEREQRVFELLDRVALpAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVSALDVVVQAQ 485
Cdd:TIGR01277 93 LGLHPGLKLNA-----EQQEKVVDAAQQVGI-ADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2524658687 486 VLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKM 526
Cdd:TIGR01277 167 MLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
319-543 |
1.21e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 95.05 E-value: 1.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 319 DSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGkrVQGRNRKEELELRRRIQPIFQNPyATL 398
Cdd:PRK13644 13 DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG--IDTGDFSKLQGIRKLVGIVFQNP-ETQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 399 DPMRTVHSSIE---EPLRIHKIGTKKereqrvfeLLDRVALPAEMGR---RFPGELSGGQRQRVAIARALALNPEVVVCD 472
Cdd:PRK13644 90 FVGRTVEEDLAfgpENLCLPPIEIRK--------RVDRALAEIGLEKyrhRSPKTLSGGQGQCVALAGILTMEPECLIFD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2524658687 473 EAVSALDVVVQAQVLELLAELQEEMDlAYLFITHDLAVVrQVADEVIVMEHGKMVEHRPTDDLFDHPEKEY 543
Cdd:PRK13644 162 EVTSMLDPDSGIAVLERIKKLHEKGK-TIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDVSLQT 230
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
323-528 |
1.38e-21 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 91.99 E-value: 1.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 323 AVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQgrnrKEELELRRRIQPIFQNPYatldpmr 402
Cdd:cd03247 17 VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVS----DLEKALSSLISVLNQRPY------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 403 tvhssieeplrihkigtkkereqrvfelLDRVALPAEMGRRFpgelSGGQRQRVAIARALALNPEVVVCDEAVSALDVVV 482
Cdd:cd03247 86 ----------------------------LFDTTLRNNLGRRF----SGGERQRLALARILLQDAPIVLLDEPTVGLDPIT 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2524658687 483 QAQVLELLAELQEemDLAYLFITHDLAVVRQVaDEVIVMEHGKMVE 528
Cdd:cd03247 134 ERQLLSLIFEVLK--DKTLIWITHHLTGIEHM-DKILFLENGKIIM 176
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
38-262 |
1.41e-21 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 93.94 E-value: 1.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPgdgeVTGGTITFDGRDITHLTdrefVSIRG-NGIGLVPQDP-- 114
Cdd:COG1137 18 VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVK----PDSGRIFLDGEDITHLP----MHKRArLGIGYLPQEAsi 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 115 MTNLnpvwTVGSQIKEALRANNIaTGSEAHKKAIELLEQAGLpnAKKRiDQYPHEFSGGMRQRALIAMGLAAHPKLLIAD 194
Cdd:COG1137 90 FRKL----TVEDNILAVLELRKL-SKKEREERLEELLEEFGI--THLR-KSKAYSLSGGERRRVEIARALATNPKFILLD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2524658687 195 EPTSALD-VTVA--KKILDHLdkltSELGTSvVLIT-HD----LGLaaerADRLVVMQAGRVVETGPALQVLTRPQ 262
Cdd:COG1137 162 EPFAGVDpIAVAdiQKIIRHL----KERGIG-VLITdHNvretLGI----CDRAYIISEGKVLAEGTPEEILNNPL 228
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
39-272 |
1.43e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 94.80 E-value: 1.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 39 VHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLpgdgEVTGGTITFDGRDithLTDREFVSIRgNGIGLVPQDPMTNL 118
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLL----EAESGQIIIDGDL---LTEENVWDIR-HKIGMVFQNPDNQF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 119 npvwtVGSQIKEalranNIATGSE----AHKKAIELLEQA----GLPNAKKRidqYPHEFSGGMRQRALIAMGLAAHPKL 190
Cdd:PRK13650 95 -----VGATVED-----DVAFGLEnkgiPHEEMKERVNEAlelvGMQDFKER---EPARLSGGQKQRVAIAGAVAMRPKI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 191 LIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAeRADRLVVMQAGRVVETGPALQVLTRPQH------- 263
Cdd:PRK13650 162 IILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRELFSRGNDllqlgld 240
|
250
....*....|
gi 2524658687 264 -PYTKQLIAA 272
Cdd:PRK13650 241 iPFTTSLVQS 250
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
299-526 |
1.55e-21 |
|
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: 91.89 E-value: 1.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 299 LVAKNLVrdFAIRGDRPWRkdsfraVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGkrvqgrnrk 378
Cdd:cd03246 1 LEVENVS--FRYPGAEPPV------LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDG--------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 379 eelelrrriQPIFQnpyatLDPMRtvhssieepLRIHkIGTkkereqrvfeLLDRVALpaemgrrFPGE-----LSGGQR 453
Cdd:cd03246 64 ---------ADISQ-----WDPNE---------LGDH-VGY----------LPQDDEL-------FSGSiaeniLSGGQR 102
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2524658687 454 QRVAIARALALNPEVVVCDEAVSALDV----VVQAQVLELLAELQEEmdlayLFITHDLAVVRQvADEVIVMEHGKM 526
Cdd:cd03246 103 QRLGLARALYGNPRILVLDEPNSHLDVegerALNQAIAALKAAGATR-----IVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
13-261 |
1.58e-21 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 95.94 E-value: 1.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 13 LTLKDVCIGFPTTTasgrrsksltdVVHDVNLEVFPGETVAIVGESGSGKSTTahaaLGLLPGDGEVTGGTITFDGRDIT 92
Cdd:PRK11432 7 VVLKNITKRFGSNT-----------VIDNLNLTIKQGTMVTLLGPSGCGKTTV----LRLVAGLEKPTEGQIFIDGEDVT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 93 HltdrefVSIRGNGIGLVPQDpmTNLNPVWTVGSQIKEALRANNIATGSEAH--KKAIELLEQAGLPnakkriDQYPHEF 170
Cdd:PRK11432 72 H------RSIQQRDICMVFQS--YALFPHMSLGENVGYGLKMLGVPKEERKQrvKEALELVDLAGFE------DRYVDQI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 171 SGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVVE 250
Cdd:PRK11432 138 SGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQ 217
|
250
....*....|.
gi 2524658687 251 TGPALQVLTRP 261
Cdd:PRK11432 218 IGSPQELYRQP 228
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
311-536 |
1.60e-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: 1.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 311 RGDRPwrkdsfrAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLfdgkRVQGRNRKEE--LELRRRI- 387
Cdd:COG1119 13 RGGKT-------ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDV----RLFGERRGGEdvWELRKRIg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 388 --QPIFQNPYATLDPMRTV-----HSSIEeplrIHKIGTKKEREqRVFELLDRVALPAEMGRRFpGELSGGQRQRVAIAR 460
Cdd:COG1119 82 lvSPALQLRFPRDETVLDVvlsgfFDSIG----LYREPTDEQRE-RARELLELLGLAHLADRPF-GTLSQGEQRRVLIAR 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2524658687 461 ALALNPEVVVCDEAVSALDVVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDLF 536
Cdd:COG1119 156 ALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVL 231
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
298-557 |
1.73e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 95.54 E-value: 1.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 298 ILVAKNLVRDFAIRGDRPWRKDSFR-----------AVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVl 366
Cdd:COG4586 1 IIEVENLSKTYRVYEKEPGLKGALKglfrreyreveAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 367 fdgkRVQGRN-RKEELELRRRIQPIFQN---------PYATLDPMRtvhssieeplRIHKIgTKKEREQRVFELLDRVAL 436
Cdd:COG4586 80 ----RVLGYVpFKRRKEFARRIGVVFGQrsqlwwdlpAIDSFRLLK----------AIYRI-PDAEYKKRLDELVELLDL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 437 PAEMGR--RfpgELSGGQRQRVAIARALALNPEVVVCDEAVSALDVVVQAQVLEllaelqeemdlaylFI---------- 504
Cdd:COG4586 145 GELLDTpvR---QLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIRE--------------FLkeynrergtt 207
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2524658687 505 ----THDLAVVRQVADEVIVMEHGKMVEHRPTDDLFDH--PEKEYTQRLLDAIPGASLD 557
Cdd:COG4586 208 illtSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKERfgPYKTIVLELAEPVPPLELP 266
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
298-527 |
2.06e-21 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 93.17 E-value: 2.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 298 ILVAkNLVRDFAIRGDRPWRKDSFR-----------AVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVL 366
Cdd:cd03267 1 IEVS-NLSKSYRVYSKEPGLIGSLKslfkrkyreveALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 367 FDGkRVQGRNRKeelELRRRIQPIF-QNPYATLD-PMRTVHSSIEEPLRIHKiGTKKEREQRVFELLDRVALPAEMGRRf 444
Cdd:cd03267 80 VAG-LVPWKRRK---KFLRRIGVVFgQKTQLWWDlPVIDSFYLLAAIYDLPP-ARFKKRLDELSELLDLEELLDTPVRQ- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 445 pgeLSGGQRQRVAIARALALNPEVVVCDEAVSALDVVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHG 524
Cdd:cd03267 154 ---LSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKG 230
|
...
gi 2524658687 525 KMV 527
Cdd:cd03267 231 RLL 233
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
311-551 |
2.07e-21 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 94.06 E-value: 2.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 311 RGDRPwrkdsfrAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEELELRRRIQPI 390
Cdd:PRK11831 17 RGNRC-------IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRMSML 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 391 FQNPYATLDpmRTVHSSIEEPLRIHKIGTKKEREQRVFELLDRVAL--PAEMgrrFPGELSGGQRQRVAIARALALNPEV 468
Cdd:PRK11831 90 FQSGALFTD--MNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLrgAAKL---MPSELSGGMARRAALARAIALEPDL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 469 VVCDEAVSALDVVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDLFDHPEKEYTQrLL 548
Cdd:PRK11831 165 IMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDPRVRQ-FL 243
|
...
gi 2524658687 549 DAI 551
Cdd:PRK11831 244 DGI 246
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
41-280 |
2.18e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 94.51 E-value: 2.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 41 DVNLEVFPGETVAIVGESGSGKSTTAHAALGLLpgdgEVTGGTITFDGRDITHLT-DREFVSIRGNgIGLVPQDPMTNL- 118
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALL----KPSSGTITIAGYHITPETgNKNLKKLRKK-VSLVFQFPEAQLf 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 119 -NpvwTVGSQIKEALRaNNIATGSEAHKKAIELLEQAGLPnaKKRIDQYPHEFSGGMRQRALIAMGLAAHPKLLIADEPT 197
Cdd:PRK13641 100 eN---TVLKDVEFGPK-NFGFSEDEAKEKALKWLKKVGLS--EDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 198 SALDVTVAKKILDhLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVLTRPQHPYTKQLIAAAPSLA 277
Cdd:PRK13641 174 AGLDPEGRKEMMQ-LFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKEWLKKHYLDEPATSRF 252
|
...
gi 2524658687 278 ARR 280
Cdd:PRK13641 253 ASK 255
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
38-252 |
2.70e-21 |
|
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: 92.43 E-value: 2.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGDGevtgGTITFDGRDithlTDREFVSIRGNgIGLVPQDpmTN 117
Cdd:cd03266 20 AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDA----GFATVDGFD----VVKEPAEARRR-LGFVSDS--TG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 118 LNPVWTVGSQIKEALRANNIAtGSEAHKKAIELLEQAGLpnaKKRIDQYPHEFSGGMRQRALIAMGLAAHPKLLIADEPT 197
Cdd:cd03266 89 LYDRLTARENLEYFAGLYGLK-GDELTARLEELADRLGM---EELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2524658687 198 SALDVTVAKKILDHLDKLtSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETG 252
Cdd:cd03266 165 TGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
41-480 |
2.86e-21 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 97.17 E-value: 2.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 41 DVNLEVFPGETVAIVGESGSGKSTTAHAALGLLP-GDGEvtgGTITFDGRdithltDREFVSIRGN---GIGLVPQDpmT 116
Cdd:NF040905 19 DVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPhGSYE---GEILFDGE------VCRFKDIRDSealGIVIIHQE--L 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 117 NLNPVWTVGSQIkeaLRANNIATG-----SEAHKKAIELLEQAGLP-NAKKRIDQYphefsG-GMRQRALIAMGLAAHPK 189
Cdd:NF040905 88 ALIPYLSIAENI---FLGNERAKRgvidwNETNRRARELLAKVGLDeSPDTLVTDI-----GvGKQQLVEIAKALSKDVK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 190 LLIADEPTSALDVTVAKKILDHLDKLTSElGTSVVLITHDLGLAAERADRLVVMQAGRVVETgpalqvLTRPQHPYTKQL 269
Cdd:NF040905 160 LLILDEPTAALNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSITVLRDGRTIET------LDCRADEVTEDR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 270 IAAA---PSLAARRGDRVvaaPTTSDadqkEILVAKNLVRDFAIRGDRpwrkdsfRAVDDISFTLRRGRTIGIVGESGSG 346
Cdd:NF040905 233 IIRGmvgRDLEDRYPERT---PKIGE----VVFEVKNWTVYHPLHPER-------KVVDDVSLNVRRGEIVGIAGLMGAG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 347 KSTVAnMAL-----GllDPTEGEVLFDGKRVQGRNRKEEL--------ELRRR-----IQPIFQN-PYATLDpmrtvhss 407
Cdd:NF040905 299 RTELA-MSVfgrsyG--RNISGTVFKDGKEVDVSTVSDAIdaglayvtEDRKGyglnlIDDIKRNiTLANLG-------- 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 408 ieeplRIHKIGTKKEREQRvfelldRVA--LPAEMGRRFP------GELSGGQRQRVAIARALALNPEVVVCDEAVSALD 479
Cdd:NF040905 368 -----KVSRRGVIDENEEI------KVAeeYRKKMNIKTPsvfqkvGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID 436
|
.
gi 2524658687 480 V 480
Cdd:NF040905 437 V 437
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
305-538 |
2.89e-21 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 93.22 E-value: 2.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 305 VRDFAIRGDRPwRKDSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVlfdgkRVQGrnrkeelelr 384
Cdd:COG1134 24 LKELLLRRRRT-RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV-----EVNG---------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 385 rRIQPIFQnpYAT-LDPMRTVHSSIEEPLRIHKIgTKKEREQRVfellDRVALPAEMGRRF--P-GELSGGQRQRVAIAR 460
Cdd:COG1134 88 -RVSALLE--LGAgFHPELTGRENIYLNGRLLGL-SRKEIDEKF----DEIVEFAELGDFIdqPvKTYSSGMRARLAFAV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 461 ALALNPEVVVCDEAVSALDVVVQAQVlellaeLQEEMDL-----AYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDL 535
Cdd:COG1134 160 ATAVDPDILLVDEVLAVGDAAFQKKC------LARIRELresgrTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEV 233
|
...
gi 2524658687 536 FDH 538
Cdd:COG1134 234 IAA 236
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
310-555 |
2.92e-21 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 97.87 E-value: 2.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 310 IRGDRPWRKDSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMaLGLLD-PTEGEVLFDGKRVQGRNRKEELELRRR-I 387
Cdd:PRK10535 10 IRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNI-LGCLDkPTSGTYRVAGQDVATLDADALAQLRREhF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 388 QPIFQNPYatLDPMRTVHSSIEEPlRIHKIGTKKEREQRVFELLDRVALPAEMGRRfPGELSGGQRQRVAIARALALNPE 467
Cdd:PRK10535 89 GFIFQRYH--LLSHLTAAQNVEVP-AVYAGLERKQRLLRAQELLQRLGLEDRVEYQ-PSQLSGGQQQRVSIARALMNGGQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 468 VVVCDEAVSALDVVVQAQVLELLAELQEEMDlAYLFITHDLAVVRQvADEVIVMEHGKMVEHRPTddlfdHPEKEYTQRL 547
Cdd:PRK10535 165 VILADEPTGALDSHSGEEVMAILHQLRDRGH-TVIIVTHDPQVAAQ-AERVIEIRDGEIVRNPPA-----QEKVNVAGGT 237
|
....*...
gi 2524658687 548 LDAIPGAS 555
Cdd:PRK10535 238 EPVVNTAS 245
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
41-527 |
3.38e-21 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 96.90 E-value: 3.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 41 DVNLEVFPGETVAIVGESGSGKSTTahaaLGLLPGDGEVTGGTITFDGRDITHLTDREFVsirGNGIGLVPQDpmTNLNP 120
Cdd:PRK11288 22 DISFDCRAGQVHALMGENGAGKSTL----LKILSGNYQPDAGSILIDGQEMRFASTTAAL---AAGVAIIYQE--LHLVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 121 VWTVgsqikealrANNIATG-----------SEAHKKAIELLEQAGL---PNAKKRidqyphEFSGGMRQRALIAMGLAA 186
Cdd:PRK11288 93 EMTV---------AENLYLGqlphkggivnrRLLNYEAREQLEHLGVdidPDTPLK------YLSIGQRQMVEIAKALAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 187 HPKLLIADEPTSALDvtvAKKIlDHLDKLTSEL---GTSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVLTRpqh 263
Cdd:PRK11288 158 NARVIAFDEPTSSLS---AREI-EQLFRVIRELraeGRVILYVSHRMEEIFALCDAITVFKDGRYVATFDDMAQVDR--- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 264 pytkqliaaapslaarrgDRVVAApttsdadqkeiLVAKNL--VRDFAIR--GDRPWRKDSFRAV---DDISFTLRRGRT 336
Cdd:PRK11288 231 ------------------DQLVQA-----------MVGREIgdIYGYRPRplGEVRLRLDGLKGPglrEPISFSVRAGEI 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 337 IGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEELEL-------RRRIQPIFqnpyatldPMRTVHSSIE 409
Cdd:PRK11288 282 VGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAgimlcpeDRKAEGII--------PVHSVADNIN 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 410 EPLRIHK------IGTKKERE--QRVFELLdRVALPAemGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVSALDVV 481
Cdd:PRK11288 354 ISARRHHlragclINNRWEAEnaDRFIRSL-NIKTPS--REQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVG 430
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2524658687 482 VQAQVLELLAELQEEmDLAYLFITHDLAVVRQVADEVIVMEHGKMV 527
Cdd:PRK11288 431 AKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
322-538 |
4.37e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 93.27 E-value: 4.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 322 RAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEELE-LRRRIQPIFQNPYATLdp 400
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKqIRKKVGLVFQFPESQL-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 401 mrtvhssIEEP-LRIHKIG------TKKEREQRVFELLDRVALPAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDE 473
Cdd:PRK13649 99 -------FEETvLKDVAFGpqnfgvSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDE 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2524658687 474 AVSALDVVVQAQVlellaelqeeMDL---------AYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDLFDH 538
Cdd:PRK13649 172 PTAGLDPKGRKEL----------MTLfkklhqsgmTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
320-545 |
6.49e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 92.54 E-value: 6.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 320 SFRAVDDISFTLRRGRTIGIVGESGSGKSTVANM--ALGLLDPT---EGEVLFDGKRVQGrNRKEELELRRRIQPIFQNP 394
Cdd:PRK14243 22 SFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnRLNDLIPGfrvEGKVTFHGKNLYA-PDVDPVEVRRRIGMVFQKP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 395 YatldPM-RTVHSSIEEPLRIHkiGTKKEREQRVFELLDRVALPAEMG---RRFPGELSGGQRQRVAIARALALNPEVVV 470
Cdd:PRK14243 101 N----PFpKSIYDNIAYGARIN--GYKGDMDELVERSLRQAALWDEVKdklKQSGLSLSGGQQQRLCIARAIAVQPEVIL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 471 CDEAVSALDVVVQAQVLELLAELQEemDLAYLFITHDLAVVRQVAD-----EVIVME----HGKMVEHRPTDDLFDHPEK 541
Cdd:PRK14243 175 MDEPCSALDPISTLRIEELMHELKE--QYTIIIVTHNMQQAARVSDmtaffNVELTEgggrYGYLVEFDRTEKIFNSPQQ 252
|
....
gi 2524658687 542 EYTQ 545
Cdd:PRK14243 253 QATR 256
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
41-252 |
7.33e-21 |
|
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: 91.02 E-value: 7.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 41 DVNLEVFPGETVAIVGESGSGKSTTahaaLGLLPGDGEVTGGTITFDGRDITHL--TDREfvsirgngIGLVPQDpmTNL 118
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTL----LNLIAGFETPQSGRVLINGVDVTAAppADRP--------VSMLFQE--NNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 119 NPVWTVGSQIKEALRANNIATgsEAHKKAIE-LLEQAGLPNAKKRIdqyPHEFSGGMRQRALIAMGLAAHPKLLIADEPT 197
Cdd:cd03298 82 FAHLTVEQNVGLGLSPGLKLT--AEDRQAIEvALARVGLAGLEKRL---PGELSGGERQRVALARVLVRDKPVLLLDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2524658687 198 SALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETG 252
Cdd:cd03298 157 AALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
36-261 |
7.54e-21 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 94.14 E-value: 7.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 36 TDVVHDVNLEVFPGETVAIVGESGSGKSTTahaaLGLLPGDGEVTGGTITFDGRDITHLTDREfvsirgNGIGLVPQdpm 115
Cdd:PRK11650 17 TQVIKGIDLDVADGEFIVLVGPSGCGKSTL----LRMVAGLERITSGEIWIGGRVVNELEPAD------RDIAMVFQ--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 116 tN--LNPVWTVgsqikealrANNIATGseahkkaielLEQAGLPNA--KKRI-------------DQYPHEFSGGMRQRa 178
Cdd:PRK11650 84 -NyaLYPHMSV---------RENMAYG----------LKIRGMPKAeiEERVaeaarilelepllDRKPRELSGGQRQR- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 179 lIAMGLAA--HPKLLIADEPTSALD--VTVAKKIldHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPA 254
Cdd:PRK11650 143 -VAMGRAIvrEPAVFLFDEPLSNLDakLRVQMRL--EIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTP 219
|
....*..
gi 2524658687 255 LQVLTRP 261
Cdd:PRK11650 220 VEVYEKP 226
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
12-252 |
8.02e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 92.60 E-value: 8.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 12 ILTLKDVCIGFPTTTasgrrsksltDVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLL-PGDGEvtggtITFDGRD 90
Cdd:PRK13636 5 ILKVEELNYNYSDGT----------HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILkPSSGR-----ILFDGKP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 91 ITHlTDREFVSIRGNgIGLVPQDPmtnlnpvwtvGSQIKEALRANNIATGS--------EAHKKAIELLEQAGLPNAKkr 162
Cdd:PRK13636 70 IDY-SRKGLMKLRES-VGMVFQDP----------DNQLFSASVYQDVSFGAvnlklpedEVRKRVDNALKRTGIEHLK-- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 163 iDQYPHEFSGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVV 242
Cdd:PRK13636 136 -DKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFV 214
|
250
....*....|
gi 2524658687 243 MQAGRVVETG 252
Cdd:PRK13636 215 MKEGRVILQG 224
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
42-262 |
1.02e-20 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 91.53 E-value: 1.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 42 VNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGDGEvtggtITFDGRDITHLTDREFVSIRGNgigLVPQDPMTNLNPV 121
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSGS-----IQFAGQPLEAWSAAELARHRAY---LSQQQTPPFAMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 122 WTVGSQIKEALRAnniatgSEAHKKAI-ELLEQAGLPNAKKR-IDQypheFSGGMRQRA-LIAMGLAAHP------KLLI 192
Cdd:PRK03695 87 FQYLTLHQPDKTR------TEAVASALnEVAEALGLDDKLGRsVNQ----LSGGEWQRVrLAAVVLQVWPdinpagQLLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 193 ADEPTSALDVTvAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVLTRPQ 262
Cdd:PRK03695 157 LDEPMNSLDVA-QQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPEN 225
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
37-243 |
1.06e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 89.99 E-value: 1.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 37 DVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPgdgeVTGGTITFDGrdithltdrefvsirGNGIGLVPQD--- 113
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLR----PTSGTVRRAG---------------GARVAYVPQRsev 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 114 ----PMTNLNPVwTVGS-QIKEALRANNIatgsEAHKKAIELLEQAGLPN-AKKRIDqyphEFSGGMRQRALIAMGLAAH 187
Cdd:NF040873 67 pdslPLTVRDLV-AMGRwARRGLWRRLTR----DDRAAVDDALERVGLADlAGRQLG----ELSGGQRQRALLAQGLAQE 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2524658687 188 PKLLIADEPTSALDVTVAKKILDHLDKLTSElGTSVVLITHDLGLAAeRADRLVVM 243
Cdd:NF040873 138 ADLLLLDEPTTGLDAESRERIIALLAEEHAR-GATVVVVTHDLELVR-RADPCVLL 191
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
36-262 |
1.19e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 92.06 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 36 TDVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLL-PGDGEV--TGGTITFDGRDIthLTDREFVsirgngiGLVPQ 112
Cdd:PRK13639 15 TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILkPTSGEVliKGEPIKYDKKSL--LEVRKTV-------GIVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 113 DPmtnlnpvwtvGSQIKEALRANNIATG--------SEAHKKAIELLEQAGLPNAKKRIdqyPHEFSGGMRQRALIAMGL 184
Cdd:PRK13639 86 NP----------DDQLFAPTVEEDVAFGplnlglskEEVEKRVKEALKAVGMEGFENKP---PHHLSGGQKKRVAIAGIL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2524658687 185 AAHPKLLIADEPTSALDVTVAKKILDHLDKLTSElGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVLTRPQ 262
Cdd:PRK13639 153 AMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIE 229
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
324-527 |
1.19e-20 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 91.76 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 324 VDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRkEELELRRRIQPifQnpyatldpmrt 403
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSP-AELARRRAVLP--Q----------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 404 vHSSIEEPLRIHKI---------GTKKEREQRVFELLDRVALPAEMGRRFPgELSGGQRQRVAIARALA------LNPEV 468
Cdd:PRK13548 84 -HSSLSFPFTVEEVvamgraphgLSRAEDDALVAAALAQVDLAHLAGRDYP-QLSGGEQQRVQLARVLAqlwepdGPPRW 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2524658687 469 VVCDEAVSALDVVVQAQVlellaelqeeMDLAYLF----------ITHDLAVVRQVADEVIVMEHGKMV 527
Cdd:PRK13548 162 LLLDEPTSALDLAHQHHV----------LRLARQLaherglavivVLHDLNLAARYADRIVLLHQGRLV 220
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
42-249 |
1.35e-20 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 90.70 E-value: 1.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 42 VNLEVFPGETVAIVGESGSGKSTTahaaLGLLPGDGEVTGGTITFDGRDITHLTDREFVSIRgNGIGLVPQDPMTNLNPv 121
Cdd:PRK10908 21 VTFHMRPGEMAFLTGHSGAGKSTL----LKLICGIERPSAGKIWFSGHDITRLKNREVPFLR-RQIGMIFQDHHLLMDR- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 122 wTVGSQIKEALRANNiATGSEAHKKAIELLEQAGLPNAKKridQYPHEFSGGMRQRALIAMGLAAHPKLLIADEPTSALD 201
Cdd:PRK10908 95 -TVYDNVAIPLIIAG-ASGDDIRRRVSAALDKVGLLDKAK---NFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2524658687 202 VTVAKKILDHLDKLtSELGTSVVLITHDLGLAAERADRLVVMQAGRVV 249
Cdd:PRK10908 170 DALSEGILRLFEEF-NRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
32-526 |
1.79e-20 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 94.41 E-value: 1.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 32 SKSLTDV--VHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGDGevtgGTITFDGRDITHLTDREFVSirgNGIGL 109
Cdd:PRK10982 5 SKSFPGVkaLDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDS----GSILFQGKEIDFKSSKEALE---NGISM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 110 VPQDpmtnLNpvwtvgsQIKEALRANNIATGSEAHKKAieLLEQAGLPNAKKR------IDQYPHE----FSGGMRQRAL 179
Cdd:PRK10982 78 VHQE----LN-------LVLQRSVMDNMWLGRYPTKGM--FVDQDKMYRDTKAifdeldIDIDPRAkvatLSVSQMQMIE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 180 IAMGLAAHPKLLIADEPTSALdvtvAKKILDHLDKLTSEL---GTSVVLITHDLGLAAERADRLVVMQAGRVVETGPaLQ 256
Cdd:PRK10982 145 IAKAFSYNAKIVIMDEPTSSL----TEKEVNHLFTIIRKLkerGCGIVYISHKMEEIFQLCDEITILRDGQWIATQP-LA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 257 VLTrpqhpyTKQLIA--AAPSLAARrgdrvvaAPTTSDADQKEILVAKNLVrdfAIRgdRPwrkdsfrAVDDISFTLRRG 334
Cdd:PRK10982 220 GLT------MDKIIAmmVGRSLTQR-------FPDKENKPGEVILEVRNLT---SLR--QP-------SIRDVSFDLHKG 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 335 RTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEELE-------LRRRIQPIFQNPYATLDPMRTVHSS 407
Cdd:PRK10982 275 EILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINhgfalvtEERRSTGIYAYLDIGFNSLISNIRN 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 408 IEEPLRIHKIGTKKEREQRVFELLdRVALPAEmgRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVSALDVVVQAQVl 487
Cdd:PRK10982 355 YKNKVGLLDNSRMKSDTQWVIDSM-RVKTPGH--RTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEI- 430
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2524658687 488 ellaeLQEEMDLA-----YLFITHDLAVVRQVADEVIVMEHGKM 526
Cdd:PRK10982 431 -----YQLIAELAkkdkgIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
323-539 |
1.98e-20 |
|
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: 89.86 E-value: 1.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 323 AVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKeelELRRRIQPIFQNPY------- 395
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLH---DLRSRISIIPQDPVlfsgtir 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 396 ATLDPmRTVHSSiEEPLRI-HKIGTKKereqRVFELLDRVALPAEMGrrfpGE-LSGGQRQRVAIARALALNPEVVVCDE 473
Cdd:cd03244 96 SNLDP-FGEYSD-EELWQAlERVGLKE----FVESLPGGLDTVVEEG----GEnLSVGQRQLLCLARALLRKSKILVLDE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2524658687 474 AVSALDVVVQAQVLELLAELQEemDLAYLFITHDLAVVRQvADEVIVMEHGKMVEhrptddlFDHP 539
Cdd:cd03244 166 ATASVDPETDALIQKTIREAFK--DCTVLTIAHRLDTIID-SDRILVLDKGRVVE-------FDSP 221
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
307-528 |
2.51e-20 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 94.50 E-value: 2.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 307 DFAIRGDRPwrkdsfrAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVqgRNRKEElELRRR 386
Cdd:COG5265 364 SFGYDPERP-------ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDI--RDVTQA-SLRAA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 387 IQPIfqnpyatldPMRTV--HSSIEEPLRIHKIG-TKKEREQ--RVFELLDRVA-LP----AEMGRRfpG-ELSGGQRQR 455
Cdd:COG5265 434 IGIV---------PQDTVlfNDTIAYNIAYGRPDaSEEEVEAaaRAAQIHDFIEsLPdgydTRVGER--GlKLSGGEKQR 502
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2524658687 456 VAIARALALNPEVVVCDEAVSALDVV----VQAQVLELLAELQEemdlayLFITHDLAVVRQvADEVIVMEHGKMVE 528
Cdd:COG5265 503 VAIARTLLKNPPILIFDEATSALDSRteraIQAALREVARGRTT------LVIAHRLSTIVD-ADEILVLEAGRIVE 572
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
298-473 |
2.74e-20 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 90.09 E-value: 2.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 298 ILVAKNLVRDFairGDRpwrkdsfRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGrnr 377
Cdd:COG1137 3 TLEAENLVKSY---GKR-------TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITH--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 378 keeLELRRRIQ------P----IFQNpyatLdpmrTVHSSIEEPLRIHKIgTKKEREQRVFELLDrvalpaEMG----RR 443
Cdd:COG1137 70 ---LPMHKRARlgigylPqeasIFRK----L----TVEDNILAVLELRKL-SKKEREERLEELLE------EFGithlRK 131
|
170 180 190
....*....|....*....|....*....|.
gi 2524658687 444 FPG-ELSGGQRQRVAIARALALNPEVVVCDE 473
Cdd:COG1137 132 SKAySLSGGERRRVEIARALATNPKFILLDE 162
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
38-270 |
2.86e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 90.49 E-value: 2.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLP-GDGEV-TGGTITFDGRDITHLtdrEFVSIRGNgIGLVPQDPm 115
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiYDSKIkVDGKVLYFGKDIFQI---DAIKLRKE-VGMVFQQP- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 116 tNLNPVWTVGSQIKEALRANNIATGSEAHKKAIELLEQAGL-PNAKKRIDQYPHEFSGGMRQRALIAMGLAAHPKLLIAD 194
Cdd:PRK14246 100 -NPFPHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLwKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2524658687 195 EPTSALDVTVAKKILDHLDKLTSELgtSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVLTRPQHPYTKQLI 270
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-270 |
2.97e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 94.51 E-value: 2.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 2 STDTNTSAAPILTLKDVCIGFPTTTASgrrsksltdVVHDVNLEVFPGETVAIVGESGSGKSTTahaaLGLLPGDGEVTG 81
Cdd:PRK11160 328 TTSTAAADQVSLTLNNVSFTYPDQPQP---------VLKGLSLQIKAGEKVALLGRTGCGKSTL----LQLLTRAWDPQQ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 82 GTITFDGRDITHLTDRefvSIRgNGIGLVPQDpmtnlnpVWTVGSQIKEALRannIATGSEAHKKAIELLEQAGLPN--- 158
Cdd:PRK11160 395 GEILLNGQPIADYSEA---ALR-QAISVVSQR-------VHLFSATLRDNLL---LAAPNASDEALIEVLQQVGLEKlle 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 159 AKKRIDQYPHE----FSGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSelGTSVVLITHDLgLAA 234
Cdd:PRK11160 461 DDKGLNAWLGEggrqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRL-TGL 537
|
250 260 270
....*....|....*....|....*....|....*.
gi 2524658687 235 ERADRLVVMQAGRVVETGPALQVLTrpQHPYTKQLI 270
Cdd:PRK11160 538 EQFDRICVMDNGQIIEQGTHQELLA--QQGRYYQLK 571
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
322-529 |
3.43e-20 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 89.17 E-value: 3.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 322 RAVDDISFTLRRGrTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVqgrnRKEELELRRRIQPIFQNPyaTLDPM 401
Cdd:cd03264 14 RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV----LKQPQKLRRRIGYLPQEF--GVYPN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 402 RTVHSSIEEPLRIHKIgTKKEREQRVFELLDRVALpAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVSALDVV 481
Cdd:cd03264 87 FTVREFLDYIAWLKGI-PSKEVKARVDEVLELVNL-GDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPE 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2524658687 482 vqAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEH 529
Cdd:cd03264 165 --ERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
31-248 |
3.73e-20 |
|
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: 89.45 E-value: 3.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 31 RSKSLTDVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPgdgeVTGGTITFDGRDITHLTDREFVSIrgngIGLV 110
Cdd:cd03248 22 PTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQ----PQGGQVLLDGKPISQYEHKYLHSK----VSLV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 111 PQDPMTNLNPVwtvgsqikealrANNIATGSeAHKKAIELLEQAGLPNAKKRIDQYPHEF-----------SGGMRQRAL 179
Cdd:cd03248 94 GQEPVLFARSL------------QDNIAYGL-QSCSFECVKEAAQKAHAHSFISELASGYdtevgekgsqlSGGQKQRVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 180 IAMGLAAHPKLLIADEPTSALDVTVAKKILD-HLDKLTSelgTSVVLITHDLGLaAERADRLVVMQAGRV 248
Cdd:cd03248 161 IARALIRNPQVLILDEATSALDAESEQQVQQaLYDWPER---RTVLVIAHRLST-VERADQILVLDGGRI 226
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
36-259 |
3.78e-20 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 93.95 E-value: 3.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 36 TDVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPgdgeVTGGTITFDGRDITHLtDREFVsirGNGIGLVPQDpm 115
Cdd:TIGR01842 331 KPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWP----PTSGSVRLDGADLKQW-DRETF---GKHIGYLPQD-- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 116 tnlnpvwtvgSQIKEALRANNIATGSEaHKKAIELLEQAGLPNAKKRIDQYPHEF-----------SGGMRQRALIAMGL 184
Cdd:TIGR01842 401 ----------VELFPGTVAENIARFGE-NADPEKIIEAAKLAGVHELILRLPDGYdtvigpggatlSGGQRQRIALARAL 469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2524658687 185 AAHPKLLIADEPTSALD----VTVAKKILdHLDKltseLGTSVVLITHDLGLaAERADRLVVMQAGRVVETGPALQVLT 259
Cdd:TIGR01842 470 YGDPKLVVLDEPNSNLDeegeQALANAIK-ALKA----RGITVVVITHRPSL-LGCVDKILVLQDGRIARFGERDEVLA 542
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
302-528 |
3.99e-20 |
|
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: 93.71 E-value: 3.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 302 KNLVRDFairgdrpwrkDSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGL--LDPTEGEVL------------- 366
Cdd:TIGR03269 4 KNLTKKF----------DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyve 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 367 ---FDGKRVQ--------------GRNRKEELELRRRIQPIFQNPYATLDPMRTVHSSIEEplrIHKIGTK-KEREQRVF 428
Cdd:TIGR03269 74 rpsKVGEPCPvcggtlepeevdfwNLSDKLRRRIRKRIAIMLQRTFALYGDDTVLDNVLEA---LEEIGYEgKEAVGRAV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 429 ELLDRVALPAEMgRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVSALDVVVQAQVLELLAELQEEMDLAYLFITHDL 508
Cdd:TIGR03269 151 DLIEMVQLSHRI-THIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWP 229
|
250 260
....*....|....*....|
gi 2524658687 509 AVVRQVADEVIVMEHGKMVE 528
Cdd:TIGR03269 230 EVIEDLSDKAIWLENGEIKE 249
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
42-262 |
4.49e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 90.18 E-value: 4.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 42 VNLEVFPGETVAIVGESGSGKSTTahaaLGLLPGDGEVTGGTITFDGRDITHLTDREfvsIRGNgIGLVPQDPMTNL--N 119
Cdd:PRK13647 24 LSLSIPEGSKTALLGPNGAGKSTL----LLHLNGIYLPQRGRVKVMGREVNAENEKW---VRSK-VGLVFQDPDDQVfsS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 120 PVW---TVGSQikealraNNIATGSEAHKKAIELLEQAGLpnaKKRIDQYPHEFSGGMRQRALIAMGLAAHPKLLIADEP 196
Cdd:PRK13647 96 TVWddvAFGPV-------NMGLDKDEVERRVEEALKAVRM---WDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2524658687 197 TSALDVTVAKKILDHLDKLTSElGTSVVLITHDLGLAAERADRLVVMQAGRVVETGpALQVLTRPQ 262
Cdd:PRK13647 166 MAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG-DKSLLTDED 229
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
38-262 |
5.56e-20 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 89.18 E-value: 5.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGDgevtGGTITFDGRDITHLTDREFVSirgNGIGLVPQDPmtN 117
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRD----AGNIIIDDEDISLLPLHARAR---RGIGYLPQEA--S 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 118 LNPVWTVGSQIKEALRANNIATGSEAHKKAIELLEQAGLPNAKKRIDQyphEFSGGMRQRALIAMGLAAHPKLLIADEPT 197
Cdd:PRK10895 89 IFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQ---SLSGGERRRVEIARALAANPKFILLDEPF 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2524658687 198 SALD---VTVAKKILDHLdkltSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVLTRPQ 262
Cdd:PRK10895 166 AGVDpisVIDIKRIIEHL----RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEH 229
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
38-261 |
5.95e-20 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 88.75 E-value: 5.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPgdgeVTGGTITFDGRDITHLTdrefVSIRGN-GIGLVPQDP-- 114
Cdd:cd03218 15 VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVK----PDSGKILLDGQDITKLP----MHKRARlGIGYLPQEAsi 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 115 MTNLnpvwTVGSQIKEALRANNIaTGSEAHKKAIELLEQAGLpnaKKRIDQYPHEFSGGMRQRALIAMGLAAHPKLLIAD 194
Cdd:cd03218 87 FRKL----TVEENILAVLEIRGL-SKKEREEKLEELLEEFHI---THLRKSKASSLSGGERRRVEIARALATNPKFLLLD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2524658687 195 EPTSALD-VTVA--KKILDHLdkltSELGTSvVLIT-HDLGLAAERADRLVVMQAGRVVETGPALQVLTRP 261
Cdd:cd03218 159 EPFAGVDpIAVQdiQKIIKIL----KDRGIG-VLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
41-252 |
6.67e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 90.18 E-value: 6.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 41 DVNLEVFPGETVAIVGESGSGKSTTAHAALGLL-PGDGEVTGGTITfdgrdITHLTDREFVSIRGNGIGLVPQDPMtnln 119
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLqPTEGKVTVGDIV-----VSSTSKQKEIKPVRKKVGVVFQFPE---- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 120 pvwtvgSQIKEALRANNIATG--------SEAHKKAIELLEQAGLpnAKKRIDQYPHEFSGGMRQRALIAMGLAAHPKLL 191
Cdd:PRK13643 95 ------SQLFEETVLKDVAFGpqnfgipkEKAEKIAAEKLEMVGL--ADEFWEKSPFELSGGQMRRVAIAGILAMEPEVL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2524658687 192 IADEPTSALDVTVAKKILDHLDKLtSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETG 252
Cdd:PRK13643 167 VLDEPTAGLDPKARIEMMQLFESI-HQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCG 226
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
43-259 |
7.52e-20 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 88.49 E-value: 7.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 43 NLEVFPGETVAIVGESGSGKSTTahaaLGLLPGDGEVTGGTITFDGRDITHLT-DREFVSIrgngiglVPQDpmTNLNPV 121
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTL----LNLIAGFLTPASGSLTLNGQDHTTTPpSRRPVSM-------LFQE--NNLFSH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 122 WTVgsqikealrANNIATG--------SEAHKKAIELLEQAGLPNAKKRIdqyPHEFSGGMRQRALIAMGLAAHPKLLIA 193
Cdd:PRK10771 86 LTV---------AQNIGLGlnpglklnAAQREKLHAIARQMGIEDLLARL---PGQLSGGQRQRVALARCLVREQPILLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2524658687 194 DEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVLT 259
Cdd:PRK10771 154 DEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
48-533 |
8.13e-20 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 92.95 E-value: 8.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 48 PGETVAIVGESGSGKSTTAHAALG-LLPGDGEVTG------------GTITFDgrdithltdrEFVSIRGNGIGLV--PQ 112
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGeLIPNLGDYEEepswdevlkrfrGTELQN----------YFKKLYNGEIKVVhkPQ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 113 dpMTNLNPVWTVGSqIKEALRANNiatgseAHKKAIELLEQAGLPNAkkrIDQYPHEFSGGMRQRALIAMGLAAHPKLLI 192
Cdd:PRK13409 168 --YVDLIPKVFKGK-VRELLKKVD------ERGKLDEVVERLGLENI---LDRDISELSGGELQRVAIAAALLRDADFYF 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 193 ADEPTSALDV----TVAKKILDhldkLTSelGTSVVLITHDLGLAAERADRLVVMQAgrvvETGpALQVLTRPqhpytkq 268
Cdd:PRK13409 236 FDEPTSYLDIrqrlNVARLIRE----LAE--GKYVLVVEHDLAVLDYLADNVHIAYG----EPG-AYGVVSKP------- 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 269 liaaapsLAARRGdrvvaapttsdadqkeI-------LVAKNL-VRDFAIRGD-RPWRKDSFRAV----DDIS-----FT 330
Cdd:PRK13409 298 -------KGVRVG----------------IneylkgyLPEENMrIRPEPIEFEeRPPRDESERETlveyPDLTkklgdFS 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 331 L-------RRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGK--------------RVQgrnrkeelELRRRIQP 389
Cdd:PRK13409 355 LeveggeiYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKisykpqyikpdydgTVE--------DLLRSITD 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 390 IFQNPYatldpmrtVHSSIEEPLRIHKIgtkkeREQRVfelldrvalpaemgrrfpGELSGGQRQRVAIARALALNPEVV 469
Cdd:PRK13409 427 DLGSSY--------YKSEIIKPLQLERL-----LDKNV------------------KDLSGGELQRVAIAACLSRDADLY 475
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2524658687 470 VCDEAVSALDVVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVME-----HGKmvEHRPTD 533
Cdd:PRK13409 476 LLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMVFEgepgkHGH--ASGPMD 542
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
314-528 |
9.19e-20 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 88.36 E-value: 9.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 314 RPWRKDSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVlfdgkrvqgrnrkeelELRRRIQPIFqN 393
Cdd:cd03220 28 RKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV----------------TVRGRVSSLL-G 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 394 PYATLDPMRTVHSSIEEPLRIHKIgTKKEREQRVfellDRVALPAEMGRRF--P-GELSGGQRQRVAIARALALNPEVVV 470
Cdd:cd03220 91 LGGGFNPELTGRENIYLNGRLLGL-SRKEIDEKI----DEIIEFSELGDFIdlPvKTYSSGMKARLAFAIATALEPDILL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2524658687 471 CDEAVSALDVVVQAQVlELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVE 528
Cdd:cd03220 166 IDEVLAVGDAAFQEKC-QRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRF 222
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
318-527 |
9.30e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 89.41 E-value: 9.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 318 KDSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEeleLRRRIQPIFQnpyat 397
Cdd:PRK13647 15 KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKW---VRSKVGLVFQ----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 398 lDPMRTVHSS-IEEPLRIHKIG---TKKEREQRVFELLDRVALpAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDE 473
Cdd:PRK13647 87 -DPDDQVFSStVWDDVAFGPVNmglDKDEVERRVEEALKAVRM-WDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2524658687 474 AVSALDVVVQAQVLELLAELQEEmDLAYLFITHDLAVVRQVADEVIVMEHGKMV 527
Cdd:PRK13647 165 PMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVL 217
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
38-255 |
1.01e-19 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 88.40 E-value: 1.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETVAIVGESGSGKSTTahaaLGLLPGDGEVTGGTITFDGRDIThltDREFVSIRGNGIGLVPQ----- 112
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTL----LGTLCGDPRATSGRIVFDGKDIT---DWQTAKIMREAVAIVPEgrrvf 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 113 DPMTnlnpvwtvgsqIKEALRANNIATGSEAHKKAIELLEQAgLPNAKKRIDQYPHEFSGGMRQRALIAMGLAAHPKLLI 192
Cdd:PRK11614 93 SRMT-----------VEENLAMGGFFAERDQFQERIKWVYEL-FPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2524658687 193 ADEPTSALDVTVAKKILDHLDKLTSElGTSVVLITHDLGLAAERADRLVVMQAGRVV--ETGPAL 255
Cdd:PRK11614 161 LDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVVleDTGDAL 224
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
328-535 |
1.20e-19 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 88.10 E-value: 1.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 328 SFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKrvqgrNRKEELELRRRIQPIFQ--NPYATLdpmrTVH 405
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQ-----DHTTTPPSRRPVSMLFQenNLFSHL----TVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 406 SSIEepLRIHKiGTKKEREQR--VFELLDRVALPAEMgRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVSALDVVVQ 483
Cdd:PRK10771 90 QNIG--LGLNP-GLKLNAAQRekLHAIARQMGIEDLL-ARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2524658687 484 AQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDL 535
Cdd:PRK10771 166 QEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
30-252 |
1.27e-19 |
|
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: 87.47 E-value: 1.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 30 RRSKSLTDVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLpgdgEVTGGTITFDGRDITHLtdrEFVSIRgNGIGL 109
Cdd:cd03369 15 RYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFL----EAEEGKIEIDGIDISTI---PLEDLR-SSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 110 VPQDPM-------TNLNPVWTVGS-QIKEALRannIATGSEahkkaielleqaglpnakkridqyphEFSGGMRQRALIA 181
Cdd:cd03369 87 IPQDPTlfsgtirSNLDPFDEYSDeEIYGALR---VSEGGL--------------------------NLSQGQRQLLCLA 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2524658687 182 MGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSelGTSVVLITHDLGLAAErADRLVVMQAGRVVETG 252
Cdd:cd03369 138 RALLKRPRVLVLDEATASIDYATDALIQKTIREEFT--NSTILTIAHRLRTIID-YDKILVMDAGEVKEYD 205
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
13-252 |
1.28e-19 |
|
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: 86.60 E-value: 1.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 13 LTLKDVCIGFPtttasgrrsKSLTDVVHDVNLEVFPGETVAIVGESGSGKSTTahaaLGLLPGDGEVTGGTITFDGRDIT 92
Cdd:cd03247 1 LSINNVSFSYP---------EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTL----LQLLTGDLKPQQGEITLDGVPVS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 93 HLTDrefvSIRgNGIGLVPQDPmtnlnpvwtvgsqikealranniatgseaHKKAIELLEQAGLPnakkridqypheFSG 172
Cdd:cd03247 68 DLEK----ALS-SLISVLNQRP-----------------------------YLFDTTLRNNLGRR------------FSG 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 173 GMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSElgTSVVLITHDLgLAAERADRLVVMQAGRVVETG 252
Cdd:cd03247 102 GERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKD--KTLIWITHHL-TGIEHMDKILFLENGKIIMQG 178
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
36-276 |
1.42e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 88.89 E-value: 1.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 36 TDVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLL-PGDGEVTGGTItfDGRDITHLTD-REFVsirgngiGLVPQD 113
Cdd:PRK13644 15 TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLrPQKGKVLVSGI--DTGDFSKLQGiRKLV-------GIVFQN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 114 PMTNLnpvwtVGSQIKEALR---ANNIATGSEAHKKAIELLEQAGLPNAKKRidqYPHEFSGGMRQRALIAMGLAAHPKL 190
Cdd:PRK13644 86 PETQF-----VGRTVEEDLAfgpENLCLPPIEIRKRVDRALAEIGLEKYRHR---SPKTLSGGQGQCVALAGILTMEPEC 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 191 LIADEPTSALDVTVAKKILDHLDKLtSELGTSVVLITHDLGlAAERADRLVVMQAGRVVETGPALQVLTRPQhpyTKQLI 270
Cdd:PRK13644 158 LIFDEVTSMLDPDSGIAVLERIKKL-HEKGKTIVYITHNLE-ELHDADRIIVMDRGKIVLEGEPENVLSDVS---LQTLG 232
|
....*.
gi 2524658687 271 AAAPSL 276
Cdd:PRK13644 233 LTPPSL 238
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
39-259 |
1.50e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 89.30 E-value: 1.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 39 VHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGDgevTGGTITFDGRDITHLTDREFVSIRGNGIGLVPQDPMTNL 118
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISE---TGQTIVGDYAIPANLKKIKEVKRLRKEIGLVFQFPEYQL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 119 npvwtVGSQIKEALRANNIATGS---EAHKKAIELLEQAGLPnaKKRIDQYPHEFSGGMRQRALIAMGLAAHPKLLIADE 195
Cdd:PRK13645 104 -----FQETIEKDIAFGPVNLGEnkqEAYKKVPELLKLVQLP--EDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDE 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2524658687 196 PTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVLT 259
Cdd:PRK13645 177 PTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFS 240
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
297-524 |
1.62e-19 |
|
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: 87.49 E-value: 1.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 297 EILVAKNLVRDFAI--RGDRpwrkdSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLF--DGKRV 372
Cdd:COG4778 3 TLLEVENLSKTFTLhlQGGK-----RLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 373 ---QGRNRkEELELRR--------------RIqpifqnpyATLDpmrtvhsSIEEPLRihKIGTKKER-EQRVFELLDRV 434
Cdd:COG4778 78 dlaQASPR-EILALRRrtigyvsqflrvipRV--------SALD-------VVAEPLL--ERGVDREEaRARARELLARL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 435 ALPAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVSALD-----VVVQaqvlelLAELQEEMDLAYLFITHDLA 509
Cdd:COG4778 140 NLPERLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDaanraVVVE------LIEEAKARGTAIIGIFHDEE 213
|
250
....*....|....*
gi 2524658687 510 VVRQVADEVIVMEHG 524
Cdd:COG4778 214 VREAVADRVVDVTPF 228
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
38-290 |
2.13e-19 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 87.81 E-value: 2.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGL-LPGDGEVTGGTITF-DGRDITHLTdreFVSIRgngigLVPqdpm 115
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLeTPSAGELLAGTAPLaEAREDTRLM---FQDAR-----LLP---- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 116 tnlnpvWtvgsqiKEALraNNIATGSEAH--KKAIELLEQAGLPNakkRIDQYPHEFSGGMRQRALIAMGLAAHPKLLIA 193
Cdd:PRK11247 95 ------W------KKVI--DNVGLGLKGQwrDAALQALAAVGLAD---RANEWPAALSGGQKQRVALARALIHRPGLLLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 194 DEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVvetGPALQV-LTRPQHPYTKQLIAa 272
Cdd:PRK11247 158 DEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI---GLDLTVdLPRPRRRGSARLAE- 233
|
250
....*....|....*...
gi 2524658687 273 apsLAARRGDRVVAAPTT 290
Cdd:PRK11247 234 ---LEAEVLQRVMSRGES 248
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
14-262 |
3.19e-19 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 89.70 E-value: 3.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 14 TLKDVCigfptttasgrrsKSLTDVV--HDVNLEVFPGETVAIVGESGSGKSTTahaaLGLLPGDGEVTGGTITFDGRDI 91
Cdd:PRK11000 5 TLRNVT-------------KAYGDVVisKDINLDIHEGEFVVFVGPSGCGKSTL----LRMIAGLEDITSGDLFIGEKRM 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 92 THLTDREfvsirgNGIGLVPQDpmTNLNPVWTVgsqikealrANNIATG--------SEAHKK---AIELLEQAGLpnak 160
Cdd:PRK11000 68 NDVPPAE------RGVGMVFQS--YALYPHLSV---------AENMSFGlklagakkEEINQRvnqVAEVLQLAHL---- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 161 krIDQYPHEFSGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRL 240
Cdd:PRK11000 127 --LDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKI 204
|
250 260
....*....|....*....|..
gi 2524658687 241 VVMQAGRVVETGPALQVLTRPQ 262
Cdd:PRK11000 205 VVLDAGRVAQVGKPLELYHYPA 226
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
33-261 |
3.86e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 87.55 E-value: 3.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 33 KSLTDVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLpgdgEVTGGTITFDGRDITHLTDREfvsIRgNGIGLVPQ 112
Cdd:PRK13652 14 SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGIL----KPTSGSVLIRGEPITKENIRE---VR-KFVGLVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 113 DPMTNL-NPvwTVGSQIkeALRANNIATGSEAHKKAI-ELLEQAGLPNAKKRIdqyPHEFSGGMRQRALIAMGLAAHPKL 190
Cdd:PRK13652 86 NPDDQIfSP--TVEQDI--AFGPINLGLDEETVAHRVsSALHMLGLEELRDRV---PHHLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2524658687 191 LIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVLTRP 261
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
319-508 |
3.95e-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: 90.50 E-value: 3.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 319 DSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQgrnRKEELELRRRIQPIFQNPYatl 398
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVS---SLDQDEVRRRVSVCAQDAH--- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 399 dpmrTVHSSIEEPLRihkIGTKKEREQRVFELLDRVALpAEMGRRFPG-----------ELSGGQRQRVAIARALALNPE 467
Cdd:TIGR02868 420 ----LFDTTVRENLR---LARPDATDEELWAALERVGL-ADWLRALPDgldtvlgeggaRLSGGERQRLALARALLADAP 491
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2524658687 468 VVVCDEAVSALDVVVQAQVLELLAELQEEmdLAYLFITHDL 508
Cdd:TIGR02868 492 ILLLDEPTEHLDAETADELLEDLLAALSG--RTVVLITHHL 530
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
323-540 |
3.99e-19 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 86.97 E-value: 3.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 323 AVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRnrKEELELRRRIQPIFQNpyATLDPMR 402
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGL--PGHQIARMGVVRTFQH--VRLFREM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 403 TV--------HSSIEEPLRIHKIGT----KKERE--QRVFELLDRVALpAEMGRRFPGELSGGQRQRVAIARALALNPEV 468
Cdd:PRK11300 96 TVienllvaqHQQLKTGLFSGLLKTpafrRAESEalDRAATWLERVGL-LEHANRQAGNLAYGQQRRLEIARCMVTQPEI 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2524658687 469 VVCDEAVSALDVVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDLFDHPE 540
Cdd:PRK11300 175 LMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNPD 246
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
299-479 |
4.06e-19 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 86.44 E-value: 4.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 299 LVAKNLVRDFAIRgdrpwrkdsfRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQgrnrK 378
Cdd:cd03218 1 LRAENLSKRYGKR----------KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDIT----K 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 379 EELELRRRI--------QPIFQNpyatldpmRTVHSSIEEPLRIHKIgTKKEREQRVFELLDRVALpAEMGRRFPGELSG 450
Cdd:cd03218 67 LPMHKRARLgigylpqeASIFRK--------LTVEENILAVLEIRGL-SKKEREEKLEELLEEFHI-THLRKSKASSLSG 136
|
170 180
....*....|....*....|....*....
gi 2524658687 451 GQRQRVAIARALALNPEVVVCDEAVSALD 479
Cdd:cd03218 137 GERRRVEIARALATNPKFLLLDEPFAGVD 165
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
323-535 |
5.26e-19 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 86.04 E-value: 5.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 323 AVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRnrKEELELRRRI------QPIFqnpya 396
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKL--PPHERARAGIayvpqgREIF----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 397 tldPMRTVHSSIEEPLRIHKiGTKKEREQRVFELLdrvalPA--EMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEA 474
Cdd:TIGR03410 88 ---PRLTVEENLLTGLAALP-RRSRKIPDEIYELF-----PVlkEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2524658687 475 VSALDVVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDL 535
Cdd:TIGR03410 159 TEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
316-479 |
6.49e-19 |
|
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: 85.79 E-value: 6.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 316 WRKDSfRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDP---TEGEVLFDGkrvQGRNRKEeleLRRRIQPIFQ 392
Cdd:cd03234 16 WNKYA-RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNG---QPRKPDQ---FQKCVAYVRQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 393 NPYatLDPMRTVHSSIE--EPLRIHKIGTKKEREQRV-FELLDRVALPAEMGRRFPGeLSGGQRQRVAIARALALNPEVV 469
Cdd:cd03234 89 DDI--LLPGLTVRETLTytAILRLPRKSSDAIRKKRVeDVLLRDLALTRIGGNLVKG-ISGGERRRVSIAVQLLWDPKVL 165
|
170
....*....|
gi 2524658687 470 VCDEAVSALD 479
Cdd:cd03234 166 ILDEPTSGLD 175
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
54-274 |
6.95e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 87.60 E-value: 6.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 54 IVGESGSGKSTTAHAALGLL-PGDGEV------TGGTITFDGRDITHLTDR--EFVSIRgNGIGLVPQDPMTNLnpvwtV 124
Cdd:PRK13631 57 IIGNSGSGKSTLVTHFNGLIkSKYGTIqvgdiyIGDKKNNHELITNPYSKKikNFKELR-RRVSMVFQFPEYQL-----F 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 125 GSQIKEALRANNIATG---SEAHKKAIELLEQAGLPNAkkRIDQYPHEFSGGMRQRALIAMGLAAHPKLLIADEPTSALD 201
Cdd:PRK13631 131 KDTIEKDIMFGPVALGvkkSEAKKLAKFYLNKMGLDDS--YLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLD 208
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2524658687 202 VTVAKKILDhLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVLTRpQHPYTKQLIAAAP 274
Cdd:PRK13631 209 PKGEHEMMQ-LILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTD-QHIINSTSIQVPR 279
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
316-530 |
7.27e-19 |
|
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: 85.16 E-value: 7.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 316 WRKDSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQgrnrKEELE-LRRRIQPIFQNP 394
Cdd:cd03369 16 YAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIS----TIPLEdLRSSLTIIPQDP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 395 yaTLdPMRTVHSSIEEplrihkigTKKEREQRVFELLdRValpAEMGRrfpgELSGGQRQRVAIARALALNPEVVVCDEA 474
Cdd:cd03369 92 --TL-FSGTIRSNLDP--------FDEYSDEEIYGAL-RV---SEGGL----NLSQGQRQLLCLARALLKRPRVLVLDEA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2524658687 475 VSALDVVVQAQVLELLAELQEemDLAYLFITHDLavvRQVA--DEVIVMEHGKMVEHR 530
Cdd:cd03369 153 TASIDYATDALIQKTIREEFT--NSTILTIAHRL---RTIIdyDKILVMDAGEVKEYD 205
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
43-248 |
7.50e-19 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 85.30 E-value: 7.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 43 NLEVFPGETVAIVGESGSGKSTTahaaLGLLPGDGEVTGGTITFDGRDITHLTDREfvsirgNGIGLVPQDpmTNLNPVW 122
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTL----LNLIAGFIEPASGSIKVNDQSHTGLAPYQ------RPVSMLFQE--NNLFAHL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 123 TV----GSQIKEALRANniatgSEAHKKAIELLEQAGLPNAKKRIdqyPHEFSGGMRQRALIAMGLAAHPKLLIADEPTS 198
Cdd:TIGR01277 86 TVrqniGLGLHPGLKLN-----AEQQEKVVDAAQQVGIADYLDRL---PEQLSGGQRQRVALARCLVRPNPILLLDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2524658687 199 ALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRV 248
Cdd:TIGR01277 158 ALDPLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
319-545 |
8.59e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 86.24 E-value: 8.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 319 DSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANmALGLLDPTEGEVLFDGK-RVQGRN---RKEEL-ELRRRIQPIFQN 393
Cdd:PRK14258 18 DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLK-CLNRMNELESEVRVEGRvEFFNQNiyeRRVNLnRLRRQVSMVHPK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 394 PyaTLDPMrTVHSSIEEPLRIHKIGTKKEREQRVFELLDRVALPAEMGRRFPG---ELSGGQRQRVAIARALALNPEVVV 470
Cdd:PRK14258 97 P--NLFPM-SVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLWDEIKHKIHKsalDLSGGQQQRLCIARALAVKPKVLL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 471 CDEAVSALDVVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEH-----GKMVEHRPTDDLFDHPEKEYTQ 545
Cdd:PRK14258 174 MDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNSPHDSRTR 253
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
44-258 |
1.02e-18 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 85.29 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 44 LEVFPGETVAIVGESGSGKSTTAHAALGLLPgdgeVTGGTITFDGRDITHLTDRefvsirgngIGLVPQdpmtNLNPVWT 123
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIP----PAKGTVKVAGASPGKGWRH---------IGYVPQ----RHEFAWD 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 124 VGSQIKEAL---RANNIA----TGSEAHKKAIELLEQAGLPNAKKRIdqyPHEFSGGMRQRALIAMGLAAHPKLLIADEP 196
Cdd:TIGR03771 64 FPISVAHTVmsgRTGHIGwlrrPCVADFAAVRDALRRVGLTELADRP---VGELSGGQRQRVLVARALATRPSVLLLDEP 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2524658687 197 TSALDVTVAKKILDHLDKLTSElGTSVVLITHDLGLAAERADRLVVMQaGRVVETGPALQVL 258
Cdd:TIGR03771 141 FTGLDMPTQELLTELFIELAGA-GTAILMTTHDLAQAMATCDRVVLLN-GRVIADGTPQQLQ 200
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
319-525 |
1.07e-18 |
|
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: 84.44 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 319 DSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGkrvqgrnrkeelelrrRI-----QPIFQN 393
Cdd:cd03250 16 ETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG----------------SIayvsqEPWIQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 394 pyatldpmRTVHSSIeeplrihkIGTKKEREQRVFELLDRVALPAEMgRRFP-------GE----LSGGQRQRVAIARAL 462
Cdd:cd03250 80 --------GTIRENI--------LFGKPFDEERYEKVIKACALEPDL-EILPdgdlteiGEkginLSGGQKQRISLARAV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2524658687 463 ALNPEVVVCDEAVSALDVVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQvADEVIVMEHGK 525
Cdd:cd03250 143 YSDADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
38-247 |
1.17e-18 |
|
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: 84.44 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPgdgeVTGGTITFDGRdithltdrefvsirgngIGLVPQDPmtn 117
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELE----KLSGSVSVPGS-----------------IAYVSQEP--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 118 lnpvWTVGSQIKEalranNIATGS----EAHKKAIELleqAGLpnaKKRIDQYPH-------E----FSGGMRQRALIAM 182
Cdd:cd03250 76 ----WIQNGTIRE-----NILFGKpfdeERYEKVIKA---CAL---EPDLEILPDgdlteigEkginLSGGQKQRISLAR 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2524658687 183 GLAAHPKLLIADEPTSALDVTVAKKILDHLdkLTSEL--GTSVVLITHDLGLaAERADRLVVMQAGR 247
Cdd:cd03250 141 AVYSDADIYLLDDPLSAVDAHVGRHIFENC--ILGLLlnNKTRILVTHQLQL-LPHADQIVVLDNGR 204
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
144-533 |
1.38e-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: 89.07 E-value: 1.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 144 HKKAIELLEQAGLPNAkkrIDQYPHEFSGGMRQRALIAMGLAAHPKLLIADEPTSALDV----TVAKKILDhldklTSEL 219
Cdd:COG1245 190 RGKLDELAEKLGLENI---LDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIyqrlNVARLIRE-----LAEE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 220 GTSVVLITHDLGLAAERADRLVVMQAgrvvETGpALQVLTRPQhpytkqliaaapslAARRGdrvvaapttsdadqkeI- 298
Cdd:COG1245 262 GKYVLVVEHDLAILDYLADYVHILYG----EPG-VYGVVSKPK--------------SVRVG----------------In 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 299 ------LVAKNL-VRDFAIRGD-RPWRKDSFRAV----DDIS-----FTL-------RRGRTIGIVGESGSGKSTVANMA 354
Cdd:COG1245 307 qyldgyLPEENVrIRDEPIEFEvHAPRREKEEETlveyPDLTksyggFSLeveggeiREGEVLGIVGPNGIGKTTFAKIL 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 355 LGLLDPTEGEVLFDGK--------------RVqgrnrkEELeLRRRIQPIFQNPYatldpmrtVHSSIEEPLRIHKIgtk 420
Cdd:COG1245 387 AGVLKPDEGEVDEDLKisykpqyispdydgTV------EEF-LRSANTDDFGSSY--------YKTEIIKPLGLEKL--- 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 421 keREQRVfelldrvalpaemgrrfpGELSGGQRQRVAIARALALNPEVVVCDEAVSALDVVVQAQVLELLAELQEEMDLA 500
Cdd:COG1245 449 --LDKNV------------------KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKT 508
|
410 420 430
....*....|....*....|....*....|....*...
gi 2524658687 501 YLFITHDLAVVRQVADEVIVME-----HGKmvEHRPTD 533
Cdd:COG1245 509 AMVVDHDIYLIDYISDRLMVFEgepgvHGH--ASGPMD 544
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
339-527 |
1.38e-18 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 87.24 E-value: 1.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 339 IVGESGSGKSTVANMALGLLDPTEGE------VLFDgkRVQGRNRKEElelRRRIQPIFQNpyATLDPmrtvHSSIEEPL 412
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRivlngrVLFD--AEKGICLPPE---KRRIGYVFQD--ARLFP----HYKVRGNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 413 RIhkiGTKKEREQ---RVFELLDRVALPaemgRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVSALDVVVQAQVLEL 489
Cdd:PRK11144 98 RY---GMAKSMVAqfdKIVALLGIEPLL----DRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPY 170
|
170 180 190
....*....|....*....|....*....|....*...
gi 2524658687 490 LAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMV 527
Cdd:PRK11144 171 LERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVK 208
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
322-528 |
2.22e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 88.36 E-value: 2.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 322 RAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLdPTEGEVLFDGKRVQgrnrkeELEL---RRRIQPIFQNPyatl 398
Cdd:PRK11174 364 TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELR------ELDPeswRKHLSWVGQNP---- 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 399 dpmRTVHSSIEEPLRIhkiGTKKEREQRVFELLDRvALPAEMGRRFP-------GE----LSGGQRQRVAIARALALNPE 467
Cdd:PRK11174 433 ---QLPHGTLRDNVLL---GNPDASDEQLQQALEN-AWVSEFLPLLPqgldtpiGDqaagLSVGQAQRLALARALLQPCQ 505
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2524658687 468 VVVCDEAVSALDVVVQAQVLELLAELQEemDLAYLFITHDLAVVRQVaDEVIVMEHGKMVE 528
Cdd:PRK11174 506 LLLLDEPTASLDAHSEQLVMQALNAASR--RQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQ 563
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
6-253 |
2.24e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 86.42 E-value: 2.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 6 NTSAAPILTLKDVCIGFptttASGRRSKSLTDVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGDGevtgGTIT 85
Cdd:PRK13536 28 EAKASIPGSMSTVAIDL----AGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDA----GKIT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 86 FDGRDIThltDREFVSIRGngIGLVPQdpMTNLNPVWTVgsqikealRANNIATGS--EAHKKAIE-----LLEQAGLpn 158
Cdd:PRK13536 100 VLGVPVP---ARARLARAR--IGVVPQ--FDNLDLEFTV--------RENLLVFGRyfGMSTREIEavipsLLEFARL-- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 159 aKKRIDQYPHEFSGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSeLGTSVVLITHDLGLAAERAD 238
Cdd:PRK13536 163 -ESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLA-RGKTILLTTHFMEEAERLCD 240
|
250
....*....|....*.
gi 2524658687 239 RLVVMQAGR-VVETGP 253
Cdd:PRK13536 241 RLCVLEAGRkIAEGRP 256
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
13-252 |
2.63e-18 |
|
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: 84.12 E-value: 2.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 13 LTLKDVCIGFPTTTASGRRSKSLTD-----------VVHDVNLEVFPGETVAIVGESGSGKSTTahaaLGLLPGDGEVTG 81
Cdd:cd03220 1 IELENVSKSYPTYKGGSSSLKKLGIlgrkgevgefwALKDVSFEVPRGERIGLIGRNGAGKSTL----LRLLAGIYPPDS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 82 GTITFDGRDithltdrefVSIRGNGIGLvpqdpmtnlNPVWTVGSQIKEALRANNIaTGSEAHKKAIELLEQAGLPNAkk 161
Cdd:cd03220 77 GTVTVRGRV---------SSLLGLGGGF---------NPELTGRENIYLNGRLLGL-SRKEIDEKIDEIIEFSELGDF-- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 162 rIDQYPHEFSGGMRQRalIAMGLAAH--PKLLIADEPTSALDVTVAKKILDHLDKLTSElGTSVVLITHDLGLAAERADR 239
Cdd:cd03220 136 -IDLPVKTYSSGMKAR--LAFAIATAlePDILLIDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDR 211
|
250
....*....|...
gi 2524658687 240 LVVMQAGRVVETG 252
Cdd:cd03220 212 ALVLEKGKIRFDG 224
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
10-260 |
2.88e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 84.36 E-value: 2.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 10 APILTLKDVCIGFPTTTASGRRSKSLTD-----------VVHDVNLEVFPGETVAIVGESGSGKSTTahaaLGLLPGDGE 78
Cdd:COG1134 2 SSMIEVENVSKSYRLYHEPSRSLKELLLrrrrtrreefwALKDVSFEVERGESVGIIGRNGAGKSTL----LKLIAGILE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 79 VTGGTITFDGRdITHLTdrEFvsirgnGIGLVPQdpMTnlnpvwtvGSQikealranNI--------ATGSEAHKKAIEL 150
Cdd:COG1134 78 PTSGRVEVNGR-VSALL--EL------GAGFHPE--LT--------GRE--------NIylngrllgLSRKEIDEKFDEI 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 151 LEQAGLpnaKKRIDQyP-HEFSGGMRQRalIAMGLAAH--PKLLIADEPTSALDVTVAKKILDHLDKLTSElGTSVVLIT 227
Cdd:COG1134 131 VEFAEL---GDFIDQ-PvKTYSSGMRAR--LAFAVATAvdPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVS 203
|
250 260 270
....*....|....*....|....*....|...
gi 2524658687 228 HDLGLAAERADRLVVMQAGRVVETGPALQVLTR 260
Cdd:COG1134 204 HSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
38-258 |
6.00e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 84.07 E-value: 6.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETVAIVGESGSGKSTTahaaLGLLPGDGEVTGGTITFDGRDITHLTDREFvsirGNGIGLVPQ----- 112
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTL----LKMLGRHQPPSEGEILLDAQPLESWSSKAF----ARKVAYLPQqlpaa 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 113 DPMTNLNPVWTVGSQIKEALRAnniaTGSEAHKKAIELLEQAGL-PNAKKRIDQypheFSGGMRQRALIAMGLAAHPKLL 191
Cdd:PRK10575 98 EGMTVRELVAIGRYPWHGALGR----FGAADREKVEEAISLVGLkPLAHRLVDS----LSGGERQRAWIAMLVAQDSRCL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2524658687 192 IADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVL 258
Cdd:PRK10575 170 LLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELM 236
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
33-254 |
9.55e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 83.60 E-value: 9.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 33 KSLTDVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLpgdgEVTGGTITFDGRditHLTDREFVSIRgNGIGLVPQ 112
Cdd:PRK13642 17 ESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLF----EEFEGKVKIDGE---LLTAENVWNLR-RKIGMVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 113 DPMTNLnpvwtVGSQIKEAL---RANNIATGSEAHKKAIELLEQAGLPNAKKRidqYPHEFSGGMRQRALIAMGLAAHPK 189
Cdd:PRK13642 89 NPDNQF-----VGATVEDDVafgMENQGIPREEMIKRVDEALLAVNMLDFKTR---EPARLSGGQKQRVAVAGIIALRPE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2524658687 190 LLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAErADRLVVMQAGRVV-ETGPA 254
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIkEAAPS 225
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
323-529 |
1.35e-17 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 85.93 E-value: 1.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 323 AVDDISFTLRRGRT--------------IGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKeelELRRRIQ 388
Cdd:PRK10790 342 DIDNVSFAYRDDNLvlqninlsvpsrgfVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHS---VLRQGVA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 389 PIFQNPYATLDPMR---TVHSSIeeplrihkigtkkeREQRVFELLDRVALpAEMGRRFP-------GE----LSGGQRQ 454
Cdd:PRK10790 419 MVQQDPVVLADTFLanvTLGRDI--------------SEEQVWQALETVQL-AELARSLPdglytplGEqgnnLSVGQKQ 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2524658687 455 RVAIARALALNPEVVVCDEAVSALDVVVQAQVLELLAELQEEMDLayLFITHDLAVVRQvADEVIVMEHGKMVEH 529
Cdd:PRK10790 484 LLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTL--VVIAHRLSTIVE-ADTILVLHRGQAVEQ 555
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
324-537 |
1.38e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 84.11 E-value: 1.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 324 VDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEelelRRRIQPIFQnpYATLDPMRT 403
Cdd:PRK13536 57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLA----RARIGVVPQ--FDNLDLEFT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 404 VHSSIEEPLRIHKIGTkKEREQRVFELLDRVALPAEMGRRFpGELSGGQRQRVAIARALALNPEVVVCDEAVSALDVVVQ 483
Cdd:PRK13536 131 VRENLLVFGRYFGMST-REIEAVIPSLLEFARLESKADARV-SDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHAR 208
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2524658687 484 aQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHG-KMVEHRPtDDLFD 537
Cdd:PRK13536 209 -HLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGrKIAEGRP-HALID 261
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
338-540 |
1.46e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 82.75 E-value: 1.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 338 GIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQgRNRKEELELRRRIQPIFQNP-----YATLDpmrtvhSSIEEPL 412
Cdd:PRK13638 31 GLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLD-YSKRGLLALRQQVATVFQDPeqqifYTDID------SDIAFSL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 413 RihKIGT-KKEREQRVFELLDRValPAEMGRRFPGE-LSGGQRQRVAIARALALNPEVVVCDEAVSALDVVVQAQVLELL 490
Cdd:PRK13638 104 R--NLGVpEAEITRRVDEALTLV--DAQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAII 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2524658687 491 AELQEEMDlAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDLFDHPE 540
Cdd:PRK13638 180 RRIVAQGN-HVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTE 228
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
323-539 |
1.47e-17 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 85.92 E-value: 1.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 323 AVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQgRNRKEELelRRRIQPIFQNPYATLDpmr 402
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLT-KLQLDSW--RSRLAVVSQTPFLFSD--- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 403 TVHSSIEeplrIHKIGTKKEREQRVFELL----DRVALP----AEMGRRfpG-ELSGGQRQRVAIARALALNPEVVVCDE 473
Cdd:PRK10789 404 TVANNIA----LGRPDATQQEIEHVARLAsvhdDILRLPqgydTEVGER--GvMLSGGQKQRISIARALLLNAEILILDD 477
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2524658687 474 AVSALDVVVQAQVLELLAELQEEMDLayLFITHDLAVVRQvADEVIVMEHGKMVEHRPTDDLFDHP 539
Cdd:PRK10789 478 ALSAVDGRTEHQILHNLRQWGEGRTV--IISAHRLSALTE-ASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
38-252 |
1.70e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 83.32 E-value: 1.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGDGevtgGTITFDGRDIThlTDREFVSIRgngIGLVPQdpMTN 117
Cdd:PRK13537 22 VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDA----GSISLCGEPVP--SRARHARQR---VGVVPQ--FDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 118 LNPVWTVGSQIKEALRANNIATGsEAHKKAIELLEQAGLPNakkRIDQYPHEFSGGMRQRALIAMGLAAHPKLLIADEPT 197
Cdd:PRK13537 91 LDPDFTVRENLLVFGRYFGLSAA-AARALVPPLLEFAKLEN---KADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2524658687 198 SALDVTVAKKILDHLDKLTSElGTSVVLITHDLGLAAERADRLVVMQAGRVVETG 252
Cdd:PRK13537 167 TGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEG 220
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
38-228 |
4.07e-17 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 80.39 E-value: 4.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGDgevtggtitfdgrdithltdrefvsiRGNGIGLVPQdpmtn 117
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGT--------------------------PVAGCVDVPD----- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 118 lNPVWTVGSQIKEALRANNIATgseahkkAIELLEQAGLPNA---KKRidqyPHEFSGGMRQRALIAMGLAAHPKLLIAD 194
Cdd:COG2401 94 -NQFGREASLIDAIGRKGDFKD-------AVELLNAVGLSDAvlwLRR----FKELSTGQKFRFRLALLLAERPKLLVID 161
|
170 180 190
....*....|....*....|....*....|....
gi 2524658687 195 EPTSALDVTVAKKILDHLDKLTSELGTSVVLITH 228
Cdd:COG2401 162 EFCSHLDRQTAKRVARNLQKLARRAGITLVVATH 195
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
24-259 |
4.66e-17 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 81.19 E-value: 4.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 24 TTTASGRRSKSLT------DVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLL-PGDGEVTggtitFDGRDITHLTD 96
Cdd:PRK10253 2 TESVARLRGEQLTlgygkyTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMtPAHGHVW-----LDGEHIQHYAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 97 REfVSIRgngIGLVPQDPMT----NLNPVWTVGSQIKEALRANNIATGSEAHKKAIELLEQAGLpnAKKRIDQypheFSG 172
Cdd:PRK10253 77 KE-VARR---IGLLAQNATTpgdiTVQELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHL--ADQSVDT----LSG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 173 GMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETG 252
Cdd:PRK10253 147 GQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQG 226
|
....*..
gi 2524658687 253 PALQVLT 259
Cdd:PRK10253 227 APKEIVT 233
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
7-254 |
7.22e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 83.70 E-value: 7.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 7 TSAAPILTLKDVCIgfptTTASGRRsksltdVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLP-GDGEVT---GG 82
Cdd:COG4178 357 TSEDGALALEDLTL----RTPDGRP------LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPyGSGRIArpaGA 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 83 TITFdgrdithltdrefvsirgngiglVPQDPMTNLnpvwtvGSqIKEAL-RANNIATGSEAhkKAIELLEQAGLPNAKK 161
Cdd:COG4178 427 RVLF-----------------------LPQRPYLPL------GT-LREALlYPATAEAFSDA--ELREALEAVGLGHLAE 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 162 RIDQ---YPHEFSGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHldkLTSEL-GTSVVLITHDLGLAAeRA 237
Cdd:COG4178 475 RLDEeadWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQL---LREELpGTTVISVGHRSTLAA-FH 550
|
250
....*....|....*..
gi 2524658687 238 DRLVVMQAGRVVETGPA 254
Cdd:COG4178 551 DRVLELTGDGSWQLLPA 567
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
8-261 |
8.24e-17 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 80.42 E-value: 8.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 8 SAAPILTLKDVCIGFPTTTAsgrrsksltdvVHDVNLEVFPGETVAIVGESGSGKSTTahaaLGLLPGDGEVTGGTITFD 87
Cdd:PRK11300 1 MSQPLLSVSGLMMRFGGLLA-----------VNNVNLEVREQEIVSLIGPNGAGKTTV----FNCLTGFYKPTGGTILLR 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 88 GRDITHLTD---------REFVSIRgngigLVPQdpMTNL-NPVWTVGSQIKEALRANNIATGS------EAHKKAIELL 151
Cdd:PRK11300 66 GQHIEGLPGhqiarmgvvRTFQHVR-----LFRE--MTVIeNLLVAQHQQLKTGLFSGLLKTPAfrraesEALDRAATWL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 152 EQAGLPNAKKRidqYPHEFSGGMRQRALIAMGLAAHPKLLIADEPTSALDVTvAKKILDHL-DKLTSELGTSVVLITHDL 230
Cdd:PRK11300 139 ERVGLLEHANR---QAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPK-ETKELDELiAELRNEHNVTVLLIEHDM 214
|
250 260 270
....*....|....*....|....*....|.
gi 2524658687 231 GLAAERADRLVVMQAGRVVETGPALQVLTRP 261
Cdd:PRK11300 215 KLVMGISDRIYVVNQGTPLANGTPEEIRNNP 245
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
327-479 |
8.90e-17 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 79.82 E-value: 8.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 327 ISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEELELR-RRIQPIFQNpyATLDPMRTVH 405
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRaKHVGFVFQS--FMLIPTLNAL 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2524658687 406 SSIEEPLRIHKIGTKKEREQRVfELLDRVALpAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVSALD 479
Cdd:PRK10584 107 ENVELPALLRGESSRQSRNGAK-ALLEQLGL-GKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
324-534 |
1.18e-16 |
|
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: 82.87 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 324 VDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEeleLRRRI--QPifQNPyaTLDPm 401
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREE---LGRHIgyLP--QDV--ELFD- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 402 rtvhssieeplrihkiGTKKE--------REQRVFELLDRVALpAEMGRRFP-------GE----LSGGQRQRVAIARAL 462
Cdd:COG4618 420 ----------------GTIAEniarfgdaDPEKVVAAAKLAGV-HEMILRLPdgydtriGEggarLSGGQRQRIGLARAL 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 463 ALNPEVVVCDEAVSALDV-----VVQAqvlellaelqeemdLAYL--------FITHDLAVVrQVADEVIVMEHGKMVEH 529
Cdd:COG4618 483 YGDPRLVVLDEPNSNLDDegeaaLAAA--------------IRALkargatvvVITHRPSLL-AAVDKLLVLRDGRVQAF 547
|
....*
gi 2524658687 530 RPTDD 534
Cdd:COG4618 548 GPRDE 552
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
334-525 |
1.26e-16 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 79.72 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 334 GRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQgrnrkeelELRRRIQPIFQNpyATLDPMRTVHSSIeeplr 413
Cdd:PRK11247 38 GQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLA--------EAREDTRLMFQD--ARLLPWKKVIDNV----- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 414 ihKIGTKKEREQRVFELLDRVALpAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVSALDVVVQAQVLELLAEL 493
Cdd:PRK11247 103 --GLGLKGQWRDAALQALAAVGL-ADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESL 179
|
170 180 190
....*....|....*....|....*....|..
gi 2524658687 494 QEEMDLAYLFITHDLAVVRQVADEVIVMEHGK 525
Cdd:PRK11247 180 WQQHGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
7-254 |
1.40e-16 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 79.69 E-value: 1.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 7 TSAAPILTLKD--VCIGfptttasgrrsksLTDVVHDVNLEVFPGETVAIVGESGSGKSTTA-----HAALgllpgdgEV 79
Cdd:CHL00131 2 NKNKPILEIKNlhASVN-------------ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSkviagHPAY-------KI 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 80 TGGTITFDGRDITHLTDREfvsiRGN-GIGLVPQdpmtnlNPVWTVGSQIKEALRANNIATGSEAHKKAIELLEQAGLPN 158
Cdd:CHL00131 62 LEGDILFKGESILDLEPEE----RAHlGIFLAFQ------YPIEIPGVSNADFLRLAYNSKRKFQGLPELDPLEFLEIIN 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 159 AK-KRIDQYPH--------EFSGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLtSELGTSVVLITH- 228
Cdd:CHL00131 132 EKlKLVGMDPSflsrnvneGFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKL-MTSENSIILITHy 210
|
250 260
....*....|....*....|....*..
gi 2524658687 229 -DLgLAAERADRLVVMQAGRVVETGPA 254
Cdd:CHL00131 211 qRL-LDYIKPDYVHVMQNGKIIKTGDA 236
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
322-527 |
1.56e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 79.74 E-value: 1.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 322 RAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVqgrNRKEELELRRRIQPIFQNPYATldpm 401
Cdd:COG1101 20 RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDV---TKLPEYKRAKYIGRVFQDPMMG---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 402 rTVHS-SIEEPLRIH---------KIGTKKEREQRVFELL--------DRvaLPAEMGrrfpgELSGGQRQrvaiarALA 463
Cdd:COG1101 93 -TAPSmTIEENLALAyrrgkrrglRRGLTKKRRELFRELLatlglgleNR--LDTKVG-----LLSGGQRQ------ALS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2524658687 464 L------NPEVVVCDEAVSALDVVVQAQVLELLAELQEEMDLAYLFITHDL--AVvrQVADEVIVMEHGKMV 527
Cdd:COG1101 159 LlmatltKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMeqAL--DYGNRLIMMHEGRII 228
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
12-252 |
1.61e-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: 78.85 E-value: 1.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 12 ILTLKDVCIGFPtttasgrRSKSLTDVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGDGeVTGGTITFDGRDI 91
Cdd:cd03234 3 VLPWWDVGLKAK-------NWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGG-TTSGQILFNGQPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 92 T-HLTDREFvsirgngiGLVPQDpmTNLNPVWTVgsqiKEALR-ANNIATGSEAHKK------AIELLEQAGLpnakKRI 163
Cdd:cd03234 75 KpDQFQKCV--------AYVRQD--DILLPGLTV----RETLTyTAILRLPRKSSDAirkkrvEDVLLRDLAL----TRI 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 164 -DQYPHEFSGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSelGTSVVLIThdlgLAAERA----- 237
Cdd:cd03234 137 gGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLAR--RNRIVILT----IHQPRSdlfrl 210
|
250
....*....|....*.
gi 2524658687 238 -DRLVVMQAGRVVETG 252
Cdd:cd03234 211 fDRILLLSSGEIVYSG 226
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
322-523 |
1.65e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 79.39 E-value: 1.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 322 RAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLfdgkrvqgrnRKEELelrrRIQPIFQNPYatLDPm 401
Cdd:PRK09544 18 RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK----------RNGKL----RIGYVPQKLY--LDT- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 402 rTVHSSIEEPLRIHKiGTKKereQRVFELLDRVA----LPAEMGRrfpgeLSGGQRQRVAIARALALNPEVVVCDEAVSA 477
Cdd:PRK09544 81 -TLPLTVNRFLRLRP-GTKK---EDILPALKRVQaghlIDAPMQK-----LSGGETQRVLLARALLNRPQLLVLDEPTQG 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2524658687 478 LDVVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEH 523
Cdd:PRK09544 151 VDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
40-253 |
1.66e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 82.79 E-value: 1.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 40 HDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGDGEVtGGTITFDGRDIthltDREFVSIRGngiGLVPQDPMtnLN 119
Cdd:TIGR00955 42 KNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKG-SGSVLLNGMPI----DAKEMRAIS---AYVQQDDL--FI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 120 PVWTVGSQ--IKEALRANNIATGSEAHKKAIELLEQAGLPNAKKRIDQYPHE---FSGGMRQRALIAMGLAAHPKLLIAD 194
Cdd:TIGR00955 112 PTLTVREHlmFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGVPGRvkgLSGGERKRLAFASELLTDPPLLFCD 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2524658687 195 EPTSALDVTVAKKILDHLDKLtSELGTSVVLITH----DLglaAERADRLVVMQAGRVVETGP 253
Cdd:TIGR00955 192 EPTSGLDSFMAYSVVQVLKGL-AQKGKTIICTIHqpssEL---FELFDKIILMAEGRVAYLGS 250
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
30-253 |
1.88e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 80.52 E-value: 1.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 30 RRSKSLTDVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLL-PgdgevTGGTITFDGRDItHLTDREFVSIrgngIG 108
Cdd:COG4586 29 RREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILvP-----TSGEVRVLGYVP-FKRRKEFARR----IG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 109 LV------------PQDPMTNLNPVWtvgsQIKEALRANNIatgseahKKAIELLEQAGLpnakkrIDQYPHEFSGGMRQ 176
Cdd:COG4586 99 VVfgqrsqlwwdlpAIDSFRLLKAIY----RIPDAEYKKRL-------DELVELLDLGEL------LDTPVRQLSLGQRM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2524658687 177 RALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETGP 253
Cdd:COG4586 162 RCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGS 238
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
39-256 |
2.00e-16 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 79.29 E-value: 2.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 39 VHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGDG------EVTGGTITFDGR---DIT-------------HLTD 96
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagshiELLGRTVQREGRlarDIRksrantgyifqqfNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 97 REFVsIRGNGIGLVPQDPMTNLNPVWTVGSQIKEALRAnniatgseahkkaielLEQAGLPN-AKKRIDQypheFSGGMR 175
Cdd:PRK09984 100 RLSV-LENVLIGALGSTPFWRTCFSWFTREQKQRALQA----------------LTRVGMVHfAHQRVST----LSGGQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 176 QRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPAL 255
Cdd:PRK09984 159 QRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQ 238
|
.
gi 2524658687 256 Q 256
Cdd:PRK09984 239 Q 239
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
30-252 |
2.25e-16 |
|
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: 78.53 E-value: 2.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 30 RRSKSLTDVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLL-PGDGEVT-GGTITFDGRdithltdREFVSirgnGI 107
Cdd:cd03267 28 KRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLqPTSGEVRvAGLVPWKRR-------KKFLR----RI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 108 GLVpqdpMTNLNPVWTVGSQIkEALRANNIATGSEAHKKAIELLEQAGLPNAKKRIDQYPHEFSGGMRQRALIAMGLAAH 187
Cdd:cd03267 97 GVV----FGQKTQLWWDLPVI-DSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2524658687 188 PKLLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETG 252
Cdd:cd03267 172 PEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
298-535 |
2.29e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 81.90 E-value: 2.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 298 ILVAKNLVRDFairgdrpwrkDSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLdPT---EGEVLFDGKRVQG 374
Cdd:PRK13549 5 LLEMKNITKTF----------GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 375 RNRKE-ElelRRRIQPIFQNpyATLDPMRTVHSSI---EEPLRiHKIGTKKEREQRVFELLDRVALPAEMGRRFpGELSG 450
Cdd:PRK13549 74 SNIRDtE---RAGIAIIHQE--LALVKELSVLENIflgNEITP-GGIMDYDAMYLRAQKLLAQLKLDINPATPV-GNLGL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 451 GQRQRVAIARALALNPEVVVCDEAVSALdVVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHR 530
Cdd:PRK13549 147 GQQQLVEIAKALNKQARLLILDEPTASL-TESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTR 225
|
....*
gi 2524658687 531 PTDDL 535
Cdd:PRK13549 226 PAAGM 230
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
42-252 |
2.64e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 82.20 E-value: 2.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 42 VNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGDGEvtggtITFDGrdiTHLTDREFVSIRGNgIGLVPQDPMTnlnpv 121
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQGS-----LKING---IELRELDPESWRKH-LSWVGQNPQL----- 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 122 wtvgsqIKEALRAnNIATG-SEAHKKAIE-LLEQAglpNAKKRIDQYPH-----------EFSGGMRQRALIAMGLAAHP 188
Cdd:PRK11174 435 ------PHGTLRD-NVLLGnPDASDEQLQqALENA---WVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPC 504
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2524658687 189 KLLIADEPTSALDVTVAKKILDHLDKLTSelGTSVVLITHDLGlAAERADRLVVMQAGRVVETG 252
Cdd:PRK11174 505 QLLLLDEPTASLDAHSEQLVMQALNAASR--RQTTLMVTHQLE-DLAQWDQIWVMQDGQIVQQG 565
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
324-538 |
2.86e-16 |
|
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: 81.63 E-value: 2.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 324 VDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEeleLRRRIQPIFQNpyATLDPmrt 403
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRET---FGKHIGYLPQD--VELFP--- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 404 vhssieeplrihkiGTKKEREQRVFELLD--------RVALPAEMGRRFP-----------GELSGGQRQRVAIARALAL 464
Cdd:TIGR01842 406 --------------GTVAENIARFGENADpekiieaaKLAGVHELILRLPdgydtvigpggATLSGGQRQRIALARALYG 471
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2524658687 465 NPEVVVCDEAVSALDVVVQAQVLELLAELQEEMDLAyLFITHDLAVVrQVADEVIVMEHGKMVEHRPTDDLFDH 538
Cdd:TIGR01842 472 DPKLVVLDEPNSNLDEEGEQALANAIKALKARGITV-VVITHRPSLL-GCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
38-278 |
3.11e-16 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 81.69 E-value: 3.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPgdgeVTGGTITFDGRDITHLTDRefvSIRgNGIGLVPQDPMTn 117
Cdd:PRK10790 356 VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYP----LTEGEIRLDGRPLSSLSHS---VLR-QGVAMVQQDPVV- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 118 lnpvwtvgsqIKEALRAnNIATG---SEAHK-KAIELLEQA----GLPNA-KKRIDQYPHEFSGGMRQRALIAMGLAAHP 188
Cdd:PRK10790 427 ----------LADTFLA-NVTLGrdiSEEQVwQALETVQLAelarSLPDGlYTPLGEQGNNLSVGQKQLLALARVLVQTP 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 189 KLLIADEPTSALDVTVAKKILDHLDKLTSElgTSVVLITHDLGLAAErADRLVVMQAGRVVETGPALQVLTRPQHPYTK- 267
Cdd:PRK10790 496 QILILDEATANIDSGTEQAIQQALAAVREH--TTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQLLAAQGRYWQMy 572
|
250
....*....|.
gi 2524658687 268 QLIAAAPSLAA 278
Cdd:PRK10790 573 QLQLAGEELAA 583
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
322-526 |
3.86e-16 |
|
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: 76.70 E-value: 3.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 322 RAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEELELR-------RRIQPIFQNp 394
Cdd:cd03215 14 GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGiayvpedRKREGLVLD- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 395 yatldpmrtvhSSIEEPLRIHKIgtkkereqrvfelldrvalpaemgrrfpgeLSGGQRQRVAIARALALNPEVVVCDEA 474
Cdd:cd03215 93 -----------LSVAENIALSSL------------------------------LSGGNQQKVVLARWLARDPRVLILDEP 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2524658687 475 VSALDVVVQAQVLELLAELQEEmDLAYLFITHDLAVVRQVADEVIVMEHGKM 526
Cdd:cd03215 132 TRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
38-480 |
5.19e-16 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 81.13 E-value: 5.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLlpgDGEVTGgtitfdgrdithltdrEFVSIRGNGIGLVPQDPmtN 117
Cdd:TIGR03719 20 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV---DKDFNG----------------EARPQPGIKVGYLPQEP--Q 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 118 LNPVWTVGSQIKEAL--------RANNIATG-----------SEAHKKAIELLEQAGLPNAKKRIDQYPH---------- 168
Cdd:TIGR03719 79 LDPTKTVRENVEEGVaeikdaldRFNEISAKyaepdadfdklAAEQAELQEIIDAADAWDLDSQLEIAMDalrcppwdad 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 169 --EFSGGMRQRALIAMGLAAHPKLLIADEPTSALDV-TVAkkildHLDKLTSELGTSVVLITHD---LGLAAE------- 235
Cdd:TIGR03719 159 vtKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAeSVA-----WLERHLQEYPGTVVAVTHDryfLDNVAGwileldr 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 236 ----------------RADRLVvMQAGRVVETGPALQ-----VLTRPQHPYTKQliaaapslAAR--RGDRVVAAPTTSD 292
Cdd:TIGR03719 234 grgipwegnysswleqKQKRLE-QEEKEESARQKTLKrelewVRQSPKGRQAKS--------KARlaRYEELLSQEFQKR 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 293 ADQKEILV------------AKNLVRDFairGDRPwrkdsfrAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDP 360
Cdd:TIGR03719 305 NETAEIYIppgprlgdkvieAENLTKAF---GDKL-------LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQP 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 361 TEGEVLFdGKRV------QGRNrkeelelrrriqpifqnpyaTLDPMRTVHSSIEEPLRIHKIGtKKEREQRVFelLDRV 434
Cdd:TIGR03719 375 DSGTIEI-GETVklayvdQSRD--------------------ALDPNKTVWEEISGGLDIIKLG-KREIPSRAY--VGRF 430
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2524658687 435 ALPAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVSALDV 480
Cdd:TIGR03719 431 NFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDV 476
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
322-535 |
7.68e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 80.21 E-value: 7.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 322 RAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEELELrrRIQPIFQNpYATLDPM 401
Cdd:PRK09700 19 HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQL--GIGIIYQE-LSVIDEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 402 rtvhsSIEEPLRIHKIGTKK----------EREQRVFELLDRVALPAEMgRRFPGELSGGQRQRVAIARALALNPEVVVC 471
Cdd:PRK09700 96 -----TVLENLYIGRHLTKKvcgvniidwrEMRVRAAMMLLRVGLKVDL-DEKVANLSISHKQMLEIAKTLMLDAKVIIM 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2524658687 472 DEAVSALdvvVQAQVLE--LLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDL 535
Cdd:PRK09700 170 DEPTSSL---TNKEVDYlfLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
39-248 |
9.47e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 80.05 E-value: 9.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 39 VHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPgdgeVTGGTITFDGRDITHLTDREFVSirgNGI----------G 108
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALP----RTSGYVTLDGHEVVTRSPQDGLA---NGIvyisedrkrdG 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 109 LVpqdpmtnlnpvwtVGSQIKE-----ALRANNIATGSEAHKKAIELLEQ-AGLPNAKK-RIDQYPHEFSGGMRQRALIA 181
Cdd:PRK10762 341 LV-------------LGMSVKEnmsltALRYFSRAGGSLKHADEQQAVSDfIRLFNIKTpSMEQAIGLLSGGNQQKVAIA 407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2524658687 182 MGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSElGTSVVLITHD----LGLaaerADRLVVMQAGRV 248
Cdd:PRK10762 408 RGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEmpevLGM----SDRILVMHEGRI 473
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
38-263 |
9.70e-16 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 77.56 E-value: 9.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGDGEVTGGTITFDgrdithltdrefVSIRGNGIGLVPQDPMTN 117
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAPRGARVTGD------------VTLNGEPLAAIDAPRLAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 118 LNPVWTVGSQIKEALRANNI----------ATGSEAHKK---AIELLEQAGlpnAKKRIDQYPHEFSGGMRQRALIAMGL 184
Cdd:PRK13547 84 LRAVLPQAAQPAFAFSAREIvllgrypharRAGALTHRDgeiAWQALALAG---ATALVGRDVTTLSGGELARVQFARVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 185 A---------AHPKLLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPAL 255
Cdd:PRK13547 161 AqlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPA 240
|
....*...
gi 2524658687 256 QVLTrPQH 263
Cdd:PRK13547 241 DVLT-PAH 247
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
323-521 |
1.23e-15 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 75.35 E-value: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 323 AVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVlfdgkRVQGRNRKEELELRRRIQPIFqnPYATLDPMR 402
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-----RRAGGARVAYVPQRSEVPDSL--PLTVRDLVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 403 TVHSSIEEPLRIHKigtkKEREQRVFELLDRVALPAEMGRRFpGELSGGQRQRVAIARALALNPEVVVCDEAVSALDVVV 482
Cdd:NF040873 80 MGRWARRGLWRRLT----RDDRAAVDDALERVGLADLAGRQL-GELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAES 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 2524658687 483 QAQVLELLAELQEEmDLAYLFITHDLAVVRQvADEVIVM 521
Cdd:NF040873 155 RERIIALLAEEHAR-GATVVVVTHDLELVRR-ADPCVLL 191
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
322-526 |
1.41e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 78.73 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 322 RAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEeleLRRRIQPIFQNpyATLDPM 401
Cdd:PRK09536 17 TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARA---ASRRVASVPQD--TSLSFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 402 RTVHSSIEEPLRIH--KIGTKKEREQRVFE-LLDRVALPAEMGRRFPgELSGGQRQRVAIARALALNPEVVVCDEAVSAL 478
Cdd:PRK09536 92 FDVRQVVEMGRTPHrsRFDTWTETDRAAVErAMERTGVAQFADRPVT-SLSGGERQRVLLARALAQATPVLLLDEPTASL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2524658687 479 DVVVQAQVLELLAELQEEmDLAYLFITHDLAVVRQVADEVIVMEHGKM 526
Cdd:PRK09536 171 DINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRV 217
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
324-479 |
1.74e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 77.54 E-value: 1.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 324 VDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEelelRRRIQ--PIFQNpyatLDPM 401
Cdd:PRK13537 23 VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA----RQRVGvvPQFDN----LDPD 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2524658687 402 RTVHSSIEEPLRIHKIGTKKEREqRVFELLDRVALPAEMGRRFpGELSGGQRQRVAIARALALNPEVVVCDEAVSALD 479
Cdd:PRK13537 95 FTVRENLLVFGRYFGLSAAAARA-LVPPLLEFAKLENKADAKV-GELSGGMKRRLTLARALVNDPDVLVLDEPTTGLD 170
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
325-473 |
1.81e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 79.34 E-value: 1.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 325 DDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEV----------------LFDGKRV-----QGRnrKEELEL 383
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVsipkglrigylpqeppLDDDLTVldtvlDGD--AELRAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 384 RRRIQPIfqnpYATLDpmrtvhSSIEEPLRIHKIGTKKER------EQRVFELLDRVALPAEMGRRFPGELSGGQRQRVA 457
Cdd:COG0488 93 EAELEEL----EAKLA------EPDEDLERLAELQEEFEAlggweaEARAEEILSGLGFPEEDLDRPVSELSGGWRRRVA 162
|
170
....*....|....*.
gi 2524658687 458 IARALALNPEVVVCDE 473
Cdd:COG0488 163 LARALLSEPDLLLLDE 178
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
298-541 |
2.03e-15 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 76.09 E-value: 2.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 298 ILVAKNLVRDFAIRgdrpwrkdsfRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNR 377
Cdd:PRK10895 3 TLTAKNLAKAYKGR----------RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 378 KEELelRRRIQPIFQNpyATLDPMRTVHSSIEEPLRIHKIGTKKEREQRVFELLDRVALpAEMGRRFPGELSGGQRQRVA 457
Cdd:PRK10895 73 HARA--RRGIGYLPQE--ASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHI-EHLRDSMGQSLSGGERRRVE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 458 IARALALNPEVVVCDEAVSALDVVVQAQVLELLAELQEEmDLAYLFITHDLAVVRQVADEVIVMEHGKMVEH-RPTDDLF 536
Cdd:PRK10895 148 IARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDS-GLGVLITDHNVRETLAVCERAYIVSQGHLIAHgTPTEILQ 226
|
....*
gi 2524658687 537 DHPEK 541
Cdd:PRK10895 227 DEHVK 231
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
7-229 |
2.16e-15 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 75.52 E-value: 2.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 7 TSAAPILTLKDVciGFPTTTasgrrskslTDVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLpgdgEVTGGTITF 86
Cdd:PRK10247 2 QENSPLLQLQNV--GYLAGD---------AKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLI----SPTSGTLLF 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 87 DGRDITHL---TDREFVSIRGNGIGLVPQDPMTNLNPVWTVGSQIKEAlranniatgseahKKAIELLEQAGLPNA--KK 161
Cdd:PRK10247 67 EGEDISTLkpeIYRQQVSYCAQTPTLFGDTVYDNLIFPWQIRNQQPDP-------------AIFLDDLERFALPDTilTK 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2524658687 162 RIDqyphEFSGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHD 229
Cdd:PRK10247 134 NIA----ELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHD 197
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
38-272 |
3.34e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 75.84 E-value: 3.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGDGEV-TGGTITFDGRDI----THLTD-REFVSIRGNGIGLVP 111
Cdd:PRK14258 22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVrVEGRVEFFNQNIyerrVNLNRlRRQVSMVHPKPNLFP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 112 QDPMTNLN-PVWTVGSQIKeaLRANNIAtgsEAHKKAIELLEQAglpnaKKRIDQYPHEFSGGMRQRALIAMGLAAHPKL 190
Cdd:PRK14258 102 MSVYDNVAyGVKIVGWRPK--LEIDDIV---ESALKDADLWDEI-----KHKIHKSALDLSGGQQQRLCIARALAVKPKV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 191 LIADEPTSALDVTVAKKI--LDHLDKLTSELgtSVVLITHDLGLAAERADRLVVMQA-----GRVVETGPALQVLTRPQH 263
Cdd:PRK14258 172 LLMDEPCFGLDPIASMKVesLIQSLRLRSEL--TMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNSPHD 249
|
....*....
gi 2524658687 264 PYTKQLIAA 272
Cdd:PRK14258 250 SRTREYVLS 258
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
32-257 |
3.54e-15 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 77.22 E-value: 3.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 32 SKSLTDVVHDVNLEVfPGETV-AIVGESGSGKSTTAHAALGLL-PGDGEVT-GGTITFDGRDITHLTDREfvsirgNGIG 108
Cdd:PRK11144 7 KQQLGDLCLTVNLTL-PAQGItAIFGRSGAGKTSLINAISGLTrPQKGRIVlNGRVLFDAEKGICLPPEK------RRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 109 LVPQDpmTNLNPVWTVgsqikealRAN---NIATGSEAH-KKAIELLeqaGLpnaKKRIDQYPHEFSGGMRQRALIAMGL 184
Cdd:PRK11144 80 YVFQD--ARLFPHYKV--------RGNlryGMAKSMVAQfDKIVALL---GI---EPLLDRYPGSLSGGEKQRVAIGRAL 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2524658687 185 AAHPKLLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQV 257
Cdd:PRK11144 144 LTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEV 216
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
298-535 |
3.78e-15 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 77.94 E-value: 3.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 298 ILVAKNLVRDFairgdrpwrkDSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLL--DPTEGEVLFDGKRVQGR 375
Cdd:TIGR02633 1 LLEMKGIVKTF----------GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKAS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 376 N-RKEElelRRRIQPIFQNpyATLDPMRTVHSSIEEPLRIHKIGTK---KEREQRVFELLDRVALPAEMGRRFPGELSGG 451
Cdd:TIGR02633 71 NiRDTE---RAGIVIIHQE--LTLVPELSVAENIFLGNEITLPGGRmayNAMYLRAKNLLRELQLDADNVTRPVGDYGGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 452 QRQRVAIARALALNPEVVVCDEAVSALdVVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRP 531
Cdd:TIGR02633 146 QQQLVEIAKALNKQARLLILDEPSSSL-TEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKD 224
|
....
gi 2524658687 532 TDDL 535
Cdd:TIGR02633 225 MSTM 228
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
20-252 |
4.36e-15 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 78.38 E-value: 4.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 20 IGFPTTTASGRRSKSLTDVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGDGEVtgGTITFDGRDITHLTDREf 99
Cdd:PLN03211 65 LGHKPKISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFT--GTILANNRKPTKQILKR- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 100 vsirgngIGLVPQDPMtnLNPVWTVGSQIK--EALRANNIATGSEAHKKAIELLEQAGLPNAKKRI--DQYPHEFSGGMR 175
Cdd:PLN03211 142 -------TGFVTQDDI--LYPHLTVRETLVfcSLLRLPKSLTKQEKILVAESVISELGLTKCENTIigNSFIRGISGGER 212
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2524658687 176 QRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETG 252
Cdd:PLN03211 213 KRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFG 289
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
39-255 |
6.77e-15 |
|
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: 78.52 E-value: 6.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 39 VHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGdgevTGGTITFDGRDITHLTDrefvSIRgNGIGLVPQDPMtnL 118
Cdd:TIGR01257 946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPP----TSGTVLVGGKDIETNLD----AVR-QSLGMCPQHNI--L 1014
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 119 NPVWTVGSQI--KEALRANniaTGSEAHKKAIELLEQAGLPNAKkriDQYPHEFSGGMRQRALIAMGLAAHPKLLIADEP 196
Cdd:TIGR01257 1015 FHHLTVAEHIlfYAQLKGR---SWEEAQLEMEAMLEDTGLHHKR---NEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEP 1088
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2524658687 197 TSALDVTVAKKILDHLDKLTSelGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPAL 255
Cdd:TIGR01257 1089 TSGVDPYSRRSIWDLLLKYRS--GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPL 1145
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
11-238 |
7.94e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 74.38 E-value: 7.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 11 PILTLKDVCIGFptttasGRRSksltdVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLpgdgEVTGGTITFDGRd 90
Cdd:PRK09544 3 SLVSLENVSVSF------GQRR-----VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLV----APDEGVIKRNGK- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 91 ithltdrefvsIRgngIGLVPQ----DPMTNLnpvwTVGS--QIKEALRANNIatgseahkkaIELLEQAglpNAKKRID 164
Cdd:PRK09544 67 -----------LR---IGYVPQklylDTTLPL----TVNRflRLRPGTKKEDI----------LPALKRV---QAGHLID 115
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2524658687 165 QYPHEFSGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERAD 238
Cdd:PRK09544 116 APMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTD 189
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
41-270 |
9.24e-15 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 74.42 E-value: 9.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 41 DVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGDGevtgGTITFDGRDITHLTDREFVSIRGNGIGLVPQDPM-TNLN 119
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDH----GEILFDGENIPAMSRSRLYTVRKRMSMLFQSGALfTDMN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 120 PVWTVGSQIKEALRANNIATGSEAHKKaielLEQAGLPNAKKRIdqyPHEFSGGMRQRALIAMGLAAHPKLLIADEPTSA 199
Cdd:PRK11831 101 VFDNVAYPLREHTQLPAPLLHSTVMMK----LEAVGLRGAAKLM---PSELSGGMARRAALARAIALEPDLIMFDEPFVG 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2524658687 200 LDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPAlQVLTRPQHPYTKQLI 270
Cdd:PRK11831 174 QDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSA-QALQANPDPRVRQFL 243
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
323-535 |
1.76e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 76.40 E-value: 1.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 323 AVDDISFTLRRGRTIGIVGESGSGKSTVanmaLGLL----DPTEGEVLFDGKRVQGRNrkeELELRRRIQPIFQNPY--- 395
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTL----LQLLtrawDPQQGEILLNGQPIADYS---EAALRQAISVVSQRVHlfs 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 396 ATLdpmrtvhssiEEPLrihKIGTKKEREQRVFELLDRVALPA-------------EMGRrfpgELSGGQRQRVAIARAL 462
Cdd:PRK11160 428 ATL----------RDNL---LLAAPNASDEALIEVLQQVGLEKlleddkglnawlgEGGR----QLSGGEQRRLGIARAL 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 463 ALNPEVVVCDEAVSALDVVVQAQVlellaelqeeMDL--------AYLFITHDLAVVRQVaDEVIVMEHGKMVEHRPTDD 534
Cdd:PRK11160 491 LHDAPLLLLDEPTEGLDAETERQI----------LELlaehaqnkTVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQE 559
|
.
gi 2524658687 535 L 535
Cdd:PRK11160 560 L 560
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
330-522 |
2.35e-14 |
|
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: 72.83 E-value: 2.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 330 TLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKeelelrrrIQPIFQnpyatldpmrtvhSSIE 409
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQY--------IKADYE-------------GTVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 410 EPLRiHKIGTKKEREQRVFELLDRVALPAEMGRRFPgELSGGQRQRVAIARALALNPEVVVCDEAVSALDVVVQAQVLEL 489
Cdd:cd03237 80 DLLS-SITKDFYTHPYFKTEIAKPLQIEQILDREVP-ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKV 157
|
170 180 190
....*....|....*....|....*....|...
gi 2524658687 490 LAELQEEMDLAYLFITHDLAVVRQVADEVIVME 522
Cdd:cd03237 158 IRRFAENNEKTAFVVEHDIIMIDYLADRLIVFE 190
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
324-535 |
3.86e-14 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 72.42 E-value: 3.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 324 VDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRV-QGRNRkeelELRRRIQPIFQNPYATldpMR 402
Cdd:COG4604 17 LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVaTTPSR----ELAKRLAILRQENHIN---SR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 403 -TV----------HSsieeplrihKIGTKKEREQRVFELLDRVALpAEMGRRFPGELSGGQRQRVAIARALALNPEVVVC 471
Cdd:COG4604 90 lTVrelvafgrfpYS---------KGRLTAEDREIIDEAIAYLDL-EDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2524658687 472 DEAVSALDVVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDL 535
Cdd:COG4604 160 DEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
33-261 |
5.20e-14 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 74.75 E-value: 5.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 33 KSLTDVVHDVNLEVFPGETVAIVGESGSGKSTTahaaLGLLPGDGEVTGGTITFDGRditHLTDREFVSIRGNgIGLVPQ 112
Cdd:PRK10789 325 QTDHPALENVNFTLKPGQMLGICGPTGSGKSTL----LSLIQRHFDVSEGDIRFHDI---PLTKLQLDSWRSR-LAVVSQ 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 113 DPMTNLNPVwtvgsqikealrANNIATGS-EAHKKAIEllEQAGLPNAKKRIDQYPHEF-----------SGGMRQRALI 180
Cdd:PRK10789 397 TPFLFSDTV------------ANNIALGRpDATQQEIE--HVARLASVHDDILRLPQGYdtevgergvmlSGGQKQRISI 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 181 AMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSelGTSVVLITHDLGLAAErADRLVVMQAGRVVETGPALQVLTR 260
Cdd:PRK10789 463 ARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGE--GRTVIISAHRLSALTE-ASEILVMQHGHIAQRGNHDQLAQQ 539
|
.
gi 2524658687 261 P 261
Cdd:PRK10789 540 S 540
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
322-548 |
7.69e-14 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 71.58 E-value: 7.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 322 RAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEeleLRRRIQPIFQNPyatLDPM 401
Cdd:PRK11231 16 RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQ---LARRLALLPQHH---LTPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 402 R-TVHSSIE---EPLRIHKIGTKKEREQRVFELLDRVALpAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVSA 477
Cdd:PRK11231 90 GiTVRELVAygrSPWLSLWGRLSAEDNARVNQAMEQTRI-NHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTY 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 478 LDVVVQAQVlellaelqeeMDL---------AYLFITHDLAVVRQVADEVIVMEHGKMVeHRPTddlfdhPEKEYTQRLL 548
Cdd:PRK11231 169 LDINHQVEL----------MRLmrelntqgkTVVTVLHDLNQASRYCDHLVVLANGHVM-AQGT------PEEVMTPGLL 231
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
317-541 |
9.98e-14 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 71.39 E-value: 9.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 317 RKDSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKrvqgrnrkeelelrrrIQPIFQNpyA 396
Cdd:PRK13546 33 KNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE----------------VSVIAIS--A 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 397 TLDPMRTVHSSIEepLRIHKIGTKKereQRVFELLDRVALPAEMGR---RFPGELSGGQRQRVAIARALALNPEVVVCDE 473
Cdd:PRK13546 95 GLSGQLTGIENIE--FKMLCMGFKR---KEIKAMTPKIIEFSELGEfiyQPVKKYSSGMRAKLGFSINITVNPDILVIDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2524658687 474 AVSALDVVVqAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDLFDHPEK 541
Cdd:PRK13546 170 ALSVGDQTF-AQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPKYEA 236
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
326-486 |
1.07e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 73.93 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 326 DISFTLRRGRTIGIVGESGSGKSTVANmALGLLDPT----EGEVLFDGKRVQGRnrkeelELRRRIQPIFQNPyaTLDPM 401
Cdd:TIGR00955 43 NVSGVAKPGELLAVMGSSGAGKTTLMN-ALAFRSPKgvkgSGSVLLNGMPIDAK------EMRAISAYVQQDD--LFIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 402 RTV--HSSIEEPLRIHKIGTKKEREQRVFELLDRVAL-PAEMGR-----RFPGeLSGGQRQRVAIARALALNPEVVVCDE 473
Cdd:TIGR00955 114 LTVreHLMFQAHLRMPRRVTKKEKRERVDEVLQALGLrKCANTRigvpgRVKG-LSGGERKRLAFASELLTDPPLLFCDE 192
|
170
....*....|...
gi 2524658687 474 AVSALDVVVQAQV 486
Cdd:TIGR00955 193 PTSGLDSFMAYSV 205
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
322-478 |
1.28e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 73.41 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 322 RAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEELElrRRIQPIFQNpyATLDPM 401
Cdd:PRK11288 18 KALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALA--AGVAIIYQE--LHLVPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 402 RTVHSSI---EEPlriHKIGTKKERE--QRVFELLDRVALPAEMGRRFpGELSGGQRQRVAIARALALNPEVVVCDEAVS 476
Cdd:PRK11288 94 MTVAENLylgQLP---HKGGIVNRRLlnYEAREQLEHLGVDIDPDTPL-KYLSIGQRQMVEIAKALARNARVIAFDEPTS 169
|
..
gi 2524658687 477 AL 478
Cdd:PRK11288 170 SL 171
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
325-525 |
1.41e-13 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 68.24 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 325 DDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVlfdgkrvqgrnrkeelelrrriqpifqnpyatldpmrTV 404
Cdd:cd03221 17 KDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV-------------------------------------TW 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 405 HSSIeeplrihKIGtkkereqrVFElldrvalpaemgrrfpgELSGGQRQRVAIARALALNPEVVVCDEAVSALDVVVQA 484
Cdd:cd03221 60 GSTV-------KIG--------YFE-----------------QLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIE 107
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2524658687 485 QVLELlaelqeemdL-----AYLFITHDLAVVRQVADEVIVMEHGK 525
Cdd:cd03221 108 ALEEA---------LkeypgTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
11-250 |
1.57e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 73.18 E-value: 1.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 11 PILTLKDVCIGFPTTTasgrrsksltdVVHDVNLEVFPGETVAIVGESGSGKSTTahaaLGLLPGDGEVTGGTITFdGRD 90
Cdd:COG0488 314 KVLELEGLSKSYGDKT-----------LLDDLSLRIDRGDRIGLIGPNGAGKSTL----LKLLAGELEPDSGTVKL-GET 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 91 IThltdrefvsirgngIGLVPQDpMTNLNPVWTVGSQIKEALRanniaTGSEAHkkAIELLEQAGLPNAkkRIDQYPHEF 170
Cdd:COG0488 378 VK--------------IGYFDQH-QEELDPDKTVLDELRDGAP-----GGTEQE--VRGYLGRFLFSGD--DAFKPVGVL 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 171 SGGMRQRALIAMGLAAHPKLLIADEPTSALDvtvakkiLDHLDKLTSEL----GTsVVLITHDLGLAAERADRLVVMQAG 246
Cdd:COG0488 434 SGGEKARLALAKLLLSPPNVLLLDEPTNHLD-------IETLEALEEALddfpGT-VLLVSHDRYFLDRVATRILEFEDG 505
|
....
gi 2524658687 247 RVVE 250
Cdd:COG0488 506 GVRE 509
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
48-480 |
1.74e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 73.06 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 48 PGETVAIVGESGSGKSTTahaaLGLLPGDGEVTGGTITFDG------------RDITHlTDREFVSirgNGIG------- 108
Cdd:PRK11147 28 DNERVCLVGRNGAGKSTL----MKILNGEVLLDDGRIIYEQdlivarlqqdppRNVEG-TVYDFVA---EGIEeqaeylk 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 109 -------LVPQDPM-TNLNPVwtvgSQIKEALRANNiatGSEAHKKAIELLEQAGLPNAKKRidqypHEFSGGMRQRALI 180
Cdd:PRK11147 100 ryhdishLVETDPSeKNLNEL----AKLQEQLDHHN---LWQLENRINEVLAQLGLDPDAAL-----SSLSGGWLRKAAL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 181 AMGLAAHPKLLIADEPTSALDVTVakkiLDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQAGRVV----------- 249
Cdd:PRK11147 168 GRALVSNPDVLLLDEPTNHLDIET----IEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVsypgnydqyll 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 250 ETGPALQVLTRPQHPYTKQL---------------------IAAAPSLAARRGDRV----VAAPTTSDADQKEILV---- 300
Cdd:PRK11147 244 EKEEALRVEELQNAEFDRKLaqeevwirqgikarrtrnegrVRALKALRRERSERRevmgTAKMQVEEASRSGKIVfeme 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 301 -------AKNLVRDFairgdrpwrkdsfravddiSFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKrvq 373
Cdd:PRK11147 324 nvnyqidGKQLVKDF-------------------SAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTK--- 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 374 grnrkeeLELrrriqPIFQNPYATLDPMRTVHSSIEEplrihkigTKKE-----REQRVFELLDRVALPAEMGRRFPGEL 448
Cdd:PRK11147 382 -------LEV-----AYFDQHRAELDPEKTVMDNLAE--------GKQEvmvngRPRHVLGYLQDFLFHPKRAMTPVKAL 441
|
490 500 510
....*....|....*....|....*....|...
gi 2524658687 449 SGGQRQRVAIARaLALNP-EVVVCDEAVSALDV 480
Cdd:PRK11147 442 SGGERNRLLLAR-LFLKPsNLLILDEPTNDLDV 473
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
48-550 |
1.80e-13 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 73.28 E-value: 1.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 48 PGETVAIVGESGSGKSTTahaaLGLLPGDGEVTGGTITFDGR-------------DITHLT-----DREFVSIRGNgigL 109
Cdd:PRK10636 26 PGQKVGLVGKNGCGKSTL----LALLKNEISADGGSYTFPGNwqlawvnqetpalPQPALEyvidgDREYRQLEAQ---L 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 110 VPQDPMTNLNPVWTVGSQIkEALRANNIATgseahkKAIELLEqaGLPNAKKRIDQYPHEFSGGMRQRALIAMGLAAHPK 189
Cdd:PRK10636 99 HDANERNDGHAIATIHGKL-DAIDAWTIRS------RAASLLH--GLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 190 LLIADEPTSALDvtvakkiLDH---LDK-LTSELGTsVVLITHDLGLAAERADRLVVMQAGRVVE-TGP----ALQVLTR 260
Cdd:PRK10636 170 LLLLDEPTNHLD-------LDAviwLEKwLKSYQGT-LILISHDRDFLDPIVDKIIHIEQQSLFEyTGNyssfEVQRATR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 261 ---PQHPYTKQL--IAAAPSLAarrgDRVVAAPTTSDADQKEILVAKNLVRDFAIRGDRPWRKdSFRA------------ 323
Cdd:PRK10636 242 laqQQAMYESQQerVAHLQSYI----DRFRAKATKAKQAQSRIKMLERMELIAPAHVDNPFHF-SFRApeslpnpllkme 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 324 -----------VDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEV-LFDGKRVqGRNRKEELELrrriqpif 391
Cdd:PRK10636 317 kvsagygdriiLDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKL-GYFAQHQLEF-------- 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 392 qnpyatldpMRTVHSSIEEPLRIhkigTKKEREQRVFELL-------DRValpAEMGRRFpgelSGGQRQRVAIARALAL 464
Cdd:PRK10636 388 ---------LRADESPLQHLARL----APQELEQKLRDYLggfgfqgDKV---TEETRRF----SGGEKARLVLALIVWQ 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 465 NPEVVVCDEAVSALDV-VVQAqvlelLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMvehrptdDLFDHPEKEY 543
Cdd:PRK10636 448 RPNLLLLDEPTNHLDLdMRQA-----LTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKV-------EPFDGDLEDY 515
|
....*..
gi 2524658687 544 TQRLLDA 550
Cdd:PRK10636 516 QQWLSDV 522
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
317-546 |
2.19e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 73.52 E-value: 2.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 317 RKDsFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLF-DGKRVQGRNRKEeleLRRRIQPIFQNP- 394
Cdd:PTZ00265 395 RKD-VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKW---WRSKIGVVSQDPl 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 395 ----------------------------------YATLDPMRTVHSSIEEPLRI--------HKIGTKKE----REQRVF 428
Cdd:PTZ00265 471 lfsnsiknnikyslyslkdlealsnyynedgndsQENKNKRNSCRAKCAGDLNDmsnttdsnELIEMRKNyqtiKDSEVV 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 429 ELLDRV-------ALPAE----MGRRfPGELSGGQRQRVAIARALALNPEVVVCDEAVSALDVVVQAQVLELLAELQEEM 497
Cdd:PTZ00265 551 DVSKKVlihdfvsALPDKyetlVGSN-ASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNE 629
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2524658687 498 DLAYLFITHDLAVVRqVADEVIVMEHGKMVEHRPTDDLFDHPEKEYTQR 546
Cdd:PTZ00265 630 NRITIIIAHRLSTIR-YANTIFVLSNRERGSTVDVDIIGEDPTKDNKEN 677
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
30-275 |
2.38e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 73.47 E-value: 2.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 30 RRSKSLTDVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLpgdgEVTGGTITFDGRDITH--LTD-REFVSIrgng 106
Cdd:PLN03232 1243 RYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIV----ELEKGRIMIDDCDVAKfgLTDlRRVLSI---- 1314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 107 iglVPQDPMT-------NLNP--------VWTV--GSQIKEALRANNIATGSEAHKKAielleqaglpnakkridqypHE 169
Cdd:PLN03232 1315 ---IPQSPVLfsgtvrfNIDPfsehndadLWEAleRAHIKDVIDRNPFGLDAEVSEGG--------------------EN 1371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 170 FSGGMRQRALIAMGLAAHPKLLIADEPTSALDVT----VAKKILDHLDKLTselgtsVVLITHDLGLAAErADRLVVMQA 245
Cdd:PLN03232 1372 FSVGQRQLLSLARALLRRSKILVLDEATASVDVRtdslIQRTIREEFKSCT------MLVIAHRLNTIID-CDKILVLSS 1444
|
250 260 270
....*....|....*....|....*....|
gi 2524658687 246 GRVVETGPALQVLTRPQHPYTKQLIAAAPS 275
Cdd:PLN03232 1445 GQVLEYDSPQELLSRDTSAFFRMVHSTGPA 1474
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
313-529 |
3.34e-13 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 68.35 E-value: 3.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 313 DRPWRKDSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDP--TEGEVLFDGKRVqgrnrkEELELRRRIQPI 390
Cdd:cd03213 14 KSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPL------DKRSFRKIIGYV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 391 FQNP--YATLdpmrTVhssiEEPLRIHkigtkkereqrvfelldrvalpAEMgRRfpgeLSGGQRQRVAIARALALNPEV 468
Cdd:cd03213 88 PQDDilHPTL----TV----RETLMFA----------------------AKL-RG----LSGGERKRVSIALELVSNPSL 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2524658687 469 VVCDEAVSALDVVVQAQVlellaeLQEEMDLA-----YLFITHDL-AVVRQVADEVIVMEHGKMVEH 529
Cdd:cd03213 133 LFLDEPTSGLDSSSALQV------MSLLRRLAdtgrtIICSIHQPsSEIFELFDKLLLLSQGRVIYF 193
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
324-479 |
4.41e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 71.76 E-value: 4.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 324 VDDISFTLRRGRTIGIVGESGSGKST----VAnmalGLLDPTEGEVLF-DGKRVqgrnrkeelelrrriqpIF--QNPYA 396
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTllraIA----GLWPYGSGRIARpAGARV-----------------LFlpQRPYL 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 397 TLDPMRTVhssIEEPLRIHKIGtkkerEQRVFELLDRVALPA-----EMGRRFPGELSGGQRQRVAIARALALNPEVVVC 471
Cdd:COG4178 438 PLGTLREA---LLYPATAEAFS-----DAELREALEAVGLGHlaerlDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFL 509
|
....*...
gi 2524658687 472 DEAVSALD 479
Cdd:COG4178 510 DEATSALD 517
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
30-249 |
6.32e-13 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 67.67 E-value: 6.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 30 RRSKSLTDVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGDGEVTGgTITFDGRDIthltdREFVSIRGNGIGL 109
Cdd:cd03233 14 GKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSVEG-DIHYNGIPY-----KEFAEKYPGEIIY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 110 VPQDpmTNLNPVWTVGSQIKEALRANNiatgseahkkaielleqaglpnakkriDQYPHEFSGGMRQRALIAMGLAAHPK 189
Cdd:cd03233 88 VSEE--DVHFPTLTVRETLDFALRCKG---------------------------NEFVRGISGGERKRVSIAEALVSRAS 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2524658687 190 LLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLIthdLGLAAERA----DRLVVMQAGRVV 249
Cdd:cd03233 139 VLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVS---LYQASDEIydlfDKVLVLYEGRQI 199
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
36-252 |
1.06e-12 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 68.28 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 36 TDVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGllPGDGEVTGGTITFDGRDITHLTDREFVsirGNGIGLVPQdpm 115
Cdd:PRK09580 14 KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAG--REDYEVTGGTVEFKGKDLLELSPEDRA---GEGIFMAFQ--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 116 tnlNPVWTVGSQIKEALRANNIATGSEAHKKAIELLEQAGLPNAKKRIDQYPHE---------FSGGMRQRALIAMGLAA 186
Cdd:PRK09580 86 ---YPVEIPGVSNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLKMPEDlltrsvnvgFSGGEKKRNDILQMAVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2524658687 187 HPKLLIADEPTSALDVTVAKKILDHLDKLTSElGTSVVLITH-DLGLAAERADRLVVMQAGRVVETG 252
Cdd:PRK09580 163 EPELCILDESDSGLDIDALKIVADGVNSLRDG-KRSFIIVTHyQRILDYIKPDYVHVLYQGRIVKSG 228
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
35-250 |
1.08e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 71.31 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 35 LTDVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLpgdgEVTGGTITFDGRDITH--LTDrefvsIRGNgIGLVPQ 112
Cdd:PLN03130 1251 LPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIV----ELERGRILIDGCDISKfgLMD-----LRKV-LGIIPQ 1320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 113 DPMT-------NLNPVwtvgsqikealranniatgSEaHKKA--IELLEQAGLPNAKKR----IDQYPHE----FSGGMR 175
Cdd:PLN03130 1321 APVLfsgtvrfNLDPF-------------------NE-HNDAdlWESLERAHLKDVIRRnslgLDAEVSEagenFSVGQR 1380
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2524658687 176 QRALIAMGLAAHPKLLIADEPTSALDV----TVAKKILDHLDKLTselgtsVVLITHDLGLAAErADRLVVMQAGRVVE 250
Cdd:PLN03130 1381 QLLSLARALLRRSKILVLDEATAAVDVrtdaLIQKTIREEFKSCT------MLIIAHRLNTIID-CDRILVLDAGRVVE 1452
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
39-271 |
1.16e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 68.27 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 39 VHDVNLEVFPGETVAIVGESGSGKSTTAHA---ALGLLPGdgEVTGGTITFDGRDItHLTDREFVSIRGNgIGLVPQDPm 115
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIPG--FRVEGKVTFHGKNL-YAPDVDPVEVRRR-IGMVFQKP- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 116 tnlNPVwtvGSQIKEalranNIATGSEAHKKAIEL-------LEQAGL-PNAKKRIDQYPHEFSGGMRQRALIAMGLAAH 187
Cdd:PRK14243 101 ---NPF---PKSIYD-----NIAYGARINGYKGDMdelversLRQAALwDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 188 PKLLIADEPTSALDVTVAKKIldhlDKLTSELGT--SVVLITHDLGLAAERADRLVVMQA---------GRVVETGPALQ 256
Cdd:PRK14243 170 PEVILMDEPCSALDPISTLRI----EELMHELKEqyTIIIVTHNMQQAARVSDMTAFFNVeltegggryGYLVEFDRTEK 245
|
250
....*....|....*
gi 2524658687 257 VLTRPQHPYTKQLIA 271
Cdd:PRK14243 246 IFNSPQQQATRDYVS 260
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
327-518 |
1.48e-12 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 66.75 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 327 ISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVqGRNRKeelELRRRIQPIfqnpyATLDPMRTVHS 406
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL-DFQRD---SIARGLLYL-----GHAPGIKTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 407 SIEEPLRIHKIGTkkeREQrVFELLDRVALPAeMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVSALDVVVQAQV 486
Cdd:cd03231 90 VLENLRFWHADHS---DEQ-VEEALARVGLNG-FEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARF 164
|
170 180 190
....*....|....*....|....*....|..
gi 2524658687 487 LELLAELQEEMDLAYLFITHDLAVVRQVADEV 518
Cdd:cd03231 165 AEAMAGHCARGGMVVLTTHQDLGLSEAGAREL 196
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
308-523 |
1.64e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 66.91 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 308 FAIRGDRpwrkDSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDptegevlfdGKRVQGRNRKEELELRRri 387
Cdd:COG2401 34 FGVELRV----VERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALK---------GTPVAGCVDVPDNQFGR-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 388 qpifqnpyatldpmrtvhssiEEPL--RIHKIGTKKEreqrVFELLDRVAL--PAEMGRRFPgELSGGQRQRVAIARALA 463
Cdd:COG2401 99 ---------------------EASLidAIGRKGDFKD----AVELLNAVGLsdAVLWLRRFK-ELSTGQKFRFRLALLLA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 464 LNPEVVVCDEAVSALDVVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEH 523
Cdd:COG2401 153 ERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYDVIDDLQPDLLIFVG 212
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
299-484 |
3.13e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 65.67 E-value: 3.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 299 LVAKNLVrdfAIRGDRPwrkdsfrAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVqgrnrk 378
Cdd:PRK13539 3 LEGEDLA---CVRGGRV-------LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 379 EELELRRRIQPIfqnpyATLDPMRTvHSSIEEPLRIHKiGTKKEREQRVFELLDRVALPAEMGRRFpGELSGGQRQRVAI 458
Cdd:PRK13539 67 DDPDVAEACHYL-----GHRNAMKP-ALTVAENLEFWA-AFLGGEELDIAAALEAVGLAPLAHLPF-GYLSAGQKRRVAL 138
|
170 180
....*....|....*....|....*.
gi 2524658687 459 ARALALNPEVVVCDEAVSALDVVVQA 484
Cdd:PRK13539 139 ARLLVSNRPIWILDEPTAALDAAAVA 164
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
316-536 |
3.59e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 66.83 E-value: 3.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 316 WRkDSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQgrnrkeelelrrriQPIFQNPY 395
Cdd:PRK15056 16 WR-NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR--------------QALQKNLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 396 ATLDPMRTVHSS----IEEPLRIHKIG-------TKKEREQRVFELLDRVALpAEMGRRFPGELSGGQRQRVAIARALAL 464
Cdd:PRK15056 81 AYVPQSEEVDWSfpvlVEDVVMMGRYGhmgwlrrAKKRDRQIVTAALARVDM-VEFRHRQIGELSGGQKKRVFLARAIAQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2524658687 465 NPEVVVCDEAVSALDVVVQAQVLELLAELQEEmDLAYLFITHDLAVVRQVADeVIVMEHGKMVEHRPTDDLF 536
Cdd:PRK15056 160 QGQVILLDEPFTGVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGPTETTF 229
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
327-535 |
5.55e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 66.35 E-value: 5.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 327 ISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEeleLRRRIQPIFQN-PYATLDPMRTVH 405
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKA---FARKVAYLPQQlPAAEGMTVRELV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 406 SSIEEPLR--IHKIGTkkEREQRVFELLDRVALpAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVSALDVVVQ 483
Cdd:PRK10575 107 AIGRYPWHgaLGRFGA--ADREKVEEAISLVGL-KPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQ 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2524658687 484 AQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDL 535
Cdd:PRK10575 184 VDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
322-535 |
6.92e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 67.83 E-value: 6.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 322 RAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEELElrRRIQPIFQNPYATLDpm 401
Cdd:PRK10982 12 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALE--NGISMVHQELNLVLQ-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 402 RTVHSSI---EEPLRIHKIGTKK--EREQRVFELLDRVALPAEMGrrfpGELSGGQRQRVAIARALALNPEVVVCDEAVS 476
Cdd:PRK10982 88 RSVMDNMwlgRYPTKGMFVDQDKmyRDTKAIFDELDIDIDPRAKV----ATLSVSQMQMIEIAKAFSYNAKIVIMDEPTS 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2524658687 477 ALdvvVQAQVLELLAELQEEMD--LAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDL 535
Cdd:PRK10982 164 SL---TEKEVNHLFTIIRKLKErgCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGL 221
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
306-546 |
7.27e-12 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 68.43 E-value: 7.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 306 RDFAIRgdrpWRKDSFRAVDDISFTLRRGRTIGIVGESGSGKSTvanMALGL---LDPTEGEVLFDGKRVQGRNRKeelE 382
Cdd:TIGR00957 1288 RNYCLR----YREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSS---LTLGLfriNESAEGEIIIDGLNIAKIGLH---D 1357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 383 LRRRIQPIFQNPY-------ATLDPMRTVhsSIEEplrihkIGTKKEreqrVFELLDRV-ALPAEMGRRFP--GE-LSGG 451
Cdd:TIGR00957 1358 LRFKITIIPQDPVlfsgslrMNLDPFSQY--SDEE------VWWALE----LAHLKTFVsALPDKLDHECAegGEnLSVG 1425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 452 QRQRVAIARALALNPEVVVCDEAVSALDV----VVQAQVLELLAelqeemDLAYLFITHDLAVVRQVAdEVIVMEHGKMV 527
Cdd:TIGR00957 1426 QRQLVCLARALLRKTKILVLDEATAAVDLetdnLIQSTIRTQFE------DCTVLTIAHRLNTIMDYT-RVIVLDKGEVA 1498
|
250
....*....|....*....
gi 2524658687 528 EhrptddlFDHPEKEYTQR 546
Cdd:TIGR00957 1499 E-------FGAPSNLLQQR 1510
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
43-479 |
9.89e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 67.35 E-value: 9.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 43 NLEVFPGETVAIVGESGSGKSTTAHAALG-LLPGDGEVTGG-----TITFDgrDITHLTDREFVsiRGNGIGLVPQDPMT 116
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGeLPLLSGERQSQfshitRLSFE--QLQKLVSDEWQ--RNNTDMLSPGEDDT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 117 NLnpvwTVGSQIKEALRANNiatgseahkKAIELLEQAGLPNAKKRIDQYpheFSGGMRQRALIAMGLAAHPKLLIADEP 196
Cdd:PRK10938 99 GR----TTAEIIQDEVKDPA---------RCEQLAQQFGITALLDRRFKY---LSTGETRKTLLCQALMSEPDLLILDEP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 197 TSALDVTVAKKILDHLDKLTSElGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVLtrpQHPYTKQLiAAAPSL 276
Cdd:PRK10938 163 FDGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEIL---QQALVAQL-AHSEQL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 277 AArrgdrvVAAPTTSDADQKEILVAKN---LVRDFAIR-GDRPwrkdsfrAVDDISFTLRRGRTIGIVGESGSGKSTvan 352
Cdd:PRK10938 238 EG------VQLPEPDEPSARHALPANEpriVLNNGVVSyNDRP-------ILHNLSWQVNPGEHWQIVGPNGAGKST--- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 353 malgLLDptegevLFDGKRVQGRNRKEELELRRR-----IQPIFQNpyatldpMRTVHSSIEEPLRIH------------ 415
Cdd:PRK10938 302 ----LLS------LITGDHPQGYSNDLTLFGRRRgsgetIWDIKKH-------IGYVSSSLHLDYRVStsvrnvilsgff 364
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2524658687 416 -KIGTKK---EREQR-VFELLDRVALPAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVSALD 479
Cdd:PRK10938 365 dSIGIYQavsDRQQKlAQQWLDILGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
326-534 |
1.04e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 68.13 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 326 DISFTLRRGRTIGIVGESGSGKSTVANMALGLLD---------------------------------------------- 359
Cdd:PTZ00265 1186 DLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkegg 1265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 360 --------PTEGEVLFDGKRVQGRNRKEeleLRRRIQPIFQNPYatldpmrTVHSSIEEPLRIHKIGTKKEREQRV--FE 429
Cdd:PTZ00265 1266 sgedstvfKNSGKILLDGVDICDYNLKD---LRNLFSIVSQEPM-------LFNMSIYENIKFGKEDATREDVKRAckFA 1335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 430 LLDRV--ALPAEMGRR---FPGELSGGQRQRVAIARALALNPEVVVCDEAVSALDVVVQAQVLELLAELQEEMDLAYLFI 504
Cdd:PTZ00265 1336 AIDEFieSLPNKYDTNvgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITI 1415
|
250 260 270
....*....|....*....|....*....|....
gi 2524658687 505 THDLAVVRQvADEVIVMEH----GKMVEHRPTDD 534
Cdd:PTZ00265 1416 AHRIASIKR-SDKIVVFNNpdrtGSFVQAHGTHE 1448
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
322-479 |
1.20e-11 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 65.42 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 322 RAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLL--DPT-EGEVLFDGKRVQ--GRNRKEELELRRRIQPIFQNpYA 396
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSaGSHIELLGRTVQreGRLARDIRKSRANTGYIFQQ-FN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 397 TLDPMrtvhsSIEEPLRIHKIGT-----------KKEREQRVFELLDRVALpAEMGRRFPGELSGGQRQRVAIARALALN 465
Cdd:PRK09984 97 LVNRL-----SVLENVLIGALGStpfwrtcfswfTREQKQRALQALTRVGM-VHFAHQRVSTLSGGQQQRVAIARALMQQ 170
|
170
....*....|....
gi 2524658687 466 PEVVVCDEAVSALD 479
Cdd:PRK09984 171 AKVILADEPIASLD 184
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
325-527 |
1.43e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 65.01 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 325 DDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEeleLRRRIQPIFQNpyATLDPMRTV 404
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKE---VARRIGLLAQN--ATTPGDITV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 405 HSSIEEPLRIHK---IGTKKEREQRVFELLDRVALpAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVSALDVV 481
Cdd:PRK10253 99 QELVARGRYPHQplfTRWRKEDEEAVTKAMQATGI-THLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIS 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2524658687 482 VQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMV 527
Cdd:PRK10253 178 HQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIV 223
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
39-250 |
1.46e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 66.73 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 39 VHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPgdgeVTGGTITFDGRDITHLTDREFVSirgNGIGLVPQD----- 113
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDK----RAGGEIRLNGKDISPRSPLDAVK---KGMAYITESrrdng 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 114 --PMTNLNPVWTVGSQIKEALRANNIATGSEAHKKAIELLEQAGLPNAKKRIDQYPHEFSGGMRQRALIAMGLAAHPKLL 191
Cdd:PRK09700 352 ffPNFSIAQNMAISRSLKDGGYKGAMGLFHEVDEQRTAENQRELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVI 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2524658687 192 IADEPTSALDVTVAKKILDHLDKLTSElGTSVVLITHDLGLAAERADRLVVMQAGRVVE 250
Cdd:PRK09700 432 IFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
41-252 |
1.47e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 67.46 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 41 DVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPgdgEVTGGTITfdgrdithltdrefvsIRGNgIGLVPQDpmtnlnp 120
Cdd:PLN03130 635 NINLDVPVGSLVAIVGSTGEGKTSLISAMLGELP---PRSDASVV----------------IRGT-VAYVPQV------- 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 121 vwtvgSQIKEALRANNIATGS----EAHKKAIEL--LEQ--AGLPNAK-KRIDQYPHEFSGGMRQRALIAMGLAAHPKLL 191
Cdd:PLN03130 688 -----SWIFNATVRDNILFGSpfdpERYERAIDVtaLQHdlDLLPGGDlTEIGERGVNISGGQKQRVSMARAVYSNSDVY 762
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2524658687 192 IADEPTSALDVTVAKKILDHLdkLTSEL-GTSVVLITHDLGLAAeRADRLVVMQAGRVVETG 252
Cdd:PLN03130 763 IFDDPLSALDAHVGRQVFDKC--IKDELrGKTRVLVTNQLHFLS-QVDRIILVHEGMIKEEG 821
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
327-537 |
1.61e-11 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 64.48 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 327 ISFTLRRGRTIGIVGESGSGKSTVANMALGLLdPTEGEVLFDGKRVqGRNRKEELELRR-----RIQPIFQNP-YATLDp 400
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPL-SDWSAAELARHRaylsqQQSPPFAMPvFQYLA- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 401 mrtvhssieepLRIHKIGTKKEREQRVFELLDRVALPAEMGRRFpGELSGGQRQRVAIARAL-----ALNPE--VVVCDE 473
Cdd:COG4138 92 -----------LHQPAGASSEAVEQLLAQLAEALGLEDKLSRPL-TQLSGGEWQRVRLAAVLlqvwpTINPEgqLLLLDE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2524658687 474 AVSALDVVVQAqvlellaelqeEMD-----LAYLFIT-----HDLAVVRQVADEVIVMEHGKMVEHRPTDDLFD 537
Cdd:COG4138 160 PMNSLDVAQQA-----------ALDrllreLCQQGITvvmssHDLNHTLRHADRVWLLKQGKLVASGETAEVMT 222
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
142-312 |
1.71e-11 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 65.91 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 142 EAHKKAIELLEQAGLPNAKKRIdqyPHEFSGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSElGT 221
Cdd:NF000106 120 DARARADELLERFSLTEAAGRA---AAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GA 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 222 SVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVLT---------RPQHPYTKQLIAAAPSLAARRG---------DR 283
Cdd:NF000106 196 TVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTkvggrtlqiRPAHAAELDRMVGAIAQAGLDGiagatadheDG 275
|
170 180
....*....|....*....|....*....
gi 2524658687 284 VVAAPTTSDaDQKEILVAKNLVRDFAIRG 312
Cdd:NF000106 276 VVNVPIVSD-EQLSAVVGMLGERGFTISG 303
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
324-524 |
1.94e-11 |
|
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: 63.89 E-value: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 324 VDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKrvqgrNRKEELELRRRIQPIFQNPYATLDPMrT 403
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNK-----NESEPSFEATRSRNRYSVAYAAQKPW-L 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 404 VHSSIEEPLrIHKIGTKKEREQRVFELL----DRVALP----AEMGRRfpG-ELSGGQRQRVAIARALALNPEVVVCDEA 474
Cdd:cd03290 91 LNATVEENI-TFGSPFNKQRYKAVTDACslqpDIDLLPfgdqTEIGER--GiNLSGGQRQRICVARALYQNTNIVFLDDP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2524658687 475 VSALDVVVQAQVLELLAELQEEMDLAYL-FITHDLAVVRQvADEVIVMEHG 524
Cdd:cd03290 168 FSALDIHLSDHLMQEGILKFLQDDKRTLvLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
32-252 |
2.19e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 66.92 E-value: 2.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 32 SKSLTDVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPgdgevtggtitfdgrditHLTDREfVSIRGNgIGLVP 111
Cdd:PLN03232 626 SKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELS------------------HAETSS-VVIRGS-VAYVP 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 112 QDPmtnlnpvWTVGSQIKEalranNIATGS----EAHKKAIE---LLEQAGLPNAKKR--IDQYPHEFSGGMRQRALIAM 182
Cdd:PLN03232 686 QVS-------WIFNATVRE-----NILFGSdfesERYWRAIDvtaLQHDLDLLPGRDLteIGERGVNISGGQKQRVSMAR 753
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2524658687 183 GLAAHPKLLIADEPTSALDVTVAKKILDHLDKltSEL-GTSVVLITHDLGLAAErADRLVVMQAGRVVETG 252
Cdd:PLN03232 754 AVYSNSDIYIFDDPLSALDAHVAHQVFDSCMK--DELkGKTRVLVTNQLHFLPL-MDRIILVSEGMIKEEG 821
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
327-473 |
2.20e-11 |
|
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: 66.36 E-value: 2.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 327 ISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRkeeLELRRRIQPIFQNPY---------AT 397
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNR---EAYRQLFSAVFSDFHlfdrllgldGE 427
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2524658687 398 LDPMRtvhssIEEPLRIHKIGTKKEREQRVFELLDrvalpaemgrrfpgeLSGGQRQRVAIARALALNPEVVVCDE 473
Cdd:COG4615 428 ADPAR-----ARELLERLELDHKVSVEDGRFSTTD---------------LSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
299-480 |
3.43e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 62.90 E-value: 3.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 299 LVAKNLVrdfAIRGDRpwrkdsfRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQgRNRK 378
Cdd:PRK13538 2 LEARNLA---CERDER-------ILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR-RQRD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 379 EELElrrriQPIFQNPYATLDPMRTVhssiEEPLRIHKIGTKKEREQRVFELLDRVAL------PAemgrrfpGELSGGQ 452
Cdd:PRK13538 71 EYHQ-----DLLYLGHQPGIKTELTA----LENLRFYQRLHGPGDDEALWEALAQVGLagfedvPV-------RQLSAGQ 134
|
170 180
....*....|....*....|....*...
gi 2524658687 453 RQRVAIARALALNPEVVVCDEAVSALDV 480
Cdd:PRK13538 135 QRRVALARLWLTRAPLWILDEPFTAIDK 162
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
327-541 |
5.31e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 65.91 E-value: 5.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 327 ISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVqgrnRKEEL-ELRRRIQPIFQNPYA-------TL 398
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDI----SKFGLmDLRKVLGIIPQAPVLfsgtvrfNL 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 399 DPMRTvHSSIE--EPL-RIHkigtKKEREQRVFELLDrvALPAEMGRRFpgelSGGQRQRVAIARALALNPEVVVCDEAV 475
Cdd:PLN03130 1334 DPFNE-HNDADlwESLeRAH----LKDVIRRNSLGLD--AEVSEAGENF----SVGQRQLLSLARALLRRSKILVLDEAT 1402
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2524658687 476 SALDVVVQA--QVLELLAELQEEMdlayLFITHDLAVVRQvADEVIVMEHGKMVEhrptddlFDHPEK 541
Cdd:PLN03130 1403 AAVDVRTDAliQKTIREEFKSCTM----LIIAHRLNTIID-CDRILVLDAGRVVE-------FDTPEN 1458
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
316-537 |
5.92e-11 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 65.74 E-value: 5.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 316 WRKDSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKrvqgrnrkeelelrrrIQPIFQNPY 395
Cdd:TIGR00957 646 WARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS----------------VAYVPQQAW 709
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 396 ATLDPMRtvhssiEEPLRIHKIGTKkeREQRVFE----LLDRVALPA----EMGRRfpG-ELSGGQRQRVAIARALALNP 466
Cdd:TIGR00957 710 IQNDSLR------ENILFGKALNEK--YYQQVLEacalLPDLEILPSgdrtEIGEK--GvNLSGGQKQRVSLARAVYSNA 779
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2524658687 467 EVVVCDEAVSALDVVVQAQVLELLAELQEEM-DLAYLFITHDLAVVRQVaDEVIVMEHGKMVEHRPTDDLFD 537
Cdd:TIGR00957 780 DIYLFDDPLSAVDAHVGKHIFEHVIGPEGVLkNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQ 850
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
38-262 |
6.82e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 63.10 E-value: 6.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLL-PGDGEVTggtitFDGRDITHlTDREFVSIRGNgIGLVPQDPMT 116
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLrPQKGAVL-----WQGKPLDY-SKRGLLALRQQ-VATVFQDPEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 117 NLnpVWT-VGSQIKEALRanNIATGSEAHKKAIEllEQAGLPNAKKRIDQYPHEFSGGMRQRALIAMGLAAHPKLLIADE 195
Cdd:PRK13638 89 QI--FYTdIDSDIAFSLR--NLGVPEAEITRRVD--EALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2524658687 196 PTSALDVTVAKKILDHLDKLTSElGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVLTRPQ 262
Cdd:PRK13638 163 PTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTE 228
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
327-536 |
9.04e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 65.00 E-value: 9.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 327 ISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQgrnrKEEL-ELRRRIQPIFQNPYA-------TL 398
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVA----KFGLtDLRRVLSIIPQSPVLfsgtvrfNI 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 399 DPMrTVHSSIEEPLRIHKIGTKKEREQRVFELLDRVAlpaEMGRRFpgelSGGQRQRVAIARALALNPEVVVCDEAVSAL 478
Cdd:PLN03232 1331 DPF-SEHNDADLWEALERAHIKDVIDRNPFGLDAEVS---EGGENF----SVGQRQLLSLARALLRRSKILVLDEATASV 1402
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2524658687 479 DVVVQAQVLELLAELQEEMDLayLFITHDLAVVRQvADEVIVMEHGKMVEHRPTDDLF 536
Cdd:PLN03232 1403 DVRTDSLIQRTIREEFKSCTM--LVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELL 1457
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
46-253 |
9.40e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 64.74 E-value: 9.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 46 VFPGETVAIVGESGSGKSTTAHAALGLLPGdGEVTGGTITFDGRDIthltDREFVSIrgngIGLVPQdpmtnlNPVWTVG 125
Cdd:TIGR00956 786 VKPGTLTALMGASGAGKTTLLNVLAERVTT-GVITGGDRLVNGRPL----DSSFQRS----IGYVQQ------QDLHLPT 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 126 SQIKEAL------RANNIATGSEAHK---KAIELLEQ-------AGLPNAKKRIDQyphefsggmRQRALIAMGLAAHPK 189
Cdd:TIGR00956 851 STVRESLrfsaylRQPKSVSKSEKMEyveEVIKLLEMesyadavVGVPGEGLNVEQ---------RKRLTIGVELVAKPK 921
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2524658687 190 LLI-ADEPTSALDVTVAKKILDHLDKLtSELGTSVVLITHD-LGLAAERADRLVVMQ-AGRVVETGP 253
Cdd:TIGR00956 922 LLLfLDEPTSGLDSQTAWSICKLMRKL-ADHGQAILCTIHQpSAILFEEFDRLLLLQkGGQTVYFGD 987
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
330-521 |
1.24e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.06 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 330 TLRRGRTIGIVGESGSGKSTVANMALGLLDP----TEGEVLFDgkRVQGRNRKEELelrrriQPIFQNPYAtlDPMRTVH 405
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPnlgdYEEEPSWD--EVLKRFRGTEL------QNYFKKLYN--GEIKVVH 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 406 ssieEPLRIHKI-----GT-----KKEREQRVF-ELLDRVALPAEMGRRFpGELSGGQRQRVAIARALALNPEVVVCDEA 474
Cdd:PRK13409 165 ----KPQYVDLIpkvfkGKvrellKKVDERGKLdEVVERLGLENILDRDI-SELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2524658687 475 VSALDV---VVQAQVLELLAElqeemDLAYLFITHDLAVVRQVADEVIVM 521
Cdd:PRK13409 240 TSYLDIrqrLNVARLIRELAE-----GKYVLVVEHDLAVLDYLADNVHIA 284
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
39-259 |
1.39e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 62.21 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 39 VHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLpgdgEVTGGTITFDGRDITHltdrefvSIRGNGIGLVPQDPMTNl 118
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFV----RLASGKISILGQPTRQ-------ALQKNLVAYVPQSEEVD- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 119 npvWTVGSQIKEAlrannIATGSEAHKKAIELL---EQAGLPNAKKRID--QYPH----EFSGGMRQRALIAMGLAAHPK 189
Cdd:PRK15056 91 ---WSFPVLVEDV-----VMMGRYGHMGWLRRAkkrDRQIVTAALARVDmvEFRHrqigELSGGQKKRVFLARAIAQQGQ 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 190 LLIADEPTSALDVTVAKKILDHLDKLTSElGTSVVLITHDLGLAAERADrLVVMQAGRVVETGPALQVLT 259
Cdd:PRK15056 163 VILLDEPFTGVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGPTETTFT 230
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
300-473 |
1.83e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 63.45 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 300 VAKNLVRDFAIRGDRP----------WRKDSFR-----------AVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLL 358
Cdd:PRK10522 294 VAFNKLNKLALAPYKAefprpqafpdWQTLELRnvtfayqdngfSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLY 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 359 DPTEGEVLFDGKRVQGRNRKeelELRRRIQPIFQNpyatldpmrtVHssieepLRIHKIGTKKER--EQRVFELLDRVA- 435
Cdd:PRK10522 374 QPQSGEILLDGKPVTAEQPE---DYRKLFSAVFTD----------FH------LFDQLLGPEGKPanPALVEKWLERLKm 434
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2524658687 436 ---LPAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDE 473
Cdd:PRK10522 435 ahkLELEDGRISNLKLSKGQKKRLALLLALAEERDILLLDE 475
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
32-260 |
2.06e-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: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 32 SKSLTDVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLpgdgEVTGGTITFDGrdithltdrefvsirgnGIGLVP 111
Cdd:TIGR00957 647 ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEM----DKVEGHVHMKG-----------------SVAYVP 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 112 QDpmtnlnpVWTVGSQIKEalranNIATGSEAHKKAIELLEQAG--------LPNA-KKRIDQYPHEFSGGMRQRALIAM 182
Cdd:TIGR00957 706 QQ-------AWIQNDSLRE-----NILFGKALNEKYYQQVLEACallpdleiLPSGdRTEIGEKGVNLSGGQKQRVSLAR 773
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2524658687 183 GLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSEL-GTSVVLITHDLGLAAErADRLVVMQAGRVVETGPALQVLTR 260
Cdd:TIGR00957 774 AVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGPEGVLkNKTRILVTHGISYLPQ-VDVIIVMSGGKISEMGSYQELLQR 851
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
11-246 |
2.34e-10 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 59.95 E-value: 2.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 11 PILTLKDVCigFPTTTASGRRSksltdVVHDVNLEVFPGETVAIVGESGSGKSTTahaaLGLLPG--DGEVTGGTITFDG 88
Cdd:cd03232 2 SVLTWKNLN--YTVPVKGGKRQ-----LLNNISGYVKPGTLTALMGESGAGKTTL----LDVLAGrkTAGVITGEILING 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 89 RDITHLTDREfvsirgngIGLVPQDPMtnLNPVWTVgsqiKEALR--ANNIATGseahkkaielLEQaglpnakkridqy 166
Cdd:cd03232 71 RPLDKNFQRS--------TGYVEQQDV--HSPNLTV----REALRfsALLRGLS----------VEQ------------- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 167 phefsggmRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSElGTSVVLITH----DLglaAERADRLVV 242
Cdd:cd03232 114 --------RKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADS-GQAILCTIHqpsaSI---FEKFDRLLL 181
|
....
gi 2524658687 243 MQAG 246
Cdd:cd03232 182 LKRG 185
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
324-486 |
2.69e-10 |
|
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: 59.09 E-value: 2.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 324 VDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLD--------PTEGEVLFdgkrvqgrnrkeelelrrriqpIFQNPY 395
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPwgsgrigmPEGEDLLF----------------------LPQRPY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 396 ATLdpmrtvhssieeplrihkiGTkkereqrvfeLLDRVALPAEMgrrfpgELSGGQRQRVAIARALALNPEVVVCDEAV 475
Cdd:cd03223 75 LPL-------------------GT----------LREQLIYPWDD------VLSGGEQQRLAFARLLLHKPKFVFLDEAT 119
|
170
....*....|.
gi 2524658687 476 SALDVVVQAQV 486
Cdd:cd03223 120 SALDEESEDRL 130
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
38-233 |
3.54e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 59.89 E-value: 3.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPgdgeVTGGTITFDGRDITHLTDREFVSIRGngiglvPQDPMtn 117
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLP----PAAGTIKLDGGDIDDPDVAEACHYLG------HRNAM-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 118 lNPVWTVGsqikEALR--ANNIATGSEAHKKAIELLEQAGLPNAKKRidqyphEFSGGMRQRALIAMGLAAHPKLLIADE 195
Cdd:PRK13539 85 -KPALTVA----ENLEfwAAFLGGEELDIAAALEAVGLAPLAHLPFG------YLSAGQKRRVALARLLVSNRPIWILDE 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2524658687 196 PTSALDVT----VAKKILDHLDKltselGTSVVLITH-DLGLA 233
Cdd:PRK13539 154 PTAALDAAavalFAELIRAHLAQ-----GGIVIAATHiPLGLP 191
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
41-246 |
4.99e-10 |
|
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: 59.65 E-value: 4.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 41 DVNLEVFPGETVAIVGESGSGKSTTAHAALGLLpgdgEVTGGTITFDGRDITHLTDREFVSIRGNGIGLVPQDPmtnlnp 120
Cdd:cd03290 19 NINIRIPTGQLTMIVGQVGCGKSSLLLAILGEM----QTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKP------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 121 vWTVGSQIKEalranNIATGSEAHKKAIELLEQAGlpNAKKRIDQYPH-----------EFSGGMRQRALIAMGLAAHPK 189
Cdd:cd03290 89 -WLLNATVEE-----NITFGSPFNKQRYKAVTDAC--SLQPDIDLLPFgdqteigergiNLSGGQRQRICVARALYQNTN 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2524658687 190 LLIADEPTSALDVTVAkkilDHLD-----KLTSELGTSVVLITHDLGLAAErADRLVVMQAG 246
Cdd:cd03290 161 IVFLDDPFSALDIHLS----DHLMqegilKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
324-528 |
6.13e-10 |
|
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: 59.08 E-value: 6.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 324 VDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLD--PTEGEVLFDGKRVqgrnrkeeLEL------RRRIQPIFQNPY 395
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEDI--------TDLppeeraRLGIFLAFQYPP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 396 atldpmrtvhssieeplRIHKIgtkkereqRVFELLdrvalpaemgrRFPGE-LSGGQRQRVAIARALALNPEVVVCDEA 474
Cdd:cd03217 88 -----------------EIPGV--------KNADFL-----------RYVNEgFSGGEKKRNEILQLLLLEPDLAILDEP 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2524658687 475 VSALDVVVQAQVLELLAELQEEmDLAYLFITHDLAVVRQV-ADEVIVMEHGKMVE 528
Cdd:cd03217 132 DSGLDIDALRLVAEVINKLREE-GKSVLIITHYQRLLDYIkPDRVHVLYDGRIVK 185
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
38-228 |
7.13e-10 |
|
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: 57.93 E-value: 7.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPgdgeVTGGTItfdgrdithltdrefVSIRGNGIGLVPQDP-MT 116
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWP----WGSGRI---------------GMPEGEDLLFLPQRPyLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 117 nlnpvwtVGSqIKEALRanniatgseahkkaielleqaglpnakkridqYP--HEFSGGMRQRALIAMGLAAHPKLLIAD 194
Cdd:cd03223 77 -------LGT-LREQLI--------------------------------YPwdDVLSGGEQQRLAFARLLLHKPKFVFLD 116
|
170 180 190
....*....|....*....|....*....|....
gi 2524658687 195 EPTSALDVTVAKKILDHLDkltsELGTSVVLITH 228
Cdd:cd03223 117 EATSALDEESEDRLYQLLK----ELGITVISVGH 146
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
30-279 |
9.90e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 61.72 E-value: 9.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 30 RRSKSLTDVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLpgdgEVTGGTITFDGRDITHLTDREfvsIRgNGIGL 109
Cdd:PTZ00243 1317 RYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMV----EVCGGEIRVNGREIGAYGLRE---LR-RQFSM 1388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 110 VPQDPM-------TNLNP--------VWT----VGsqikeaLRaNNIATGSEahkkAIELLEQAGLPNakkridqypheF 170
Cdd:PTZ00243 1389 IPQDPVlfdgtvrQNVDPfleassaeVWAalelVG------LR-ERVASESE----GIDSRVLEGGSN-----------Y 1446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 171 SGGMRQ-----RALIAMGLAahpkLLIADEPTSALDVTVAKKILDHLdkLTSELGTSVVLITHDLGLAAErADRLVVMQA 245
Cdd:PTZ00243 1447 SVGQRQlmcmaRALLKKGSG----FILMDEATANIDPALDRQIQATV--MSAFSAYTVITIAHRLHTVAQ-YDKIIVMDH 1519
|
250 260 270
....*....|....*....|....*....|....
gi 2524658687 246 GRVVETGPALQVLTRPQHPYTKQLIAAAPSLAAR 279
Cdd:PTZ00243 1520 GAVAEMGSPRELVMNRQSIFHSMVEALGRSEAKR 1553
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
40-249 |
1.79e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 60.31 E-value: 1.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 40 HDVNLEVFPGETVAIVGESGSGKSTTAHaalgLLPGDGEVTGGTITFDGRDITHLTDREfvSIRGnGIGLVPQD-PMTNL 118
Cdd:PRK11288 270 EPISFSVRAGEIVGLFGLVGAGRSELMK----LLYGATRRTAGQVYLDGKPIDIRSPRD--AIRA-GIMLCPEDrKAEGI 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 119 NPVWTVGSQIKEALRANNIATGSEAHKKAiellEQAglpNAKKRI----------DQYPHEFSGGMRQRALIAMGLAAHP 188
Cdd:PRK11288 343 IPVHSVADNINISARRHHLRAGCLINNRW----EAE---NADRFIrslniktpsrEQLIMNLSGGNQQKAILGRWLSEDM 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2524658687 189 KLLIADEPTSALDVTVAKKILDHLDKLtSELGTSVVLITHDLGLAAERADRLVVMQAGRVV 249
Cdd:PRK11288 416 KVILLDEPTRGIDVGAKHEIYNVIYEL-AAQGVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
317-480 |
1.99e-09 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 57.37 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 317 RKDSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQgrnrkeelelRRRIQPIFQNPYA 396
Cdd:TIGR01189 9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLA----------EQRDEPHENILYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 397 T-LDPMRTVHSSIEEPLRIHKIGTKKEREqrVFELLDRVALPAEMGRRFpGELSGGQRQRVAIARALALNPEVVVCDEAV 475
Cdd:TIGR01189 79 GhLPGLKPELSALENLHFWAAIHGGAQRT--IEDALAAVGLTGFEDLPA-AQLSAGQQRRLALARLWLSRRPLWILDEPT 155
|
....*
gi 2524658687 476 SALDV 480
Cdd:TIGR01189 156 TALDK 160
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
327-534 |
2.04e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 58.41 E-value: 2.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 327 ISFTLRRGRTIGIVGESGSGKSTVANMALGLLdPTEGEVLFDGKRVQGRnRKEELELRR-----RIQPIFQNP-YATLDP 400
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAW-SAAELARHRaylsqQQTPPFAMPvFQYLTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 401 MRTVHSSIEEPlrihkigtkkerEQRVFELLDRVALPAEMGRRFpGELSGGQRQRVAIARAL-----ALNPE--VVVCDE 473
Cdd:PRK03695 93 HQPDKTRTEAV------------ASALNEVAEALGLDDKLGRSV-NQLSGGEWQRVRLAAVVlqvwpDINPAgqLLLLDE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2524658687 474 AVSALDVVVQAqvlellaelqeEMD----------LAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDD 534
Cdd:PRK03695 160 PMNSLDVAQQA-----------ALDrllselcqqgIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDE 219
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
322-486 |
2.27e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 57.97 E-value: 2.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 322 RAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEelelrrriqpIFQNPYATLDPM 401
Cdd:PRK11614 19 QALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAK----------IMREAVAIVPEG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 402 RTVHS--SIEEPLRIHKIGTKKEREQ----RVFELLDRVAlpaEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAV 475
Cdd:PRK11614 89 RRVFSrmTVEENLAMGGFFAERDQFQerikWVYELFPRLH---ERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPS 165
|
170
....*....|.
gi 2524658687 476 SALDVVVQAQV 486
Cdd:PRK11614 166 LGLAPIIIQQI 176
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
324-483 |
2.86e-09 |
|
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: 59.76 E-value: 2.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 324 VDDISFTLRRGRTIGIVGESGSGKSTVANMaLGLLDPTEGevlfdgkrvqGRNRKEElelRRRIQPIFQNPYATLdpmRT 403
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRI-LGELWPVYG----------GRLTKPA---KGKLFYVPQRPYMTL---GT 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 404 VHSSIEEPLRIHKIGTKKEREQRVFELLDRVAL----PAEMG----RRFPGELSGGQRQRVAIARALALNPEVVVCDEAV 475
Cdd:TIGR00954 531 LRDQIIYPDSSEDMKRRGLSDKDLEQILDNVQLthilEREGGwsavQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECT 610
|
....*...
gi 2524658687 476 SALDVVVQ 483
Cdd:TIGR00954 611 SAVSVDVE 618
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
41-480 |
3.43e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 59.36 E-value: 3.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 41 DVNLEVFPGETVAIVGESGSGKSTTahaaLGLLPG-DGEVTGGTITFDGrdIThltdrefvsirgngIGLVPQDPmtNLN 119
Cdd:PRK11819 25 DISLSFFPGAKIGVLGLNGAGKSTL----LRIMAGvDKEFEGEARPAPG--IK--------------VGYLPQEP--QLD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 120 PVWTVGSQIKEAL--------RANNI------------ATGSE--------AHKKAIEL---LEQA----GLPNAKKRID 164
Cdd:PRK11819 83 PEKTVRENVEEGVaevkaaldRFNEIyaayaepdadfdALAAEqgelqeiiDAADAWDLdsqLEIAmdalRCPPWDAKVT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 165 QypheFSGGMRQRALIAMGLAAHPKLLIADEPTSALDvtvAKKIL---DHLDKLTselGTsVVLITHD---LGLAAE--- 235
Cdd:PRK11819 163 K----LSGGERRRVALCRLLLEKPDMLLLDEPTNHLD---AESVAwleQFLHDYP---GT-VVAVTHDryfLDNVAGwil 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 236 --------------------RADRLVVMQ---AGRV---------VETGP-ALQV-----LTR----PQHPYTKQL---- 269
Cdd:PRK11819 232 eldrgrgipwegnysswleqKAKRLAQEEkqeAARQkalkrelewVRQSPkARQAkskarLARyeelLSEEYQKRNetne 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 270 --IAAAPslaaRRGDRVVAApttsdadqkeilvaKNLVRDFairGDRpwrkdsfRAVDDISFTLRRGRTIGIVGESGSGK 347
Cdd:PRK11819 312 ifIPPGP----RLGDKVIEA--------------ENLSKSF---GDR-------LLIDDLSFSLPPGGIVGIIGPNGAGK 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 348 STVANMALGLLDPTEGEVLFdGKRV------QGRnrkeelelrrriqpifqnpyATLDPMRTVHSSIEEPLRIHKIGtKK 421
Cdd:PRK11819 364 STLFKMITGQEQPDSGTIKI-GETVklayvdQSR--------------------DALDPNKTVWEEISGGLDIIKVG-NR 421
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2524658687 422 EREQRvfelldrvalpAEMGR---------RFPGELSGGQRQRVAIARALALNPEVVVCDEAVSALDV 480
Cdd:PRK11819 422 EIPSR-----------AYVGRfnfkggdqqKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDV 478
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
46-267 |
4.12e-09 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 59.64 E-value: 4.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 46 VFPGETVAIVGESGSGKSTTahaaLGLLPGDGEVTGGTITFDGRDIthLTDrefVSIRGNGIGLVPQdpMTNLNPVWTVG 125
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTT----FKMLTGDTTVTSGDATVAGKSI--LTN---ISDVHQNMGYCPQ--FDAIDDLLTGR 2030
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 126 SQIKEALRANNIATgSEAHKKAIELLEQAGLpnaKKRIDQYPHEFSGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVA 205
Cdd:TIGR01257 2031 EHLYLYARLRGVPA-EEIEKVANWSIQSLGL---SLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQAR 2106
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2524658687 206 KKILDHLDKLTSElGTSVVLITHDLGLAAERADRLVVMQAGrvvetgpALQVLTRPQHPYTK 267
Cdd:TIGR01257 2107 RMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG-------AFQCLGTIQHLKSK 2160
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
334-544 |
4.34e-09 |
|
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: 57.61 E-value: 4.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 334 GRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQgrnrKEELE-LRRRIQPIFQNPYA-------TLDPMRT-V 404
Cdd:cd03288 47 GQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDIS----KLPLHtLRSRLSIILQDPILfsgsirfNLDPECKcT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 405 HSSIEEPLRIHKIgtkKEREQRVFELLDrvALPAEMGRRFpgelSGGQRQRVAIARALALNPEVVVCDEAVSALDVVVQA 484
Cdd:cd03288 123 DDRLWEALEIAQL---KNMVKSLPGGLD--AVVTEGGENF----SVGQRQLFCLARAFVRKSSILIMDEATASIDMATEN 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 485 QVLELLAELQEemDLAYLFITHDLAVVRQvADEVIVMEHGKMVEHRPTDDLFDHPEKEYT 544
Cdd:cd03288 194 ILQKVVMTAFA--DRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQEDGVFA 250
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
323-545 |
5.19e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 58.75 E-value: 5.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 323 AVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRV-----QGRNRK----EELELRRRIqpifqn 393
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAAliaisSGLNGQltgiENIELKGLM------ 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 394 pyatldpmrtvhssieeplrihkIGTKKEREQrvfELLDRVALPAEMGRRFPGEL---SGGQRQRVAIARALALNPEVVV 470
Cdd:PRK13545 113 -----------------------MGLTKEKIK---EIIPEIIEFADIGKFIYQPVktySSGMKSRLGFAISVHINPDILV 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2524658687 471 CDEAVSALDVVVQAQVLELLAELQEEMDLAYlFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDLFDHPE---KEYTQ 545
Cdd:PRK13545 167 IDEALSVGDQTFTKKCLDKMNEFKEQGKTIF-FISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDHYDeflKKYNQ 243
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
13-266 |
5.31e-09 |
|
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: 57.23 E-value: 5.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 13 LTLKDVCIgfptttasgRRSKSLTDVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLpgdgEVTGGTITFDGRDIT 92
Cdd:cd03288 20 IKIHDLCV---------RYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMV----DIFDGKIVIDGIDIS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 93 HL---TDREFVSIrgngiglVPQDPMT-------NLNPVWT-VGSQIKEALRANNIATGSEAHKKAIELLEQAGLPNakk 161
Cdd:cd03288 87 KLplhTLRSRLSI-------ILQDPILfsgsirfNLDPECKcTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGEN--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 162 ridqypheFSGGMRQRALIAMGLAAHPKLLIADEPTSALDVTvAKKILDHLdKLTSELGTSVVLITHDLGLAAErADRLV 241
Cdd:cd03288 157 --------FSVGQRQLFCLARAFVRKSSILIMDEATASIDMA-TENILQKV-VMTAFADRTVVTIAHRVSTILD-ADLVL 225
|
250 260
....*....|....*....|....*
gi 2524658687 242 VMQAGRVVETGPALQVLTRPQHPYT 266
Cdd:cd03288 226 VLSRGILVECDTPENLLAQEDGVFA 250
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
23-252 |
5.46e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 59.41 E-value: 5.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 23 PTTTASGRRSKSLTD---------VVHDVNLEVFPGETVAIVGESGSGKSTTahaaLGLLPGDGEVTGGTItFDGRDITH 93
Cdd:PTZ00243 651 PTSERSAKTPKMKTDdffelepkvLLRDVSVSVPRGKLTVVLGATGSGKSTL----LQSLLSQFEISEGRV-WAERSIAY 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 94 LTDREFV---SIRGNGIGLVPQDPmTNLNPVWTVgSQIKEALRANNIATGSEAHKKAIELleqaglpnakkridqyphef 170
Cdd:PTZ00243 726 VPQQAWImnaTVRGNILFFDEEDA-ARLADAVRV-SQLEADLAQLGGGLETEIGEKGVNL-------------------- 783
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 171 SGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLdKLTSELGTSVVLITHDLGLAAeRADRLVVMQAGRVVE 250
Cdd:PTZ00243 784 SGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEEC-FLGALAGKTRVLATHQVHVVP-RADYVVALGDGRVEF 861
|
..
gi 2524658687 251 TG 252
Cdd:PTZ00243 862 SG 863
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
41-229 |
6.24e-09 |
|
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: 54.76 E-value: 6.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 41 DVNLEVFPGETVAIVGESGSGKSTTahaaLGLLPGDGEVTGGTITfdgrdithltdrefvSIRGNGIGLVPQdpmtnlnp 120
Cdd:cd03221 18 DISLTINPGDRIGLVGRNGAGKSTL----LKLIAGELEPDEGIVT---------------WGSTVKIGYFEQ-------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 121 vwtvgsqikealranniatgseahkkaielleqaglpnakkridqypheFSGGMRQRALIAMGLAAHPKLLIADEPTSAL 200
Cdd:cd03221 71 -------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHL 101
|
170 180 190
....*....|....*....|....*....|...
gi 2524658687 201 DvtvakkiLDHLDKLTSEL----GTsVVLITHD 229
Cdd:cd03221 102 D-------LESIEALEEALkeypGT-VILVSHD 126
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
327-528 |
7.00e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 59.02 E-value: 7.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 327 ISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVlfdgkRVQGRN------RkeelELRRRIQPIFQNPY----- 395
Cdd:PTZ00243 1329 VSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEI-----RVNGREigayglR----ELRRQFSMIPQDPVlfdgt 1399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 396 --ATLDPMrtVHSSIEEPLRIHKIGTKKEREQRVFELLDRVALpaEMGRRFpgelSGGQRQRVAIARA-LALNPEVVVCD 472
Cdd:PTZ00243 1400 vrQNVDPF--LEASSAEVWAALELVGLRERVASESEGIDSRVL--EGGSNY----SVGQRQLMCMARAlLKKGSGFILMD 1471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2524658687 473 EAVS----ALDVVVQAQVLELLAelqeemdlAYLFIT--HDLAVVRQVaDEVIVMEHGKMVE 528
Cdd:PTZ00243 1472 EATAnidpALDRQIQATVMSAFS--------AYTVITiaHRLHTVAQY-DKIIVMDHGAVAE 1524
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
48-247 |
7.68e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 54.69 E-value: 7.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 48 PGETVAIVGESGSGKSTTAHAALGLLPGDGevtGGTITFDGRDIthltdrefvsirgngiglvpqdpmtnlnpvwtvgsq 127
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPG---GGVIYIDGEDI------------------------------------ 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 128 ikealranniatgseahkkaielLEQAGLPNAKKRIDQYPHEFSGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKK 207
Cdd:smart00382 42 -----------------------LEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEAL 98
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2524658687 208 ILDH-----LDKLTSELGTSVVLITHDL-----GLAAERADRLVVMQAGR 247
Cdd:smart00382 99 LLLLeelrlLLLLKSEKNLTVILTTNDEkdlgpALLRRRFDRRIVLLLIL 148
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
332-521 |
7.78e-09 |
|
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: 56.61 E-value: 7.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 332 RRGRTIGIVGESGSGKSTVANMALGLLDPTEG---------EVL--FDGKRVQgrNRKEELeLRRRIQPIFQNPYATLDP 400
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGkfddppdwdEILdeFRGSELQ--NYFTKL-LEGDVKVIVKPQYVDLIP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 401 mRTVHSSIEEPLrihkigTKKEREQRVFELLDRVALPAEMGRRFpGELSGGQRQRVAIARALALNPEVVVCDEAVSALDV 480
Cdd:cd03236 101 -KAVKGKVGELL------KKKDERGKLDELVDQLELRHVLDRNI-DQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2524658687 481 ---VVQAQVLELLAELQEEMdlayLFITHDLAVVRQVADEVIVM 521
Cdd:cd03236 173 kqrLNAARLIRELAEDDNYV----LVVEHDLAVLDYLSDYIHCL 212
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
326-486 |
1.25e-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: 58.00 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 326 DISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGkrvqgrnrkeelelrrRIQPIFQNPYatldpmrTVH 405
Cdd:TIGR01271 444 NISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG----------------RISFSPQTSW-------IMP 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 406 SSIEEPLrIHKIGTKKEREQRVF---ELLDRVALPAEMGRRFPGE----LSGGQRQRVAIARALALNPEVVVCDEAVSAL 478
Cdd:TIGR01271 501 GTIKDNI-IFGLSYDEYRYTSVIkacQLEEDIALFPEKDKTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFTHL 579
|
....*...
gi 2524658687 479 DVVVQAQV 486
Cdd:TIGR01271 580 DVVTEKEI 587
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
322-535 |
1.28e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 57.32 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 322 RAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEELElrRRIQPIFQNpyATLDPM 401
Cdd:PRK10762 18 KALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQE--AGIGIIHQE--LNLIPQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 402 RTVHSSI----EEPLRIHKIGTKKEREQrVFELLDRVALPAEmGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVSA 477
Cdd:PRK10762 94 LTIAENIflgrEFVNRFGRIDWKKMYAE-ADKLLARLNLRFS-SDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2524658687 478 L-DVVVQAQVLELLAELQEEMDLAYlfITHDLAVVRQVADEVIVMEHGKMVEHRPTDDL 535
Cdd:PRK10762 172 LtDTETESLFRVIRELKSQGRGIVY--ISHRLKEIFEICDDVTVFRDGQFIAEREVADL 228
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
330-521 |
1.37e-08 |
|
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: 57.49 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 330 TLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEvlFDGK----RVQGRNRKEELelrrriQPIFQNPYAtlDPMRTVH 405
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGELKPNLGD--YDEEpswdEVLKRFRGTEL------QDYFKKLAN--GEIKVAH 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 406 ssieEPLRIHKI-----GT-----KKEREQRVF-ELLDRVALPAEMGRRFpGELSGGQRQRVAIARALALNPEVVVCDEA 474
Cdd:COG1245 165 ----KPQYVDLIpkvfkGTvrellEKVDERGKLdELAEKLGLENILDRDI-SELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2524658687 475 VSALDV---VVQAQVLELLAELQEEMdlayLFITHDLAVVRQVADEVIVM 521
Cdd:COG1245 240 SSYLDIyqrLNVARLIRELAEEGKYV----LVVEHDLAILDYLADYVHIL 285
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
327-560 |
1.60e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 56.98 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 327 ISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEELELRRRIQPifQNPYatLDPMRTVHS 406
Cdd:PRK15439 30 IDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIYLVP--QEPL--LFPNLSVKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 407 SIeePLRIHKigtKKEREQRVFELLdrvalpAEMGRRF-----PGELSGGQRQRVAIARALALNPEVVVCDEAVSALdVV 481
Cdd:PRK15439 106 NI--LFGLPK---RQASMQKMKQLL------AALGCQLdldssAGSLEVADRQIVEILRGLMRDSRILILDEPTASL-TP 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2524658687 482 VQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDLFDhpekeytQRLLDAIPGASLDLDL 560
Cdd:PRK15439 174 AETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLST-------DDIIQAITPAAREKSL 245
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
324-479 |
2.00e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 54.57 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 324 VDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQGRNRKEELELRRRIQPIFQNPYATL--DPM 401
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPYLTLreNCL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 402 RTVHSS-----IEEPLRIHKIGtkkereqrvfELLDrvalpaemgrrFP-GELSGGQRQRVAIARALALNPEVVVCDEAV 475
Cdd:PRK13540 97 YDIHFSpgavgITELCRLFSLE----------HLID-----------YPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPL 155
|
....
gi 2524658687 476 SALD 479
Cdd:PRK13540 156 VALD 159
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
334-479 |
2.94e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 56.43 E-value: 2.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 334 GRTIGIVGESGSGKSTVANMALGLLDPTEgevlFDGKrVQGRNRKEELELRRRIQPIFQNPyaTLDPMRTVHSSIE--EP 411
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNN----FTGT-ILANNRKPTKQILKRTGFVTQDD--ILYPHLTVRETLVfcSL 166
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2524658687 412 LRIHKIGTKKEREQRVFELLDRVALP----AEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVSALD 479
Cdd:PLN03211 167 LRLPKSLTKQEKILVAESVISELGLTkcenTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
30-252 |
3.33e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 56.88 E-value: 3.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 30 RRSKSLTDVVHDVNLEVFPGETVAIVGESGSGKSTTahaALGLLPGDgEVTGGTITFDGRDITH--LTDREFvsirgnGI 107
Cdd:TIGR00957 1293 RYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSL---TLGLFRIN-ESAEGEIIIDGLNIAKigLHDLRF------KI 1362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 108 GLVPQDpmtnlnPVWTVGSqikeaLRANNIATGSEAHKKAIELLEQAGLPN-AKKRIDQYPHE-------FSGGMRQRAL 179
Cdd:TIGR00957 1363 TIIPQD------PVLFSGS-----LRMNLDPFSQYSDEEVWWALELAHLKTfVSALPDKLDHEcaeggenLSVGQRQLVC 1431
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2524658687 180 IAMGLAAHPKLLIADEPTSALDVTVakkilDHLDKLT--SELGTSVVL-ITHDLGLAAERAdRLVVMQAGRVVETG 252
Cdd:TIGR00957 1432 LARALLRKTKILVLDEATAAVDLET-----DNLIQSTirTQFEDCTVLtIAHRLNTIMDYT-RVIVLDKGEVAEFG 1501
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
42-240 |
4.31e-08 |
|
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: 53.52 E-value: 4.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 42 VNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGDGevtgGTITFDGRDITHLTDrefvsIRGNGIGLVPQDPmtNLNPV 121
Cdd:TIGR01189 19 LSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDS----GEVRWNGTPLAEQRD-----EPHENILYLGHLP--GLKPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 122 WTVgsqiKEALRANNiATGSEAHKKAIELLEQAGLPNAKKRIdqyPHEFSGGMRQRALIAMGLAAHPKLLIADEPTSALD 201
Cdd:TIGR01189 88 LSA----LENLHFWA-AIHGGAQRTIEDALAAVGLTGFEDLP---AAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2524658687 202 VT----VAKKILDHLDKltselGTSVVLITH-DLGLAAERADRL 240
Cdd:TIGR01189 160 KAgvalLAGLLRAHLAR-----GGIVLLTTHqDLGLVEARELRL 198
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
326-527 |
5.71e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 55.94 E-value: 5.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 326 DISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDgkrvqgrnrkeelelrRRIQPIFQNPYAtldpMR-TV 404
Cdd:PTZ00243 678 DVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE----------------RSIAYVPQQAWI----MNaTV 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 405 HSSI-----EEPLRIHKIgtkkereQRVFELLDRVA-----LPAEMGRRfpG-ELSGGQRQRVAIARALALNPEVVVCDE 473
Cdd:PTZ00243 738 RGNIlffdeEDAARLADA-------VRVSQLEADLAqlgggLETEIGEK--GvNLSGGQKARVSLARAVYANRDVYLLDD 808
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2524658687 474 AVSALDVVVQAQVLELLAELQEEMDLAYLfITHDLAVVRQvADEVIVMEHGKMV 527
Cdd:PTZ00243 809 PLSALDAHVGERVVEECFLGALAGKTRVL-ATHQVHVVPR-ADYVVALGDGRVE 860
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
333-522 |
5.72e-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: 51.99 E-value: 5.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 333 RGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLfdgkrvqgrnrkeelelrrriqpifqnpYATLDPMRTVhssieepl 412
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVI----------------------------YIDGEDILEE-------- 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 413 rihkigtkkereqrvfellDRVALPAEMGRRFPGELSGGQRQRVAIARALALNPEVVVCDEAVSALDVVVQAQVLELLAE 492
Cdd:smart00382 45 -------------------VLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEEL 105
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2524658687 493 LQEEMDLAY-----LFITHDL-----AVVRQVADEVIVME 522
Cdd:smart00382 106 RLLLLLKSEknltvILTTNDEkdlgpALLRRRFDRRIVLL 145
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
249-295 |
6.93e-08 |
|
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: 49.32 E-value: 6.93e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2524658687 249 VETGPALQVLTRPQHPYTKQLIAAAPSLAARRGDRVVAAPTTSDADQ 295
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPRLDPPKRPLYTIPGNVPSLLE 47
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
324-480 |
7.61e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 55.25 E-value: 7.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 324 VDDISFTLRRGRTIGIVGESGSGKST-VANMALGLLD--PTEGEVLFDGKRVQGRN-------------RKEELELRRRI 387
Cdd:PLN03073 193 IVDASVTLAFGRHYGLVGRNGTGKTTfLRYMAMHAIDgiPKNCQILHVEQEVVGDDttalqcvlntdieRTQLLEEEAQL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 388 ---QPIFQNPYATLDPMRTVHSSIEEPL---RIHKIGTKKER------EQRVFELLDRVALPAEMGRRFPGELSGGQRQR 455
Cdd:PLN03073 273 vaqQRELEFETETGKGKGANKDGVDKDAvsqRLEEIYKRLELidaytaEARAASILAGLSFTPEMQVKATKTFSGGWRMR 352
|
170 180
....*....|....*....|....*
gi 2524658687 456 VAIARALALNPEVVVCDEAVSALDV 480
Cdd:PLN03073 353 IALARALFIEPDLLLLDEPTNHLDL 377
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
50-242 |
7.94e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.42 E-value: 7.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 50 ETVAIVGESGSGKSTTA------------HAALGLLPGDGEVT------------------------------------- 80
Cdd:PTZ00265 1195 KTTAIVGETGSGKSTVMsllmrfydlkndHHIVFKNEHTNDMTneqdyqgdeeqnvgmknvnefsltkeggsgedstvfk 1274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 81 -GGTITFDGRDIThltDREFVSIRgNGIGLVPQDPMT-NLNpvwtvgsqIKEALRANNIATGSEAHKKAI------ELLE 152
Cdd:PTZ00265 1275 nSGKILLDGVDIC---DYNLKDLR-NLFSIVSQEPMLfNMS--------IYENIKFGKEDATREDVKRACkfaaidEFIE 1342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 153 QagLPNA-KKRIDQYPHEFSGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLG 231
Cdd:PTZ00265 1343 S--LPNKyDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIA 1420
|
250
....*....|.
gi 2524658687 232 lAAERADRLVV 242
Cdd:PTZ00265 1421 -SIKRSDKIVV 1430
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
41-242 |
9.10e-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: 9.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 41 DVNLEVFPG-----ETVAIVGESGSGKSTTAHAALGLLP---GDGEVTGGTITFDGRDIT---HLTDREFVSIRGNGIGL 109
Cdd:cd03237 12 EFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKpdeGDIEIELDTVSYKPQYIKadyEGTVRDLLSSITKDFYT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 110 VPQDPMTNLNPVwtvgsqikealranniatgseahkKAIELLEQaglpnakkridQYPhEFSGGMRQRALIAMGLAAHPK 189
Cdd:cd03237 92 HPYFKTEIAKPL------------------------QIEQILDR-----------EVP-ELSGGELQRVAIAACLSKDAD 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 190 LLIADEPTSALDV-------TVAKKILDHLDKltselgTSVVlITHDLGLAAERADRLVV 242
Cdd:cd03237 136 IYLLDEPSAYLDVeqrlmasKVIRRFAENNEK------TAFV-VEHDIIMIDYLADRLIV 188
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
322-528 |
9.64e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 54.80 E-value: 9.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 322 RAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLdPT---EGEVLFDGKRVQGRN-RKEElelRRRIQPIFQN---- 393
Cdd:NF040905 15 KALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGEVCRFKDiRDSE---ALGIVIIHQElali 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 394 PYAtldpmrtvhsSIEEPLRI-HKIGTK-----KEREQRVFELLDRVALpaemgRRFPGELSG----GQRQRVAIARALA 463
Cdd:NF040905 91 PYL----------SIAENIFLgNERAKRgvidwNETNRRARELLAKVGL-----DESPDTLVTdigvGKQQLVEIAKALS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2524658687 464 LNPEVVVCDEAVSAL---------DVVVQ--AQvlellaelqeemDLAYLFITHDLAVVRQVADEVIVMEHGKMVE 528
Cdd:NF040905 156 KDVKLLILDEPTAALneedsaallDLLLElkAQ------------GITSIIISHKLNEIRRVADSITVLRDGRTIE 219
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
319-528 |
1.98e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 52.34 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 319 DSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGllDP----TEGEVLFDGKRVQgrnrKEELELRRR--IQPIFQ 392
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPaykiLEGDILFKGESIL----DLEPEERAHlgIFLAFQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 393 NPY-----ATLDPMRTVHSSIE--------EPLRIHKIGTKKereqrvfelLDRVALPAEMGRRFPGE-LSGGQRQRVAI 458
Cdd:CHL00131 92 YPIeipgvSNADFLRLAYNSKRkfqglpelDPLEFLEIINEK---------LKLVGMDPSFLSRNVNEgFSGGEKKRNEI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2524658687 459 ARALALNPEVVVCDEAVSALDVVVQAQVLELLAELQEEmDLAYLFITHDLAVVRQVA-DEVIVMEHGKMVE 528
Cdd:CHL00131 163 LQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTS-ENSIILITHYQRLLDYIKpDYVHVMQNGKIIK 232
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
326-486 |
2.29e-07 |
|
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: 52.55 E-value: 2.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 326 DISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGkrvqgrnrkeelelrrRIQpiFQNPYATLDPmrtvh 405
Cdd:cd03291 55 NINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG----------------RIS--FSSQFSWIMP----- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 406 SSIEEPLrIHKIGTKKEREQRVF---ELLDRVALPAEMGRRFPGE----LSGGQRQRVAIARALALNPEVVVCDEAVSAL 478
Cdd:cd03291 112 GTIKENI-IFGVSYDEYRYKSVVkacQLEEDITKFPEKDNTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFGYL 190
|
....*...
gi 2524658687 479 DVVVQAQV 486
Cdd:cd03291 191 DVFTEKEI 198
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
38-211 |
2.37e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 54.15 E-value: 2.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGDGEVTGGTITFDgrDITHLTDREfvsirgnGIGLVPQDpmtn 117
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGEIQIDGVSWN--SVTLQTWRK-------AFGVIPQK---- 1300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 118 lnpVWTVGSQIKEALRANNIATGSEAHKKAiellEQAGLpnaKKRIDQYPHE-----------FSGGMRQRALIAMGLAA 186
Cdd:TIGR01271 1301 ---VFIFSGTFRKNLDPYEQWSDEEIWKVA----EEVGL---KSVIEQFPDKldfvlvdggyvLSNGHKQLMCLARSILS 1370
|
170 180
....*....|....*....|....*...
gi 2524658687 187 HPKLLIADEPTSALD-VT--VAKKILDH 211
Cdd:TIGR01271 1371 KAKILLLDEPSAHLDpVTlqIIRKTLKQ 1398
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
38-248 |
2.55e-07 |
|
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: 52.16 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGDGEvtggtITFDGRDITHLTDREFvsirGNGIGLVPQDpmtn 117
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGD-----IQIDGVSWNSVPLQKW----RKAFGVIPQK---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 118 lnpVWTVGSQIKEALRANNIATGSEAHKKAiellEQAGLpnaKKRIDQYPHE-----------FSGGMRQRALIAMGLAA 186
Cdd:cd03289 86 ---VFIFSGTFRKNLDPYGKWSDEEIWKVA----EEVGL---KSVIEQFPGQldfvlvdggcvLSHGHKQLMCLARSVLS 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2524658687 187 HPKLLIADEPTSALD---VTVAKKILDHldkltSELGTSVVLITHDLGLAAErADRLVVMQAGRV 248
Cdd:cd03289 156 KAKILLLDEPSAHLDpitYQVIRKTLKQ-----AFADCTVILSEHRIEAMLE-CQRFLVIEENKV 214
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
302-479 |
3.64e-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: 53.48 E-value: 3.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 302 KNLVRDFAIRGdRPwrkdsfrAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVQgrnrkEEL 381
Cdd:TIGR01257 932 KNLVKIFEPSG-RP-------AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIE-----TNL 998
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 382 ELRRRiqpifqnpYATLDPMRTV---HSSIEEPLRIHKIGTKKEREQRVFE---LLDRVALPAEMGRRfPGELSGGQRQR 455
Cdd:TIGR01257 999 DAVRQ--------SLGMCPQHNIlfhHLTVAEHILFYAQLKGRSWEEAQLEmeaMLEDTGLHHKRNEE-AQDLSGGMQRK 1069
|
170 180
....*....|....*....|....
gi 2524658687 456 VAIARALALNPEVVVCDEAVSALD 479
Cdd:TIGR01257 1070 LSVAIAFVGDAKVVVLDEPTSGVD 1093
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
326-486 |
4.58e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.06 E-value: 4.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 326 DISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTEgevlfdgkrvqgrnrKEELELRRRIQPIFQNPYatldpmrTVH 405
Cdd:PLN03232 635 DINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAE---------------TSSVVIRGSVAYVPQVSW-------IFN 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 406 SSIEEPLRIhkiGTKKEREqRVFELLDRVALPAEMGRrFPGE-----------LSGGQRQRVAIARALALNPEVVVCDEA 474
Cdd:PLN03232 693 ATVRENILF---GSDFESE-RYWRAIDVTALQHDLDL-LPGRdlteigergvnISGGQKQRVSMARAVYSNSDIYIFDDP 767
|
170
....*....|..
gi 2524658687 475 VSALDVVVQAQV 486
Cdd:PLN03232 768 LSALDAHVAHQV 779
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
38-228 |
5.14e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.32 E-value: 5.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETVAIVGESGSGKSTTahaaLGLLPGD------GEVT--------GGTITFDGRDI------THLTDR 97
Cdd:PRK10938 275 ILHNLSWQVNPGEHWQIVGPNGAGKSTL----LSLITGDhpqgysNDLTlfgrrrgsGETIWDIKKHIgyvsssLHLDYR 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 98 EFVSIRG-------NGIGLVpqdpmtnlnpvwtvgSQIKEALRanniatgseahKKAIELLEQAGLPNAKKriDQYPHEF 170
Cdd:PRK10938 351 VSTSVRNvilsgffDSIGIY---------------QAVSDRQQ-----------KLAQQWLDILGIDKRTA--DAPFHSL 402
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2524658687 171 SGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITH 228
Cdd:PRK10938 403 SWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSH 460
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
37-230 |
6.04e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 52.72 E-value: 6.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 37 DVVHDVNLEVFPGETVAIVGESGSGKSTTahaaLGLLPGDGEVTGGTITFDgrDITHLTDREFVSIRGNgIGLVPQDPMT 116
Cdd:PTZ00265 399 EIYKDLNFTLTEGKTYAFVGESGCGKSTI----LKLIERLYDPTEGDIIIN--DSHNLKDINLKWWRSK-IGVVSQDPLL 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 117 NLNpvwTVGSQIK---------EALRANNIATGSEAH--------------------------------KKAIELLEQAG 155
Cdd:PTZ00265 472 FSN---SIKNNIKyslyslkdlEALSNYYNEDGNDSQenknkrnscrakcagdlndmsnttdsneliemRKNYQTIKDSE 548
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 156 LPNAKKRI----------DQY-------PHEFSGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSE 218
Cdd:PTZ00265 549 VVDVSKKVlihdfvsalpDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGN 628
|
250
....*....|..
gi 2524658687 219 LGTSVVLITHDL 230
Cdd:PTZ00265 629 ENRITIIIAHRL 640
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
45-242 |
7.16e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.12 E-value: 7.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 45 EVFPGETVAIVGESGSGKSTTAHaalgLLPGDGEVTGGTITFDGRdithltdrefVSIRGNGIglVPQDPMTnlnpvwtv 124
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAK----LLAGVLKPDEGEVDPELK----------ISYKPQYI--KPDYDGT-------- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 125 gsqIKEALRANNIATGSEAHKkaIELLEQAGLPnakKRIDQYPHEFSGGMRQRALIAMGLAAHPKLLIADEPTSALDV-- 202
Cdd:PRK13409 417 ---VEDLLRSITDDLGSSYYK--SEIIKPLQLE---RLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVeq 488
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2524658687 203 --TVAKKIldhlDKLTSELGTSVVLITHDLGLAAERADRLVV 242
Cdd:PRK13409 489 rlAVAKAI----RRIAEEREATALVVDHDIYMIDYISDRLMV 526
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
247-285 |
1.04e-06 |
|
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model represents a domain found in the C-terminal regions of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 213647 [Multi-domain] Cd Length: 87 Bit Score: 46.97 E-value: 1.04e-06
10 20 30
....*....|....*....|....*....|....*....
gi 2524658687 247 RVVETGPALQVLTRPQHPYTKQLIAAAPSLAARRGDRVV 285
Cdd:TIGR01727 1 KIVETGPAEEIFKNPLHPYTKALLSAIPTIKKRDRKLIS 39
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
38-249 |
1.87e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 50.56 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGDGevTGGTITFDGRDITHLTDREFVsirGNGIGLVPQD---- 113
Cdd:NF040905 275 VVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSYGRN--ISGTVFKDGKEVDVSTVSDAI---DAGLAYVTEDrkgy 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 114 ------------PMTNLNPV--WTVGSQIKEALRAN------NIATGSeahkkaielleqaglpnakkrIDQYPHEFSGG 173
Cdd:NF040905 350 glnliddikrniTLANLGKVsrRGVIDENEEIKVAEeyrkkmNIKTPS---------------------VFQKVGNLSGG 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 174 MRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSElGTSVVLITHD----LGLaaerADRLVVMQAGRVV 249
Cdd:NF040905 409 NQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAE-GKGVIVISSElpelLGM----CDRIYVMNEGRIT 483
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
331-522 |
1.99e-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: 48.34 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 331 LRRGRTIGIVGESGSGKSTVANMALGLLDPTEGEVLFDGKRVqgrnrkeelelrrriqpifqnpyatldpmrtvhssIEE 410
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITP-----------------------------------VYK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 411 PLRIhkigtkkereqrvfelldrvalpaemgrrfpgELSGGQRQRVAIARALALNPEVVVCDEAVSALDVVVQAQVLELL 490
Cdd:cd03222 67 PQYI--------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAI 114
|
170 180 190
....*....|....*....|....*....|..
gi 2524658687 491 AELQEEMDLAYLFITHDLAVVRQVADEVIVME 522
Cdd:cd03222 115 RRLSEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
171-252 |
2.61e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 47.70 E-value: 2.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 171 SGGMRQRALIA--MGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSeLGTSVVLITHDLGLaAERADRLVVM----- 243
Cdd:cd03238 89 SGGELQRVKLAseLFSEPPGTLFILDEPSTGLHQQDINQLLEVIKGLID-LGNTVILIEHNLDV-LSSADWIIDFgpgsg 166
|
90
....*....|
gi 2524658687 244 -QAGRVVETG 252
Cdd:cd03238 167 kSGGKVVFSG 176
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
326-486 |
3.65e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 50.12 E-value: 3.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 326 DISFTLRRGRTIGIVGESGSGKSTVANMALGLLDPTE-GEVLFDGK--RVQGRNRKEELELRRRIqpIFQNPYatlDPMR 402
Cdd:PLN03130 635 NINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdASVVIRGTvaYVPQVSWIFNATVRDNI--LFGSPF---DPER 709
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 403 TvhssieeplrihkigtkkEREQRVFELL-DRVALPA----EMGRRfpG-ELSGGQRQRVAIARALALNPEVVVCDEAVS 476
Cdd:PLN03130 710 Y------------------ERAIDVTALQhDLDLLPGgdltEIGER--GvNISGGQKQRVSMARAVYSNSDVYIFDDPLS 769
|
170
....*....|
gi 2524658687 477 ALDVVVQAQV 486
Cdd:PLN03130 770 ALDAHVGRQV 779
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
42-240 |
3.71e-06 |
|
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: 47.87 E-value: 3.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 42 VNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGDGevtggtitfdGRdithltdrefvsIRGNGIGLVPQDPMTNLNPV 121
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLA----------GR------------VLLNGGPLDFQRDSIARGLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 122 WtVGSQ--IKEALRA-NNIATGSEAHKKA--IELLEQAGLPNAKKRIdqyPHEFSGGMRQRALIAMGLAAHPKLLIADEP 196
Cdd:cd03231 77 Y-LGHApgIKTTLSVlENLRFWHADHSDEqvEEALARVGLNGFEDRP---VAQLSAGQQRRVALARLLLSGRPLWILDEP 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2524658687 197 TSALDVTVAKKILDHLDKLTsELGTSVVLITH-DLGLAAERADRL 240
Cdd:cd03231 153 TTALDKAGVARFAEAMAGHC-ARGGMVVLTTHqDLGLSEAGAREL 196
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
325-527 |
3.81e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.56 E-value: 3.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 325 DDISFTLRRGRTIGIVGESGSGKSTvanmalgLLDPTEGEVLFDGKRVQgrnRKEELELRRRIQpifqnpyatlDPMR-- 402
Cdd:PRK11147 20 DNAELHIEDNERVCLVGRNGAGKST-------LMKILNGEVLLDDGRII---YEQDLIVARLQQ----------DPPRnv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 403 --TVHSSIEEPL--------RIHKIGTKKEREQ-------------------------RVFELLDRVALPAEMGRrfpGE 447
Cdd:PRK11147 80 egTVYDFVAEGIeeqaeylkRYHDISHLVETDPseknlnelaklqeqldhhnlwqlenRINEVLAQLGLDPDAAL---SS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 448 LSGGQRQRVAIARALALNPEVVVCDEAVSALDVvvqaQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMV 527
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDI----ETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
149-311 |
5.33e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 49.35 E-value: 5.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 149 ELLEQAGLPNAkkrIDQYPHEFSGGMRQRALIAMGLAAHPKLLIADEPTSALDvTVAKkilD----HLDKLTSELGTSVV 224
Cdd:NF033858 380 EMLERFDLADV---ADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD-PVAR---DmfwrLLIELSREDGVTIF 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 225 LITHDLGlAAERADRLVVMQAGRVVETGPalqvltrPQHpytkqLIAA--APSL----------AARRGDRVVAAPTTSD 292
Cdd:NF033858 453 ISTHFMN-EAERCDRISLMHAGRVLASDT-------PAA-----LVAArgAATLeeafiayleeAAGAAAAPAAAAAPAA 519
|
170
....*....|....*....
gi 2524658687 293 ADQKEILVAKNLVRDFAIR 311
Cdd:NF033858 520 AAAAPAAPAPAPRRRFSLR 538
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
41-258 |
5.94e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 47.89 E-value: 5.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 41 DVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGdgevTGGTITFDGRdithltdrefVSIRGNGIGLVPQ-DPMTNLN 119
Cdd:PRK13546 42 DISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSP----TVGKVDRNGE----------VSVIAISAGLSGQlTGIENIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 120 -PVWTVGSQIKEAlranniatgSEAHKKAIELLEQAGLpnakkrIDQYPHEFSGGMRQRALIAMGLAAHPKLLIADEPTS 198
Cdd:PRK13546 108 fKMLCMGFKRKEI---------KAMTPKIIEFSELGEF------IYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALS 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 199 ALDVTVAKKILDHLDKLtSELGTSVVLITHDLGLAAERADRLVVMQAGRVVETGPALQVL 258
Cdd:PRK13546 173 VGDQTFAQKCLDKIYEF-KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVL 231
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
318-535 |
6.38e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 47.90 E-value: 6.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 318 KDSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLdptEGEVLFDGKRVQGrnrkeelELRRRIQPIFQNPYAT 397
Cdd:PRK13547 11 RRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDL---TGGGAPRGARVTG-------DVTLNGEPLAAIDAPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 398 LDPMRTVHSSIEEPL---------------RIHKIGTKKEREQRVFELLDRVALPAEMGRRFPGELSGGQRQRVAIARAL 462
Cdd:PRK13547 81 LARLRAVLPQAAQPAfafsareivllgrypHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 463 A---------LNPEVVVCDEAVSALDVVVQAQVLELLAELQEEMDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTD 533
Cdd:PRK13547 161 AqlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPA 240
|
..
gi 2524658687 534 DL 535
Cdd:PRK13547 241 DV 242
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
322-559 |
6.78e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 48.58 E-value: 6.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 322 RAVDDISFTLRRGRTIGIVGESGSGKSTVAnMALGLLDPTEGEVLFDGKRVQGRNRKeeleLRRriqpifqnpyaTLDPM 401
Cdd:NF000106 27 KAVDGVDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAGRRPWRF*TWCANRRA----LRR-----------TIG*H 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 402 RTVHSSIEEPL----RIHKIG-----TKKEREQRVFELLDRVALPAEMGRRfPGELSGGQRQRVAIARALALNPEVVVCD 472
Cdd:NF000106 91 RPVR*GRRESFsgreNLYMIGr*ldlSRKDARARADELLERFSLTEAAGRA-AAKYSGGMRRRLDLAASMIGRPAVLYLD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 473 EAVSALDVVVQAQVLELLAELQEEmDLAYLFITHDLAVVRQVADEVIVMEHGKMVEHRPTDDLfdhpEKEYTQRLLDAIP 552
Cdd:NF000106 170 EPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL----KTKVGGRTLQIRP 244
|
....*..
gi 2524658687 553 GASLDLD 559
Cdd:NF000106 245 AHAAELD 251
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
13-260 |
8.77e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 48.43 E-value: 8.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 13 LTLKDVCIGFPTTTASgrrsksltdvVHDVNLEVFPGETVAIVGESGSGKSTTAHaalgLLPGDGEVTGGTITFDGRDIT 92
Cdd:PRK10522 323 LELRNVTFAYQDNGFS----------VGPINLTIKRGELLFLIGGNGSGKSTLAM----LLTGLYQPQSGEILLDGKPVT 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 93 HLTDREFVSIrgngIGLVPQDpmtnlnpVWTV-------GSQIKEALRANNIATGSEAHKKAielLEQAGLPNAKkridq 165
Cdd:PRK10522 389 AEQPEDYRKL----FSAVFTD-------FHLFdqllgpeGKPANPALVEKWLERLKMAHKLE---LEDGRISNLK----- 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 166 ypheFSGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDlGLAAERADRLVVMQA 245
Cdd:PRK10522 450 ----LSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRN 524
|
250
....*....|....*.
gi 2524658687 246 GRVVE-TGPALQVLTR 260
Cdd:PRK10522 525 GQLSElTGEERDAASR 540
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
322-481 |
9.23e-06 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 48.75 E-value: 9.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 322 RAV-DDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDpTEGEVLFDG---KRVQGRNRKEELELRRRIQPIFQNPY-A 396
Cdd:TIGR01271 1232 RAVlQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGvswNSVTLQTWRKAFGVIPQKVFIFSGTFrK 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 397 TLDPMrtvhssieeplrihkigtKKEREQRVFELLDRVALPAeMGRRFPGE-----------LSGGQRQRVAIARALALN 465
Cdd:TIGR01271 1311 NLDPY------------------EQWSDEEIWKVAEEVGLKS-VIEQFPDKldfvlvdggyvLSNGHKQLMCLARSILSK 1371
|
170
....*....|....*.
gi 2524658687 466 PEVVVCDEAVSALDVV 481
Cdd:TIGR01271 1372 AKILLLDEPSAHLDPV 1387
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
324-481 |
1.07e-05 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 47.54 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 324 VDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDpTEGEVLFDGKRVQgrnrKEELELRRR---IQP----IFQNPY- 395
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWN----SVPLQKWRKafgVIPqkvfIFSGTFr 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 396 ATLDPMrtvhssieeplrihkigtKKEREQRVFELLDRVALPAEMgRRFPGE-----------LSGGQRQRVAIARALAL 464
Cdd:cd03289 95 KNLDPY------------------GKWSDEEIWKVAEEVGLKSVI-EQFPGQldfvlvdggcvLSHGHKQLMCLARSVLS 155
|
170
....*....|....*..
gi 2524658687 465 NPEVVVCDEAVSALDVV 481
Cdd:cd03289 156 KAKILLLDEPSAHLDPI 172
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
48-253 |
1.13e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 48.69 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 48 PGETVAIVGESGSGKsTTAHAALGllpgdGEVTGGTITFDGRdITHLTDRE--FVSIRG----NGIGlvpqdpmtnlNPV 121
Cdd:PLN03140 905 PGVLTALMGVSGAGK-TTLMDVLA-----GRKTGGYIEGDIR-ISGFPKKQetFARISGyceqNDIH----------SPQ 967
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 122 WTVG-SQIKEA-LRANNIATGSEAHKKAIELLEQAGLPNAKKRIDQYP--HEFSGGMRQRALIAMGLAAHPKLLIADEPT 197
Cdd:PLN03140 968 VTVReSLIYSAfLRLPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPT 1047
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2524658687 198 SALDVTVAKKILDHLdKLTSELGTSVVLITHDLGLAA-ERADRLVVMQ-AGRVVETGP 253
Cdd:PLN03140 1048 SGLDARAAAIVMRTV-RNTVDTGRTVVCTIHQPSIDIfEAFDELLLMKrGGQVIYSGP 1104
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
318-479 |
1.18e-05 |
|
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: 46.08 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 318 KDSFRAVDDISFTLRRGRTIGIVGESGSGKSTvanmalgLLD---------PTEGEVLFDGKRVqgrnrkeELELRRRIQ 388
Cdd:cd03232 17 GGKRQLLNNISGYVKPGTLTALMGESGAGKTT-------LLDvlagrktagVITGEILINGRPL-------DKNFQRSTG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 389 PIFQNPyaTLDPMRTVhssiEEPLRihkigtkkereqrvFELLDRvalpaemgrrfpgELSGGQRQRVAIARALALNPEV 468
Cdd:cd03232 83 YVEQQD--VHSPNLTV----REALR--------------FSALLR-------------GLSVEQRKRLTIGVELAAKPSI 129
|
170
....*....|.
gi 2524658687 469 VVCDEAVSALD 479
Cdd:cd03232 130 LFLDEPTSGLD 140
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
45-242 |
1.35e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 47.86 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 45 EVFPGETVAIVGESGSGKSTTAHAALGLL-PGDGEVTGG-TITFDGRDITHLTDRefvsirgngiglvpqdpmtnlnpvw 122
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLkPDEGEVDEDlKISYKPQYISPDYDG------------------------- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 123 TVgsqiKEALR-ANNIATGSEAHKkaIELLEQAGLpnaKKRIDQYPHEFSGGMRQRALIAMGLAAHPKLLIADEPTSALD 201
Cdd:COG1245 417 TV----EEFLRsANTDDFGSSYYK--TEIIKPLGL---EKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2524658687 202 V----TVAKKIldhlDKLTSELGTSVVLITHDLGLAAERADRLVV 242
Cdd:COG1245 488 VeqrlAVAKAI----RRFAENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
37-259 |
1.78e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 47.80 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 37 DVVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGDGEVTGGTITFDGrdithLTDREFVS-IRGNGIGLVPQDpm 115
Cdd:TIGR00956 75 DILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFHIGVEGVITYDG-----ITPEEIKKhYRGDVVYNAETD-- 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 116 tNLNPVWTVGSQIKEA-------LRANNIATGSEAHKKAIELLEQAGLPNAK--KRIDQYPHEFSGGMRQRALIAMGLAA 186
Cdd:TIGR00956 148 -VHFPHLTVGETLDFAarcktpqNRPDGVSREEYAKHIADVYMATYGLSHTRntKVGNDFVRGVSGGERKRVSIAEASLG 226
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2524658687 187 HPKLLIADEPTSALDVTVAKKILDHLDKLTSELGTSvVLIThdLGLAAERA----DRLVVMQAGRVVETGPALQVLT 259
Cdd:TIGR00956 227 GAKIQCWDNATRGLDSATALEFIRALKTSANILDTT-PLVA--IYQCSQDAyelfDKVIVLYEGYQIYFGPADKAKQ 300
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
32-229 |
2.30e-05 |
|
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: 47.24 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 32 SKSLTD--VVHDVNLEVFPGETVAIVGESGSGKSTTAHaalgLLPGDGEVTGGTITFDgrdithltdrEFVSIrgngiGL 109
Cdd:TIGR03719 329 TKAFGDklLIDDLSFKLPPGGIVGVIGPNGAGKSTLFR----MITGQEQPDSGTIEIG----------ETVKL-----AY 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 110 VPQ--DPMTNLNPVWTVGSQIKEALRANNIATGSEAHkkaielleqAGLPNAK-----KRIDQypheFSGGMRQRALIAM 182
Cdd:TIGR03719 390 VDQsrDALDPNKTVWEEISGGLDIIKLGKREIPSRAY---------VGRFNFKgsdqqKKVGQ----LSGGERNRVHLAK 456
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2524658687 183 GLAAHPKLLIADEPTSALDVTVAKKILDHLDkltsELGTSVVLITHD 229
Cdd:TIGR03719 457 TLKSGGNVLLLDEPTNDLDVETLRALEEALL----NFAGCAVVISHD 499
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
13-92 |
2.77e-05 |
|
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: 46.71 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 13 LTLKDVCIGFPTTTASGRRSksltdvVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPGDgevtGGTITFDGRDIT 92
Cdd:COG4615 328 LELRGVTYRYPGEDGDEGFT------LGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPE----SGEILLDGQPVT 397
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
40-236 |
2.83e-05 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 45.18 E-value: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 40 HDVNLEVFPGETVAIVGESGSGKSTTahaaLGLLPGDGEVTGGTITFDGRDITHltdrefvsirgngiglvpQDPMTNLN 119
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSL----LRILAGLARPDAGEVLWQGEPIRR------------------QRDEYHQD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 120 PVWtVGSQ--IKEALRA--N---NIATGSEAHKKAI-ELLEQAGLpnaKKRIDQYPHEFSGGMRQRALIAMGLAAHPKLL 191
Cdd:PRK13538 76 LLY-LGHQpgIKTELTAleNlrfYQRLHGPGDDEALwEALAQVGL---AGFEDVPVRQLSAGQQRRVALARLWLTRAPLW 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2524658687 192 IADEPTSALDVTVAKKILDHLDKLTSELGTsVVLITH-DLGLAAER 236
Cdd:PRK13538 152 ILDEPFTAIDKQGVARLEALLAQHAEQGGM-VILTTHqDLPVASDK 196
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
313-479 |
9.77e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 45.48 E-value: 9.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 313 DRPWRKDSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMalgLLDPTEGEVLFDGKR-VQGRNRKEELElrRRIQPIF 391
Cdd:TIGR00956 768 EVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNV---LAERVTTGVITGGDRlVNGRPLDSSFQ--RSIGYVQ 842
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 392 QNpyatlD---PMRTVHSSIE--EPLRIHKIGTKKEREQRVFELLDRVALP--AEMGRRFPGE-LSGGQRQRVAIARALA 463
Cdd:TIGR00956 843 QQ-----DlhlPTSTVRESLRfsAYLRQPKSVSKSEKMEYVEEVIKLLEMEsyADAVVGVPGEgLNVEQRKRLTIGVELV 917
|
170
....*....|....*..
gi 2524658687 464 LNPEVVV-CDEAVSALD 479
Cdd:TIGR00956 918 AKPKLLLfLDEPTSGLD 934
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
39-251 |
1.03e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.11 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 39 VHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLpgdgEVTGGTITFDGRDITHLTDREFVSirgNGIGLVPQDPMTNl 118
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIR----EKSAGTITLHGKKINNHNANEAIN---HGFALVTEERRST- 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 119 npvwtvGSQIKEALRANNIATGSEAHKKAIELLEQAGLPNAKK------RIDQYPHE-----FSGGMRQRALIAMGLAAH 187
Cdd:PRK10982 336 ------GIYAYLDIGFNSLISNIRNYKNKVGLLDNSRMKSDTQwvidsmRVKTPGHRtqigsLSGGNQQKVIIGRWLLTQ 409
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2524658687 188 PKLLIADEPTSALDVTVAKKILDHLDKLTSElGTSVVLITHDLGLAAERADRLVVMQAGRV---VET 251
Cdd:PRK10982 410 PEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLVagiVDT 475
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
48-230 |
1.87e-04 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 43.51 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 48 PGETVAIVGESGSGKSTtahaALGLLPGdgEVTGGTITFDGRDITHLTDREFvsiRGNGIglvpQDPMTNLnpvwtVGSQ 127
Cdd:cd03236 25 EGQVLGLVGPNGIGKST----ALKILAG--KLKPNLGKFDDPPDWDEILDEF---RGSEL----QNYFTKL-----LEGD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 128 IKEALRANNIATGSEAHK-KAIELLEQAGLPNAKKRI----------DQYPHEFSGGMRQRALIAMGLAAHPKLLIADEP 196
Cdd:cd03236 87 VKVIVKPQYVDLIPKAVKgKVGELLKKKDERGKLDELvdqlelrhvlDRNIDQLSGGELQRVAIAAALARDADFYFFDEP 166
|
170 180 190
....*....|....*....|....*....|....*...
gi 2524658687 197 TSALDV----TVAKKIldhldKLTSELGTSVVLITHDL 230
Cdd:cd03236 167 SSYLDIkqrlNAARLI-----RELAEDDNYVLVVEHDL 199
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
38-228 |
2.28e-04 |
|
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: 43.97 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 38 VVHDVNLEVFPGETVAIVGESGSGKSTTAHAALGLLPgdgeVTGGTITFDGRdithltdrefvsirgNGIGLVPQDP-MT 116
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWP----VYGGRLTKPAK---------------GKLFYVPQRPyMT 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 117 NlnpvWTVGSQIKEALRANNIATGSEAHKKAIELLEQAGLPNAKKR------IDQYPHEFSGGMRQRalIAMG-LAAH-P 188
Cdd:TIGR00954 528 L----GTLRDQIIYPDSSEDMKRRGLSDKDLEQILDNVQLTHILEReggwsaVQDWMDVLSGGEKQR--IAMArLFYHkP 601
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2524658687 189 KLLIADEPTSALDVTVAKKILDHLdkltSELGTSVVLITH 228
Cdd:TIGR00954 602 QFAILDECTSAVSVDVEGYMYRLC----REFGITLFSVSH 637
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
318-486 |
3.57e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 43.68 E-value: 3.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 318 KDSFRAVDDISFTLRRGRTIGIVGESGSGKSTVANMALGLLDP--TEGEVlfdgkRVQGRNRKEElELRRRIQPIFQNPY 395
Cdd:PLN03140 890 EDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGgyIEGDI-----RISGFPKKQE-TFARISGYCEQNDI 963
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 396 ATldPMRTVHSSI--EEPLRIHKIGTKKEREQRVFELLDRVALP----AEMGrrFPG--ELSGGQRQRVAIARALALNPE 467
Cdd:PLN03140 964 HS--PQVTVRESLiySAFLRLPKEVSKEEKMMFVDEVMELVELDnlkdAIVG--LPGvtGLSTEQRKRLTIAVELVANPS 1039
|
170
....*....|....*....
gi 2524658687 468 VVVCDEAVSALDVVVQAQV 486
Cdd:PLN03140 1040 IIFMDEPTSGLDARAAAIV 1058
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
171-350 |
3.86e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.66 E-value: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 171 SGGMRQRALIAMGLAA---HPKLLIADEPTSALDVTVAKKILDHLDKLTsELGTSVVLITHDLGlaaeradrlVVMQAGR 247
Cdd:PRK00635 811 SGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLT-HQGHTVVIIEHNMH---------VVKVADY 880
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 248 VVETGPA-------LQVLTRPQ---HPYTKQLIAAAPSLAARRgdrvvAAPTTSDADQKEilvakNLVRDFAIrgdrpwr 317
Cdd:PRK00635 881 VLELGPEggnlggyLLASCSPEeliHLHTPTAKALRPYLSSPQ-----ELPYLPDPSPKP-----PVPADITI------- 943
|
170 180 190
....*....|....*....|....*....|....
gi 2524658687 318 KDSFR-AVDDISFTLRRGRTIGIVGESGSGKSTV 350
Cdd:PRK00635 944 KNAYQhNLKHIDLSLPRNALTAVTGPSASGKHSL 977
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
171-253 |
4.24e-04 |
|
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: 43.46 E-value: 4.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 171 SGGMRQRALIAMGL---AAHPKLLIADEPTSALDVTVAKKILDHLDKLTsELGTSVVLITHDLGlaaeradrlVVMQAGR 247
Cdd:TIGR00630 831 SGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLV-DKGNTVVVIEHNLD---------VIKTADY 900
|
....*.
gi 2524658687 248 VVETGP 253
Cdd:TIGR00630 901 IIDLGP 906
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
37-526 |
5.73e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.92 E-value: 5.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 37 DVVHDVNLEVFPGETVAIVGESGSGKST-----TAHAALGL------LPGDGEVTGGTITF-----------------DG 88
Cdd:PLN03073 191 DLIVDASVTLAFGRHYGLVGRNGTGKTTflrymAMHAIDGIpkncqiLHVEQEVVGDDTTAlqcvlntdiertqlleeEA 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 89 RDITHLTDREFVSIRGNGIGlvPQDPMTNLNPVWTVGSQIKEALRANNiATGSEAHKKAIelleQAGLPNAKKRIDQYPH 168
Cdd:PLN03073 271 QLVAQQRELEFETETGKGKG--ANKDGVDKDAVSQRLEEIYKRLELID-AYTAEARAASI----LAGLSFTPEMQVKATK 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 169 EFSGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSelgtSVVLITHDLGLAAERADRLVVMQAGRV 248
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPK----TFIVVSHAREFLNTVVTDILHLHGQKL 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 249 VETGPALQVLTRPQHPYTKQLIAAAPSLAARRG------DRVVAAPTTSDADQKEILVAKNLVRDFAIRGDrPWRKDSFR 322
Cdd:PLN03073 420 VTYKGDYDTFERTREEQLKNQQKAFESNERSRShmqafiDKFRYNAKRASLVQSRIKALDRLGHVDAVVND-PDYKFEFP 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 323 AVDD------ISF-----------TLRRGRTIGI--------VGESGSGKSTVANMALGLLDPTEGEVLFDGK---RVQG 374
Cdd:PLN03073 499 TPDDrpgppiISFsdasfgypggpLLFKNLNFGIdldsriamVGPNGIGKSTILKLISGELQPSSGTVFRSAKvrmAVFS 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 375 RNRKEELELRrriqpifQNPYatLDPMRTVHSSIEEPLRIHkIGTkkereqrvFELLDRVALPAEMgrrfpgELSGGQRQ 454
Cdd:PLN03073 579 QHHVDGLDLS-------SNPL--LYMMRCFPGVPEQKLRAH-LGS--------FGVTGNLALQPMY------TLSGGQKS 634
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2524658687 455 RVAIARALALNPEVVVCDEAVSALDV-VVQAQVLELLAELQeemdlAYLFITHDLAVVRQVADEVIVMEHGKM 526
Cdd:PLN03073 635 RVAFAKITFKKPHILLLDEPSNHLDLdAVEALIQGLVLFQG-----GVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
171-243 |
5.95e-04 |
|
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: 40.81 E-value: 5.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 171 SGGMRQRALIA--MGLAAHPK--LLIADEPTSALDVT----VAKKILDHLDKltselGTSVVLITHDLGLaAERADRLVV 242
Cdd:cd03227 79 SGGEKELSALAliLALASLKPrpLYILDEIDRGLDPRdgqaLAEAILEHLVK-----GAQVIVITHLPEL-AELADKLIH 152
|
.
gi 2524658687 243 M 243
Cdd:cd03227 153 I 153
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
328-489 |
9.59e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.92 E-value: 9.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 328 SFTLRRGRTIGIVGESGSGKSTVANmALglldptEGE-VLFDGKRVQGRNRKEEL---ELRRRIQPIFQNPYATL----- 398
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALAR-AL------AGElPLLSGERQSQFSHITRLsfeQLQKLVSDEWQRNNTDMlspge 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 399 -DPMRTVHSSIEEplrihkiGTKKEreQRVFELLDRVALPAEMGRRFPgELSGGQRQRVAIARALALNPEVVVCDEAVSA 477
Cdd:PRK10938 96 dDTGRTTAEIIQD-------EVKDP--ARCEQLAQQFGITALLDRRFK-YLSTGETRKTLLCQALMSEPDLLILDEPFDG 165
|
170
....*....|..
gi 2524658687 478 LDVVVQAQVLEL 489
Cdd:PRK10938 166 LDVASRQQLAEL 177
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
169-244 |
3.60e-03 |
|
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: 38.71 E-value: 3.60e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2524658687 169 EFSGGMRQRALIAMGLAAHPKLLIADEPTSALDVTVAKKILDHLDKLTSELGTSVVLITHDLGLAAERADRLVVMQ 244
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
322-524 |
3.61e-03 |
|
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: 38.46 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 322 RAVDDISFTLRRGRTIGIVGESGSGKSTVanmalglldptegevLFDGKRVQGRNRKEELelrrrIQPIFQNPYATLDPM 401
Cdd:cd03238 9 HNLQNLDVSIPLNVLVVVTGVSGSGKSTL---------------VNEGLYASGKARLISF-----LPKFSRNKLIFIDQL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 402 RTvhssieeplrIHKIGtkkereqrvfelLDRVALPAEMGrrfpgELSGGQRQRVAIARALALNPE--VVVCDEAVSALD 479
Cdd:cd03238 69 QF----------LIDVG------------LGYLTLGQKLS-----TLSGGELQRVKLASELFSEPPgtLFILDEPSTGLH 121
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2524658687 480 vvvQAQVLELLAELQEEMDLAY--LFITHDLAVVRQvADEVIVMEHG 524
Cdd:cd03238 122 ---QQDINQLLEVIKGLIDLGNtvILIEHNLDVLSS-ADWIIDFGPG 164
|
|
| HprK_C |
cd01918 |
HprK/P, the bifunctional histidine-containing protein kinase/phosphatase, controls the ... |
39-107 |
4.33e-03 |
|
HprK/P, the bifunctional histidine-containing protein kinase/phosphatase, controls the phosphorylation state of the phosphocarrier protein HPr and regulates the utilization of carbon sources by gram-positive bacteria. It catalyzes both the ATP-dependent phosphorylation of Ser-46 of HPr and its dephosphorylation by phosphorolysis. The latter reaction uses inorganic phosphate as substrate and produces pyrophosphate. Phosphoenolpyruvate carboxykinase (PEPCK) and the C-terminal catalytic domain of HprK/P are structurally similar with conserved active site residues suggesting these two phosphotransferases have related functions. The HprK/P N-terminal domain is structurally similar to the N-terminal domains of the MurE and MurF amino acid ligases.
Pssm-ID: 238899 Cd Length: 149 Bit Score: 37.98 E-value: 4.33e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2524658687 39 VHDVNLEVFpGETVAIVGESGSGKSTTAHAAL---GLLPGDG--EVTGGTITFDGR--DIThltdREFVSIRGNGI 107
Cdd:cd01918 5 VHGVLVEVG-GIGVLITGPSGIGKSELALELIkrgHRLVADDrvVVKREGGRLVGRapEAL----KGLIEIRGLGI 75
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
39-229 |
4.69e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 39.93 E-value: 4.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 39 VHDVNLEVFPGETVAIVGESGSGKSTTahaaLGLLPGDGEVTGGTItfdgRDITHLTDREFVSIRgngiglvpqdpmTNL 118
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTL----LKLMLGQLQADSGRI----HCGTKLEVAYFDQHR------------AEL 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 119 NPVWTVgsqikealrANNIATGseahKKAIELleqaglpNAKKR-IDQYPHEF--------------SGGMRQRALIAMG 183
Cdd:PRK11147 395 DPEKTV---------MDNLAEG----KQEVMV-------NGRPRhVLGYLQDFlfhpkramtpvkalSGGERNRLLLARL 454
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2524658687 184 LAAHPKLLIADEPTSALDVtvakKILDHLDKLTSELGTSVVLITHD 229
Cdd:PRK11147 455 FLKPSNLLILDEPTNDLDV----ETLELLEELLDSYQGTVLLVSHD 496
|
|
| formate_dh_like |
cd05198 |
Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase ... |
257-357 |
5.41e-03 |
|
Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase family; Formate dehydrogenase, D-specific 2-hydroxy acid dehydrogenase, Phosphoglycerate Dehydrogenase, Lactate dehydrogenase, Thermostable Phosphite Dehydrogenase, and Hydroxy(phenyl)pyruvate reductase, among others, share a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. 2-hydroxyacid dehydrogenases are enzymes that catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. Formate dehydrogenase (FDH) catalyzes the NAD+-dependent oxidation of formate ion to carbon dioxide with the concomitant reduction of NAD+ to NADH. FDHs of this family contain no metal ions or prosthetic groups. Catalysis occurs though direct transfer of hydride ion to NAD+ without the stages of acid-base catalysis typically found in related dehydrogenases. FDHs are found in all methylotrophic microorganisms in energy production and in the stress responses of plants. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine Hydrolase, among others. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.
Pssm-ID: 240622 [Multi-domain] Cd Length: 302 Bit Score: 39.15 E-value: 5.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658687 257 VLTRPQHPYTKQLIAAAPSL-----------------AARRGDRVVAAPTTSDADQKE------ILVAKNLVR-DFAIRG 312
Cdd:cd05198 45 LIVSSTTPVTAEVLAKAPKLkfiqvagagvdnidldaAKKRGITVTNVPGANAEAVAEhalgllLALLRRLPRaDAAVRR 124
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2524658687 313 DRPWRKDSFravddISFTLRrGRTIGIVGESGSGKStVANMALGL 357
Cdd:cd05198 125 GWGWLWAGF-----PGYELE-GKTVGIVGLGRIGQR-VAKRLQAF 162
|
|
| |
