|
Name |
Accession |
Description |
Interval |
E-value |
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
363-606 |
4.10e-105 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 317.75 E-value: 4.10e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 363 GQDILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADgqfHAPKNPADFA 442
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRD---ITGLPPHRIA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 443 ALGLGRTFQIVQPFAAMTVEENIMVGAFYRHHH---------------EKDAREAARETAWRMGLGPLLGAEARGLTIGG 507
Cdd:COG0411 78 RLGIARTFQNPRLFPELTVLENVLVAAHARLGRgllaallrlprarreEREARERAEELLERVGLADRADEPAGNLSYGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 508 LKRLEVARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRD-SGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRP 586
Cdd:COG0411 158 QRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDeRGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTP 237
|
250 260
....*....|....*....|
gi 489057211 587 QDVVRDPQVVEAYLGKEFAH 606
Cdd:COG0411 238 AEVRADPRVIEAYLGEEAAA 257
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
367-595 |
2.39e-100 |
|
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: 304.75 E-value: 2.39e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 367 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGqfhAPKNPADFAALGL 446
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDI---TGLPPHEIARLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 447 GRTFQIVQPFAAMTVEENIMVGAFYRHHH----------EKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARV 516
Cdd:cd03219 78 GRTFQIPRLFPELTVLENVMVAAQARTGSglllararreEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489057211 517 MAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDPQV 595
Cdd:cd03219 158 LATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPRV 236
|
|
| LivM |
COG4177 |
ABC-type branched-chain amino acid transport system, permease component [Amino acid transport ... |
40-329 |
3.75e-79 |
|
ABC-type branched-chain amino acid transport system, permease component [Amino acid transport and metabolism];
Pssm-ID: 443336 [Multi-domain] Cd Length: 285 Bit Score: 251.54 E-value: 3.75e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 40 NAFVSHIFITICLFAALSTAWNIVGGFAGQMSLGHAVFYGIGGYTGVILF-NMGISPWFSMFIGTFIAALVGMVISYPCF 118
Cdd:COG4177 1 SPYYLSLLTLILIYAILALGLNLLLGYTGLLSLGHAAFFGIGAYAAALLTtHLGLPFWLALLLAGLVAALLGLLIGLPAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 119 RLKGPFYSLASIAFLEVFRVLALHFGWLTGGATGLMIQLKLGWVWMVFRERWPSLLIVFGMLLVTLAITWAARRSRLGFY 198
Cdd:COG4177 81 RLRGDYLAIATLAFAEIVRLLALNLESLTGGADGLSGIPRPTLFGLDLGSPLAFYYLVLALLVLVLLLLRRLVRSRFGRA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 199 LVATRERESAARAAGVRTVRVRLIAVAISSALCAMLGTFHAMYLTFIEPaAMFSLAFSIQIAMFALNGGLGTVAGPLLGA 278
Cdd:COG4177 161 LRAIRENEIAAEALGINVTRYKLLAFVLSAALAGLAGALYAHYVGFVSP-ESFSFLLSIEILLMVVLGGLGSLLGPVLGA 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 489057211 279 VLLVPITEWARaslgaSALGLHGFVYGLVLILVVLFMPNGIMGAINRFVRK 329
Cdd:COG4177 240 VLLVLLPELLR-----SLPEYRLLIFGLLLILVVLFRPRGLAGLLRRLRRR 285
|
|
| TM_PBP1_LivM_like |
cd06581 |
Transmembrane subunit (TM) of Escherichia coli LivM and related proteins. LivM is one of two ... |
50-321 |
1.91e-78 |
|
Transmembrane subunit (TM) of Escherichia coli LivM and related proteins. LivM is one of two TMs of the E. coli LIV-1/LS transporter, a Periplasmic Binding Protein (PBP)-dependent ATP-Binding Cassette (ABC) transporter involved in the uptake of branched-chain amino acids (AAs). These types of transporters generally bind type 1 PBPs. PBP-dependent ABC transporters consist of a PBP, two TMs, and two cytoplasmic ABCs, and are mainly involved in importing solutes from the environment. The solute is captured by the PBP, which delivers it to a gated translocation pathway formed by the two TMs. The two ABCs bind and hydrolyze ATP and drive the transport reaction. E. coli LivM forms a heterodimer with another TM, LivH, to generate the transmembrane pore. LivH is not included in this subgroup. The LIV-1/LS transporter is comprised of two TMs (LivM and LivH), two ABCs (LivG and LivF), and one of two alternative PBPs, LivJ (LIV-BP) or LivK (LS-BP). In addition to transporting branched-chain AAs including leucine, isoleucine and valine, the E. coli LIV-1/LS transporter is involved in the uptake of the aromatic AA, phenylalanine.
Pssm-ID: 119323 [Multi-domain] Cd Length: 268 Bit Score: 249.28 E-value: 1.91e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 50 ICLFAALSTAWNIVGGFAGQMSLGHAVFYGIGGYTGVILFNM-GISPWFSMFIGTFIAALVGMVISYPCFRLKGPFYSLA 128
Cdd:cd06581 1 ILIYAILALGLNLLLGYAGQLSLGHAAFFGIGAYTAALLATRlGLPFWLALLAAGLVAALVGLLLGLPALRLRGVYFAIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 129 SIAFLEVFRVLALHFGWLTGGATGLMIQLKLGWVWMVFRERWPSLLIVFGMLLVTLAITWAARRSRLGFYLVATRERESA 208
Cdd:cd06581 81 TLAFAEIVRLLALNWSSLTGGSNGLSGIPPPLLGGLLLSSPLAFYYLVLAVLLLVLLLLRRLVRSPFGRALRAIRENEVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 209 ARAAGVRTVRVRLIAVAISSALCAMLGTFHAMYLTFIEPaAMFSLAFSIQIAMFALNGGLGTVAGPLLGAVLLVPITEWA 288
Cdd:cd06581 161 AEALGINVTRYKLLAFALSAALAGLAGALYAHYLGFVSP-ESFGFALSIELLLMVVLGGLGSLLGPVLGAALLVLLPELL 239
|
250 260 270
....*....|....*....|....*....|...
gi 489057211 289 RASLGasalGLHGFVYGLVLILVVLFMPNGIMG 321
Cdd:cd06581 240 RSLGP----GLRLLVFGLLLILVVLFLPRGLVG 268
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
364-603 |
9.92e-61 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 202.53 E-value: 9.92e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 364 QDILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQFHAPKNPADFAA 443
Cdd:PRK11300 3 QPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILL---RGQHIEGLPGHQIAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 444 LGLGRTFQIVQPFAAMTVEENIMVgAFYRH----------------HHEKDAREAARETAWRMGLGPLLGAEARGLTIGG 507
Cdd:PRK11300 80 MGVVRTFQHVRLFREMTVIENLLV-AQHQQlktglfsgllktpafrRAESEALDRAATWLERVGLLEHANRQAGNLAYGQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 508 LKRLEVARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRDS-GVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRP 586
Cdd:PRK11300 159 QRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTP 238
|
250
....*....|....*..
gi 489057211 587 QDVVRDPQVVEAYLGKE 603
Cdd:PRK11300 239 EEIRNNPDVIKAYLGEA 255
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
366-604 |
4.21e-49 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 170.92 E-value: 4.21e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 366 ILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQFHAPKNPADFAALG 445
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILI---DGQDITHLPMHERARLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 446 LGRTFQIVQPFAAMTVEENIMVGAFYRHHHEKDAREAARETAW-RMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRIL 524
Cdd:TIGR04406 78 IGYLPQEASIFRKLTVEENIMAVLEIRKDLDRAEREERLEALLeEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 525 LLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDPQVVEAYLGKEF 604
Cdd:TIGR04406 158 LLDEPFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEKVRRVYLGEQF 237
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
367-591 |
5.55e-49 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 170.24 E-value: 5.55e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 367 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADgqfhAPKNPADFAALgL 446
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGED----VARDPAEVRRR-I 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 447 GRTFQIVQPFAAMTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTiGGLK-RLEVARVMAMEPRILL 525
Cdd:COG1131 76 GYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLS-GGMKqRLGLALALLHDPELLI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489057211 526 LDEVMAGInqtDV--RRAI-DLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVR 591
Cdd:COG1131 155 LDEPTSGL---DPeaRRELwELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKA 220
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
366-606 |
5.03e-48 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 175.21 E-value: 5.03e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 366 ILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQFHAPKNPADFAALG 445
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILL---DGEPVRFRSPRDAQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 446 LGRTFQIVQPFAAMTVEENIMVGAFYRHH---HEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPR 522
Cdd:COG1129 81 IAIIHQELNLVPNLSVAENIFLGREPRRGgliDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 523 ILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDpQVVEAYLGK 602
Cdd:COG1129 161 VLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTED-ELVRLMVGR 239
|
....
gi 489057211 603 EFAH 606
Cdd:COG1129 240 ELED 243
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
366-601 |
2.05e-47 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 166.45 E-value: 2.05e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 366 ILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGAD--GqfhapKNPADFAA 443
Cdd:COG4674 10 ILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDltG-----LDEHEIAR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 444 LGLGRTFQIVQPFAAMTVEENIMVGA----------FYRHHHEKDAREAarETAWRMGLGPLLGAEARGLTIGGLKRLEV 513
Cdd:COG4674 85 LGIGRKFQKPTVFEELTVFENLELALkgdrgvfaslFARLTAEERDRIE--EVLETIGLTDKADRLAGLLSHGQKQWLEI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 514 ARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRdSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDP 593
Cdd:COG4674 163 GMLLAQDPKLLLLDEPVAGMTDAETERTAELLKSLA-GKHSVVVVEHDMEFVRQIARKVTVLHQGSVLAEGSLDEVQADP 241
|
....*...
gi 489057211 594 QVVEAYLG 601
Cdd:COG4674 242 RVIEVYLG 249
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
366-604 |
3.31e-47 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 165.59 E-value: 3.31e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 366 ILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQfhapknpaDF---- 441
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFL---DGE--------DIthlp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 442 ----AALGLGRTFQivQP--FAAMTVEENIMvgAFyRHHHEKDAREAARETAWRM---GLGPLlgAEARGLTI-GGLKR- 510
Cdd:COG1137 72 mhkrARLGIGYLPQ--EAsiFRKLTVEDNIL--AV-LELRKLSKKEREERLEELLeefGITHL--RKSKAYSLsGGERRr 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 511 LEVARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVV 590
Cdd:COG1137 145 VEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEIL 224
|
250
....*....|....
gi 489057211 591 RDPQVVEAYLGKEF 604
Cdd:COG1137 225 NNPLVRKVYLGEDF 238
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
367-601 |
2.83e-46 |
|
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: 163.10 E-value: 2.83e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 367 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQFHAPKNPADFAALGL 446
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILL---DGQDITKLPMHKRARLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 447 GRTFQIVQPFAAMTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLL 526
Cdd:cd03218 78 GYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489057211 527 DEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDPQVVEAYLG 601
Cdd:cd03218 158 DEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVRKVYLG 232
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
366-601 |
4.70e-46 |
|
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: 162.46 E-value: 4.70e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 366 ILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADgqfHAPKNPADFAALG 445
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGED---ITGLPPHRIARLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 446 L-----GRtfQIvqpFAAMTVEENIMVGAFyrhhhekdAREAARETAWRMG--------LGPLLGAEARGLTiGGLKR-L 511
Cdd:COG0410 80 IgyvpeGR--RI---FPSLTVEENLLLGAY--------ARRDRAEVRADLErvyelfprLKERRRQRAGTLS-GGEQQmL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 512 EVARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVR 591
Cdd:COG0410 146 AIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLA 225
|
250
....*....|
gi 489057211 592 DPQVVEAYLG 601
Cdd:COG0410 226 DPEVREAYLG 235
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
367-589 |
1.72e-45 |
|
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: 161.18 E-value: 1.72e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 367 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKNPADFAALGL 446
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 447 GRTFqivqpFAAMTVEENI-MVGAFYRHHHEkDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILL 525
Cdd:COG4555 82 ERGL-----YDRLTVRENIrYFAELYGLFDE-ELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489057211 526 LDEVMAGInqtDV--RRAI-DLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDV 589
Cdd:COG4555 156 LDEPTNGL---DVmaRRLLrEILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
367-592 |
2.21e-45 |
|
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: 160.29 E-value: 2.21e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 367 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADgqfHAPKNPADFAALGL 446
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRD---ITGLPPHERARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 447 GRTFQIVQPFAAMTVEENIMVGAFYRHhheKDAREAARETAWRM--GLGPLLGAEARGLTIGGLKRLEVARVMAMEPRIL 524
Cdd:cd03224 78 GYVPEGRRIFPELTVEENLLLGAYARR---RAKRKARLERVYELfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489057211 525 LLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRD 592
Cdd:cd03224 155 LLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
367-598 |
1.92e-42 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 152.49 E-value: 1.92e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 367 LRVQNLN-KHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADgqfHAPKNPADFAAL- 444
Cdd:COG1122 1 IELENLSfSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKD---ITKKNLRELRRKv 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 445 GLgrTFQivQP---FAAMTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEP 521
Cdd:COG1122 78 GL--VFQ--NPddqLFAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEP 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489057211 522 RILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDPQVVEA 598
Cdd:COG1122 154 EVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYELLEE 230
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
367-580 |
1.65e-40 |
|
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: 145.23 E-value: 1.65e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 367 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKNPADFAALgl 446
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 447 grtFQIVQPFAAMTVEENIMvgafyrhhhekdareaaretawrmglgpllgaeargLTIGGLKRLEVARVMAMEPRILLL 526
Cdd:cd03230 79 ---PEEPSLYENLTVRENLK------------------------------------LSGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489057211 527 DEVMAGInqtDV--RRAI-DLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEV 580
Cdd:cd03230 120 DEPTSGL---DPesRREFwELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
339-594 |
4.46e-40 |
|
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: 153.52 E-value: 4.46e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 339 ARTEPIAAVPA-RAIKAPSPDRAGIGQDILRVQNLNKHF-----GGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMI 412
Cdd:COG1123 232 AAPQALAAVPRlGAARGRAAPAAAAAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 413 SGFLAPDEGTVNLCGADGQFHAPKNPADFAalglgRTFQIV-Q-PFAA----MTVEENIMVGAfyRHHHEKDAREAARET 486
Cdd:COG1123 312 LGLLRPTSGSILFDGKDLTKLSRRSLRELR-----RRVQMVfQdPYSSlnprMTVGDIIAEPL--RLHGLLSRAERRERV 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 487 AW---RMGLGP-LLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGInqtDVR-RA--IDLMLSIRDS-GVSIIAI 558
Cdd:COG1123 385 AElleRVGLPPdLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSAL---DVSvQAqiLNLLRDLQRElGLTYLFI 461
|
250 260 270
....*....|....*....|....*....|....*.
gi 489057211 559 EHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDPQ 594
Cdd:COG1123 462 SHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQ 497
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
366-589 |
6.59e-39 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 149.79 E-value: 6.59e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 366 ILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQFHAPKNPADFAALG 445
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILI---DGKPVRIRSPRDAIALG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 446 LGRTFQIVQPFAAMTVEENIMVGA---FYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPR 522
Cdd:COG3845 82 IGMVHQHFMLVPNLTVAENIVLGLeptKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGAR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489057211 523 ILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDV 589
Cdd:COG3845 162 ILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAET 228
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
383-579 |
1.40e-38 |
|
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: 141.07 E-value: 1.40e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 383 RNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKNPADFAALglgrTFQivQP---FAAM 459
Cdd:cd03225 18 DDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL----VFQ--NPddqFFGP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 460 TVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGINQTDVR 539
Cdd:cd03225 92 TVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRR 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489057211 540 RAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGE 579
Cdd:cd03225 172 ELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
366-600 |
1.44e-38 |
|
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: 142.04 E-value: 1.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 366 ILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQfhapknpaDFAALG 445
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILV---DGQ--------DITGLS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 446 LGRTFQIVQP----------FAAMTVEENImvgAF--YRHHH--EKDAREAARETAWRMGLGpllGAEAR------Glti 505
Cdd:COG1127 74 EKELYELRRRigmlfqggalFDSLTVFENV---AFplREHTDlsEAEIRELVLEKLELVGLP---GAADKmpselsG--- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 506 GGLKRLEVARVMAMEPRILLLDE-------VMAginqtdvrRAID-LMLSIRDS-GVSIIAIEHVMQAVMSLSDRVIVLA 576
Cdd:COG1127 145 GMRKRVALARALALDPEILLYDEptagldpITS--------AVIDeLIRELRDElGLTSVVVTHDLDSAFAIADRVAVLA 216
|
250 260
....*....|....*....|....*
gi 489057211 577 SGEVIAQGRPQDVVR-DPQVVEAYL 600
Cdd:COG1127 217 DGKIIAEGTPEELLAsDDPWVRQFL 241
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
367-595 |
3.67e-38 |
|
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: 140.71 E-value: 3.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 367 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQFHAPKNPADFAALGL 446
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLI---DGEDISGLSEAELYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 447 --GRTFQIVQPFAAMTVEENImvgAFYRHHH----EKDAREAARETAWRMGLGP---LLGAEARGltiGGLKRLEVARVM 517
Cdd:cd03261 78 rmGMLFQSGALFDSLTVFENV---AFPLREHtrlsEEEIREIVLEKLEAVGLRGaedLYPAELSG---GMKKRVALARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 518 AMEPRILLLDEVMAG---INQTDVrraIDLMLSIRDS-GVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVR-- 591
Cdd:cd03261 152 ALDPELLLYDEPTAGldpIASGVI---DDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRAsd 228
|
....
gi 489057211 592 DPQV 595
Cdd:cd03261 229 DPLV 232
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
367-583 |
7.11e-38 |
|
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: 137.56 E-value: 7.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 367 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQFHAPKNPADFAALGL 446
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILV---DGKEVSFASPRDARRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 447 GRTFQivqpfaamtveenimvgafyrhhhekdareaaretawrmglgpllgaeargLTIGGLKRLEVARVMAMEPRILLL 526
Cdd:cd03216 78 AMVYQ---------------------------------------------------LSVGERQMVEIARALARNARLLIL 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489057211 527 DEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQ 583
Cdd:cd03216 107 DEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
366-609 |
2.39e-37 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 139.07 E-value: 2.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 366 ILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKnpadfaaLG 445
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR-------IG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 446 -------LGRTFQIvqpfaamTVEENIMVGaFYRHH-----HEKDAREAARETAWRMGLGPLlgaeaRGLTIGGL----- 508
Cdd:COG1121 79 yvpqraeVDWDFPI-------TVRDVVLMG-RYGRRglfrrPSRADREAVDEALERVGLEDL-----ADRPIGELsggqq 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 509 KRLEVARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLAsGEVIAQGRPQD 588
Cdd:COG1121 146 QRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLN-RGLVAHGPPEE 224
|
250 260
....*....|....*....|.
gi 489057211 589 VVRDPQVVEAYLGKEFAHAHA 609
Cdd:COG1121 225 VLTPENLSRAYGGPVALLAHG 245
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
367-584 |
5.97e-37 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 136.88 E-value: 5.97e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 367 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPknpadfAALGL 446
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPP------ERRNI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 447 GRTFQIVQPFAAMTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLL 526
Cdd:cd03259 75 GMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 527 DEVMAGINQtDVRRAIDLMLS--IRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQG 584
Cdd:cd03259 155 DEPLSALDA-KLREELREELKelQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
366-598 |
2.81e-36 |
|
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: 136.33 E-value: 2.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 366 ILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADgqfHAPKNPADFAALg 445
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRD---LASLSRRELARR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 446 LGRTFQIVQPFAAMTVEENIMVGafyRHHH--------EKDaREAARETAWRMGLGPLlgAEARGLTI-GG-LKRLEVAR 515
Cdd:COG1120 77 IAYVPQEPPAPFGLTVRELVALG---RYPHlglfgrpsAED-REAVEEALERTGLEHL--ADRPVDELsGGeRQRVLIAR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 516 VMAMEPRILLLDEVMAGInqtDVRRAIDLMLSIRD----SGVSIIAIEH-VMQAVMsLSDRVIVLASGEVIAQGRPQDVV 590
Cdd:COG1120 151 ALAQEPPLLLLDEPTSHL---DLAHQLEVLELLRRlareRGRTVVMVLHdLNLAAR-YADRLVLLKDGRIVAQGPPEEVL 226
|
....*...
gi 489057211 591 rDPQVVEA 598
Cdd:COG1120 227 -TPELLEE 233
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
367-603 |
1.97e-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: 133.23 E-value: 1.97e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 367 LRVQNLNKHFGGLHVtRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKNpadfaalgl 446
Cdd:cd03299 1 LKVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 447 gRTFQIVQP----FAAMTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPR 522
Cdd:cd03299 71 -RDISYVPQnyalFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 523 ILLLDEVMAGINQTDVRRAIDLMLSIRDS-GVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDPQ--VVEAY 599
Cdd:cd03299 150 ILLLDEPFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKneFVAEF 229
|
....
gi 489057211 600 LGKE 603
Cdd:cd03299 230 LGFN 233
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
367-587 |
4.26e-35 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 131.86 E-value: 4.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 367 LRVQNLNKHFGGL--HVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKnpadfAAL 444
Cdd:cd03263 1 LQIRNLTKTYKKGtkPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKA-----ARQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 445 GLGRTFQIVQPFAAMTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRIL 524
Cdd:cd03263 76 SLGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489057211 525 LLDEVMAGInqtDV--RRAI-DLMLSIRdSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQ 587
Cdd:cd03263 156 LLDEPTSGL---DPasRRAIwDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQ 217
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
366-604 |
5.03e-35 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 132.32 E-value: 5.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 366 ILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQ---FHAPknpadfA 442
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllpLHAR------A 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 443 ALGLGRTFQIVQPFAAMTVEENIMVGAFYRHHHEKDAREA-ARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEP 521
Cdd:PRK10895 77 RRGIGYLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDrANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 522 RILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDPQVVEAYLG 601
Cdd:PRK10895 157 KFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVYLG 236
|
...
gi 489057211 602 KEF 604
Cdd:PRK10895 237 EDF 239
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
366-589 |
6.00e-35 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 133.70 E-value: 6.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 366 ILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQFHAPKNPADFAAL- 444
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLW---DGEPLDPEDRRRIGYLp 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 445 ---GLgrtfqivqpFAAMTVEENIMvgafY----RHHHEKDAREAAREtaW--RMGLGPLLGAEARGLTIGGLKRLEVAR 515
Cdd:COG4152 78 eerGL---------YPKMKVGEQLV----YlarlKGLSKAEAKRRADE--WleRLGLGDRANKKVEELSKGNQQKVQLIA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489057211 516 VMAMEPRILLLDEVMAG---INQTDVRraiDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDV 589
Cdd:COG4152 143 ALLHDPELLILDEPFSGldpVNVELLK---DVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
366-584 |
4.73e-34 |
|
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: 129.02 E-value: 4.73e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 366 ILRVQNLNKHF----GGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADgqfhAPKNPADf 441
Cdd:cd03266 1 MITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFD----VVKEPAE- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 442 AALGLGRTFQIVQPFAAMTVEENimVGAFYRHHHEKDAREAAR--ETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAM 519
Cdd:cd03266 76 ARRRLGFVSDSTGLYDRLTAREN--LEYFAGLYGLKGDELTARleELADRLGMEELLDRRVGGFSTGMRQKVAIARALVH 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489057211 520 EPRILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQG 584
Cdd:cd03266 154 DPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
366-594 |
9.14e-34 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 132.14 E-value: 9.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 366 ILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQfhapknpaDFAAL- 444
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILL---DGR--------DVTGLp 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 445 ----GLGrtfqIV-QPFAA---MTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTiGGLK-RLEVAR 515
Cdd:COG3842 74 pekrNVG----MVfQDYALfphLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLS-GGQQqRVALAR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 516 VMAMEPRILLLDEVMAGInqtDVRRAIDLMLSIRD----SGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVR 591
Cdd:COG3842 149 ALAPEPRVLLLDEPLSAL---DAKLREEMREELRRlqreLGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYE 225
|
...
gi 489057211 592 DPQ 594
Cdd:COG3842 226 RPA 228
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
367-589 |
1.64e-33 |
|
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: 127.68 E-value: 1.64e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 367 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFL-----APDEGTVNLCGADgqfhAPKNPADF 441
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKD----IYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 442 AAL--GLGRTFQIVQPFaAMTVEENIMVGAfyRHHHEKDAREAARETAW---RMGLGPLLG--AEARGLTIGGLKRLEVA 514
Cdd:cd03260 77 LELrrRVGMVFQKPNPF-PGSIYDNVAYGL--RLHGIKLKEELDERVEEalrKAALWDEVKdrLHALGLSGGQQQRLCLA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489057211 515 RVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRDSgVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDV 589
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
366-584 |
2.03e-33 |
|
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: 127.62 E-value: 2.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 366 ILRVQNLNKHF--GGLHVT--RNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGqfhaPKNPADF 441
Cdd:cd03257 1 LLEVKNLSVSFptGGGSVKalDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDL----LKLSRRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 442 AALgLGRTFQIV-Q-PFAA----MTVEENIMVGafYRHHHEKDAREAARETAW--RMGLGP---LLGAEARGLTIGGLKR 510
Cdd:cd03257 77 RKI-RRKEIQMVfQdPMSSlnprMTIGEQIAEP--LRIHGKLSKKEARKEAVLllLVGVGLpeeVLNRYPHELSGGQRQR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489057211 511 LEVARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRDS-GVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQG 584
Cdd:cd03257 154 VAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
367-580 |
2.23e-33 |
|
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: 127.22 E-value: 2.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 367 LRVQNLNKHFGG----LHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKNPADFA 442
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 443 ALGLGRTFQ----IvqPFaaMTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMA 518
Cdd:cd03255 81 RRHIGFVFQsfnlL--PD--LTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489057211 519 MEPRILLLDEVMAGINQTDVRRAIDLMLSI-RDSGVSIIAIEHVMQAVmSLSDRVIVLASGEV 580
Cdd:cd03255 157 NDPKIILADEPTGNLDSETGKEVMELLRELnKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
365-591 |
2.59e-33 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 127.51 E-value: 2.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 365 DILRVQNLNKHF----------------------GGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGT 422
Cdd:COG1134 3 SMIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 423 VNLcgaDGQFHAPknpadfaaLGLGRTFQivqpfAAMTVEENI-MVGAFYRhHHEKDAREAARETAWRMGLGPLLGAEAR 501
Cdd:COG1134 83 VEV---NGRVSAL--------LELGAGFH-----PELTGRENIyLNGRLLG-LSRKEIDEKFDEIVEFAELGDFIDQPVK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 502 GLTIGGLKRLEVARVMAMEPRILLLDEVMAGinqTDV---RRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASG 578
Cdd:COG1134 146 TYSSGMRARLAFAVATAVDPDILLVDEVLAV---GDAafqKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKG 222
|
250
....*....|...
gi 489057211 579 EVIAQGRPQDVVR 591
Cdd:COG1134 223 RLVMDGDPEEVIA 235
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
367-583 |
1.14e-32 |
|
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: 125.28 E-value: 1.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 367 LRVQNLNKHFGG----LHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKnpadfa 442
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 443 algLGRTFQivQP--FAAMTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTiGGLK-RLEVARVMAM 519
Cdd:cd03293 75 ---RGYVFQ--QDalLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLS-GGMRqRVALARALAV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 520 EPRILLLDEVMAGIN-QTdvRRAI-DLMLSI-RDSGVSIIAIEH-VMQAVMsLSDRVIVLAS--GEVIAQ 583
Cdd:cd03293 149 DPDVLLLDEPFSALDaLT--REQLqEELLDIwRETGKTVLLVTHdIDEAVF-LADRVVVLSArpGRIVAE 215
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
367-599 |
1.14e-32 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 126.38 E-value: 1.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 367 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGadgqfhapKNPADFAALGL 446
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNG--------RPLAAWSPWEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 447 GR-----------TFqivqPFaamTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTiGGLK-RLEVA 514
Cdd:COG4559 74 ARrravlpqhsslAF----PF---TVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLS-GGEQqRVQLA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 515 RVMA-------MEPRILLLDEVMAGInqtDVRRAIDLMLSIRD---SGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQG 584
Cdd:COG4559 146 RVLAqlwepvdGGPRWLFLDEPTSAL---DLAHQHAVLRLARQlarRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQG 222
|
250
....*....|....*
gi 489057211 585 RPQDVVRDPQVVEAY 599
Cdd:COG4559 223 TPEEVLTDELLERVY 237
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
367-579 |
1.48e-32 |
|
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: 123.45 E-value: 1.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 367 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKNPADFAALGL 446
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 447 grTFQIVQPFAAMTVEENIMVgafyrhhhekdareaaretawrmglgpllgaearGLTIGGLKRLEVARVMAMEPRILLL 526
Cdd:cd03229 81 --VFQDFALFPHLTVLENIAL----------------------------------GLSGGQQQRVALARALAMDPDVLLL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489057211 527 DEVMAGINQTDVRRAIDLMLSIRD-SGVSIIAIEHVMQAVMSLSDRVIVLASGE 579
Cdd:cd03229 125 DEPTSALDPITRREVRALLKSLQAqLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
367-594 |
1.94e-32 |
|
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: 125.04 E-value: 1.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 367 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQfhaPKNPADFAALGL 446
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILL---DGK---DITNLPPHKRPV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 447 GRTFQIVQPFAAMTVEENImvgAFYRHHHEKDAREAARETAWRMGLGPLLGAEAR---GLTIGGLKRLEVARVMAMEPRI 523
Cdd:cd03300 75 NTVFQNYALFPHLTVFENI---AFGLRLKKLPKAEIKERVAEALDLVQLEGYANRkpsQLSGGQQQRVAIARALVNEPKV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489057211 524 LLLDEVMAGInqtDVRRAIDLMLSI----RDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDPQ 594
Cdd:cd03300 152 LLLDEPLGAL---DLKLRKDMQLELkrlqKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
383-528 |
7.91e-32 |
|
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: 120.45 E-value: 7.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 383 RNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQFHAPKNPADFAAlGLGRTFQIVQPFAAMTVE 462
Cdd:pfam00005 2 KNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILL---DGQDLTDDERKSLRK-EIGYVFQDPQLFPRLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489057211 463 ENIMVGA--FYRHHHEKDAR-EAAREtawRMGLGPL----LGAEARGLTIGGLKRLEVARVMAMEPRILLLDE 528
Cdd:pfam00005 78 ENLRLGLllKGLSKREKDARaEEALE---KLGLGDLadrpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDE 147
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
367-584 |
4.65e-31 |
|
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: 120.46 E-value: 4.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 367 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFhAPKNpaDFAAL-- 444
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI-AARN--RIGYLpe 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 445 --GLGRTfqivqpfaaMTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPR 522
Cdd:cd03269 78 erGLYPK---------MKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489057211 523 ILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQG 584
Cdd:cd03269 149 LLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
350-597 |
7.62e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 123.04 E-value: 7.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 350 RAIKAPSPDRAGIgqdILRVQNLNKHFGG-----LHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVN 424
Cdd:PRK13631 8 KKLKVPNPLSDDI---ILRVKNLYCVFDEkqeneLVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 425 L----CGADGQF------HAPKNPADFAALGlgRTFQIVQPFAAM-----TVEENIMVGAFYRHHHEKDAREAARETAWR 489
Cdd:PRK13631 85 VgdiyIGDKKNNhelitnPYSKKIKNFKELR--RRVSMVFQFPEYqlfkdTIEKDIMFGPVALGVKKSEAKKLAKFYLNK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 490 MGLG-PLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSL 568
Cdd:PRK13631 163 MGLDdSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEV 242
|
250 260
....*....|....*....|....*....
gi 489057211 569 SDRVIVLASGEVIAQGRPQDVVRDPQVVE 597
Cdd:PRK13631 243 ADEVIVMDKGKILKTGTPYEIFTDQHIIN 271
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
367-576 |
8.43e-31 |
|
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: 119.51 E-value: 8.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 367 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKNPADFAALG- 445
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLGh 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 446 -LGrtfqivqPFAAMTVEENImvgAFYRH-HHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRI 523
Cdd:COG4133 83 aDG-------LKPELTVRENL---RFWAAlYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489057211 524 LLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHvmQAVMSLSDRVIVLA 576
Cdd:COG4133 153 WLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTH--QPLELAAARVLDLG 203
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
368-584 |
1.40e-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: 119.18 E-value: 1.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 368 RVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGadgqFHAPKNPADFA----A 443
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG----KPLEKERKRIGyvpqR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 444 LGLGRTFQIvqpfaamTVEENIMVGAFYR----HHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAM 519
Cdd:cd03235 77 RSIDRDFPI-------SVRDVVLMGLYGHkglfRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQ 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489057211 520 EPRILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLAsGEVIAQG 584
Cdd:cd03235 150 DPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLN-RTVVASG 213
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
367-601 |
1.92e-30 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 119.37 E-value: 1.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 367 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKNPadfaalGL 446
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQER------NV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 447 GRTFQIVQPFAAMTVEENIMVGAFYRHHHEKDAREAARETAWR-MGLGPLLGAEAR---GLTIGGLKRLEVARVMAMEPR 522
Cdd:cd03296 77 GFVFQHYALFRHMTVFDNVAFGLRVKPRSERPPEAEIRAKVHElLKLVQLDWLADRypaQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 523 ILLLDEVMAGINqTDVRRaiDLMLSIR----DSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDPQ--VV 596
Cdd:cd03296 157 VLLLDEPFGALD-AKVRK--ELRRWLRrlhdELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPAspFV 233
|
....*
gi 489057211 597 EAYLG 601
Cdd:cd03296 234 YSFLG 238
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
367-599 |
5.88e-30 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 118.72 E-value: 5.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 367 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGadgqfhapKNPADFAALGL 446
Cdd:PRK13548 3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNG--------RPLADWSPAEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 447 GR-----------TFqivqPFaamTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTiGGLK-RLEVA 514
Cdd:PRK13548 75 ARrravlpqhsslSF----PF---TVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLS-GGEQqRVQLA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 515 RVMA------MEPRILLLDEVMAGInqtDVRRAIDLMLSIRD----SGVSIIAIEH-VMQAVMsLSDRVIVLASGEVIAQ 583
Cdd:PRK13548 147 RVLAqlwepdGPPRWLLLDEPTSAL---DLAHQHHVLRLARQlaheRGLAVIVVLHdLNLAAR-YADRIVLLHQGRLVAD 222
|
250
....*....|....*.
gi 489057211 584 GRPQDVVRDPQVVEAY 599
Cdd:PRK13548 223 GTPAEVLTPETLRRVY 238
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
367-580 |
5.90e-30 |
|
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: 117.25 E-value: 5.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 367 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQfHAPKNPADFAAL-- 444
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIII---DGL-KLTDDKKNINELrq 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 445 GLGRTFQIVQPFAAMTVEENIMVGAFYRHHHEKD-AREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRI 523
Cdd:cd03262 77 KVGMVFQQFNLFPHLTVLENITLAPIKVKGMSKAeAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489057211 524 LLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEV 580
Cdd:cd03262 157 MLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
368-584 |
6.16e-30 |
|
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: 116.00 E-value: 6.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 368 RVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGadgqfhapknpadfaalglg 447
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDG-------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 448 rtfqivQPFAAMtveenimvgafyrhhhekDAREAARETAW------RMGLGPLLGAEARGLTIGGLKRLEVARVMAMEP 521
Cdd:cd03214 61 ------KDLASL------------------SPKELARKIAYvpqaleLLGLAHLADRPFNELSGGERQRVLLARALAQEP 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489057211 522 RILLLDEVMAGInqtDVRRAIDLMLSIRD----SGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQG 584
Cdd:cd03214 117 PILLLDEPTSHL---DIAHQIELLELLRRlareRGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
367-584 |
6.35e-30 |
|
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: 116.93 E-value: 6.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 367 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQfhapKNPADFAALGL 446
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ----KNIEALRRIGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 447 GRTFQIVqpFAAMTVEENIMVGAFYRHHHEKDAREAAREtawrMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLL 526
Cdd:cd03268 77 LIEAPGF--YPNLTARENLRLLARLLGIRKKRIDEVLDV----VGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLIL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489057211 527 DEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQG 584
Cdd:cd03268 151 DEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
364-598 |
1.30e-29 |
|
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: 122.70 E-value: 1.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 364 QDILRVQNLNKHF--GGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPD---EGTVNLCGADgqfhAPKNP 438
Cdd:COG1123 2 TPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRD----LLELS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 439 ADFAALGLGRTFQivQPFAAM---TVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVAR 515
Cdd:COG1123 78 EALRGRRIGMVFQ--DPMTQLnpvTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 516 VMAMEPRILLLDEVMAGINQTDVRRAIDLMLSI-RDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDPQ 594
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
....
gi 489057211 595 VVEA 598
Cdd:COG1123 236 ALAA 239
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
369-586 |
2.38e-29 |
|
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: 115.93 E-value: 2.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 369 VQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADgqfhAPKNPADFAAlGLGR 448
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHD----VVREPREVRR-RIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 449 TFQIVQPFAAMTVEENI-MVGAFYRHHHEKdAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLD 527
Cdd:cd03265 78 VFQDLSVDDELTGWENLyIHARLYGVPGAE-RRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489057211 528 EVMAGIN---QTDVRRAIDLMLsiRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRP 586
Cdd:cd03265 157 EPTIGLDpqtRAHVWEYIEKLK--EEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTP 216
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
366-594 |
3.61e-29 |
|
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: 115.76 E-value: 3.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 366 ILRVQNLNKHFGG----LHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKNPADF 441
Cdd:cd03258 1 MIELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 442 AAlGLGRTFQIVQPFAAMTVEENIMVgAFYRHHHEKDAREA-ARETAWRMGLGPLLGAEARGLTiGGLK-RLEVARVMAM 519
Cdd:cd03258 81 RR-RIGMIFQHFNLLSSRTVFENVAL-PLEIAGVPKAEIEErVLELLELVGLEDKADAYPAQLS-GGQKqRVGIARALAN 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489057211 520 EPRILLLDEVMAGINQTDVRRAIDLMLSI-RDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDPQ 594
Cdd:cd03258 158 NPKVLLCDEATSALDPETTQSILALLRDInRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
367-603 |
7.10e-29 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 120.66 E-value: 7.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 367 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQFHAPKNPADFAALGL 446
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITI---NNINYNKLDHKLAAQLGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 447 GRTFQIVQPFAAMTVEENIMVGafyRHHHEK----------DAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARV 516
Cdd:PRK09700 83 GIIYQELSVIDELTVLENLYIG---RHLTKKvcgvniidwrEMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 517 MAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDpQVV 596
Cdd:PRK09700 160 LMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSND-DIV 238
|
....*..
gi 489057211 597 EAYLGKE 603
Cdd:PRK09700 239 RLMVGRE 245
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
380-584 |
2.12e-28 |
|
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: 113.01 E-value: 2.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 380 HVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQFHAPknpadfaaLGLGRTFQivqpfAAM 459
Cdd:cd03220 36 WALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTV---RGRVSSL--------LGLGGGFN-----PEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 460 TVEENI-MVGAFYRhHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGINQTDV 538
Cdd:cd03220 100 TGRENIyLNGRLLG-LSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQ 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489057211 539 RRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQG 584
Cdd:cd03220 179 EKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
368-579 |
3.58e-28 |
|
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: 110.41 E-value: 3.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 368 RVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADgqfhapknpadfaalglg 447
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKD------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 448 rtfqivqpfaamtveenimvgafyrhHHEKDAREAARETAWRMGLGpllgaeargltiGGLK-RLEVARVMAMEPRILLL 526
Cdd:cd00267 63 --------------------------IAKLPLEELRRRIGYVPQLS------------GGQRqRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489057211 527 DEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGE 579
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
364-594 |
5.40e-28 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 113.10 E-value: 5.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 364 QDILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHapknpaDFAA 443
Cdd:PRK11701 4 QPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLR------DLYA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 444 LG------LGRT-FQIVQPFAA----MTVE------ENIM-VGAfyRHHheKDAREAARETAWRMGLGPLLGAEARGLTI 505
Cdd:PRK11701 78 LSeaerrrLLRTeWGFVHQHPRdglrMQVSaggnigERLMaVGA--RHY--GDIRATAGDWLERVEIDAARIDDLPTTFS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 506 GGLK-RLEVARVMAMEPRILLLDEVMAGInqtDVR---RAIDLMLS-IRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEV 580
Cdd:PRK11701 154 GGMQqRLQIARNLVTHPRLVFMDEPTGGL---DVSvqaRLLDLLRGlVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRV 230
|
250
....*....|....
gi 489057211 581 IAQGRPQDVVRDPQ 594
Cdd:PRK11701 231 VESGLTDQVLDDPQ 244
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
366-596 |
7.49e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 113.40 E-value: 7.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 366 ILRVQNLNKHFG-GLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQfhapknPADFAAL 444
Cdd:PRK13636 5 ILKVEELNYNYSdGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILF---DGK------PIDYSRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 445 GL-------GRTFQIV--QPFAAmTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVAR 515
Cdd:PRK13636 76 GLmklresvGMVFQDPdnQLFSA-SVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 516 VMAMEPRILLLDEVMAGINQTDVRRAIDLMLSI-RDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDPQ 594
Cdd:PRK13636 155 VLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMqKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKE 234
|
..
gi 489057211 595 VV 596
Cdd:PRK13636 235 ML 236
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
367-603 |
1.73e-27 |
|
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: 111.24 E-value: 1.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 367 LRVQNLNKHFGGLH-VTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGadgqfhapKNPADFAALG 445
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDG--------EDIREQDPVE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 446 LGRT----FQIVQPFAAMTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGP--LLGAEARGLTIGGLKRLEVARVMAM 519
Cdd:cd03295 73 LRRKigyvIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPaeFADRYPHELSGGQQQRVGVARALAA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 520 EPRILLLDEVMAGINQTDVRRAIDLMLSI-RDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDP--QVV 596
Cdd:cd03295 153 DPPLLLMDEPFGALDPITRDQLQEEFKRLqQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPanDFV 232
|
....*..
gi 489057211 597 EAYLGKE 603
Cdd:cd03295 233 AEFVGAD 239
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
367-589 |
1.90e-27 |
|
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: 111.12 E-value: 1.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 367 LRVQNLNKHFG-GLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKNPADFAAlg 445
Cdd:cd03256 1 IEVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 446 lgRTFQIVQPFA---AMTVEENIMVGAFYRHH---------HEKDaREAARETAWRMGLGPLLGAEARGLTIGGLKRLEV 513
Cdd:cd03256 79 --QIGMIFQQFNlieRLSVLENVLSGRLGRRStwrslfglfPKEE-KQRALAALERVGLLDKAYQRADQLSGGQQQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489057211 514 ARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSI-RDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDV 589
Cdd:cd03256 156 ARALMQQPKLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
367-593 |
4.20e-27 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 112.86 E-value: 4.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 367 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKNPadfaalGL 446
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDR------NI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 447 GRTFQ--IVQPFaaMTVEENImvgAFY---RHHHEKDAREAARETAWRMGLGPLLGAEARGLTiGGLK-RLEVARVMAME 520
Cdd:COG3839 78 AMVFQsyALYPH--MTVYENI---AFPlklRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLS-GGQRqRVALGRALVRE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 521 PRILLLDEVMAGInqtDVRRAIDLMLSI----RDSGVSII-----AIEhvmqaVMSLSDRVIVLASGEVIAQGRPQDVVR 591
Cdd:COG3839 152 PKVFLLDEPLSNL---DAKLRVEMRAEIkrlhRRLGTTTIyvthdQVE-----AMTLADRIAVMNDGRIQQVGTPEELYD 223
|
..
gi 489057211 592 DP 593
Cdd:COG3839 224 RP 225
|
|
| urea_trans_UrtC |
TIGR03408 |
urea ABC transporter, permease protein UrtC; Members of this protein family are ABC ... |
53-321 |
7.40e-27 |
|
urea ABC transporter, permease protein UrtC; Members of this protein family are ABC transporter permease proteins 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: 132449 Cd Length: 313 Bit Score: 111.20 E-value: 7.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 53 FAALSTAWNIVGGFAGQMSLGHAVFYGIGGY---------------TGVILFnMGI--------------SPWFSMFIGT 103
Cdd:TIGR03408 18 YAIVALGIDLIWGYTGILSLGQGVFFGLGGYamamylklqasgegtTGLPDF-MLWngvtelpwfwqpfaSFPFALLAVV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 104 FIAALVGMVISYPCF--RLKGPFYSLASIAFLEVFRVLALHFGWLTGGATGLMiqlKLGWVwMVFRERWPSLLIVF---- 177
Cdd:TIGR03408 97 LVPGLLAFLLGYFVFrsRIKGVYFSIITQALALALALLFVGQQTGTGGTNGLT---DFKTL-LGFDLSSDSTKRALyflt 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 178 -GMLLVTLAITWAARRSRLGFYLVATRERESAARAAGVRTVRVRLIAVAISSALCAMLGTFHAMYLTFIEPaAMFSLAFS 256
Cdd:TIGR03408 173 aALLALAFLLCRWLVRSRFGRVLIAIRDAENRVRFLGYDPANYKVFVFVLSAGIAGIAGALYVPQVGIISP-SEMGIVPS 251
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489057211 257 IQIAMFALNGGLGTVAGPLLGAVLlvpiTEWARASLGASALGLHGFVYGLVLILVVLFMPNGIMG 321
Cdd:TIGR03408 252 IEMVIWVAVGGRGTLIGAVLGALL----VNYAKTFFSEAFPEAWLYILGALFVVVVLFLPKGLAG 312
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
383-597 |
1.09e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 109.70 E-value: 1.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 383 RNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCG----ADGQFHAPKNpadfaalgLGRTFQivQP--- 455
Cdd:PRK13632 26 KNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGitisKENLKEIRKK--------IGIIFQ--NPdnq 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 456 FAAMTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGINQ 535
Cdd:PRK13632 96 FIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDP 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489057211 536 TDVRRAIDLMLSIRDSGV-SIIAIEHVMQAVMsLSDRVIVLASGEVIAQGRPQDVVRDPQVVE 597
Cdd:PRK13632 176 KGKREIKKIMVDLRKTRKkTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEILNNKEILE 237
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
367-584 |
2.20e-26 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 106.89 E-value: 2.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 367 LRVQNLNKHFGGLHVTRNVSFTLREGeVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADgqfhAPKNPADFAALgL 446
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQD----VLKQPQKLRRR-I 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 447 GRTFQIVQPFAAMTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLL 526
Cdd:cd03264 75 GYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 527 DEVMAGInqtDVRRAIDL--MLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQG 584
Cdd:cd03264 155 DEPTAGL---DPEERIRFrnLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
367-601 |
3.57e-26 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 107.15 E-value: 3.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 367 LRVQNLNKHFGGLHVtrNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADgqfHAPKNPAD--FAAL 444
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQD---LTALPPAErpVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 445 glgrtFQIVQPFAAMTVEENIMVGafyRHHHEK---DAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEP 521
Cdd:COG3840 77 -----FQENNLFPHLTVAQNIGLG---LRPGLKltaEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 522 RILLLDEVMAginqtdvrrAID--L---MLSI-----RDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVV- 590
Cdd:COG3840 149 PILLLDEPFS---------ALDpaLrqeMLDLvdelcRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLd 219
|
250
....*....|..
gi 489057211 591 -RDPQVVEAYLG 601
Cdd:COG3840 220 gEPPPALAAYLG 231
|
|
| BPD_transp_2 |
pfam02653 |
Branched-chain amino acid transport system / permease component; This is a large family mainly ... |
46-312 |
3.93e-26 |
|
Branched-chain amino acid transport system / permease component; This is a large family mainly comprising high-affinity branched-chain amino acid transporter proteins such as E. coli LivH and LivM, both of which are form the LIV-I transport system. Also found with in this family are proteins from the galactose transport system permease and a ribose transport system.
Pssm-ID: 396977 [Multi-domain] Cd Length: 269 Bit Score: 108.11 E-value: 3.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 46 IFITICLFAALSTAWNIVGGFAGQMSLGHAVFYGIGGYTGVILFNMGIS-PWFSMFIGTFIAALVGMVISYPCFRLKGPF 124
Cdd:pfam02653 5 ILTLASIYAIAALGLTLIYGIAGVINLGHGGFMMLGAYVAAMLLNLLGPgLWLALPVGILVGAAVGLLIGILTLRLKINE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 125 YSLASIAFLEVFRVLALHFGWLTGGATGLMIQLKLGWVWMVFRERWPSLLIVFGmLLVTLAITWAARRSRLGFYLVATRE 204
Cdd:pfam02653 85 VIITLLLNLAALGLALFLVTGILGGEGGTSGITGPSGFPGAFLSFAFAFIFLLA-LLLVLALWLLLYRTKFGRALRAVGE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 205 RESAARAAGVRTVRVRLIAVAISSALCAMLGTFHAMYLTFIEPAAmFSLAFSIQIAMFALNGGLGTVAGPLLGAVLLVPI 284
Cdd:pfam02653 164 NEEAARAAGINVKKLKLLTFVISGALAGLAGALLALYTGVVPPSN-FGVGLGLDAIAAVVLGGAGSPIGVVIGSLIIGLV 242
|
250 260
....*....|....*....|....*...
gi 489057211 285 TEWARASLGASALgLHGFVYGLVLILVV 312
Cdd:pfam02653 243 QSLGLGALGSPPE-LSLLVLGALLILVL 269
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
351-601 |
4.56e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 109.54 E-value: 4.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 351 AIKAPSPDRAGIGQDILRVqnlNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADg 430
Cdd:PRK13536 29 AKASIPGSMSTVAIDLAGV---SKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVP- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 431 qfhAPKNpADFAALGLGRTFQIVQPFAAMTVEENIMV-GAFYRHHhekdAREAarETAwrmgLGPLL-------GAEAR- 501
Cdd:PRK13536 105 ---VPAR-ARLARARIGVVPQFDNLDLEFTVRENLLVfGRYFGMS----TREI--EAV----IPSLLefarlesKADARv 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 502 GLTIGGLKR-LEVARVMAMEPRILLLDEVMAGINqTDVRRAI-DLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGE 579
Cdd:PRK13536 171 SDLSGGMKRrLTLARALINDPQLLILDEPTTGLD-PHARHLIwERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGR 249
|
250 260
....*....|....*....|....*
gi 489057211 580 VIAQGRPQDVVRDP---QVVEAYLG 601
Cdd:PRK13536 250 KIAEGRPHALIDEHigcQVIEIYGG 274
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
366-597 |
6.42e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 107.47 E-value: 6.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 366 ILRVQNLN-KHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGadgqfhapkNPADFAAL 444
Cdd:PRK13639 1 ILETRDLKySYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKG---------EPIKYDKK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 445 GLGRTFQIV---------QPFAAmTVEENIMVGAFYRHHHEKDAREAARETAWRMGLgplLGAEARG---LTIGGLKRLE 512
Cdd:PRK13639 72 SLLEVRKTVgivfqnpddQLFAP-TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGM---EGFENKPphhLSGGQKKRVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 513 VARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRD 592
Cdd:PRK13639 148 IAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSD 227
|
....*
gi 489057211 593 PQVVE 597
Cdd:PRK13639 228 IETIR 232
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
367-584 |
7.21e-26 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 105.65 E-value: 7.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 367 LRVQNLNKHFgglhvtrnvSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADgqfHAPKNPADFAALGL 446
Cdd:cd03298 8 FSYGEQPMHF---------DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVD---VTAAPPADRPVSML 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 447 grtFQIVQPFAAMTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLL 526
Cdd:cd03298 76 ---FQENNLFAHLTVEQNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489057211 527 DEVMAGINQTDVRRAIDLMLSI-RDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQG 584
Cdd:cd03298 153 DEPFAALDPALRAEMLDLVLDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
350-582 |
9.16e-26 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 111.26 E-value: 9.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 350 RAIKAPSPDRAG-IGQDILRVQNLNKHfgglHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcga 428
Cdd:COG1129 239 RELEDLFPKRAAaPGEVVLEVEGLSVG----GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRL--- 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 429 DGQFHAPKNPADFAALGLG------RTFQIVQPfaaMTVEENIMVGAFYRHHH-----EKDAREAARETAWRMGL-GPLL 496
Cdd:COG1129 312 DGKPVRIRSPRDAIRAGIAyvpedrKGEGLVLD---LSIRENITLASLDRLSRgglldRRRERALAEEYIKRLRIkTPSP 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 497 GAEARGLTiGG------LkrlevARVMAMEPRILLLDEVMAGInqtDV--RRAI-DLMLSIRDSGVSIIAI--EhvMQAV 565
Cdd:COG1129 389 EQPVGNLS-GGnqqkvvL-----AKWLATDPKVLILDEPTRGI---DVgaKAEIyRLIRELAAEGKAVIVIssE--LPEL 457
|
250
....*....|....*..
gi 489057211 566 MSLSDRVIVLASGEVIA 582
Cdd:COG1129 458 LGLSDRILVMREGRIVG 474
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
366-599 |
1.28e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 107.58 E-value: 1.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 366 ILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKNPadfAALG 445
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHAR---QRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 446 LGRTFQIVQPfaAMTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILL 525
Cdd:PRK13537 84 VVPQFDNLDP--DFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489057211 526 LDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDP---QVVEAY 599
Cdd:PRK13537 162 LDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESEigcDVIEIY 238
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
383-584 |
4.11e-25 |
|
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: 104.34 E-value: 4.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 383 RNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKNPADFAALgLGRTFQIVQPFAAMTve 462
Cdd:cd03267 38 KGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVV-FGQKTQLWWDLPVID-- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 463 enimvgAFYRHHH-----EKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGIN--- 534
Cdd:cd03267 115 ------SFYLLAAiydlpPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDvva 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489057211 535 QTDVRRAIDLMlsIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQG 584
Cdd:cd03267 189 QENIRNFLKEY--NRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
351-593 |
5.24e-25 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 107.23 E-value: 5.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 351 AIKAPSPDRAGIGQDILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADG 430
Cdd:PRK11607 4 AIPRPQAKTRKALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 431 QFHAP-KNPADFaalglgrTFQIVQPFAAMTVEENIMVGAfyrhHHEKDAR-EAARETAWRMGLGPLLGAEARG---LTI 505
Cdd:PRK11607 84 SHVPPyQRPINM-------MFQSYALFPHMTVEQNIAFGL----KQDKLPKaEIASRVNEMLGLVHMQEFAKRKphqLSG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 506 GGLKRLEVARVMAMEPRILLLDEVMAGINQT-DVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQG 584
Cdd:PRK11607 153 GQRQRVALARSLAKRPKLLLLDEPMGALDKKlRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIG 232
|
....*....
gi 489057211 585 RPQDVVRDP 593
Cdd:PRK11607 233 EPEEIYEHP 241
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
367-603 |
5.25e-25 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 108.85 E-value: 5.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 367 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQFHAPKNPADFAALGL 446
Cdd:PRK11288 5 LSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILI---DGQEMRFASTTAALAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 447 GRTFQIVQPFAAMTVEENIMVGAFYRHH---HEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRI 523
Cdd:PRK11288 82 AIIYQELHLVPEMTVAENLYLGQLPHKGgivNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 524 LLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRP-QDVVRDpQVVEAYLGK 602
Cdd:PRK11288 162 IAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVATFDDmAQVDRD-QLVQAMVGR 240
|
.
gi 489057211 603 E 603
Cdd:PRK11288 241 E 241
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
366-598 |
3.31e-24 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 106.67 E-value: 3.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 366 ILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQFHAPKNPADFAALG 445
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEI---GGNPCARLTPAKAHQLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 446 LGRTFQIVQPFAAMTVEENIMVGAfyrHHHEKDAREAARETAwRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILL 525
Cdd:PRK15439 88 IYLVPQEPLLFPNLSVKENILFGL---PKRQASMQKMKQLLA-ALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489057211 526 LDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGrPQDVVRDPQVVEA 598
Cdd:PRK15439 164 LDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSG-KTADLSTDDIIQA 235
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
384-598 |
3.50e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 102.79 E-value: 3.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 384 NVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgADGQFHAPKNPADFAAL--GLGRTFQIV--QPFAAm 459
Cdd:PRK13634 25 DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI--GERVITAGKKNKKLKPLrkKVGIVFQFPehQLFEE- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 460 TVEENIMVGAFYRHHHEKDAREAARETAWRMGLGP-LLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGINQTDV 538
Cdd:PRK13634 102 TVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGR 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489057211 539 RRAIDLMLSI-RDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDPQVVEA 598
Cdd:PRK13634 182 KEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDELEA 242
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
366-594 |
4.14e-24 |
|
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: 103.21 E-value: 4.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 366 ILRVQNLNKHF----GGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAP---DEGTVNLCGADgqfHAPKNP 438
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGED---LLKLSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 439 ADFAALgLGRTFQIV-Q-PFAA----MTVEENIMVGafYRHHH---EKDAREAARETAWRMGLGPllgAEARgltI---- 505
Cdd:COG0444 78 KELRKI-RGREIQMIfQdPMTSlnpvMTVGDQIAEP--LRIHGglsKAEARERAIELLERVGLPD---PERR---Ldryp 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 506 ----GGLK-RLEVARVMAMEPRILLLDE--------VMAGInqtdvrraIDLMLSIRDS-GVSIIAIEHVMQAVMSLSDR 571
Cdd:COG0444 149 helsGGMRqRVMIARALALEPKLLIADEpttaldvtIQAQI--------LNLLKDLQRElGLAILFITHDLGVVAEIADR 220
|
250 260
....*....|....*....|...
gi 489057211 572 VIVLASGEVIAQGRPQDVVRDPQ 594
Cdd:COG0444 221 VAVMYAGRIVEEGPVEELFENPR 243
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
367-580 |
4.39e-24 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 100.41 E-value: 4.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 367 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKNPadfaalGL 446
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDR------DI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 447 GRTFQIVQPFAAMTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLL 526
Cdd:cd03301 75 AMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLM 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489057211 527 DEVMAGINqTDVRRAIDLMLS--IRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEV 580
Cdd:cd03301 155 DEPLSNLD-AKLRVQMRAELKrlQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
290-590 |
5.36e-24 |
|
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: 106.84 E-value: 5.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 290 ASLGASALGLHGFVYGLVLILVVLFMPNG----------------IMGAINRFVRKPQDSEETATA--RTEPIAAVPA-R 350
Cdd:COG2274 379 NLLSTLSGLLQQLATVALLWLGAYLVIDGqltlgqliafnilsgrFLAPVAQLIGLLQRFQDAKIAleRLDDILDLPPeR 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 351 AIKAPSPDRAGIGQDIlRVQNLNKHFGGLH--VTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGA 428
Cdd:COG2274 459 EEGRSKLSLPRLKGDI-ELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGI 537
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 429 D-GQFhapkNPADFAALgLGRTFQIVQPFAAmTVEENIMVGAfyRHHHEKDAREAARET-------AWRMGLGPLLGAEA 500
Cdd:COG2274 538 DlRQI----DPASLRRQ-IGVVLQDVFLFSG-TIRENITLGD--PDATDEEIIEAARLAglhdfieALPMGYDTVVGEGG 609
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 501 RGLTIGGLKRLEVARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRdSGVSIIAIEHVMqAVMSLSDRVIVLASGEV 580
Cdd:COG2274 610 SNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRL-STIRLADRIIVLDKGRI 687
|
330
....*....|
gi 489057211 581 IAQGRPQDVV 590
Cdd:COG2274 688 VEDGTHEELL 697
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
367-594 |
7.07e-24 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 101.20 E-value: 7.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 367 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCG--------ADGQFHApknp 438
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlvrdKDGQLKV---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 439 ADFAALGLGRT-----FQIVQPFAAMTVEENIMVGAFYRHHHEK-DAREAARETAWRMGLGpllgAEARG-----LTIGG 507
Cdd:PRK10619 82 ADKNQLRLLRTrltmvFQHFNLWSHMTVLENVMEAPIQVLGLSKqEARERAVKYLAKVGID----ERAQGkypvhLSGGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 508 LKRLEVARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQ 587
Cdd:PRK10619 158 QQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPE 237
|
....*..
gi 489057211 588 DVVRDPQ 594
Cdd:PRK10619 238 QLFGNPQ 244
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
366-581 |
8.85e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 100.93 E-value: 8.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 366 ILRVQNLNKHFG-GL----HVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADgqfhAPKNPAD 440
Cdd:COG1101 1 MLELKNLSKTFNpGTvnekRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKD----VTKLPEY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 441 FAALGLGRTFQivQPFA----AMTVEENIMVgAFYRHH-------HEKDAREAARETAWRMGLGpL---LGAEArGLTIG 506
Cdd:COG1101 77 KRAKYIGRVFQ--DPMMgtapSMTIEENLAL-AYRRGKrrglrrgLTKKRRELFRELLATLGLG-LenrLDTKV-GLLSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 507 GlKRLEVARVMAM--EPRILLLDEVMAGInqtDVRRAIDLM-LS---IRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEV 580
Cdd:COG1101 152 G-QRQALSLLMATltKPKLLLLDEHTAAL---DPKTAALVLeLTekiVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
.
gi 489057211 581 I 581
Cdd:COG1101 228 I 228
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
384-597 |
1.38e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 101.06 E-value: 1.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 384 NVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGadgqFHAPKNPADFA------ALGLGRTFQIVQPFA 457
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAG----YHITPETGNKNlkklrkKVSLVFQFPEAQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 458 AmTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGP-LLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGINQT 536
Cdd:PRK13641 101 N-TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEdLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPE 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489057211 537 DVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDPQVVE 597
Cdd:PRK13641 180 GRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKEWLK 240
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
363-580 |
2.49e-23 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 97.50 E-value: 2.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 363 GQDILRVQNLNKHfgglHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADgqfHAPKNPADFA 442
Cdd:cd03215 1 GEPVLEVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKP---VTRRSPRDAI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 443 ALGLG------RTFQIVQPfaaMTVEENIMVGAFyrhhhekdareaaretawrmglgpLLGaeargltiGGLKRLEVARV 516
Cdd:cd03215 74 RAGIAyvpedrKREGLVLD---LSVAENIALSSL------------------------LSG--------GNQQKVVLARW 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489057211 517 MAMEPRILLLDEVMAGInqtDV--RRAI-DLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEV 580
Cdd:cd03215 119 LARDPRVLILDEPTRGV---DVgaKAEIyRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
371-593 |
3.46e-23 |
|
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: 101.33 E-value: 3.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 371 NLNKHFGGLHVtrNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCG------ADGQFHAP-KNPadfaa 443
Cdd:COG4148 6 DFRLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlqdsARGIFLPPhRRR----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 444 lgLGRTFQIVQPFAAMTVEENIMVGAfyrhhheKDAREAARETAW-----RMGLGPLLGAEARGLTiGGLK-RLEVARVM 517
Cdd:COG4148 79 --IGYVFQEARLFPHLSVRGNLLYGR-------KRAPRAERRISFdevveLLGIGHLLDRRPATLS-GGERqRVAIGRAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489057211 518 AMEPRILLLDEVMAGINQTdvRRA--IDLMLSIRDS-GVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDP 593
Cdd:COG4148 149 LSSPRLLLMDEPLAALDLA--RKAeiLPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
368-593 |
4.81e-23 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 98.62 E-value: 4.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 368 RVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGqfhapKNPADFAALGLG 447
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLV---DG-----LDVATTPSRELA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 448 RTFQIVQ---PFAA-MTVEENIMVGAFyRHHH----EKDaREAARETAWRMGLGPLlgaEARGLT--IGGLK-RLEVARV 516
Cdd:COG4604 75 KRLAILRqenHINSrLTVRELVAFGRF-PYSKgrltAED-REIIDEAIAYLDLEDL---ADRYLDelSGGQRqRAFIAMV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 517 MAMEPRILLLDEVMagiNQTDVRRAIDLMLSIR----DSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRD 592
Cdd:COG4604 150 LAQDTDYVLLDEPL---NNLDMKHSVQMMKLLRrladELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITP 226
|
.
gi 489057211 593 P 593
Cdd:COG4604 227 E 227
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
366-601 |
7.95e-23 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 97.64 E-value: 7.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 366 ILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGAD-GQFHAPK-NPADFAA 443
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDiTDWQTAKiMREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 444 LGLGRtfqivQPFAAMTVEENIMVGAFYrhhheKDAREAARETAWRMGLGPLLG---AEARGLTIGGLKR-LEVARVMAM 519
Cdd:PRK11614 85 VPEGR-----RVFSRMTVEENLAMGGFF-----AERDQFQERIKWVYELFPRLHerrIQRAGTMSGGEQQmLAIGRALMS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 520 EPRILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDPQVVEAY 599
Cdd:PRK11614 155 QPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVRSAY 234
|
..
gi 489057211 600 LG 601
Cdd:PRK11614 235 LG 236
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
342-588 |
1.50e-22 |
|
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: 101.76 E-value: 1.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 342 EPIAAVPARAIKAPSPDRAGIgqdilRVQNLN-KHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDE 420
Cdd:COG4988 317 APEPAAPAGTAPLPAAGPPSI-----ELEDVSfSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYS 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 421 GTVNLCGADgqfhapknPADFAALGLGRTFQIV--QPF-AAMTVEENImvgAFYRHHHEKDA-REAARET-AWRM----- 490
Cdd:COG4988 392 GSILINGVD--------LSDLDPASWRRQIAWVpqNPYlFAGTIRENL---RLGRPDASDEElEAALEAAgLDEFvaalp 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 491 -GLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGInqtDVRRAIDLMLSIRD--SGVSIIAIEHVMqAVMS 567
Cdd:COG4988 461 dGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHL---DAETEAEILQALRRlaKGRTVILITHRL-ALLA 536
|
250 260
....*....|....*....|.
gi 489057211 568 LSDRVIVLASGEVIAQGRPQD 588
Cdd:COG4988 537 QADRILVLDDGRIVEQGTHEE 557
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
344-599 |
1.72e-22 |
|
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: 101.30 E-value: 1.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 344 IAAVPARAiKAPSPDRAGIgqdILRVQNLNKHF-----------GGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMI 412
Cdd:COG4172 257 LAAEPRGD-PRPVPPDAPP---LLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLAL 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 413 SGfLAPDEGTVNLCGADGQfhapknPADFAAL-GLGRTFQIV-Q-PFAA----MTVEENIMVGaFYRHHHEKDA---REA 482
Cdd:COG4172 333 LR-LIPSEGEIRFDGQDLD------GLSRRALrPLRRRMQVVfQdPFGSlsprMTVGQIIAEG-LRVHGPGLSAaerRAR 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 483 ARETAWRMGLGPllgaEAR--------GltiGGLKRLEVARVMAMEPRILLLDE--------VMAGInqtdvrraIDLML 546
Cdd:COG4172 405 VAEALEEVGLDP----AARhryphefsG---GQRQRIAIARALILEPKLLVLDEptsaldvsVQAQI--------LDLLR 469
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 489057211 547 SI-RDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDPQvvEAY 599
Cdd:COG4172 470 DLqREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQ--HPY 521
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
367-592 |
2.32e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 97.85 E-value: 2.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 367 LRVQNLNKHFGG-----LHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHapKNPADF 441
Cdd:PRK13651 3 IKVKNIVKIFNKklpteLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNK--KKTKEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 442 AALG----------------------LGRTFQIV--QPFAAmTVEENIMVGAFYRHHHEKDAREAARETAWRMGLgPL-- 495
Cdd:PRK13651 81 EKVLeklviqktrfkkikkikeirrrVGVVFQFAeyQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGL-DEsy 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 496 LGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVL 575
Cdd:PRK13651 159 LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFF 238
|
250
....*....|....*..
gi 489057211 576 ASGEVIAQGRPQDVVRD 592
Cdd:PRK13651 239 KDGKIIKDGDTYDILSD 255
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
366-593 |
2.89e-22 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 98.87 E-value: 2.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 366 ILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGAD-GQFHAPKNPadfaal 444
Cdd:PRK09452 14 LVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDiTHVPAENRH------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 445 gLGRTFQIVQPFAAMTVEENIMVGAFYRHHHEKDAREAAREtAWRM-GLGPLLGAEARGLTIGGLKRLEVARVMAMEPRI 523
Cdd:PRK09452 88 -VNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVME-ALRMvQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKV 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489057211 524 LLLDEVMAGINQTdVRRAIDLMLSI--RDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDP 593
Cdd:PRK09452 166 LLLDESLSALDYK-LRKQMQNELKAlqRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEP 236
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
364-599 |
3.24e-22 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 96.31 E-value: 3.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 364 QDILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEG-TVNLCGADgqfhapknpadfa 442
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGER------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 443 algLGRT--FQI------VQPF------AAMTVEENIMVGAF-----YRHHHEKDaREAARETAWRMGLGPLLGAEARGL 503
Cdd:COG1119 68 ---RGGEdvWELrkriglVSPAlqlrfpRDETVLDVVLSGFFdsiglYREPTDEQ-RERARELLELLGLAHLADRPFGTL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 504 TIGGLKRLEVARVMAMEPRILLLDEVMAG---INQTDVRRAIDLMlsIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEV 580
Cdd:COG1119 144 SQGEQRRVLIARALVKDPELLILDEPTAGldlGARELLLALLDKL--AAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRV 221
|
250
....*....|....*....
gi 489057211 581 IAQGRPQDVVRDPQVVEAY 599
Cdd:COG1119 222 VAAGPKEEVLTSENLSEAF 240
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
367-590 |
3.44e-22 |
|
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: 100.26 E-value: 3.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 367 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGF--LAPDEGT----VNLCGADGQFHAP----- 435
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRiiyhVALCEKCGYVERPskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 436 ----------KNPADF--------------AALGLGRTFQIvqpFAAMTVEENIMVGAFYRHHHEKDAREAARETAWRMG 491
Cdd:TIGR03269 81 pcpvcggtlePEEVDFwnlsdklrrrirkrIAIMLQRTFAL---YGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 492 LGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGIN-QTD--VRRAidLMLSIRDSGVSIIAIEHVMQAVMSL 568
Cdd:TIGR03269 158 LSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDpQTAklVHNA--LEEAVKASGISMVLTSHWPEVIEDL 235
|
250 260
....*....|....*....|..
gi 489057211 569 SDRVIVLASGEVIAQGRPQDVV 590
Cdd:TIGR03269 236 SDKAIWLENGEIKEEGTPDEVV 257
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
367-599 |
3.62e-22 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 99.15 E-value: 3.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 367 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADgqfhapknPADFAALGL 446
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDD--------VEALSARAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 447 GRTFQIVQPFAAM----TVEENIMVGafyRHHH-------EKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVAR 515
Cdd:PRK09536 76 SRRVASVPQDTSLsfefDVRQVVEMG---RTPHrsrfdtwTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLAR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 516 VMAMEPRILLLDEVMAGInqtDVRRAIDLMLSIR---DSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRD 592
Cdd:PRK09536 153 ALAQATPVLLLDEPTASL---DINHQVRTLELVRrlvDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTA 229
|
....*..
gi 489057211 593 PQVVEAY 599
Cdd:PRK09536 230 DTLRAAF 236
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
364-594 |
5.46e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 95.61 E-value: 5.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 364 QDILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMIS--GFLAPD---EGTVNLCGADgqFHAPKnp 438
Cdd:PRK14239 3 EPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPEvtiTGSIVYNGHN--IYSPR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 439 ADFAAL--GLGRTFQIVQPFAaMTVEENIMVGAFYRHHHEKDAREAARETAWRMG-----LGPLLGAEARGLTIGGLKRL 511
Cdd:PRK14239 79 TDTVDLrkEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQVLDEAVEKSLKGAsiwdeVKDRLHDSALGLSGGQQQRV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 512 EVARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRDSgVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVR 591
Cdd:PRK14239 158 CIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFM 236
|
...
gi 489057211 592 DPQ 594
Cdd:PRK14239 237 NPK 239
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
366-600 |
6.29e-22 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 95.49 E-value: 6.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 366 ILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTL---FN----MISGFLApdEGTVNLCGADgqFHAPKnp 438
Cdd:COG1117 11 KIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLlrcLNrmndLIPGARV--EGEILLDGED--IYDPD-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 439 ADFAALglgRT-----FQIVQPFaAMTVEENIMVGAfyRHHHEKDAREAAR--ETA------W-----RmglgplLGAEA 500
Cdd:COG1117 85 VDVVEL---RRrvgmvFQKPNPF-PKSIYDNVAYGL--RLHGIKSKSELDEivEESlrkaalWdevkdR------LKKSA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 501 RGLTIGGLKRLEVARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRDSgVSIIAIEHVMQAVMSLSDRVIVLASGEV 580
Cdd:COG1117 153 LGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQAARVSDYTAFFYLGEL 231
|
250 260
....*....|....*....|..
gi 489057211 581 IAQGRPQDVVRDP--QVVEAYL 600
Cdd:COG1117 232 VEFGPTEQIFTNPkdKRTEDYI 253
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
369-593 |
6.61e-22 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 97.46 E-value: 6.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 369 VQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGAD-GQFHAPKNPADFaalglg 447
Cdd:PRK10851 5 IANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDvSRLHARDRKVGF------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 448 rTFQIVQPFAAMTVEENIMVGAFYRHHHEKDAREAARETAWRM----GLGPLLGAEARGLTIGGLKRLEVARVMAMEPRI 523
Cdd:PRK10851 79 -VFQHYALFRHMTVFDNIAFGLTVLPRRERPNAAAIKAKVTQLlemvQLAHLADRYPAQLSGGQKQRVALARALAVEPQI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489057211 524 LLLDEVMAGIN---QTDVRRAI-DLMLSIRDSGVsiiAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDP 593
Cdd:PRK10851 158 LLLDEPFGALDaqvRKELRRWLrQLHEELKFTSV---FVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREP 228
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
366-581 |
7.07e-22 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 94.35 E-value: 7.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 366 ILRVQNLNKHF-GGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQfHAPKNpaDFAAL 444
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLS-RLKRR--EIPYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 445 --GLGRTFQIVQPFAAMTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPR 522
Cdd:COG2884 78 rrRIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489057211 523 ILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVI 581
Cdd:COG2884 158 LLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLV 216
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
380-584 |
7.51e-22 |
|
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: 94.19 E-value: 7.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 380 HVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGAD-GQFHapknPADFAAlGLGRTFQIVQPFAA 458
Cdd:cd03245 18 PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDiRQLD----PADLRR-NIGYVPQDVTLFYG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 459 mTVEENIMVGAfyRHHHEKDAREAAR-----ETAWR--MGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMA 531
Cdd:cd03245 93 -TLRDNITLGA--PLADDERILRAAElagvtDFVNKhpNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489057211 532 GINQTDVRRAID-LMLSIRDSgvSIIAIEHVMqAVMSLSDRVIVLASGEVIAQG 584
Cdd:cd03245 170 AMDMNSEERLKErLRQLLGDK--TLIIITHRP-SLLDLVDRIIVMDSGRIVADG 220
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
367-584 |
1.86e-21 |
|
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: 93.13 E-value: 1.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 367 LRVQnLNKHFGGLHVtrNVSFTLrEGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQ--FHAPKN---PADF 441
Cdd:cd03297 2 LCVD-IEKRLPDFTL--KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVL---NGTvlFDSRKKinlPPQQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 442 AALGLgrTFQIVQPFAAMTVEENIMVGafYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEP 521
Cdd:cd03297 75 RKIGL--VFQQYALFPHLNVRENLAFG--LKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489057211 522 RILLLDEVMAGInqtDVRRAIDLMLSIRDS----GVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQG 584
Cdd:cd03297 151 ELLLLDEPFSAL---DRALRLQLLPELKQIkknlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
369-528 |
2.78e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.44 E-value: 2.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 369 VQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGA--------DGQFHAPKNPAD 440
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGlrigylpqEPPLDDDLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 441 FAALGLGRTFQIVQPFAAM-----TVEENIM----VGAFYRHHHEKDAREAARETAWRMGLGP-LLGAEARGLTiGGLK- 509
Cdd:COG0488 81 TVLDGDAELRALEAELEELeaklaEPDEDLErlaeLQEEFEALGGWEAEARAEEILSGLGFPEeDLDRPVSELS-GGWRr 159
|
170
....*....|....*....
gi 489057211 510 RLEVARVMAMEPRILLLDE 528
Cdd:COG0488 160 RVALARALLSEPDLLLLDE 178
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
369-594 |
5.51e-21 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 92.51 E-value: 5.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 369 VQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNL--CGADGQFHAPKNPADFAAL-- 444
Cdd:PRK11264 6 VKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgdITIDTARSLSQQKGLIRQLrq 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 445 GLGRTFQIVQPFAAMTVEENIMVGAFYRHHHEKDAREA-ARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRI 523
Cdd:PRK11264 86 HVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATArARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEV 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489057211 524 LLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDPQ 594
Cdd:PRK11264 166 ILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQ 236
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
366-601 |
7.61e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 92.74 E-value: 7.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 366 ILRVQNLNKHF-GGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGqfhapknpADFAAL 444
Cdd:PRK13644 1 MIRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDT--------GDFSKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 445 -GLGRTFQIV-----QPFAAMTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMA 518
Cdd:PRK13644 73 qGIRKLVGIVfqnpeTQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 519 MEPRILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAvMSLSDRVIVLASGEVIAQGRPQDVVRDPQVveA 598
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVSL--Q 229
|
...
gi 489057211 599 YLG 601
Cdd:PRK13644 230 TLG 232
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
362-592 |
8.04e-21 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 96.02 E-value: 8.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 362 IGQDILRVQNLNKHF-----GGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPK 436
Cdd:TIGR03269 275 VGEPIIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWVDMTK 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 437 NPADF---AALGLGRTFQIVQPFAAMTVEENIMvgafyrhhhEKDAREAARETAWRMGLGPLLGA-----EARG------ 502
Cdd:TIGR03269 355 PGPDGrgrAKRYIGILHQEYDLYPHRTVLDNLT---------EAIGLELPDELARMKAVITLKMVgfdeeKAEEildkyp 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 503 --LTIGGLKRLEVARVMAMEPRILLLDE---VMAGINQTDVRRAIdlMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLAS 577
Cdd:TIGR03269 426 deLSEGERHRVALAQVLIKEPRIVILDEptgTMDPITKVDVTHSI--LKAREEMEQTFIIVSHDMDFVLDVCDRAALMRD 503
|
250
....*....|....*
gi 489057211 578 GEVIAQGRPQDVVRD 592
Cdd:TIGR03269 504 GKIVKIGDPEEIVEE 518
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
367-579 |
1.23e-20 |
|
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: 89.36 E-value: 1.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 367 LRVQNLNKHFGG--LHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKNPADFAAL 444
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 445 glgrTFQIVQPFaAMTVEENIMVGafyrhhhekdareaaretawrmglgpllgaeargltiGGLKRLEVARVMAMEPRIL 524
Cdd:cd03228 81 ----VPQDPFLF-SGTIRENILSG-------------------------------------GQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489057211 525 LLDEVMAGI---NQTDVRRAIDLMLsirdSGVSIIAIEHVMQAVMsLSDRVIVLASGE 579
Cdd:cd03228 119 ILDEATSALdpeTEALILEALRALA----KGKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
162-591 |
1.68e-20 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 95.62 E-value: 1.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 162 VWMVFRERWPSLLIVFGMLLVTLAITWAARRSRLGFYLVATRERESAARA----AGVRTVRvrliavaissaLCAMLGTF 237
Cdd:COG1132 154 VVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLqeslSGIRVVK-----------AFGREERE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 238 HAMYLTFIEpaAMFSLAFSIQIAMFALNGGLGTVAGPLLGAVLLVPITEWARASLGASALGLhgfvygLVLILVVLFMP- 316
Cdd:COG1132 223 LERFREANE--ELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVA------FILYLLRLFGPl 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 317 NGIMGAINRFVRkpqdsEETATARTEPIAAVPARAIKAPSPDRAGIGQDILRVQNLnkHF---GGLHVTRNVSFTLREGE 393
Cdd:COG1132 295 RQLANVLNQLQR-----ALASAERIFELLDEPPEIPDPPGAVPLPPVRGEIEFENV--SFsypGDRPVLKDISLTIPPGE 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 394 VLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQfhapkNPADFAALGLGRTFQIV--QPF-AAMTVEENIMVGAf 470
Cdd:COG1132 368 TVALVGPSGSGKSTLVNLLLRFYDPTSGRILI---DGV-----DIRDLTLESLRRQIGVVpqDTFlFSGTIRENIRYGR- 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 471 yRHHHEKDAREAARET-AWRM------GLGPLLGaeARGLTI-GGLK-RLEVARVMAMEPRILLLDEVMAGI-NQTD--V 538
Cdd:COG1132 439 -PDATDEEVEEAAKAAqAHEFiealpdGYDTVVG--ERGVNLsGGQRqRIAIARALLKDPPILILDEATSALdTETEalI 515
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 489057211 539 RRAID-LMlsirdSGVSIIAIEH----VMQAvmslsDRVIVLASGEVIAQGRPQDVVR 591
Cdd:COG1132 516 QEALErLM-----KGRTTIVIAHrlstIRNA-----DRILVLDDGRIVEQGTHEELLA 563
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
352-528 |
2.01e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 94.75 E-value: 2.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 352 IKAPSPDRagIGQDILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNlcgadgq 431
Cdd:COG0488 303 IRFPPPER--LGKKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVK------- 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 432 fhapknpadfaalgLGRTFQIVQpFA--------AMTVEENImvgafyrhhheKDAREAARETAWRMGLGPLL--GAEAR 501
Cdd:COG0488 374 --------------LGETVKIGY-FDqhqeeldpDKTVLDEL-----------RDGAPGGTEQEVRGYLGRFLfsGDDAF 427
|
170 180 190
....*....|....*....|....*....|..
gi 489057211 502 GLtIGGL-----KRLEVARVMAMEPRILLLDE 528
Cdd:COG0488 428 KP-VGVLsggekARLALAKLLLSPPNVLLLDE 458
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
370-593 |
2.36e-20 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 90.54 E-value: 2.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 370 QNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMI-------SGFLAPDEGTVNlcgadgqfhAPKNPADFA 442
Cdd:PRK09493 5 KNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCInkleeitSGDLIVDGLKVN---------DPKVDERLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 443 ALGLGRTFQIVQPFAAMTVEENIMVGAFY-RHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEP 521
Cdd:PRK09493 76 RQEAGMVFQQFYLFPHLTALENVMFGPLRvRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489057211 522 RILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDP 593
Cdd:PRK09493 156 KLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNP 227
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
381-591 |
3.19e-20 |
|
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: 90.24 E-value: 3.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 381 VTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQFHAPKNPADFAAlGLGRTFQIVQPFAAmT 460
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLV---DGHDLALADPAWLRR-QVGVVLQENVLFNR-S 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 461 VEENIMVG--AFYRHHHEKDAREA-ARETAWRM--GLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGINQ 535
Cdd:cd03252 92 IRDNIALAdpGMSMERVIEAAKLAgAHDFISELpeGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDY 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489057211 536 TDVRRAIDLMLSIRDsGVSIIAIEHVMQAVMSlSDRVIVLASGEVIAQGRPQDVVR 591
Cdd:cd03252 172 ESEHAIMRNMHDICA-GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLA 225
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
367-600 |
7.21e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 89.52 E-value: 7.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 367 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFL-----APDEGTVNLCGADgqFHAPKNPADF 441
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLelneeARVEGEVRLFGRN--IYSPDVDPIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 442 AALGLGRTFQIVQPFAAMTVEENIMVGAFYrHHHEKDAREAARETAWRMGLGPL-------LGAEARGLTIGGLKRLEVA 514
Cdd:PRK14267 83 VRREVGMVFQYPNPFPHLTIYDNVAIGVKL-NGLVKSKKELDERVEWALKKAALwdevkdrLNDYPSNLSGGQRQRLVIA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 515 RVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRDSgVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDP- 593
Cdd:PRK14267 162 RALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPe 240
|
....*...
gi 489057211 594 -QVVEAYL 600
Cdd:PRK14267 241 hELTEKYV 248
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
346-589 |
8.32e-20 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 92.78 E-value: 8.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 346 AVPARAIKAPSPDragiGQDILRVQNLN-KHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVN 424
Cdd:COG3845 241 EVLLRVEKAPAEP----GEVVLEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIR 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 425 LCGADgqfHAPKNPADFAALGLGRtfqIvqP--------FAAMTVEENIMVGAFYRHH-------HEKDAREAARETAWR 489
Cdd:COG3845 317 LDGED---ITGLSPRERRRLGVAY---I--PedrlgrglVPDMSVAENLILGRYRRPPfsrggflDRKAIRAFAEELIEE 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 490 MGL-GPLLGAEARGLTIGGLKRLEVARVMAMEPRILL-------LDeVMAgINQtdVRRAIdlmLSIRDSGVSIIAI--- 558
Cdd:COG3845 389 FDVrTPGPDTPARSLSGGNQQKVILARELSRDPKLLIaaqptrgLD-VGA-IEF--IHQRL---LELRDAGAAVLLIsed 461
|
250 260 270
....*....|....*....|....*....|...
gi 489057211 559 --EhvmqaVMSLSDRVIVLASGEVIAQGRPQDV 589
Cdd:COG3845 462 ldE-----ILALSDRIAVMYEGRIVGEVPAAEA 489
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
367-601 |
1.02e-19 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 89.28 E-value: 1.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 367 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKNpadfAALGL 446
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKE----VARRI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 447 GRTFQIVQPFAAMTVEENIMVGAF--------YRHHHEKDAREAARETawrmGLGPLLGAEARGLTIGGLKRLEVARVMA 518
Cdd:PRK10253 84 GLLAQNATTPGDITVQELVARGRYphqplftrWRKEDEEAVTKAMQAT----GITHLADQSVDTLSGGQRQRAWIAMVLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 519 MEPRILLLDEVMAGInqtDVRRAIDLMLSI----RDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVrDPQ 594
Cdd:PRK10253 160 QETAIMLLDEPTTWL---DISHQIDLLELLselnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIV-TAE 235
|
....*..
gi 489057211 595 VVEAYLG 601
Cdd:PRK10253 236 LIERIYG 242
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
366-596 |
1.27e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 89.09 E-value: 1.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 366 ILRVQNLNKHF-GGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKNPADFAAL 444
Cdd:PRK13652 3 LIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 445 GLGRT-FQIVQPfaamTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRI 523
Cdd:PRK13652 83 VFQNPdDQIFSP----TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489057211 524 LLLDEVMAGINQTDVRRAIDLMLSIRDS-GVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDPQVV 596
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPDLL 232
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
381-590 |
2.03e-19 |
|
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: 87.67 E-value: 2.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 381 VTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADgqfhapknPADFAALGLGRTFQIVQPFAAM- 459
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHD--------VRDYTLASLRRQIGLVSQDVFLf 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 460 --TVEENIMVGAfyRHHHEKDAREAAR-----ETAWRM--GLGPLLGaeARGLTI-GGLK-RLEVARVMAMEPRILLLDE 528
Cdd:cd03251 89 ndTVAENIAYGR--PGATREEVEEAARaanahEFIMELpeGYDTVIG--ERGVKLsGGQRqRIAIARALLKDPPILILDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489057211 529 VMAGI-NQTD--VRRAIDLMLSIRDSgvsiIAIEHVMQAVMSlSDRVIVLASGEVIAQGRPQDVV 590
Cdd:cd03251 165 ATSALdTESErlVQAALERLMKNRTT----FVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEELL 224
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
367-560 |
2.11e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 86.85 E-value: 2.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 367 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGqfHAPKNPADFAALGL 446
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI--DDPDVAEACHYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 447 GRTFQivqpfAAMTVEENIMVGAFYRHHHEKDAREAARetawRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLL 526
Cdd:PRK13539 81 RNAMK-----PALTVAENLEFWAAFLGGEELDIAAALE----AVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWIL 151
|
170 180 190
....*....|....*....|....*....|....
gi 489057211 527 DEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEH 560
Cdd:PRK13539 152 DEPTAALDAAAVALFAELIRAHLAQGGIVIAATH 185
|
|
| TM_PBP1_LivH_like |
cd06582 |
Transmembrane subunit (TM) of Escherichia coli LivH and related proteins. LivH is one of two ... |
51-320 |
2.75e-19 |
|
Transmembrane subunit (TM) of Escherichia coli LivH and related proteins. LivH is one of two TMs of the E. coli LIV-1/LS transporter, a Periplasmic Binding Protein (PBP)-dependent ATP-Binding Cassette (ABC) transporter involved in the uptake of branched-chain amino acids (AAs). These types of transporters generally bind type 1 PBPs. PBP-dependent ABC transporters consist of a PBP, two TMs, and two cytoplasmic ABCs, and are mainly involved in importing solutes from the environment. The solute is captured by the PBP, which delivers it to a gated translocation pathway formed by the two TMs. The two ABCs bind and hydrolyze ATP and drive the transport reaction. E. coli LivH forms a heterodimer with another TM, LivM, to generate the transmembrane pore. LivM is not included in this subgroup. The LIV-1/LS transporter is comprised of two TMs (LivM and LivH), two ABCs (LivG and LivF), and one of two alternative PBPs, LivJ (LIV-BP) or LivK (LS-BP). In addition to transporting branched-chain AAs including leucine, isoleucine and valine, the E. coli LIV-1/LS transporter is involved in the uptake of the aromatic AA, phenylalanine.
Pssm-ID: 119324 [Multi-domain] Cd Length: 272 Bit Score: 88.26 E-value: 2.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 51 CLFAALSTAWNIVGGFAGQMSLGHAVFYGIGGYTGVILFN-MGISPWFSMFIGTFIAALVGMVISYPCFRL---KGPFYS 126
Cdd:cd06582 6 AIYALIALGLTLIFGVTGVINFAHGEFYMLGAYVAYTLLVaLGLPFWLALLLALLVAALLGVLLERLVLRPlrgAPLLTL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 127 LASIAFLEVFRVLALHFGWLTGGATGLMIqLKLGWVWMVFRERWPSLLIVFGMLLVTLAITWAARRSRLGFYLVATRERE 206
Cdd:cd06582 86 LITFGGLLILLQGLLLIFGGDPRVPPPPL-LSGSVELGGVTIPPYRLFIIAVALVLLAALYLFLRRTRLGRAIRAVAQNP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 207 SAARAAGVRTVRVRLIAVAISSALCAMLGTFHAMYlTFIEPAAMFSLAFSIQIAmfALNGGLGTVAGPLLGAVLLVPITE 286
Cdd:cd06582 165 EAARLLGINVRRVFALTFALGAALAGLAGVLLAPI-TGVSPTMGLLLLLKAFAA--VVLGGLGSIPGAVVGGLLLGLAES 241
|
250 260 270
....*....|....*....|....*....|....
gi 489057211 287 WARASLGASALGLHGFVyglVLILVVLFMPNGIM 320
Cdd:cd06582 242 LAAAYLSSGYKDAVAFV---LLILVLLVRPQGLF 272
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
384-597 |
3.20e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 88.26 E-value: 3.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 384 NVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKNPADFAALGLGRTFQI--VQPFAAmTV 461
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIRKKVGLVFQFpeSQLFEE-TV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 462 EENIMVGAFYRHHHEKDAREAARETAWRMGLGP-LLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGINQTDVRR 540
Cdd:PRK13649 104 LKDVAFGPQNFGVSQEEAEALAREKLALVGISEsLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKE 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489057211 541 AIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDPQVVE 597
Cdd:PRK13649 184 LMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQDVDFLE 240
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
366-581 |
3.26e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 88.99 E-value: 3.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 366 ILRVQNLNKHF----------GGL-----------HVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVN 424
Cdd:COG4586 1 IIEVENLSKTYrvyekepglkGALkglfrreyrevEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 425 LCGadgqfHAP-KNPADFAalglgRTFQIV-----QPFAAMTVEENimvgaFYRHHH-----EKDAREAARETAWRMGLG 493
Cdd:COG4586 81 VLG-----YVPfKRRKEFA-----RRIGVVfgqrsQLWWDLPAIDS-----FRLLKAiyripDAEYKKRLDELVELLDLG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 494 PLLGAEARGLTIGGLKRLEVArvMAM--EPRILLLDE------VMAginQTDVRRAIDLMlsIRDSGVSIIAIEHVMQAV 565
Cdd:COG4586 146 ELLDTPVRQLSLGQRMRCELA--AALlhRPKILFLDEptigldVVS---KEAIREFLKEY--NRERGTTILLTSHDMDDI 218
|
250
....*....|....*.
gi 489057211 566 MSLSDRVIVLASGEVI 581
Cdd:COG4586 219 EALCDRVIVIDHGRII 234
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
366-594 |
3.38e-19 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 88.98 E-value: 3.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 366 ILRVQNLNKHF----GGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQfhapknpaDF 441
Cdd:COG1135 1 MIELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLV---DGV--------DL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 442 AAL---GLgRTFQ-----IVQPFAAM---TVEENImvgAF--YRHHHEKDAREA-AREtawrmgLGPLLGAEARG----- 502
Cdd:COG1135 70 TALserEL-RAARrkigmIFQHFNLLssrTVAENV---ALplEIAGVPKAEIRKrVAE------LLELVGLSDKAdayps 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 503 -LTiGGLK-RLEVARVMAMEPRILLLDEVMAGIN-QTDvrRAI-DLMLSIRDS-GVSIIAIEHVMQAVMSLSDRVIVLAS 577
Cdd:COG1135 140 qLS-GGQKqRVGIARALANNPKVLLCDEATSALDpETT--RSIlDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLEN 216
|
250
....*....|....*..
gi 489057211 578 GEVIAQGRPQDVVRDPQ 594
Cdd:COG1135 217 GRIVEQGPVLDVFANPQ 233
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
364-591 |
4.73e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 87.76 E-value: 4.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 364 QDILRVQNLNKHFGGL--HVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQFHAPKNPADF 441
Cdd:PRK13635 3 EEIIRVEHISFRYPDAatYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITV---GGMVLSEETVWDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 442 AALgLGRTFQivQP---FAAMTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMA 518
Cdd:PRK13635 80 RRQ-VGMVFQ--NPdnqFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489057211 519 MEPRILLLDEVMAGInqtDVRRAIDLMLSIRD----SGVSIIAIEHVMQAVMSlSDRVIVLASGEVIAQGRPQDVVR 591
Cdd:PRK13635 157 LQPDIIILDEATSML---DPRGRREVLETVRQlkeqKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFK 229
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
370-580 |
5.43e-19 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 85.92 E-value: 5.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 370 QNLNKHFGGLHVT-RNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQfHAPKNPADFAALGLGR 448
Cdd:cd03292 4 INVTKTYPNGTAAlDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVS-DLRGRAIPYLRRKIGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 449 TFQIVQPFAAMTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDE 528
Cdd:cd03292 83 VFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489057211 529 VMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEV 580
Cdd:cd03292 163 PTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
384-599 |
5.91e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 87.48 E-value: 5.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 384 NVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKNPADFAALGLGRTFQIVQP-FAAMTVE 462
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQFPESqLFEETVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 463 ENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEAR-GLTIGGLKRLEVARVMAMEPRILLLDEVMAGINQTDVRRA 541
Cdd:PRK13643 104 KDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPfELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEM 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489057211 542 IDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDPQVVEAY 599
Cdd:PRK13643 184 MQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEVDFLKAH 241
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
384-589 |
7.68e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 87.09 E-value: 7.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 384 NVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQFHAPKNPADFAALgLGRTFQivQP---FAAMT 460
Cdd:PRK13650 25 DVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIII---DGDLLTEENVWDIRHK-IGMVFQ--NPdnqFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 461 VEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGINQTDVRR 540
Cdd:PRK13650 99 VEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489057211 541 AIDLMLSIRDS-GVSIIAIEHVMQAVmSLSDRVIVLASGEVIAQGRPQDV 589
Cdd:PRK13650 179 LIKTIKGIRDDyQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPREL 227
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
381-597 |
8.95e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 86.78 E-value: 8.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 381 VTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKNPADFAAlGLGRTFQivQP---FA 457
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKTVWDIRE-KVGIVFQ--NPdnqFV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 458 AMTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGINQTD 537
Cdd:PRK13640 99 GATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAG 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489057211 538 VRRAIDLMLSI-RDSGVSIIAIEH-VMQAVMslSDRVIVLASGEVIAQGRPQDVVRDPQVVE 597
Cdd:PRK13640 179 KEQILKLIRKLkKKNNLTVISITHdIDEANM--ADQVLVLDDGKLLAQGSPVEIFSKVEMLK 238
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
383-584 |
1.15e-18 |
|
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: 84.52 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 383 RNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAP--DEGTVNLcgaDGQfhaPKNPADFAALgLGRTFQIVQPFAAMT 460
Cdd:cd03213 26 KNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLI---NGR---PLDKRSFRKI-IGYVPQDDILHPTLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 461 VEENIMVgafyrhhhekdareaaretawrmglgpllGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGInqtDVRR 540
Cdd:cd03213 99 VRETLMF-----------------------------AAKLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGL---DSSS 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489057211 541 AIDLMLSIR---DSGVSIIAIEHVMQAVM-SLSDRVIVLASGEVIAQG 584
Cdd:cd03213 147 ALQVMSLLRrlaDTGRTIICSIHQPSSEIfELFDKLLLLSQGRVIYFG 194
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
367-584 |
1.38e-18 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 85.45 E-value: 1.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 367 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKNPADFAAL-- 444
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTPSDKAIRELrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 445 GLGRTFQIVQPFAAMTVEENIM------VGAfyrhhHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMA 518
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNLIeapcrvLGL-----SKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489057211 519 MEPRILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQG 584
Cdd:PRK11124 158 MEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQG 223
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
366-594 |
2.45e-18 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 85.23 E-value: 2.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 366 ILRVQNLNKHF---GGL----HV--TRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQfhaPK 436
Cdd:PRK15112 4 LLEVRNLSKTFryrTGWfrrqTVeaVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLI---DDH---PL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 437 NPADFAALGlGRTFQIVQ-PFAAMTVEENI--MVGAFYRHHHEKD--AREAARETAWRM-GLGP-LLGAEARGLTIGGLK 509
Cdd:PRK15112 78 HFGDYSYRS-QRIRMIFQdPSTSLNPRQRIsqILDFPLRLNTDLEpeQREKQIIETLRQvGLLPdHASYYPHMLAPGQKQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 510 RLEVARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRDS-GVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQD 588
Cdd:PRK15112 157 RLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTAD 236
|
....*.
gi 489057211 589 VVRDPQ 594
Cdd:PRK15112 237 VLASPL 242
|
|
| livM |
PRK11301 |
leucine/isoleucine/valine transporter permease subunit; Provisional |
61-320 |
2.95e-18 |
|
leucine/isoleucine/valine transporter permease subunit; Provisional
Pssm-ID: 236896 [Multi-domain] Cd Length: 419 Bit Score: 87.33 E-value: 2.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 61 NIVGGFAGQMSLGHAVFYGIGGYTGVILFN-MGISPWFSMFIGTFIAALVGMVISYPCFRLKGPFYSLASIAFLEVFRVL 139
Cdd:PRK11301 129 NVVVGLAGLLDLGYVGFYAVGAYTYALLNHyYGLGFWECLPIAGLMAALFGFLLGFPVLRLRGDYLAIVTLGFGEIIRIL 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 140 ALHFGWLTGGATGLMIQLKLGWVWMVFRER-----W------------PSLLIVF----GMLLVTLAITWAAR--RSRLG 196
Cdd:PRK11301 209 LLNNTEITGGPNGISQIPKPTLFGLEFSRTareggWdtfheffglkydPSDRVIFlylvALLLVVLTLFVINRllRMPLG 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 197 FYLVATRERESAARAAGVRTVRVRLIAVAISSALCAMLGTFHAMYLTFIEPAAmFSLAFSIQIAMFALNGGLGTVAGPLL 276
Cdd:PRK11301 289 RAWEALREDEIACRSLGLNPTRIKLSAFTIGAAFAGFAGTFFAARQGFVSPES-FTFIESAFILAIVVLGGMGSQFGVIL 367
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 489057211 277 GAVLLVPITEWARASLGASALglhgfVYGLVLILVVLFMPNGIM 320
Cdd:PRK11301 368 AAILLVVLPELMRDFNEYRML-----MFGLLMVLMMIWRPQGLL 406
|
|
| LivH |
COG0559 |
Branched-chain amino acid ABC-type transport system, permease component [Amino acid transport ... |
72-321 |
4.25e-18 |
|
Branched-chain amino acid ABC-type transport system, permease component [Amino acid transport and metabolism];
Pssm-ID: 440325 [Multi-domain] Cd Length: 290 Bit Score: 85.11 E-value: 4.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 72 LGHAVFYGIGGYTGVILFN-MGISPWFSMFIGTFIAALVGMVISYPCFRlkgPFYS-------LASIAFLEVFRVLALHF 143
Cdd:COG0559 37 FAHGEFVMLGAYVAYTLATlLGLPLWLALLLAVLVAALLGVLLERLVIR---PLRGapplallLATIGLSLVLQGLVLLI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 144 gWltgGATGLMIQLKLGWVWMVFRERWPS--LLIVFGMLLVTLAITWAARRSRLGFYLVATRERESAARAAGVRTVRVRL 221
Cdd:COG0559 114 -F---GADPRSFPALLSGSVELGGVSIPAyrLFIIVVALVLLAALWLFLRRTRLGLAMRAVAQNREAARLMGINVDRVIA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 222 IAVAISSALCAMLGTFHAMYlTFIEPAAMFSLAFSIQIAmfALNGGLGTVAGPLLGAVLLVPITEWARASLGASALGLHG 301
Cdd:COG0559 190 LTFALGAALAGLAGVLLAPI-YSVSPTMGFLLGLKAFAA--VVLGGLGSIPGAVVGGLLLGLAESLGAAYLPSGYKDVVA 266
|
250 260
....*....|....*....|
gi 489057211 302 FVyglVLILVVLFMPNGIMG 321
Cdd:COG0559 267 FV---LLILVLLVRPQGLFG 283
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
384-597 |
4.88e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 84.71 E-value: 4.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 384 NVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADgqFHAPKNPADFAALGLGRTFQI--VQPFAAmTV 461
Cdd:PRK13637 25 NVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVD--ITDKKVKLSDIRKKVGLVFQYpeYQLFEE-TI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 462 EENIMVGAFYRHHHEKDAREAARETAWRMGLG--PLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGInqtDVR 539
Cdd:PRK13637 102 EKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGL---DPK 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489057211 540 RAIDLMLSIRD----SGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDPQVVE 597
Cdd:PRK13637 179 GRDEILNKIKElhkeYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEVETLE 240
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
384-603 |
4.89e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 84.75 E-value: 4.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 384 NVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQ---------------FHAPKNpadfaalglgr 448
Cdd:PRK13633 28 DVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSdeenlwdirnkagmvFQNPDN----------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 449 tfQIVqpfaAMTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDE 528
Cdd:PRK13633 97 --QIV----ATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 529 VMAGINQTDVRRAIDLMLSI-RDSGVSIIAIEHVMQAVMSlSDRVIVLASGEVIAQGRPQDVVRD-----------PQVV 596
Cdd:PRK13633 171 PTAMLDPSGRREVVNTIKELnKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKEvemmkkigldvPQVT 249
|
....*....
gi 489057211 597 E-AY-LGKE 603
Cdd:PRK13633 250 ElAYeLKKE 258
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
366-598 |
5.23e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 84.40 E-value: 5.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 366 ILRVQNLnkHF---GGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGadgQFHAPKNPADFA 442
Cdd:PRK13647 4 IIEVEDL--HFrykDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMG---REVNAENEKWVR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 443 ALgLGRTFQIV--QPFAaMTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAME 520
Cdd:PRK13647 79 SK-VGLVFQDPddQVFS-STVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489057211 521 PRILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQdVVRDPQVVEA 598
Cdd:PRK13647 157 PDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKS-LLTDEDIVEQ 233
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
368-581 |
5.27e-18 |
|
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: 82.69 E-value: 5.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 368 RVQNLN-KHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGadgqfhapknpADFAALGL 446
Cdd:cd03226 1 RIENISfSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG-----------KPIKAKER 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 447 GRTFQIV------QPFAAmTVEENIMVGAfyrhhHEKDAREAARETAWR-MGLGPLLGAEARGLTIGGLKRLEVARVMAM 519
Cdd:cd03226 70 RKSIGYVmqdvdyQLFTD-SVREELLLGL-----KELDAGNEQAETVLKdLDLYALKERHPLSLSGGQKQRLAIAAALLS 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489057211 520 EPRILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVI 581
Cdd:cd03226 144 GKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
364-587 |
6.88e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 83.91 E-value: 6.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 364 QDILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPD---EGTVNLCGADGQfHAPKNPAD 440
Cdd:PRK09984 2 QTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDksaGSHIELLGRTVQ-REGRLARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 441 F--AALGLGRTFQIVQPFAAMTVEENIMVGA-----FYR---HHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKR 510
Cdd:PRK09984 81 IrkSRANTGYIFQQFNLVNRLSVLENVLIGAlgstpFWRtcfSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489057211 511 LEVARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSI-RDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQ 587
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQ 238
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
366-603 |
1.19e-17 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 86.14 E-value: 1.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 366 ILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGfLAPD---EGTVNLCGADGQFHapkNPADFA 442
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHgtyEGEIIFEGEELQAS---NIRDTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 443 ALGLGRTFQIVQPFAAMTVEENIMVGAFYRHHHEKD-AREAARETAW--RMGLGPLLGAEARGLTIGGLKRLEVARVMAM 519
Cdd:PRK13549 81 RAGIAIIHQELALVKELSVLENIFLGNEITPGGIMDyDAMYLRAQKLlaQLKLDINPATPVGNLGLGQQQLVEIAKALNK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 520 EPRILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQgRPQDVVRDPQVVEAY 599
Cdd:PRK13549 161 QARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGT-RPAAGMTEDDIITMM 239
|
....
gi 489057211 600 LGKE 603
Cdd:PRK13549 240 VGRE 243
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
367-580 |
1.70e-17 |
|
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: 80.34 E-value: 1.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 367 LRVQNLNKHFGGLH--VTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKNPADFaal 444
Cdd:cd03246 1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDH--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 445 gLGRTFQIVQPFAAmTVEENIMVGafyrhhhekdareaaretawrmglgpllgaeargltiGGLKRLEVARVMAMEPRIL 524
Cdd:cd03246 78 -VGYLPQDDELFSG-SIAENILSG-------------------------------------GQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489057211 525 LLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMqAVMSLSDRVIVLASGEV 580
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
366-578 |
1.84e-17 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 82.44 E-value: 1.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 366 ILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGadgqfhapkNPADFAALG 445
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDG---------KPVEGPGAE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 446 LGRTFQIVQPFAAMTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGpllGAEAR---GLTIGGLKRLEVARVMAMEPR 522
Cdd:PRK11248 72 RGVVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLE---GAEKRyiwQLSGGQRQRVGIARALAANPQ 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489057211 523 ILLLDEVMAGINQTDVRRAIDLMLSI-RDSGVSIIAIEHVMQAVMSLSDRVIVLASG 578
Cdd:PRK11248 149 LLLLDEPFGALDAFTREQMQTLLLKLwQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
364-602 |
2.40e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 85.06 E-value: 2.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 364 QDILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKnpaDFAA 443
Cdd:PRK10762 2 QALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPK---SSQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 444 LGLGRTFQIVQPFAAMTVEENIMVG-----AFYRHHHEKDAREAARETAwRMGLG----PLLGAeargLTIGGLKRLEVA 514
Cdd:PRK10762 79 AGIGIIHQELNLIPQLTIAENIFLGrefvnRFGRIDWKKMYAEADKLLA-RLNLRfssdKLVGE----LSIGEQQMVEIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 515 RVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDpQ 594
Cdd:PRK10762 154 KVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLTED-S 232
|
....*...
gi 489057211 595 VVEAYLGK 602
Cdd:PRK10762 233 LIEMMVGR 240
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
369-586 |
2.43e-17 |
|
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: 86.61 E-value: 2.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 369 VQNLNKHF--GGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQfhapkNPADFAALGL 446
Cdd:TIGR01257 931 VKNLVKIFepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIE-----TNLDAVRQSL 1005
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 447 GRTFQIVQPFAAMTVEENIMvgaFYRHHHEKDAREAARETAWRM---GLGPLLGAEARGLTIGGLKRLEVARVMAMEPRI 523
Cdd:TIGR01257 1006 GMCPQHNILFHHLTVAEHIL---FYAQLKGRSWEEAQLEMEAMLedtGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKV 1082
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489057211 524 LLLDEVMAGINQTDVRRAIDLMLSIRdSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRP 586
Cdd:TIGR01257 1083 VVLDEPTSGVDPYSRRSIWDLLLKYR-SGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
366-601 |
2.56e-17 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 82.57 E-value: 2.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 366 ILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLaPDEGTVNLCGADGQFHAPKNP-ADFAAL 444
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDL-TGGGAPRGARVTGDVTLNGEPlAAIDAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 445 GLGRTF----QIVQPFAAMTVEENIMVGafyRHHHEKDAREAARET---AW----RMGLGPLLGAEARGLTIGGLKRLEV 513
Cdd:PRK13547 80 RLARLRavlpQAAQPAFAFSAREIVLLG---RYPHARRAGALTHRDgeiAWqalaLAGATALVGRDVTTLSGGELARVQF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 514 ARVMAM---------EPRILLLDEVMAGINQTDVRRAIDLMLSI-RDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQ 583
Cdd:PRK13547 157 ARVLAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLaRDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAH 236
|
250
....*....|....*...
gi 489057211 584 GRPQDVVRdPQVVEAYLG 601
Cdd:PRK13547 237 GAPADVLT-PAHIARCYG 253
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
366-581 |
2.80e-17 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 84.84 E-value: 2.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 366 ILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGfLAPD---EGTVNLCGADGQFhapKNPADFA 442
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG-VYPHgsyEGEILFDGEVCRF---KDIRDSE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 443 ALGlgrtfqIV---QPFA---AMTVEENIMVGafyrhhHEK------DAREAARETA---WRMGLGPLLGAEARGLTIGG 507
Cdd:NF040905 77 ALG------IViihQELAlipYLSIAENIFLG------NERakrgviDWNETNRRARellAKVGLDESPDTLVTDIGVGK 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489057211 508 LKRLEVARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVI 581
Cdd:NF040905 145 QQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTI 218
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
335-600 |
3.34e-17 |
|
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: 84.88 E-value: 3.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 335 ETATARTEP--IAAVPARAIKAPSPDRA-GIGQDILRVQNLNK-HFGGLHVTR--NVSFTLREGEVLGLIGPNGAGKTTL 408
Cdd:TIGR02633 223 KDMSTMSEDdiITMMVGREITSLYPHEPhEIGDVILEARNLTCwDVINPHRKRvdDVSFSLRRGEILGVAGLVGAGRTEL 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 409 FNMISG-FLAPDEGTVNLcgaDGQFHAPKNPADFAALGLG-----RTFQIVQPfaAMTVEENIMVGAFYRHHHEKDAREA 482
Cdd:TIGR02633 303 VQALFGaYPGKFEGNVFI---NGKPVDIRNPAQAIRAGIAmvpedRKRHGIVP--ILGVGKNITLSVLKSFCFKMRIDAA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 483 ARETAWRMGLGPL-LGAEARGLTIGGL-----KRLEVARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSII 556
Cdd:TIGR02633 378 AELQIIGSAIQRLkVKTASPFLPIGRLsggnqQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAII 457
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 489057211 557 AIEHVMQAVMSLSDRVIVLASGEVIAqgrpqDVVRD----PQVVEAYL 600
Cdd:TIGR02633 458 VVSSELAEVLGLSDRVLVIGEGKLKG-----DFVNHaltqEQVLAAAL 500
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
364-600 |
4.06e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 81.50 E-value: 4.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 364 QDILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGF--LAPD---EGTVNLCGADgqfhAPKNP 438
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLieLYPEarvSGEVYLDGQD----IFKMD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 439 ADFAALGLGRTFQIVQPFAAMTVEENIMVGaFYRHHHEKDAREAARETAWRMGLGPL-------LGAEARGLTIGGLKRL 511
Cdd:PRK14247 77 VIELRRRVQMVFQIPNPIPNLSIFENVALG-LKLNRLVKSKKELQERVRWALEKAQLwdevkdrLDAPAGKLSGGQQQRL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 512 EVARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRDSgVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVR 591
Cdd:PRK14247 156 CIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFT 234
|
250
....*....|.
gi 489057211 592 DP--QVVEAYL 600
Cdd:PRK14247 235 NPrhELTEKYV 245
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
364-563 |
4.09e-17 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 80.59 E-value: 4.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 364 QDILRVQNLNKHFGG----LHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKNPA 439
Cdd:PRK10584 4 ENIVEVHHLKKSVGQgeheLSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 440 DFAALGLGRTFQIVQPFAAMTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAM 519
Cdd:PRK10584 84 KLRAKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNG 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489057211 520 EPRILLLDEVMAGINQTDVRRAIDLMLSI-RDSGVSIIAIEHVMQ 563
Cdd:PRK10584 164 RPDVLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHDLQ 208
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
363-600 |
7.79e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 80.48 E-value: 7.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 363 GQDILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQ-FHAPKNPADF 441
Cdd:PRK14246 7 AEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKV---DGKvLYFGKDIFQI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 442 AALGL----GRTFQIVQPFAAMTVEENIMVGafYRHHHEKDAREAAR---ETAWRMGLGP----LLGAEARGLTIGGLKR 510
Cdd:PRK14246 84 DAIKLrkevGMVFQQPNPFPHLSIYDNIAYP--LKSHGIKEKREIKKiveECLRKVGLWKevydRLNSPASQLSGGQQQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 511 LEVARVMAMEPRILLLDEVMAGINQTDvRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVV 590
Cdd:PRK14246 162 LTIARALALKPKVLLMDEPTSMIDIVN-SQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIF 240
|
250
....*....|..
gi 489057211 591 RDP--QVVEAYL 600
Cdd:PRK14246 241 TSPknELTEKYV 252
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
336-575 |
9.15e-17 |
|
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: 83.49 E-value: 9.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 336 TATARTEPIAAVPARAiKAPSPDRAGIGQD---ILRVQNLNKHFGG-LHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNM 411
Cdd:TIGR02857 289 DGVAAAEALFAVLDAA-PRPLAGKAPVTAApasSLEFSGVSVAYPGrRPALRPVSFTVPPGERVALVGPSGAGKSTLLNL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 412 ISGFLAPDEGTVNLCGADgqfhapknPADFAALGLGRTFQIV--QPFA-AMTVEENImvgAFYRhhheKDAREAA-RETA 487
Cdd:TIGR02857 368 LLGFVDPTEGSIAVNGVP--------LADADADSWRDQIAWVpqHPFLfAGTIAENI---RLAR----PDASDAEiREAL 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 488 WRMGLGPL-----------LGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRdSGVSII 556
Cdd:TIGR02857 433 ERAGLDEFvaalpqgldtpIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA-QGRTVL 511
|
250
....*....|....*....
gi 489057211 557 AIEHVMqAVMSLSDRVIVL 575
Cdd:TIGR02857 512 LVTHRL-ALAALADRIVVL 529
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
373-589 |
1.24e-16 |
|
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: 79.19 E-value: 1.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 373 NKHFG---GLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQfhaPKNPADFAAL--GLG 447
Cdd:cd03254 7 NVNFSydeKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILI---DGI---DIRDISRKSLrsMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 448 RTFQIVQPFAAmTVEENIMVGAFYrhHHEKDAREAARETAWRM-------GLGPLLGAEARGLTIGGLKRLEVARVMAME 520
Cdd:cd03254 81 VVLQDTFLFSG-TIMENIRLGRPN--ATDEEVIEAAKEAGAHDfimklpnGYDTVLGENGGNLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489057211 521 PRILLLDEVMAGIN---QTDVRRAidlMLSIRDSGVSIIaIEHVMQAVMSlSDRVIVLASGEVIAQGRPQDV 589
Cdd:cd03254 158 PKILILDEATSNIDtetEKLIQEA---LEKLMKGRTSII-IAHRLSTIKN-ADKILVLDDGKIIEEGTHDEL 224
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
366-589 |
1.37e-16 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 79.67 E-value: 1.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 366 ILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVnlcgadgqFHAPKNPADFAALG 445
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTV--------FLGDKPISMLSSRQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 446 LGRTF-----QIVQPfAAMTVEENIMVG-AFYRHHHEKDAREAARETAWRM---GLGPLLGAEARGLTIGGLKRLEVARV 516
Cdd:PRK11231 74 LARRLallpqHHLTP-EGITVRELVAYGrSPWLSLWGRLSAEDNARVNQAMeqtRINHLADRRLTDLSGGQRQRAFLAMV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489057211 517 MAMEPRILLLDEVMAGInqtDVRRAIDLMLSIR---DSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDV 589
Cdd:PRK11231 153 LAQDTPVVLLDEPTTYL---DINHQVELMRLMRelnTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEV 225
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
362-603 |
1.55e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 82.67 E-value: 1.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 362 IGQDILRVQNLNK-HFGGLHVTR--NVSFTLREGEVLGLIGPNGAGKTTLFNMISG-FLAPDEGTVNLcgaDGQFHAPKN 437
Cdd:PRK13549 255 IGEVILEVRNLTAwDPVNPHIKRvdDVSFSLRRGEILGIAGLVGAGRTELVQCLFGaYPGRWEGEIFI---DGKPVKIRN 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 438 PADFAALGLG------RTFQIVqpfAAMTVEENIMVGA---FYRHHHEKDARE--AARETAWRMGL---GPLLgAEARgL 503
Cdd:PRK13549 332 PQQAIAQGIAmvpedrKRDGIV---PVMGVGKNITLAAldrFTGGSRIDDAAElkTILESIQRLKVktaSPEL-AIAR-L 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 504 TIGGLKRLEVARVMAMEPRILLLDEVMAGInqtDV--RRAI-DLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEV 580
Cdd:PRK13549 407 SGGNQQKAVLAKCLLLNPKILILDEPTRGI---DVgaKYEIyKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
250 260
....*....|....*....|....*..
gi 489057211 581 ----IAQGRPQDvvrdpQVVEAYLGKE 603
Cdd:PRK13549 484 kgdlINHNLTQE-----QVMEAALRSE 505
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
380-590 |
1.57e-16 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 79.24 E-value: 1.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 380 HVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADgqfHAPKNPADFAALGLgrtFQIVQPFAAM 459
Cdd:PRK10771 13 HLPMRFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD---HTTTPPSRRPVSML---FQENNLFSHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 460 TVEENIMVGAF--YRHHHEKdaREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAginqtd 537
Cdd:PRK10771 87 TVAQNIGLGLNpgLKLNAAQ--REKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFS------ 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489057211 538 vrrAID-----LMLSI-----RDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVV 590
Cdd:PRK10771 159 ---ALDpalrqEMLTLvsqvcQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELL 218
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
385-599 |
1.60e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 79.50 E-value: 1.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 385 VSFTLREGEVLGLIGPNGAGKTTLFNMISGfLAPDEGTVNLCGadgqfhapKNPADFAALGLGR-----TFQIVQPFaAM 459
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLNG--------RPLSDWSAAELARhraylSQQQSPPF-AM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 460 TVEENImvgAFYRHHHEKDA--REAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAM-------EPRILLLDEVM 530
Cdd:COG4138 85 PVFQYL---ALHQPAGASSEavEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489057211 531 AGInqtDVR--RAIDLMLS-IRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDPQVVEAY 599
Cdd:COG4138 162 NSL---DVAqqAALDRLLReLCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPENLSEVF 230
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
381-588 |
1.94e-16 |
|
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: 79.12 E-value: 1.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 381 VTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQfhapkNPADFAALGLGRTFQIVQ--P--F 456
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILL---DGV-----DIRDLNLRWLRSQIGLVSqePvlF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 457 aAMTVEENIMVGAFYRhhHEKDAREAARE-------TAWRMGLGPLLGaeARGLTI-GGLK-RLEVARVMAMEPRILLLD 527
Cdd:cd03249 90 -DGTIAENIRYGKPDA--TDEEVEEAAKKanihdfiMSLPDGYDTLVG--ERGSQLsGGQKqRIAIARALLRNPKILLLD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489057211 528 EVMAGI-NQTD--VRRAID-LMLsirdsGVSIIAIEHVMQAVMSlSDRVIVLASGEVIAQGRPQD 588
Cdd:cd03249 165 EATSALdAESEklVQEALDrAMK-----GRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDE 223
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
367-592 |
1.96e-16 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 77.95 E-value: 1.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 367 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFlaPD----EGTVNLcgaDGQFHAPKNPADFA 442
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH--PKyevtEGEILF---KGEDITDLPPEERA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 443 ALGLGRTFQIVQPFAAMTVEEnimvgaFYRHHHEkdareaaretawrmglgpllgaearGLTIGGLKRLEVARVMAMEPR 522
Cdd:cd03217 76 RLGIFLAFQYPPEIPGVKNAD------FLRYVNE-------------------------GFSGGEKKRNEILQLLLLEPD 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489057211 523 ILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQ-AVMSLSDRVIVLASGEVIAQGrPQDVVRD 592
Cdd:cd03217 125 LAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRlLDYIKPDRVHVLYDGRIVKSG-DKELALE 194
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
367-423 |
2.03e-16 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 76.33 E-value: 2.03e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 489057211 367 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTV 423
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV 57
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
385-599 |
2.45e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 78.82 E-value: 2.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 385 VSFTLREGEVLGLIGPNGAGKTTLFNMISGFLaPDEGTVNLCGAD-GQFHAPKnpadfaaLGLGRTF--QIVQPFAAMTV 461
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPlEAWSAAE-------LARHRAYlsQQQTPPFAMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 462 EENImvgAFYRHH--HEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKR-------LEVARVMAMEPRILLLDEVMAG 532
Cdd:PRK03695 87 FQYL---TLHQPDktRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRvrlaavvLQVWPDINPAGQLLLLDEPMNS 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 533 InqtDV--RRAIDLMLS-IRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDPQVVEAY 599
Cdd:PRK03695 164 L---DVaqQAALDRLLSeLCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVF 230
|
|
| AraH |
COG1172 |
Ribose/xylose/arabinose/galactoside ABC-type transport system, permease component ... |
84-314 |
2.55e-16 |
|
Ribose/xylose/arabinose/galactoside ABC-type transport system, permease component [Carbohydrate transport and metabolism];
Pssm-ID: 440785 Cd Length: 322 Bit Score: 80.15 E-value: 2.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 84 TGVILFNMGISPWFSMFIGTFIAALVGMVISYPCFRLKGP-FysLASIAFLEVFRVLALhfgWLTGGATglmIQLKLGWV 162
Cdd:COG1172 86 AALLLVALGLPILLAILLALLVGALLGLLNGLLVAKLRIPpF--IVTLGTMFIARGLAL---LLTGGRP---ISGLPDAF 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 163 WMVFRERWPSL-LIVFGMLLVTLAITWAARRSRLGFYLVATRERESAARAAGVRTVRVRLIAVAISSALCAMLGTFHAMY 241
Cdd:COG1172 158 RALGQGSLLGIpVPVLIALVVALVAWFLLRRTRFGRYIYAVGGNEEAARLSGINVRRVKILAYVLSGLLAGLAGILLAAR 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 242 LTFIEPAAMFSLAFSIQIAMF----ALNGGLGTVAGPLLGAVLLvpitewaraSLGASALGLHG-------FVYGLVLIL 310
Cdd:COG1172 238 LGSAQPNAGSGYELDAIAAVViggtSLTGGRGSVLGTLLGALIL---------GVLNNGLNLLGvssywqqIVKGAIILL 308
|
....
gi 489057211 311 VVLF 314
Cdd:COG1172 309 AVLL 312
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
385-601 |
2.80e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 79.06 E-value: 2.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 385 VSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQFHAPKNPADFAAlGLGRTFQIVQPFAAMTVEEN 464
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILL---DAQPLESWSSKAFAR-KVAYLPQQLPAAEGMTVREL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 465 IMVGAFYRH----HHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGIN---QTD 537
Cdd:PRK10575 106 VAIGRYPWHgalgRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDiahQVD 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489057211 538 VRRAIDLMLSIRdsGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRdPQVVEAYLG 601
Cdd:PRK10575 186 VLALVHRLSQER--GLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMR-GETLEQIYG 246
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
367-576 |
3.06e-16 |
|
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: 77.53 E-value: 3.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 367 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKNPADFAALGL 446
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 447 GRTFQivqpfAAMTVEENImvgAFYRHHHEKDAREAAREtawRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLL 526
Cdd:cd03231 81 APGIK-----TTLSVLENL---RFWHADHSDEQVEEALA---RVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWIL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489057211 527 DEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLA 576
Cdd:cd03231 150 DEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGARELDLG 199
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
368-594 |
3.51e-16 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 80.23 E-value: 3.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 368 RVQNLNKHFGG----LHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQfhapknpaDFAA 443
Cdd:PRK11153 3 ELKNISKVFPQggrtIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLV---DGQ--------DLTA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 444 L---GLGRTFQ----IVQPF---AAMTVEENImvgAFYRHHHEKDAREAARETAwrmglgPLLgaEARGLT--------- 504
Cdd:PRK11153 72 LsekELRKARRqigmIFQHFnllSSRTVFDNV---ALPLELAGTPKAEIKARVT------ELL--ELVGLSdkadrypaq 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 505 -IGGLK-RLEVARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSI-RDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVI 581
Cdd:PRK11153 141 lSGGQKqRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDInRELGLTIVLITHEMDVVKRICDRVAVIDAGRLV 220
|
250
....*....|...
gi 489057211 582 AQGRPQDVVRDPQ 594
Cdd:PRK11153 221 EQGTVSEVFSHPK 233
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
366-603 |
3.55e-16 |
|
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: 81.41 E-value: 3.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 366 ILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGflapdegtVNLCGA-DGQFHAPKNP------ 438
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG--------VYPHGTwDGEIYWSGSPlkasni 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 439 ADFAALGLGRTFQIVQPFAAMTVEENIMVGAFYRHHHEKDAREA----ARETAWRMGLGPLLGAEARGLTIGGLKRL-EV 513
Cdd:TIGR02633 73 RDTERAGIVIIHQELTLVPELSVAENIFLGNEITLPGGRMAYNAmylrAKNLLRELQLDADNVTRPVGDYGGGQQQLvEI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 514 ARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQgRPQDVVRDP 593
Cdd:TIGR02633 153 AKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVAT-KDMSTMSED 231
|
250
....*....|
gi 489057211 594 QVVEAYLGKE 603
Cdd:TIGR02633 232 DIITMMVGRE 241
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
340-594 |
3.88e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 81.83 E-value: 3.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 340 RTEPIAAVPARAIKAPSPDRAGI--GQDILRVQNLNKHF---GGL--------HVTRNVSFTLREGEVLGLIGPNGAGKT 406
Cdd:PRK10261 285 RRFPLISLEHPAKQEPPIEQDTVvdGEPILQVRNLVTRFplrSGLlnrvtrevHAVEKVSFDLWPGETLSLVGESGSGKS 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 407 TLFNMISGFLAPDEGTVNLCG------ADGQFHAPKNPADFaalglgrTFQivQPFAAM----TVEENIMvgAFYRHHHE 476
Cdd:PRK10261 365 TTGRALLRLVESQGGEIIFNGqridtlSPGKLQALRRDIQF-------IFQ--DPYASLdprqTVGDSIM--EPLRVHGL 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 477 KDAREAARETAW---RMGLGPLLGAEARGLTIGGLK-RLEVARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSI-RDS 551
Cdd:PRK10261 434 LPGKAAAARVAWlleRVGLLPEHAWRYPHEFSGGQRqRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLqRDF 513
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 489057211 552 GVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDPQ 594
Cdd:PRK10261 514 GIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQ 556
|
|
| TM_PBP1_transp_AraH_like |
cd06579 |
Transmembrane subunit (TM) of Escherichia coli AraH and related proteins. E. coli AraH is the ... |
84-314 |
4.09e-16 |
|
Transmembrane subunit (TM) of Escherichia coli AraH and related proteins. E. coli AraH is the TM of a Periplasmic Binding Protein (PBP)-dependent ATP-Binding Cassette (ABC) transporter involved in the uptake of the monosaccharide arabinose. This group also contains E. coli RbsC, AlsC, and MglC, which are TMs of other monosaccharide transporters, the ribose transporter, the D-allose transporter and the galactose transporter, respectively. The D-allose transporter may also be involved in low affinity ribose transport. These transporters generally bind type 1 PBPs. PBP-dependent ABC transporters consist of a PBP, two TMs, and two cytoplasmic ABCs, and are mainly involved in importing solutes from the environment. The solute is captured by the PBP, which delivers it to a gated translocation pathway formed by the two TMs. The two ABCs bind and hydrolyze ATP and drive the transport reaction. Proteins in this subgroup have a single TM which homodimerizes to generate the transmembrane pore.
Pssm-ID: 119321 [Multi-domain] Cd Length: 263 Bit Score: 78.60 E-value: 4.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 84 TGVILFNMGISPWFSMFIGTFIAALVGMVISYPCFRLKGP-FysLASIAFLEVFRVLALhfgWLTGGATGLMIQLKLGWV 162
Cdd:cd06579 35 AALLLVNAGLPIPLAILAALAVGALIGLLNGLLVAYLRIPpF--IVTLGTMFILRGLAL---LITGGRPISGLPPLFSFF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 163 WMVFRERWPSLLIVFgMLLVTLAITWAARRSRLGFYLVATRERESAARAAGVRTVRVRLIAVAISSALCAMLGTFHAMYL 242
Cdd:cd06579 110 LGGGLILGIPVPVLI-ALAVALVAWFLLRRTRFGRYLYAVGGNPEAARLSGINVRRVKILAYVLSGLLAGLAGILLAARL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 243 TFIEPAAMFSLAFSIQIAMF----ALNGGLGTVAGPLLGAVLLvpitewaraSLGASALGLHG-------FVYGLVLILV 311
Cdd:cd06579 189 GSAQPTAGNGYELDAIAAVVlggtSLTGGRGSVLGTLLGALLL---------GVLNNGLNLLGvssfwqqIVKGAILLLA 259
|
...
gi 489057211 312 VLF 314
Cdd:cd06579 260 VAL 262
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
384-590 |
4.47e-16 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 81.48 E-value: 4.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 384 NVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgadgqfhapKNPADFAALGLGRTFQivqpfaaMTVEE 463
Cdd:PRK13545 42 NISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDI----------KGSAALIAISSGLNGQ-------LTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 464 NIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGINQTDVRRAID 543
Cdd:PRK13545 105 NIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLD 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489057211 544 LMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVV 590
Cdd:PRK13545 185 KMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVV 231
|
|
| TM_PBP1_branched-chain-AA_like |
cd06574 |
Transmembrane subunit (TM) of Periplasmic Binding Protein (PBP)-dependent ATP-Binding Cassette ... |
61-312 |
4.60e-16 |
|
Transmembrane subunit (TM) of Periplasmic Binding Protein (PBP)-dependent ATP-Binding Cassette (ABC) transporters which are involved in the uptake of branched-chain amino acids (AAs), as well as TMs of transporters involved in the uptake of monosaccharides including ribose, galactose, and arabinose. These transporters generally bind type 1 PBPs. PBP-dependent ABC transporters consist of a PBP, two TMs, and two cytoplasmic ABCs, and are mainly involved in importing solutes from the environment. The solute is captured by the PBP which delivers it to a gated translocation pathway formed by the two TMs. The two ABCs bind and hydrolyze ATP and drive the transport reaction. This group includes Escherichia coli LivM and LivH, two TMs which heterodimerize to form the translocation pathway of the E. coli branched-chain AA LIV-1/LS transporter. This transporter is comprised of two TMs (LivM and LivH), two ABCs (LivG and LivF), and one of two alternative PBPs, LivJ (LIV-BP) and LivK (LS-BP). In addition to transporting branched-chain AAs including leucine, isoleucine and valine, the E. coli LIV-1/LS transporter is involved in the uptake of the aromatic AA, phenylalanine. Included in this group are proteins from transport systems that contain a single TM which homodimerizes to generate the transmembrane pore; for example E. coli RbsC, AlsC, and MglC, the TMs of the high affinity ribose transporter, the D-allose transporter and the galactose transporter, respectively. The D-allose transporter may also to be involved in low affinity ribose transport.
Pssm-ID: 119320 [Multi-domain] Cd Length: 266 Bit Score: 78.47 E-value: 4.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 61 NIVGGFAGQMSLGHAVFYGIGGYTGVILFNMGISPWFSMFIGTFIAALVGMVISYPCFRLKGPfYSLASIAFLEVFRVLA 140
Cdd:cd06574 12 YIVFRILGFPDLTVDGSFPLGAAVAAILIVAGYNPWLALIAAILAGAAAGLVTGFLHTRLKIN-GLLAGILIMIGLYSIN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 141 LHFGWLTGGATGLMIQLKLGWVWMVFRERWPSLLIVFGMLLVTLAITWAARRSRLGFYLVATRERESAARAAGVRTVRVR 220
Cdd:cd06574 91 LRIMGGPNIPLGTRDTLLGLLLLFGISGTLSIPVVLLLIVLLVLFLVIWFLRTKLGLAMRATGDNPDMARSLGINVDRTR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 221 LIAVAISSALCAMLGTFHAMYLTFIEP-----AAMFSLAfSIQI--AMFALNGGLGTVAGPLLGAVLLVPITEWARASLG 293
Cdd:cd06574 171 ILGLVISNALAALGGALYAQYQGFADVnmgigTGVIGLA-AVIIggAIVGRRTIKASILGVIIGAILYRIALALALGSGL 249
|
250
....*....|....*....
gi 489057211 294 ASalGLHGFVYGLVLILVV 312
Cdd:cd06574 250 IP--SDLKLITAGVIVLVL 266
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
384-584 |
1.07e-15 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 76.54 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 384 NVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLapdEGTVNLCGA---DGQfhaPKNPADFA-ALGLGRTFQIVQPFaaM 459
Cdd:cd03234 25 DVSLHVESGQVMAILGSSGSGKTTLLDAISGRV---EGGGTTSGQilfNGQ---PRKPDQFQkCVAYVRQDDILLPG--L 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 460 TVEENIMVGAFYR-HHHEKDAREAARETAWRM---GLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGInq 535
Cdd:cd03234 97 TVRETLTYTAILRlPRKSSDAIRKKRVEDVLLrdlALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGL-- 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489057211 536 tDVRRAIDLMLSIRDSGVS----IIAIEHVMQAVMSLSDRVIVLASGEVIAQG 584
Cdd:cd03234 175 -DSFTALNLVSTLSQLARRnrivILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
366-589 |
1.16e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 77.44 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 366 ILRVQNLNKHF---GGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQFHAPKNPADFA 442
Cdd:PRK13642 4 ILEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKI---DGELLTAENVWNLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 443 AlGLGRTFQivQP---FAAMTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAM 519
Cdd:PRK13642 81 R-KIGMVFQ--NPdnqFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489057211 520 EPRILLLDEVMAGINQTDVRRAIDLMLSIRDS-GVSIIAIEHVMQAVMSlSDRVIVLASGEVIAQGRPQDV 589
Cdd:PRK13642 158 RPEIIILDESTSMLDPTGRQEIMRVIHEIKEKyQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSEL 227
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
366-594 |
2.43e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 78.98 E-value: 2.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 366 ILRVQNLNKHF---GGL--------HVTRNVSFTLREGEVLGLIGPNGAGKTT----LFNMIsgflaPDEGTVNLCGADG 430
Cdd:PRK15134 275 LLDVEQLQVAFpirKGIlkrtvdhnVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 431 QFHAPKnpadfAALGLGRTFQIV--QPFAA----MTVEENIMVGafYRHHH------EKDAR--EAAREtawrMGLGPLL 496
Cdd:PRK15134 350 HNLNRR-----QLLPVRHRIQVVfqDPNSSlnprLNVLQIIEEG--LRVHQptlsaaQREQQviAVMEE----VGLDPET 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 497 ----GAEARGltiGGLKRLEVARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRDS-GVSIIAIEHVMQAVMSLSDR 571
Cdd:PRK15134 419 rhryPAEFSG---GQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQ 495
|
250 260
....*....|....*....|...
gi 489057211 572 VIVLASGEVIAQGRPQDVVRDPQ 594
Cdd:PRK15134 496 VIVLRQGEVVEQGDCERVFAAPQ 518
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
345-591 |
2.62e-15 |
|
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: 79.02 E-value: 2.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 345 AAVPARAIKAPSPDRAGIgqdiLRVQNLNKHFGG--LHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGT 422
Cdd:COG4618 313 AAVPAEPERMPLPRPKGR----LSVENLTVVPPGskRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGS 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 423 VNLCGAD-GQFhapkNPADfaalgLGRTF----QIVQPFAAmTVEENImvgafyrhhhekdAR----------EAAR--- 484
Cdd:COG4618 389 VRLDGADlSQW----DREE-----LGRHIgylpQDVELFDG-TIAENI-------------ARfgdadpekvvAAAKlag 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 485 --ETAWRM--GLGPLLGAEARGLTiGGLK-RLEVARVMAMEPRILLLDEVMAGINQT---DVRRAIDLMlsiRDSGVSII 556
Cdd:COG4618 446 vhEMILRLpdGYDTRIGEGGARLS-GGQRqRIGLARALYGDPRLVVLDEPNSNLDDEgeaALAAAIRAL---KARGATVV 521
|
250 260 270
....*....|....*....|....*....|....*
gi 489057211 557 AIEHVMqAVMSLSDRVIVLASGEVIAQGRPQDVVR 591
Cdd:COG4618 522 VITHRP-SLLAAVDKLLVLRDGRVQAFGPRDEVLA 555
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
356-579 |
4.03e-15 |
|
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: 78.67 E-value: 4.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 356 SPDRAGIGQDILRVQNLNKHFGG--LHVTRNvsfTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgadgqfh 433
Cdd:COG1245 331 APRREKEEETLVEYPDLTKSYGGfsLEVEGG---EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDE-------- 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 434 apknpadfaALGLGRTFQIVQPFAAMTVEENImvgafyrhhheKDAREAARETAW-------RMGLGPLLGAEARGLTIG 506
Cdd:COG1245 400 ---------DLKISYKPQYISPDYDGTVEEFL-----------RSANTDDFGSSYykteiikPLGLEKLLDKNVKDLSGG 459
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489057211 507 GLKRLEVARVMAMEPRILLLDEVMAGInqtDV--R----RAIDLMlsIRDSGVSIIAIEHVMQAVMSLSDRVIVLaSGE 579
Cdd:COG1245 460 ELQRVAIAACLSRDADLYLLDEPSAHL---DVeqRlavaKAIRRF--AENRGKTAMVVDHDIYLIDYISDRLMVF-EGE 532
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
352-425 |
4.94e-15 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 78.24 E-value: 4.94e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489057211 352 IKAPSPDRagIGQDILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNL 425
Cdd:PRK11819 312 IFIPPGPR--LGDKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI 383
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
345-560 |
6.01e-15 |
|
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: 77.79 E-value: 6.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 345 AAVPARAIKAPSPDRAGIGQDILRVQNLNKHF-GGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTV 423
Cdd:TIGR02868 313 AAGPVAEGSAPAAGAVGLGKPTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEV 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 424 NLCGAdgqfHAPKNPADFAALGLGRTFQIVQPFAAmTVEENIMVGAfyrhhheKDAREAARETAWRM------------G 491
Cdd:TIGR02868 393 TLDGV----PVSSLDQDEVRRRVSVCAQDAHLFDT-TVRENLRLAR-------PDATDEELWAALERvgladwlralpdG 460
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489057211 492 LGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIrDSGVSIIAIEH 560
Cdd:TIGR02868 461 LDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAA-LSGRTVVLITH 528
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
381-586 |
6.05e-15 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 73.99 E-value: 6.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 381 VTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQfhapknpaDFAALGLG---RTFQIV--QP 455
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEI---DGI--------DISTIPLEdlrSSLTIIpqDP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 456 FAAM-TVEENIMVgafYRHHHEKDAREAARETawrmGLGPLLGAEARGLtigglkrLEVARVMAMEPRILLLDEVMAGIN 534
Cdd:cd03369 92 TLFSgTIRSNLDP---FDEYSDEEIYGALRVS----EGGLNLSQGQRQL-------LCLARALLKRPRVLVLDEATASID 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489057211 535 -QTDVRraidLMLSIRD--SGVSIIAIEHVMQAVMSLsDRVIVLASGEVIAQGRP 586
Cdd:cd03369 158 yATDAL----IQKTIREefTNSTILTIAHRLRTIIDY-DKILVMDAGEVKEYDHP 207
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
365-596 |
6.74e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 74.77 E-value: 6.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 365 DILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNlcgadgqfHAPKnpadfaaL 444
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK--------RNGK-------L 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 445 GLGRTFQIVQPFAAMTveenIMVGAFYRHH---HEKDAREAARetawRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEP 521
Cdd:PRK09544 68 RIGYVPQKLYLDTTLP----LTVNRFLRLRpgtKKEDILPALK----RVQAGHLIDAPMQKLSGGETQRVLLARALLNRP 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489057211 522 RILLLDEVMAGINQTDVRRAIDLMLSIRDS-GVSIIAIEHVMQAVMSLSDRVIVLaSGEVIAQGRPQDVVRDPQVV 596
Cdd:PRK09544 140 QLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGTPEVVSLHPEFI 214
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
367-560 |
8.77e-15 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 73.16 E-value: 8.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 367 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKNPADFAALGL 446
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 447 GRTFQivqpfAAMTVEENImvgAFYRHHHeKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLL 526
Cdd:TIGR01189 81 LPGLK-----PELSALENL---HFWAAIH-GGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWIL 151
|
170 180 190
....*....|....*....|....*....|....
gi 489057211 527 DEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEH 560
Cdd:TIGR01189 152 DEPTTALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
356-579 |
9.13e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 77.54 E-value: 9.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 356 SPDRAGIGQDILRVQNLNKHFGG--LHVTrnvSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNlcgadgqfh 433
Cdd:PRK13409 330 PPRDESERETLVEYPDLTKKLGDfsLEVE---GGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD--------- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 434 apknpadfAALGLGRTFQIVQPFAAMTVEENIM-VGAFYRHHHEKDareaarETAWRMGLGPLLGAEARGLTIGGLKRLE 512
Cdd:PRK13409 398 --------PELKISYKPQYIKPDYDGTVEDLLRsITDDLGSSYYKS------EIIKPLQLERLLDKNVKDLSGGELQRVA 463
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 513 VARVMAMEPRILLLDEVMAGIN---QTDVRRAIDLMlsIRDSGVSIIAIEHVMQAVMSLSDRVIVLaSGE 579
Cdd:PRK13409 464 IAACLSRDADLYLLDEPSAHLDveqRLAVAKAIRRI--AEEREATALVVDHDIYMIDYISDRLMVF-EGE 530
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
381-597 |
9.89e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 74.66 E-value: 9.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 381 VTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGadgqfhapkNPADFAALGLGRTFQIV------- 453
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQG---------KPLDYSKRGLLALRQQVatvfqdp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 454 -QPFAAMTVEENImvgAFYRHHHEKDAREAARETAWRMGLgpllgAEARG--------LTIGGLKRLEVARVMAMEPRIL 524
Cdd:PRK13638 87 eQQIFYTDIDSDI---AFSLRNLGVPEAEITRRVDEALTL-----VDAQHfrhqpiqcLSHGQKKRVAIAGALVLQARYL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489057211 525 LLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDPQVVE 597
Cdd:PRK13638 159 LLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTEAME 231
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
364-593 |
1.23e-14 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 75.53 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 364 QDILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKNpADFAA 443
Cdd:PRK11432 4 KNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ-RDICM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 444 LglgrtFQIVQPFAAMTVEENIMVGAFYRHHHEKDAREAARETawrMGLGPLLGAEAR---GLTIGGLKRLEVARVMAME 520
Cdd:PRK11432 83 V-----FQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEA---LELVDLAGFEDRyvdQISGGQQQRVALARALILK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 521 PRILLLDEVMAGINqTDVRRaidlmlSIRDS--------GVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRD 592
Cdd:PRK11432 155 PKVLLFDEPLSNLD-ANLRR------SMREKirelqqqfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
|
.
gi 489057211 593 P 593
Cdd:PRK11432 228 P 228
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
383-593 |
1.51e-14 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 75.84 E-value: 1.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 383 RNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADgqfHAPKNPADFAALGLGRTFQIVQPFAA---M 459
Cdd:PRK10070 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVD---IAKISDAELREVRRKKIAMVFQSFALmphM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 460 TVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGINQTDVR 539
Cdd:PRK10070 122 TVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489057211 540 RAIDLMLSIR-DSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDP 593
Cdd:PRK10070 202 EMQDELVKLQaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNP 256
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
380-590 |
2.75e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 75.85 E-value: 2.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 380 HVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPD---EGTVNLCGAdgqfhaPKNPADFAAL-GLGRTFQIVQP 455
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGM------PIDAKEMRAIsAYVQQDDLFIP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 456 faAMTVEENIMVGAFYR---HHHEKDAREAARETAWRMGLGP----LLGAEAR--GLTIGGLKRLEVARVMAMEPRILLL 526
Cdd:TIGR00955 113 --TLTVREHLMFQAHLRmprRVTKKEKRERVDEVLQALGLRKcantRIGVPGRvkGLSGGERKRLAFASELLTDPPLLFC 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489057211 527 DEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQA-VMSLSDRVIVLASGEVIAQGRPQDVV 590
Cdd:TIGR00955 191 DEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSeLFELFDKIILMAEGRVAYLGSPDQAV 255
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
381-580 |
4.83e-14 |
|
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: 71.73 E-value: 4.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 381 VTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGqfhapKNPADFAALGLGRTFQIV--QP-FA 457
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLL---DG-----KPISQYEHKYLHSKVSLVgqEPvLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 458 AMTVEENIMVGAFYRHHHE-KDAREAARETAWRMGL--GPLLGAEARG--LTIGGLKRLEVARVMAMEPRILLLDEVMAG 532
Cdd:cd03248 101 ARSLQDNIAYGLQSCSFECvKEAAQKAHAHSFISELasGYDTEVGEKGsqLSGGQKQRVAIARALIRNPQVLILDEATSA 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489057211 533 INqTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSlSDRVIVLASGEV 580
Cdd:cd03248 181 LD-AESEQQVQQALYDWPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
352-425 |
5.44e-14 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 74.97 E-value: 5.44e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489057211 352 IKAPSPDRagIGQDILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNL 425
Cdd:TIGR03719 310 IYIPPGPR--LGDKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI 381
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
383-599 |
6.28e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 72.50 E-value: 6.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 383 RNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgADGQFHAPKNPADFAAL--GLGRTFQI--VQPFAA 458
Cdd:PRK13646 24 HDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTV--DDITITHKTKDKYIRPVrkRIGMVFQFpeSQLFED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 459 mTVEENIMVGAfyrhHHEKDAREAARETAWR--MGLG---PLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGI 533
Cdd:PRK13646 102 -TVEREIIFGP----KNFKMNLDEVKNYAHRllMDLGfsrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489057211 534 NQTDVRRAIDLMLSIR-DSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDPQVVEAY 599
Cdd:PRK13646 177 DPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKKKLADW 243
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
371-606 |
6.60e-14 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 74.38 E-value: 6.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 371 NLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKNpadfaAL--GLGR 448
Cdd:PRK10982 3 NISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKE-----ALenGISM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 449 TFQIVQPFAAMTVEENIMVGAFYRHHHEKDAREAARET-AWRMGLGPLLGAEARG--LTIGGLKRLEVARVMAMEPRILL 525
Cdd:PRK10982 78 VHQELNLVLQRSVMDNMWLGRYPTKGMFVDQDKMYRDTkAIFDELDIDIDPRAKVatLSVSQMQMIEIAKAFSYNAKIVI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 526 LDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDpQVVEAYLGKEFA 605
Cdd:PRK10982 158 MDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMD-KIIAMMVGRSLT 236
|
.
gi 489057211 606 H 606
Cdd:PRK10982 237 Q 237
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
366-594 |
7.37e-14 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 72.82 E-value: 7.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 366 ILRVQNLNKHFG-------------GLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGAD--- 429
Cdd:PRK15079 8 LLEVADLKVHFDikdgkqwfwqppkTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDllg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 430 ---GQFHAPKNPadfaalgLGRTFQivQPFAA----MTVEENIM--VGAFYRHHHEKDAREAARETAWRMGLGP-LLGAE 499
Cdd:PRK15079 88 mkdDEWRAVRSD-------IQMIFQ--DPLASlnprMTIGEIIAepLRTYHPKLSRQEVKDRVKAMMLKVGLLPnLINRY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 500 ARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSI-RDSGVSIIAIEHVMQAVMSLSDRVIVLASG 578
Cdd:PRK15079 159 PHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVMYLG 238
|
250
....*....|....*.
gi 489057211 579 EVIAQGRPQDVVRDPQ 594
Cdd:PRK15079 239 HAVELGTYDEVYHNPL 254
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
371-594 |
8.56e-14 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 73.14 E-value: 8.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 371 NLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQFHAPKNPADfaaLGLGRTF 450
Cdd:PRK11000 8 NVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFI---GEKRMNDVPPAE---RGVGMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 451 QIVQPFAAMTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVM 530
Cdd:PRK11000 82 QSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489057211 531 AGINQT-DVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDPQ 594
Cdd:PRK11000 162 SNLDAAlRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPA 226
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
373-586 |
1.05e-13 |
|
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: 71.11 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 373 NKHFG---GLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQfhapknpaDFAALGL--- 446
Cdd:cd03253 5 NVTFAydpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILI---DGQ--------DIREVTLdsl 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 447 ----GRTFQIVQPFAAmTVEENIMVG---AfyrhhHEKDAREAARE-------TAWRMGLGPLLGAeaRGLTI-GGLK-R 510
Cdd:cd03253 74 rraiGVVPQDTVLFND-TIGYNIRYGrpdA-----TDEEVIEAAKAaqihdkiMRFPDGYDTIVGE--RGLKLsGGEKqR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489057211 511 LEVARVMAMEPRILLLDEVMAGINqTDVRRAIdlMLSIRD--SGVSIIAIEHVMQAVMSlSDRVIVLASGEVIAQGRP 586
Cdd:cd03253 146 VAIARAILKNPPILLLDEATSALD-THTEREI--QAALRDvsKGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTH 219
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
363-580 |
1.43e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 73.50 E-value: 1.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 363 GQDILRVQNLNkhfgGLHVtRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQFHAPKNPADFA 442
Cdd:PRK10762 254 GEVRLKVDNLS----GPGV-NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTL---DGHEVVTRSPQDGL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 443 ALG--------------LGrtfqivqpfaaMTVEENIMVGAF---------YRHHHEKDA----------REAARETAwr 489
Cdd:PRK10762 326 ANGivyisedrkrdglvLG-----------MSVKENMSLTALryfsraggsLKHADEQQAvsdfirlfniKTPSMEQA-- 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 490 mgLGPLLGaeargltiGGLKRLEVARVMAMEPRILLLDEVMAGInqtDV--RRAI-DLMLSIRDSGVSIIAIEHVMQAVM 566
Cdd:PRK10762 393 --IGLLSG--------GNQQKVAIARGLMTRPKVLILDEPTRGV---DVgaKKEIyQLINQFKAEGLSIILVSSEMPEVL 459
|
250
....*....|....
gi 489057211 567 SLSDRVIVLASGEV 580
Cdd:PRK10762 460 GMSDRILVMHEGRI 473
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
384-596 |
2.07e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 71.19 E-value: 2.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 384 NVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgadGQFHAPKNPADFAA-------LGLGRTFQIVQPF 456
Cdd:PRK13645 29 NTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIV----GDYAIPANLKKIKEvkrlrkeIGLVFQFPEYQLF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 457 AAmTVEENIMVGAFyrhHHEKDAREAARETAWRMGLGPLLGAEAR----GLTIGGLKRLEVARVMAMEPRILLLDEVMAG 532
Cdd:PRK13645 105 QE-TIEKDIAFGPV---NLGENKQEAYKKVPELLKLVQLPEDYVKrspfELSGGQKRRVALAGIIAMDGNTLVLDEPTGG 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489057211 533 INQTDVRRAIDLMLSI-RDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDPQVV 596
Cdd:PRK13645 181 LDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQELL 245
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
367-584 |
2.99e-13 |
|
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: 68.11 E-value: 2.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 367 LRVQNLNKHFGG--LHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGadgqfhapKNPADFAAL 444
Cdd:cd03247 1 LSINNVSFSYPEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDG--------VPVSDLEKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 445 gLGRTFQIV--QPFA-AMTVEENimvgafyrhhhekdareaaretawrmglgplLGAEARGltiGGLKRLEVARVMAMEP 521
Cdd:cd03247 73 -LSSLISVLnqRPYLfDTTLRNN-------------------------------LGRRFSG---GERQRLALARILLQDA 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489057211 522 RILLLDEVMAGINQTDVRRAIDLMLSIRDsGVSIIAIEHVMQAvMSLSDRVIVLASGEVIAQG 584
Cdd:cd03247 118 PIVLLDEPTVGLDPITERQLLSLIFEVLK-DKTLIWITHHLTG-IEHMDKILFLENGKIIMQG 178
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
366-581 |
3.80e-13 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 70.10 E-value: 3.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 366 ILRVQNLNKHFGG---------LHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGAD-GQFhap 435
Cdd:PRK10419 3 LLNVSGLSHHYAHgglsgkhqhQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPlAKL--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 436 kNPADFAAlgLGRTFQIV--QPFAAMTVEENI--MVGAFYRH--HHEKDAREA-ARETAWRMGLGPLLGAEARGLTIGG- 507
Cdd:PRK10419 80 -NRAQRKA--FRRDIQMVfqDSISAVNPRKTVreIIREPLRHllSLDKAERLArASEMLRAVDLDDSVLDKRPPQLSGGq 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489057211 508 LKRLEVARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRD-SGVSIIAIEHVMQAVMSLSDRVIVLASGEVI 581
Cdd:PRK10419 157 LQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQqFGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
384-595 |
4.27e-13 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 69.79 E-value: 4.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 384 NVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQfhapknpaDFAALGLGR----------TFQIV 453
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILF---DGE--------NIPAMSRSRlytvrkrmsmLFQSG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 454 QPFAAMTVEENImvgAFYRHHHEKDAREAARETAWR-------MGLGPLLGAEARGltiGGLKRLEVARVMAMEPRILLL 526
Cdd:PRK11831 94 ALFTDMNVFDNV---AYPLREHTQLPAPLLHSTVMMkleavglRGAAKLMPSELSG---GMARRAALARAIALEPDLIMF 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489057211 527 DEVMAGINQTDVRRAIDLMLSIRDS-GVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVR--DPQV 595
Cdd:PRK11831 168 DEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQAnpDPRV 239
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
362-580 |
2.03e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 69.55 E-value: 2.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 362 IGQDILRVQNLNkhfgGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKN---- 437
Cdd:PRK11288 253 LGEVRLRLDGLK----GPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDaira 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 438 -----PADFAALGlgrtfqIVqpfAAMTVEENIMVGAfYRHH-------HEKDAREAARETAWRMGL-GPLLGAEARGLT 504
Cdd:PRK11288 329 gimlcPEDRKAEG------II---PVHSVADNINISA-RRHHlragcliNNRWEAENADRFIRSLNIkTPSREQLIMNLS 398
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489057211 505 IGGLKRLEVARVMAMEPRILLLDEVMAGInqtDV--RRAI-DLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEV 580
Cdd:PRK11288 399 GGNQQKAILGRWLSEDMKVILLDEPTRGI---DVgaKHEIyNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
363-585 |
3.20e-12 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 68.22 E-value: 3.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 363 GQDILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAG--KTTLFNMISGflaPDEGtvnlcgadgqfhapKNPAD 440
Cdd:NF000106 10 ARNAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAG--------------RRPWR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 441 FAAL-----GLGRTFQIVQPF-----AAMTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKR 510
Cdd:NF000106 73 F*TWcanrrALRRTIG*HRPVr*grrESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489057211 511 LEVARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGR 585
Cdd:NF000106 153 LDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGK 227
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
370-591 |
4.09e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 69.38 E-value: 4.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 370 QNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGAdgqfhaPKNPADFAalglgrT 449
Cdd:NF033858 270 RGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQ------PVDAGDIA------T 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 450 FQIV----QPF---AAMTVEENIMVGAfyRHHHEKDAREAAR--ETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAME 520
Cdd:NF033858 338 RRRVgymsQAFslyGELTVRQNLELHA--RLFHLPAAEIAARvaEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHK 415
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489057211 521 PRILLLDEVMAGInqtD-VRRaiD----LM--LSiRDSGVSIIAIEHVMQAVMsLSDRVIVLASGEVIAQGRPQDVVR 591
Cdd:NF033858 416 PELLILDEPTSGV---DpVAR--DmfwrLLieLS-REDGVTIFISTHFMNEAE-RCDRISLMHAGRVLASDTPAALVA 486
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
366-570 |
4.40e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 66.73 E-value: 4.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 366 ILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTL---FN----MISGFLApdEGTVNLCGADgqFHAPK-N 437
Cdd:PRK14243 10 VLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTIlrcFNrlndLIPGFRV--EGKVTFHGKN--LYAPDvD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 438 PADFAALgLGRTFQIVQPFAAmTVEENIMVGAF---YRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVA 514
Cdd:PRK14243 86 PVEVRRR-IGMVFQKPNPFPK-SIYDNIAYGARingYKGDMDELVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489057211 515 RVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRDSgVSIIAIEHVMQAVMSLSD 570
Cdd:PRK14243 164 RAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAARVSD 218
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
383-584 |
4.92e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 66.83 E-value: 4.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 383 RNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKNPADFAAlglgRTFQIVQPFAAMtVE 462
Cdd:PRK15056 24 RDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVP----QSEEVDWSFPVL-VE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 463 ENIMVG-----AFYRHHHEKDaREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGINQTD 537
Cdd:PRK15056 99 DVVMMGryghmGWLRRAKKRD-RQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKT 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489057211 538 VRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRViVLASGEVIAQG 584
Cdd:PRK15056 178 EARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYT-VMVKGTVLASG 223
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
333-580 |
6.03e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 68.15 E-value: 6.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 333 SEETATART-EPIAAVPARAIKAPSPD-------------RAGIGQDILRVQNLN-KHFgglhvtRNVSFTLREGEVLGL 397
Cdd:PRK15439 221 SGKTADLSTdDIIQAITPAAREKSLSAsqklwlelpgnrrQQAAGAPVLTVEDLTgEGF------RNISLEVRAGEILGL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 398 IGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKN---------PADFAALGLGRTFQIVQPFAAMTVEENimvG 468
Cdd:PRK15439 295 AGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrlarglvylPEDRQSSGLYLDAPLAWNVCALTHNRR---G 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 469 AFYRhhhekDAREAARETAWRMGLG-PLLGAE--ARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGInqtDV--RRAI- 542
Cdd:PRK15439 372 FWIK-----PARENAVLERYRRALNiKFNHAEqaARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGV---DVsaRNDIy 443
|
250 260 270
....*....|....*....|....*....|....*...
gi 489057211 543 DLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEV 580
Cdd:PRK15439 444 QLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
384-593 |
7.60e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 67.95 E-value: 7.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 384 NVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLaPDEG--TVNlcgadGQFHAPKNPADF----AALGlgrtfQIVQPFA 457
Cdd:PRK11174 368 PLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGslKIN-----GIELRELDPESWrkhlSWVG-----QNPQLPH 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 458 AmTVEENIMVGafyRHHHEKDAREAARETAW--------RMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDE- 528
Cdd:PRK11174 437 G-TLRDNVLLG---NPDASDEQLQQALENAWvseflpllPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEp 512
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489057211 529 -----------VMAGINQTdVRRAIDLMLSIRdsgvsiiaIEHVMQAvmslsDRVIVLASGEVIAQGRPQDVVRDP 593
Cdd:PRK11174 513 tasldahseqlVMQALNAA-SRRQTTLMVTHQ--------LEDLAQW-----DQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
364-572 |
7.86e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 65.22 E-value: 7.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 364 QDILRVQNLNKHF--GGLH--VTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKNPA 439
Cdd:PRK11629 3 KILLQCDNLCKRYqeGSVQtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 440 DFAALGLGRTFQIVQPFAAMTVEENIMVGAFYRHHHEKDAREAARETAWRMGLgpllgaEARG------LTIGGLKRLEV 513
Cdd:PRK11629 83 ELRNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGL------EHRAnhrpseLSGGERQRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 514 ARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSI-RDSGVSIIAIEHVMQAVMSLSDRV 572
Cdd:PRK11629 157 ARALVNNPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKRMSRQL 216
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
381-587 |
9.83e-12 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 67.83 E-value: 9.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 381 VTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADgqfHAPKNPADFAAL---GLGRTFQIVQPFA 457
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQD---VATLDADALAQLrreHFGFIFQRYHLLS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 458 AMTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGINQTD 537
Cdd:PRK10535 100 HLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHS 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489057211 538 VRRAIDLMLSIRDSGVSIIAIEHVMQaVMSLSDRVIVLASGEVIAQGRPQ 587
Cdd:PRK10535 180 GEEVMAILHQLRDRGHTVIIVTHDPQ-VAAQAERVIEIRDGEIVRNPPAQ 228
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
363-580 |
1.22e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.12 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 363 GQDILRVQNLNKHFGGLhvTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADgqfHAPKNPADFA 442
Cdd:PRK09700 262 HETVFEVRNVTSRDRKK--VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKD---ISPRSPLDAV 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 443 ALGLG------------RTFQIVQpfaAMTVEENIMVGAF------YRHHHEKDAREAARE------TAWRMGLGPLLGA 498
Cdd:PRK09700 337 KKGMAyitesrrdngffPNFSIAQ---NMAISRSLKDGGYkgamglFHEVDEQRTAENQREllalkcHSVNQNITELSGG 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 499 EARGLTIGglkrlevaRVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASG 578
Cdd:PRK09700 414 NQQKVLIS--------KWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEG 485
|
..
gi 489057211 579 EV 580
Cdd:PRK09700 486 RL 487
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
383-528 |
2.42e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 63.28 E-value: 2.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 383 RNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCG-----ADGQFHapknpADFAALG--LGrtfqiVQP 455
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGepirrQRDEYH-----QDLLYLGhqPG-----IKT 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489057211 456 faAMTVEENImvgAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDE 528
Cdd:PRK13538 88 --ELTALENL---RFYQRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDE 155
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
384-594 |
2.99e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 64.39 E-value: 2.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 384 NVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTV---NLcgadgqfhaPKNPADFAAL--GLGRTFQivQP--- 455
Cdd:PRK13648 27 DVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynNQ---------AITDDNFEKLrkHIGIVFQ--NPdnq 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 456 FAAMTVE-------ENIMVGafyrhhHEKDAREAArETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDE 528
Cdd:PRK13648 96 FVGSIVKydvafglENHAVP------YDEMHRRVS-EALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDE 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489057211 529 VMAGINQTDVRRAIDLMLSIR-DSGVSIIAIEHVMQAVMSlSDRVIVLASGEVIAQGRPQDVVRDPQ 594
Cdd:PRK13648 169 ATSMLDPDARQNLLDLVRKVKsEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHAE 234
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
364-604 |
3.18e-11 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 64.07 E-value: 3.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 364 QDILRVQNLNKHFGGLHvtrNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGAdgqfhapknpADFAA 443
Cdd:PRK13546 25 KDALIPKHKNKTFFALD---DISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE----------VSVIA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 444 LGLGRTFQivqpfaaMTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRI 523
Cdd:PRK13546 92 ISAGLSGQ-------LTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 524 LLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDpqvVEAYLgKE 603
Cdd:PRK13546 165 LVIDEALSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPK---YEAFL-ND 240
|
.
gi 489057211 604 F 604
Cdd:PRK13546 241 F 241
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
286-587 |
4.53e-11 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 66.19 E-value: 4.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 286 EWARASLGASALGLHGFVYGLVLILVVLFMpngimgAINRFVRKPqdSEETATARTEPIAAVPARAIKApspdraGIGQD 365
Cdd:TIGR01257 1871 QWDLIGKNLVAMAVEGVVYFLLTLLIQHHF------FLSRWIAEP--AKEPIFDEDDDVAEERQRIISG------GNKTD 1936
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 366 ILRVQNLNKHFGGLH--VTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADgqfhAPKNPADF-A 442
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKS----ILTNISDVhQ 2012
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 443 ALGLGRTFQIVQPFaaMTVEENIMVGAFYRHhheKDAREAARETAWRM-GLGPLLGAEA-RGLTIGGLKR-LEVARVMAM 519
Cdd:TIGR01257 2013 NMGYCPQFDAIDDL--LTGREHLYLYARLRG---VPAEEIEKVANWSIqSLGLSLYADRlAGTYSGGNKRkLSTAIALIG 2087
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489057211 520 EPRILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQ 587
Cdd:TIGR01257 2088 CPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQ 2155
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
371-589 |
6.15e-11 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 64.13 E-value: 6.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 371 NLNKHFGGLHVTRNVsfTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCG-----ADGQFHAPKNPAdfaalG 445
Cdd:PRK11144 5 NFKQQLGDLCLTVNL--TLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdAEKGICLPPEKR-----R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 446 LGRTFQIVQPFAAMTVEENIMVGAfyrhhHEKDAREAARETAWrMGLGPLLGAEARGLTiGGLK-RLEVARVMAMEPRIL 524
Cdd:PRK11144 78 IGYVFQDARLFPHYKVRGNLRYGM-----AKSMVAQFDKIVAL-LGIEPLLDRYPGSLS-GGEKqRVAIGRALLTAPELL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 525 LLDEVMAGInqtDVRRAIDLM-----LSiRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDV 589
Cdd:PRK11144 151 LMDEPLASL---DLPRKRELLpylerLA-REINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEV 216
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
349-597 |
6.65e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 63.19 E-value: 6.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 349 ARAIKAPSPDRAGIgqdilrvqNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLF-------NMISGFLApdEG 421
Cdd:PRK14271 12 AADVDAAAPAMAAV--------NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLrtlnrmnDKVSGYRY--SG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 422 TVnLCGADGQFHApKNPADFAALgLGRTFQIVQPFaAMTVEENIMVGAfyRHHH---EKDAREAARETAWRMGL----GP 494
Cdd:PRK14271 82 DV-LLGGRSIFNY-RDVLEFRRR-VGMLFQRPNPF-PMSIMDNVLAGV--RAHKlvpRKEFRGVAQARLTEVGLwdavKD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 495 LLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRDSgVSIIAIEHVMQAVMSLSDRVIV 574
Cdd:PRK14271 156 RLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAAL 234
|
250 260
....*....|....*....|...
gi 489057211 575 LASGEVIAQGRPQDVVRDPQVVE 597
Cdd:PRK14271 235 FFDGRLVEEGPTEQLFSSPKHAE 257
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
381-586 |
7.02e-11 |
|
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: 62.13 E-value: 7.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 381 VTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQfhapknpaDFAALGLG--RTF-----QIV 453
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILI---DGV--------DISKIGLHdlRSRisiipQDP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 454 QPFAAmTVEENImvGAFyrHHHEKDAREAAREtawRMGLGPLLGAEARGL----TIGGL-----KR--LEVARVMAMEPR 522
Cdd:cd03244 88 VLFSG-TIRSNL--DPF--GEYSDEELWQALE---RVGLKEFVESLPGGLdtvvEEGGEnlsvgQRqlLCLARALLRKSK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489057211 523 ILLLDEVMAGI-NQTDvrRAIDLMLSIRDSGVSIIAIEHVMQAVMSlSDRVIVLASGEVIAQGRP 586
Cdd:cd03244 160 ILVLDEATASVdPETD--ALIQKTIREAFKDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFDSP 221
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
388-587 |
1.18e-10 |
|
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: 62.04 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 388 TLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFhapkNPadfaalglgrtfQIVQPFAAMTVEENIM- 466
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSY----KP------------QYIKADYEGTVRDLLSs 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 467 -VGAFYRHHHEKDareaarETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGIN---QTDVRRAI 542
Cdd:cd03237 85 iTKDFYTHPYFKT------EIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDveqRLMASKVI 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489057211 543 DLMLSIRDSGVSIiaIEHVMQAVMSLSDRVIVLaSGEVIAQGR---PQ 587
Cdd:cd03237 159 RRFAENNEKTAFV--VEHDIIMIDYLADRLIVF-EGEPSVNGVanpPQ 203
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
366-577 |
3.67e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 60.11 E-value: 3.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 366 ILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAP---------- 435
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPeiyrqqvsyc 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 436 -KNPADFAAlglgrtfqivqpfaamTVEENIMVGAFYRHHHeKDAREAARETAwRMGLgP--LLGAEARGLTIGGLKRLE 512
Cdd:PRK10247 87 aQTPTLFGD----------------TVYDNLIFPWQIRNQQ-PDPAIFLDDLE-RFAL-PdtILTKNIAELSGGEKQRIS 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489057211 513 VARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLS-IRDSGVSIIAIEHVMQAVmSLSDRVIVLAS 577
Cdd:PRK10247 148 LIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRyVREQNIAVLWVTHDKDEI-NHADKVITLQP 212
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
383-587 |
5.07e-10 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 62.43 E-value: 5.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 383 RNVSFTLREGEV--------------LGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQfhaPKNPADFAALGLGr 448
Cdd:PRK10790 344 DNVSFAYRDDNLvlqninlsvpsrgfVALVGHTGSGKSTLASLLMGYYPLTEGEIRL---DGR---PLSSLSHSVLRQG- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 449 tFQIVQ--PFA-AMTVEENIMVGAFYRHHHEKDAREAAR--ETAWRM--GLGPLLGAEARGLTIGGLKRLEVARVMAMEP 521
Cdd:PRK10790 417 -VAMVQqdPVVlADTFLANVTLGRDISEEQVWQALETVQlaELARSLpdGLYTPLGEQGNNLSVGQKQLLALARVLVQTP 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489057211 522 RILLLDEVMAGINqTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSlSDRVIVLASGEVIAQGRPQ 587
Cdd:PRK10790 496 QILILDEATANID-SGTEQAIQQALAAVREHTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQ 559
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
367-423 |
5.34e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 62.22 E-value: 5.34e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 489057211 367 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTV 423
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
383-590 |
7.74e-10 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 61.52 E-value: 7.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 383 RNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADgqfhapKNPADFAAL--GLGRTFQIVQPFAaMT 460
Cdd:PRK13657 352 EDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTD------IRTVTRASLrrNIAVVFQDAGLFN-RS 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 461 VEENIMVG---AFYRHHHEKDAREAARETAWR--MGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGIN- 534
Cdd:PRK13657 425 IEDNIRVGrpdATDEEMRAAAERAQAHDFIERkpDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDv 504
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489057211 535 --QTDVRRAIDLMLSIRDSGVsiiaIEHVMQAVMSlSDRVIVLASGEVIAQGRPQDVV 590
Cdd:PRK13657 505 etEAKVKAALDELMKGRTTFI----IAHRLSTVRN-ADRILVFDNGRVVESGSFDELV 557
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
381-595 |
1.83e-09 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 60.51 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 381 VTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQfhapknP-ADFAALGLGRTFQIVQP---F 456
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLL---DGV------PlVQYDHHYLHRQVALVGQepvL 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 457 AAMTVEENIMVGafYRHHHEKDAREAARE-------TAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEV 529
Cdd:TIGR00958 567 FSGSVRENIAYG--LTDTPDEEIMAAAKAanahdfiMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEA 644
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489057211 530 MAGInqtDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSlSDRVIVLASGEVIAQGRPQDVVRDPQV 595
Cdd:TIGR00958 645 TSAL---DAECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQGC 706
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
367-579 |
4.99e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 57.35 E-value: 4.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 367 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGfLAPDEGTVNLCGADGQFHAPKNPADFAALGL 446
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNR-MNELESEVRVEGRVEFFNQNIYERRVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 447 GRTFQIVQP---FAAMTVEENIMVGAFYRHHHEKDAREAARETAWRMG-----LGPLLGAEARGLTIGGLKRLEVARVMA 518
Cdd:PRK14258 87 RRQVSMVHPkpnLFPMSVYDNVAYGVKIVGWRPKLEIDDIVESALKDAdlwdeIKHKIHKSALDLSGGQQQRLCIARALA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489057211 519 MEPRILLLDEVMAGINQTDVRRAIDLMLSIR-DSGVSIIAIEHVMQAVMSLSDRVIVLASGE 579
Cdd:PRK14258 167 VKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLHQVSRLSDFTAFFKGNE 228
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
490-584 |
5.35e-09 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 55.79 E-value: 5.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 490 MGLGPL-LGAEARGLTIGGLKRLEVARVMAMEPR--ILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHvMQAVM 566
Cdd:cd03238 74 VGLGYLtLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEH-NLDVL 152
|
90 100
....*....|....*....|....
gi 489057211 567 SLSDRVIVLA------SGEVIAQG 584
Cdd:cd03238 153 SSADWIIDFGpgsgksGGKVVFSG 176
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
366-594 |
5.44e-09 |
|
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: 58.93 E-value: 5.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 366 ILRVQNLNKHFGG----LHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPD----EGTVNLCGADGqFHAPkn 437
Cdd:COG4172 6 LLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPaahpSGSILFDGQDL-LGLS-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 438 PADFAAL---GLGRTFQivQPFAA----MTVEENIM-VGAFYRHHHEKDAREAARETAWRMGLgPllGAEARgLTI---- 505
Cdd:COG4172 83 ERELRRIrgnRIAMIFQ--EPMTSlnplHTIGKQIAeVLRLHRGLSGAAARARALELLERVGI-P--DPERR-LDAyphq 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 506 --GGLKRlevaRVM-AM----EPRILLLDE--------VMAGInqtdvrraIDLMLSI-RDSGVSIIAIEHVMQAVMSLS 569
Cdd:COG4172 157 lsGGQRQ----RVMiAMalanEPDLLIADEpttaldvtVQAQI--------LDLLKDLqRELGMALLLITHDLGVVRRFA 224
|
250 260
....*....|....*....|....*
gi 489057211 570 DRVIVLASGEVIAQGRPQDVVRDPQ 594
Cdd:COG4172 225 DRVAVMRQGEIVEQGPTAELFAAPQ 249
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
383-584 |
5.78e-09 |
|
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: 56.50 E-value: 5.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 383 RNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPD---EGTVNLCGADGQFHAPKNPADfaalglgrtfqivqpfAAM 459
Cdd:cd03233 24 KDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGE----------------IIY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 460 TVEENImvgafyrHHHEKDARE----AARetawrmglgpLLGAE-ARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGIn 534
Cdd:cd03233 88 VSEEDV-------HFPTLTVREtldfALR----------CKGNEfVRGISGGERKRVSIAEALVSRASVLCWDNSTRGL- 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489057211 535 qtDVRRAIDLMLSIRD----SGVSIIAIehVMQA---VMSLSDRVIVLASGEVIAQG 584
Cdd:cd03233 150 --DSSTALEILKCIRTmadvLKTTTFVS--LYQAsdeIYDLFDKVLVLYEGRQIYYG 202
|
|
| TM_PBP1_transp_TpRbsC_like |
cd06580 |
Transmembrane subunit (TM) of Treponema pallidum (Tp) RbsC-1, RbsC-2 and related proteins. ... |
49-282 |
7.22e-09 |
|
Transmembrane subunit (TM) of Treponema pallidum (Tp) RbsC-1, RbsC-2 and related proteins. This is a functionally uncharacterized subgroup of TMs which belong to a larger group of TMs of Periplasmic Binding Protein (PBP)-dependent ATP-Binding Cassette (ABC) transporters, which are mainly involved in the uptake of branched-chain amino acids (AAs) or in the uptake of monosaccharides including ribose, galactose, and arabinose, and which generally bind type 1 PBPs. PBP-dependent ABC transporters consist of a PBP, two TMs, and two cytoplasmic ABCs, and are mainly involved in importing solutes from the environment. The solute is captured by the PBP, which delivers it to a gated translocation pathway formed by the two TMs. The two ABCs bind and hydrolyze ATP and drive the transport reaction.
Pssm-ID: 119322 [Multi-domain] Cd Length: 234 Bit Score: 56.68 E-value: 7.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 49 TICLFAALSTA-------WNIvgGFAGQMSLGhAVFYGIGGYTGVILFnmGISPWFSMFIGTFIAALVGMVISYPCFRLK 121
Cdd:cd06580 2 TPLILAALGVAisfragvFNI--GLEGQMLLG-AFAAALVALYLGLPA--TGSLPLGLLAAALAGALWALLPALLKAKLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 122 GPfyslasiaflEVFRVLALHFGwltggATGLMiqlklgwvwmvfrerwpSLLIVFGMLLVtLAITWAARRSRLGFYLVA 201
Cdd:cd06580 77 VN----------EVISGLMLNYI-----ALGLT-----------------SYLLLLALLLV-ILVWLLLYRTRFGLRLRA 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 202 TRERESAARAAGVRTVRVRLIAVAISSALCAMLGTFHAMYLTFIEPAAMFS-LAFS-IQIAMFALNGGLGTVAGPLLGAV 279
Cdd:cd06580 124 VGENPRAARYAGINVKRVRLLAMLISGALAGLAGAYLVLGVQGRFTEGMSAgYGFIaIAVALLGRWNPLGILLAALLFGA 203
|
...
gi 489057211 280 LLV 282
Cdd:cd06580 204 LEA 206
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
366-580 |
9.86e-09 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 56.04 E-value: 9.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 366 ILRVQNLNK-HFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGAD-GQFHAPKNPadFAA 443
Cdd:PRK10908 1 MIRFEHVSKaYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDiTRLKNREVP--FLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 444 LGLGRTFQIVQPFAAMTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRI 523
Cdd:PRK10908 79 RQIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489057211 524 LLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEV 580
Cdd:PRK10908 159 LLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
388-579 |
1.53e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.51 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 388 TLREGEVLGLIGPNGAGKTTLFNMISGFLAPdegtvNLCGADgqfhapkNPAD-------FAALGLGRTFQ--------- 451
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIP-----NLGDYE-------EEPSwdevlkrFRGTELQNYFKklyngeikv 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 452 IVQP----FAAM----TVEENIMvgafyrhhhEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRI 523
Cdd:PRK13409 163 VHKPqyvdLIPKvfkgKVRELLK---------KVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADF 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489057211 524 LLLDEVMagiNQTDVRRAIDLMLSIRD--SGVSIIAIEHVMqAVMS-LSDrVIVLASGE 579
Cdd:PRK13409 234 YFFDEPT---SYLDIRQRLNVARLIRElaEGKYVLVVEHDL-AVLDyLAD-NVHIAYGE 287
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
384-578 |
1.81e-08 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 54.56 E-value: 1.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 384 NVSFTLREGEVLGLIGPNGAGKTTLFNMISG--FLAPDEGTVNLCGadgqfhapknpadfaaLGLGRTFQIVQPFaamtV 461
Cdd:cd03232 25 NISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILING----------------RPLDKNFQRSTGY----V 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 462 EENimvgafYRHHHEKDAREAARETAWrmglgpllgaeARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGInqtDVRRA 541
Cdd:cd03232 85 EQQ------DVHSPNLTVREALRFSAL-----------LRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGL---DSQAA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489057211 542 IDLMLSIR---DSGVSII-AIEHVMQAVMSLSDRVIVLASG 578
Cdd:cd03232 145 YNIVRFLKklaDSGQAILcTIHQPSASIFEKFDRLLLLKRG 185
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
364-594 |
2.03e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 57.17 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 364 QDILRVQNLNKHF----GGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNlCG------------ 427
Cdd:PRK10261 10 RDVLAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQ-CDkmllrrrsrqvi 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 428 -----ADGQFHAPKNpADFAALglgrtFQivQPFAAM----TVEENImvgAFYRHHHEKDAREAARETAWRM-------G 491
Cdd:PRK10261 89 elseqSAAQMRHVRG-ADMAMI-----FQ--EPMTSLnpvfTVGEQI---AESIRLHQGASREEAMVEAKRMldqvripE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 492 LGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSI-RDSGVSIIAIEHVMQAVMSLSD 570
Cdd:PRK10261 158 AQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLqKEMSMGVIFITHDMGVVAEIAD 237
|
250 260
....*....|....*....|....
gi 489057211 571 RVIVLASGEVIAQGRPQDVVRDPQ 594
Cdd:PRK10261 238 RVLVMYQGEAVETGSVEQIFHAPQ 261
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
367-590 |
2.21e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 57.14 E-value: 2.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 367 LRVQNLnkHFG----GLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGadgqfhapKNPADF- 441
Cdd:PRK11160 339 LTLNNV--SFTypdqPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNG--------QPIADYs 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 442 -AALGLGRTF--QIVQPFAAmTVEENIMVGAfyrhHHEKDarEAARETAWRMGLGPLL----------GAEARGLTIGGL 508
Cdd:PRK11160 409 eAALRQAISVvsQRVHLFSA-TLRDNLLLAA----PNASD--EALIEVLQQVGLEKLLeddkglnawlGEGGRQLSGGEQ 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 509 KRLEVARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRdSGVSIIAIEHVMQAVMSLsDRVIVLASGEVIAQGRPQD 588
Cdd:PRK11160 482 RRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHA-QNKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQE 559
|
..
gi 489057211 589 VV 590
Cdd:PRK11160 560 LL 561
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
381-590 |
2.31e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 57.29 E-value: 2.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 381 VTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADgqfhapknPADFAALGLGRTFQIVQPFAAM- 459
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCD--------VAKFGLTDLRRVLSIIPQSPVLf 1322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 460 --TVEENImvgAFYRHHHEKDAREAARETAWR-------MGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVM 530
Cdd:PLN03232 1323 sgTVRFNI---DPFSEHNDADLWEALERAHIKdvidrnpFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEAT 1399
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489057211 531 AGInqtDVRRAIDLMLSIRDS--GVSIIAIEHVMQAVMSlSDRVIVLASGEVIAQGRPQDVV 590
Cdd:PLN03232 1400 ASV---DVRTDSLIQRTIREEfkSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELL 1457
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
366-594 |
2.92e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 55.90 E-value: 2.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 366 ILRVQNLNKHFGG----LHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGflapdegtvnLCGADGQFHAPK---NP 438
Cdd:PRK11022 3 LLNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMG----------LIDYPGRVMAEKlefNG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 439 ADFAALGLGRTFQIVQPFAAM-------------TVEENIMVGAfyrHHHEKDAREAARETAwrMGLGPLLG---AEAR- 501
Cdd:PRK11022 73 QDLQRISEKERRNLVGAEVAMifqdpmtslnpcyTVGFQIMEAI---KVHQGGNKKTRRQRA--IDLLNQVGipdPASRl 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 502 -----GLTIGGLKRLEVARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSI-RDSGVSIIAIEHVMQAVMSLSDRVIVL 575
Cdd:PRK11022 148 dvyphQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqQKENMALVLITHDLALVAEAAHKIIVM 227
|
250
....*....|....*....
gi 489057211 576 ASGEVIAQGRPQDVVRDPQ 594
Cdd:PRK11022 228 YAGQVVETGKAHDIFRAPR 246
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
388-579 |
2.95e-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: 56.72 E-value: 2.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 388 TLREGEVLGLIGPNGAGKTTLFNMISGFLAPdegtvNLcgadGQFHapkNPAD-------FAALGLGRTFQIVqpfaamt 460
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGELKP-----NL----GDYD---EEPSwdevlkrFRGTELQDYFKKL------- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 461 VEENI-------MVGAFYRHHH-------EK-DAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILL 525
Cdd:COG1245 156 ANGEIkvahkpqYVDLIPKVFKgtvrellEKvDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYF 235
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489057211 526 LDEVmaginqT---DVRRAIDLMLSIRD---SGVSIIAIEHVMqAVMS-LSDrVIVLASGE 579
Cdd:COG1245 236 FDEP------SsylDIYQRLNVARLIRElaeEGKYVLVVEHDL-AILDyLAD-YVHILYGE 288
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
368-581 |
3.97e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 54.19 E-value: 3.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 368 RVQNLNKHFG------GLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFL--APDEGTVNLcgadgqfhaPKNPA 439
Cdd:COG2401 26 RVAIVLEAFGvelrvvERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDV---------PDNQF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 440 DfaalglgrtfqivqpfaamtvEENIMVGAFYRHHHEKDAREAARetawRMGLG--PLLGAEARGLTIGGLKRLEVARVM 517
Cdd:COG2401 97 G---------------------REASLIDAIGRKGDFKDAVELLN----AVGLSdaVLWLRRFKELSTGQKFRFRLALLL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489057211 518 AMEPRILLLDEVMAGIN-QTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLS-DRVIVLASGEVI 581
Cdd:COG2401 152 AERPKLLVIDEFCSHLDrQTAKRVARNLQKLARRAGITLVVATHHYDVIDDLQpDLLIFVGYGGVP 217
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
383-585 |
8.05e-08 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 55.41 E-value: 8.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 383 RNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKNPADFAALglgrTFQIVQPFAAmTVE 462
Cdd:PRK11176 360 RNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVAL----VSQNVHLFND-TIA 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 463 ENImvgAFYRH-HHEKDAREAARETAWRM--------GLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGI 533
Cdd:PRK11176 435 NNI---AYARTeQYSREQIEEAARMAYAMdfinkmdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSAL 511
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489057211 534 NqTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSlSDRVIVLASGEVIAQGR 585
Cdd:PRK11176 512 D-TESERAIQAALDELQKNRTSLVIAHRLSTIEK-ADEILVVEDGEIVERGT 561
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
392-590 |
8.18e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 55.27 E-value: 8.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 392 GEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKnpadfaalgLGRTFQIVQP---FAAMTVEENIMVG 468
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANNRKPTKQI---------LKRTGFVTQDdilYPHLTVRETLVFC 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 469 AFYRHHH---EKDAREAARETAWRMGL----GPLLGAE-ARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGINQTDVRR 540
Cdd:PLN03211 165 SLLRLPKsltKQEKILVAESVISELGLtkceNTIIGNSfIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYR 244
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489057211 541 AIDLMLSIRDSGVSIIAIEHVMQA-VMSLSDRVIVLASGEVIAQGRPQDVV 590
Cdd:PLN03211 245 LVLTLGSLAQKGKTIVTSMHQPSSrVYQMFDSVLVLSEGRCLFFGKGSDAM 295
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
366-560 |
9.26e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 52.64 E-value: 9.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 366 ILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVnlcgadgQFHAPKNPADFAALG 445
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEI-------LFERQSIKKDLCTYQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 446 LGRTF----QIVQPFaaMTVEENimvgAFYRHHHEKDAREAArETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEP 521
Cdd:PRK13540 74 KQLCFvghrSGINPY--LTLREN----CLYDIHFSPGAVGIT-ELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKA 146
|
170 180 190
....*....|....*....|....*....|....*....
gi 489057211 522 RILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEH 560
Cdd:PRK13540 147 KLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSH 185
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
385-594 |
1.09e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 54.20 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 385 VSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADgqfhAPKNPADFAALgLGRTFQIV--QPFAAM--- 459
Cdd:PRK11308 34 VSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQD----LLKADPEAQKL-LRQKIQIVfqNPYGSLnpr 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 460 -----TVEE----NIMVGAFYRhhhekdaREAARETAWRMGLGPLLGAEARGLTIGGLK-RLEVARVMAMEPRILLLDE- 528
Cdd:PRK11308 109 kkvgqILEEplliNTSLSAAER-------REKALAMMAKVGLRPEHYDRYPHMFSGGQRqRIAIARALMLDPDVVVADEp 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 529 VMAginqTDVR-RA--IDLMLSI-RDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDPQ 594
Cdd:PRK11308 182 VSA----LDVSvQAqvLNLMMDLqQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPR 247
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
344-580 |
1.22e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 54.35 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 344 IAAVPARAIKAPSPDRAGI-GQDILRVQNLNKHfgGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGT 422
Cdd:PRK10982 227 IAMMVGRSLTQRFPDKENKpGEVILEVRNLTSL--RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGT 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 423 VNLCGadgqfHAPKNPADFAALGLGrtFQIVQP-------FAAMTVEENIMVgAFYRHHHEK----DAREAARETAW--- 488
Cdd:PRK10982 305 ITLHG-----KKINNHNANEAINHG--FALVTEerrstgiYAYLDIGFNSLI-SNIRNYKNKvgllDNSRMKSDTQWvid 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 489 ---------RMGLGPLLGAEARGLTIGglkrlevaRVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIE 559
Cdd:PRK10982 377 smrvktpghRTQIGSLSGGNQQKVIIG--------RWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIIS 448
|
250 260
....*....|....*....|.
gi 489057211 560 HVMQAVMSLSDRVIVLASGEV 580
Cdd:PRK10982 449 SEMPELLGITDRILVMSNGLV 469
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
363-427 |
1.23e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.57 E-value: 1.23e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489057211 363 GQDILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNlCG 427
Cdd:PRK11147 316 GKIVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIH-CG 379
|
|
| BCA_ABC_TP_C |
pfam12399 |
Branched-chain amino acid ATP-binding cassette transporter; This domain family is found in ... |
579-603 |
1.28e-07 |
|
Branched-chain amino acid ATP-binding cassette transporter; This domain family is found in bacteria, archaea and eukaryotes, and is approximately 30 amino acids in length. The family is found in association with pfam00005. There is a conserved AYLG sequence motif. This family is the C terminal of an ATP dependent branched-chain amino acid transporter. This domain is essential for LPS transport, through critical interactions with Walker A and switch helix domains.
Pssm-ID: 463560 Cd Length: 25 Bit Score: 47.63 E-value: 1.28e-07
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
354-580 |
2.05e-07 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 52.37 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 354 APSPDRAGIGQDILrVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVnLCGAdgqfh 433
Cdd:PRK11247 1 MMNTARLNQGTPLL-LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGT----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 434 APKNPA-DFAALglgrTFQIVQPFAAMTVEENIMVGAfyrhhhEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLE 512
Cdd:PRK11247 74 APLAEArEDTRL----MFQDARLLPWKKVIDNVGLGL------KGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 513 VARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSI-RDSGVSIIAIEH-VMQAVmSLSDRVIVLASGEV 580
Cdd:PRK11247 144 LARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHdVSEAV-AMADRVLLIEEGKI 212
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
366-593 |
2.57e-07 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 52.88 E-value: 2.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 366 ILRVQNLNKHF----GGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGF---------------------LAPDE 420
Cdd:PRK15093 3 LLDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVtkdnwrvtadrmrfddidllrLSPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 421 GTvNLCGADGQ--FHAPKNPADFAAlGLGRtfQIVQPFAAMTVEenimvGAFYRHHHEKDAReaARETAWRMGLG---PL 495
Cdd:PRK15093 83 RR-KLVGHNVSmiFQEPQSCLDPSE-RVGR--QLMQNIPGWTYK-----GRWWQRFGWRKRR--AIELLHRVGIKdhkDA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 496 LGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSI-RDSGVSIIAIEHVMQAVMSLSDRVIV 574
Cdd:PRK15093 152 MRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADKINV 231
|
250
....*....|....*....
gi 489057211 575 LASGEVIAQGRPQDVVRDP 593
Cdd:PRK15093 232 LYCGQTVETAPSKELVTTP 250
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
367-593 |
3.26e-07 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 52.54 E-value: 3.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 367 LRVQNLNKHF-GGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQFHAPKNPADfaaLG 445
Cdd:PRK11650 4 LKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWI---GGRVVNELEPAD---RD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 446 LGRTFQIVQPFAAMTVEENIMVG----AFYRHHHEKDAREAARetawRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEP 521
Cdd:PRK11650 78 IAMVFQNYALYPHMSVRENMAYGlkirGMPKAEIEERVAEAAR----ILELEPLLDRKPRELSGGQRQRVAMGRAIVREP 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489057211 522 RILLLDEVMAGInqtDVRRAIDLMLSI----RDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDP 593
Cdd:PRK11650 154 AVFLFDEPLSNL---DAKLRVQMRLEIqrlhRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKP 226
|
|
| PRK10740 |
PRK10740 |
high-affinity branched-chain amino acid ABC transporter permease LivH; |
53-321 |
7.33e-07 |
|
high-affinity branched-chain amino acid ABC transporter permease LivH;
Pssm-ID: 182689 [Multi-domain] Cd Length: 308 Bit Score: 51.46 E-value: 7.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 53 FAALSTAWNIVGGFAGQMSLGHAVFYGIGGYTGVI----LFNMGISPWFSMFIGTFIAALVGMV--------ISYPCFRL 120
Cdd:PRK10740 22 YALIAIGYTMVYGIIGMINFAHGEVYMIGSYVSFMiiaaLMMMGIDTSWLLVAAGFVGAIVIASaygwsierVAYRPVRN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 121 KGPFYSLASIAFLEVFrvlALHFGWLTGGATGLMIQLKLGWVWMVFRERWPS-------LLIVFGMLLVTLAITWAARRS 193
Cdd:PRK10740 102 SKRLIALISAIGMSIF---LQNYVSLTEGSRDVALPSLFNGQWVVGHSENFSasittmqAVIWIVTFLAMLALTIFIRYS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 194 RLGFYLVATRERESAARAAGVRTVRVRLIAVAISSALCAMLGTFHAMYLTFIEPAAMFSLAFSIQIAmfALNGGLGTVAG 273
Cdd:PRK10740 179 RMGRACRACAEDLKMASLLGINTDRVIALTFVIGAAMAAVAGVLLGQFYGVINPYIGFMAGMKAFTA--AVLGGIGSIPG 256
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 489057211 274 PLLGAVLLVPITEWARASLGASALGLHGFVyglVLILVVLFMPNGIMG 321
Cdd:PRK10740 257 AMIGGLILGIAEALSSAYLSTEYKDVVSFA---LLILVLLVMPTGILG 301
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
381-590 |
9.39e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 52.26 E-value: 9.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 381 VTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCG---ADGQFH--------APKNPADFAalglGRT 449
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGlniAKIGLHdlrfkitiIPQDPVLFS----GSL 1376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 450 FQIVQPFAAMTvEENIMVGAFYRHHHEKDAREAAretawrmGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEV 529
Cdd:TIGR00957 1377 RMNLDPFSQYS-DEEVWWALELAHLKTFVSALPD-------KLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEA 1448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489057211 530 MAGIN-QTDvrraiDLMLS-IRDS--GVSIIAIEHVMQAVMSLSdRVIVLASGEVIAQGRPQDVV 590
Cdd:TIGR00957 1449 TAAVDlETD-----NLIQStIRTQfeDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLL 1507
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
526-604 |
1.01e-06 |
|
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: 51.94 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 526 LDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAvMSLSDRVIVLA------SGEVIAQGRPQDVVRDPQ-VVEA 598
Cdd:TIGR00630 514 LDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDT-IRAADYVIDIGpgagehGGEVVASGTPEEILANPDsLTGQ 592
|
....*.
gi 489057211 599 YLGKEF 604
Cdd:TIGR00630 593 YLSGRK 598
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
381-593 |
1.27e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 51.25 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 381 VTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGtvnlcgaDGQFHAPKNPaDFAALGLGRTFQIVQ--PFA- 457
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEG-------DIRFHDIPLT-KLQLDSWRSRLAVVSqtPFLf 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 458 AMTVEENIMVG--AFYRHHHEKDAREAA-RETAWRMGLGPLLGAEARGLTI-GGLK-RLEVARVMAMEPRILLLDEVMAG 532
Cdd:PRK10789 402 SDTVANNIALGrpDATQQEIEHVARLASvHDDILRLPQGYDTEVGERGVMLsGGQKqRISIARALLLNAEILILDDALSA 481
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489057211 533 InqtDVRRAIDLMLSIRD--SGVSIIAIEHVMQAvMSLSDRVIVLASGEVIAQGRPQDVVRDP 593
Cdd:PRK10789 482 V---DGRTEHQILHNLRQwgEGRTVIISAHRLSA-LTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
170-431 |
1.49e-06 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 50.95 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 170 WPSLLIVFGMLLVTLAITWAARRsRLGFYLVATRERE-------------------SAARAAGVRTVRVRLIAVAISSal 230
Cdd:COG4615 147 PPLFLLTLVLLGLGVAGYRLLVR-RARRHLRRAREAEdrlfkhfrallegfkelklNRRRRRAFFDEDLQPTAERYRD-- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 231 camlgtfhamylTFIEPAAMFSLAFS-IQIAMFALngglgtvagplLGAVL-LVPITEWARASLgasalgLHGFVyglvl 308
Cdd:COG4615 224 ------------LRIRADTIFALANNwGNLLFFAL-----------IGLILfLLPALGWADPAV------LSGFV----- 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 309 iLVVLFM--P-NGIMGAINRFVRkpqdseetatartepiAAVPARAIKA--PSPDRAGIGQDILRVQNLNKHFGGLHVtR 383
Cdd:COG4615 270 -LVLLFLrgPlSQLVGALPTLSR----------------ANVALRKIEEleLALAAAEPAAADAAAPPAPADFQTLEL-R 331
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489057211 384 NVSF------------------TLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQ 431
Cdd:COG4615 332 GVTYrypgedgdegftlgpidlTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILL---DGQ 394
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
366-589 |
1.80e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 51.28 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 366 ILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQfhapkNPADFAAL- 444
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMA-----DARHRRAVc 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 445 --------GLGRTFqivqpFAAMTVEENImvgAFYrhhhekdAR---EAARETAWRM-------GLGPLLGAEARGLTiG 506
Cdd:NF033858 76 priaympqGLGKNL-----YPTLSVFENL---DFF-------GRlfgQDAAERRRRIdellratGLAPFADRPAGKLS-G 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 507 GLKR---LEVARVmaMEPRILLLDEVMAGINQTDVRRAIDLMLSIRDS--GVSIIaiehVMQAVMSLSDR---VIVLASG 578
Cdd:NF033858 140 GMKQklgLCCALI--HDPDLLILDEPTTGVDPLSRRQFWELIDRIRAErpGMSVL----VATAYMEEAERfdwLVAMDAG 213
|
250
....*....|.
gi 489057211 579 EVIAQGRPQDV 589
Cdd:NF033858 214 RVLATGTPAEL 224
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
390-575 |
2.37e-06 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 49.29 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 390 REGEVLGLIGPNGAGKTTLFNMISGFLAPdegtvNLCGADGQ---------FHAPKNPADFAALGLGRTFQIVQP----- 455
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKP-----NLGKFDDPpdwdeildeFRGSELQNYFTKLLEGDVKVIVKPqyvdl 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 456 ---FAAMTVEENImvgafyrhhHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAG 532
Cdd:cd03236 99 ipkAVKGKVGELL---------KKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSY 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489057211 533 InqtDVRRAIDLMLSIR---DSGVSIIAIEHVMQAVMSLSDRVIVL 575
Cdd:cd03236 170 L---DIKQRLNAARLIRelaEDDNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
383-579 |
2.85e-06 |
|
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: 48.23 E-value: 2.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 383 RNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGqfhapknpadFAAlglgrtfQivQPFA-AMTV 461
Cdd:cd03250 22 KDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIA----------YVS-------Q--EPWIqNGTI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 462 EENIMVGAFYRHHHEKDAREAAretawrmGLGPLL-----GAEA----RGLTI-GGLK-RLEVARVMAMEPRILLLDEVM 530
Cdd:cd03250 83 RENILFGKPFDEERYEKVIKAC-------ALEPDLeilpdGDLTeigeKGINLsGGQKqRISLARAVYSDADIYLLDDPL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489057211 531 AGINqTDVRRAI--DLMLSIRDSGVSIIAIEHVMQAVmSLSDRVIVLASGE 579
Cdd:cd03250 156 SAVD-AHVGRHIfeNCILGLLLNNKTRILVTHQLQLL-PHADQIVVLDNGR 204
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
383-594 |
2.98e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 48.93 E-value: 2.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 383 RNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPdeGTVNLCG---ADGQfhaPKNPADFAalglGRT---------- 449
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPA--GVRQTAGrvlLDGK---PVAPCALR----GRKiatimqnprs 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 450 -FQIVQPFAAMTVEENIMVGafyRHHHEKDAREAAREtawrMGLGP---LLGAEARGLTIGGLKRLEVARVMAMEPRILL 525
Cdd:PRK10418 91 aFNPLHTMHTHARETCLALG---KPADDATLTAALEA----VGLENaarVLKLYPFEMSGGMLQRMMIALALLCEAPFII 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 526 LDEVMAGINQTDVRRAIDLMLSI-RDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDPQ 594
Cdd:PRK10418 164 ADEPTTDLDVVAQARILDLLESIvQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPK 233
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
491-589 |
4.23e-06 |
|
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: 50.01 E-value: 4.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 491 GLGPL-LGAEARGLTIGGLKRLEVARVM---AMEPRILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQaVM 566
Cdd:TIGR00630 817 GLGYIrLGQPATTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLD-VI 895
|
90 100
....*....|....*....|....*....
gi 489057211 567 SLSDRVIVL------ASGEVIAQGRPQDV 589
Cdd:TIGR00630 896 KTADYIIDLgpeggdGGGTVVASGTPEEV 924
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
379-560 |
4.85e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 49.84 E-value: 4.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 379 LHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPD--EGTVNLCGadgqfhAPKNPADFAAL-GLGRTFQIVQP 455
Cdd:PLN03140 893 LQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISG------FPKKQETFARIsGYCEQNDIHSP 966
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 456 faAMTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPL--LGAEARGLT-IGGL-----KRLEVARVMAMEPRILLLD 527
Cdd:PLN03140 967 --QVTVRESLIYSAFLRLPKEVSKEEKMMFVDEVMELVELdnLKDAIVGLPgVTGLsteqrKRLTIAVELVANPSIIFMD 1044
|
170 180 190
....*....|....*....|....*....|....*.
gi 489057211 528 EVMAGInqtDVRRAIDLMLSIR---DSGVSIIAIEH 560
Cdd:PLN03140 1045 EPTSGL---DARAAAIVMRTVRntvDTGRTVVCTIH 1077
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
363-427 |
6.54e-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: 49.52 E-value: 6.54e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489057211 363 GQDILRVQNLNKHfgGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCG 427
Cdd:TIGR01271 425 GDDGLFFSNFSLY--VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG 487
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
383-560 |
8.57e-06 |
|
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: 46.38 E-value: 8.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 383 RNVSFTLREGEVLGLIGPNGAGKTTLFNMISGfLAP-DEGTVNLCGADGQFHAPKNPadFAALGLGRTfQIVQPfaamtv 461
Cdd:cd03223 18 KDLSFEIKPGDRLLITGPSGTGKSSLFRALAG-LWPwGSGRIGMPEGEDLLFLPQRP--YLPLGTLRE-QLIYP------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 462 eenimvgafyrhhhekdareaaretaWRMGLGPllgaeargltiGGLKRLEVARVMAMEPRILLLDEVMAGINQTDVRRA 541
Cdd:cd03223 88 --------------------------WDDVLSG-----------GEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRL 130
|
170
....*....|....*....
gi 489057211 542 IDLmlsIRDSGVSIIAIEH 560
Cdd:cd03223 131 YQL---LKELGITVISVGH 146
|
|
| NupP |
COG4603 |
ABC-type guanosine uptake system NupNOPQ, permease component NupP [Nucleotide transport and ... |
176-282 |
1.17e-05 |
|
ABC-type guanosine uptake system NupNOPQ, permease component NupP [Nucleotide transport and metabolism];
Pssm-ID: 443653 [Multi-domain] Cd Length: 356 Bit Score: 47.81 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 176 VFGMLLVTLAITWAARRSRLGFYLVATRERESAARAAGVRTVRVRLIAVAISSALCAMLGTFHAM-YLTFIEPAAMFSLA 254
Cdd:COG4603 200 LLIALLAAVLVWVLLNRTTLGYELRAVGLNPRAARYAGINVKRLIVLAMLISGALAGLAGAVEVLgVQGRLTPGFSPGYG 279
|
90 100
....*....|....*....|....*....
gi 489057211 255 FS-IQIAMFALNGGLGTVAGPLLGAVLLV 282
Cdd:COG4603 280 FTgIAVALLGRNNPLGIILAALLFGALYV 308
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
389-482 |
1.35e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 46.03 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 389 LREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGT--------------VNLCGADGQFHApknpadfAALGLGRT---FQ 451
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNdewdgitpvykpqyIDLSGGELQRVA-------IAAALLRNatfYL 94
|
90 100 110
....*....|....*....|....*....|.
gi 489057211 452 IVQPFAAMTVEENIMVGAFYRHHHEKDAREA 482
Cdd:cd03222 95 FDEPSAYLDIEQRLNAARAIRRLSEEGKKTA 125
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
384-560 |
2.14e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 47.64 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 384 NVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVN----LCGADGQFHAPKNPA----DFAALGLGRTFQIVQP 455
Cdd:PRK11147 21 NAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIyeqdLIVARLQQDPPRNVEgtvyDFVAEGIEEQAEYLKR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 456 FAAMT--VEENIMvgafyrhhhEKDAREAAR-------ETAWRMG------LGPL-LGAEAR--GLTIGGLKRLEVARVM 517
Cdd:PRK11147 101 YHDIShlVETDPS---------EKNLNELAKlqeqldhHNLWQLEnrinevLAQLgLDPDAAlsSLSGGWLRKAALGRAL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489057211 518 AMEPRILLLDEvmaGINQTDVrRAID-LMLSIRDSGVSIIAIEH 560
Cdd:PRK11147 172 VSNPDVLLLDE---PTNHLDI-ETIEwLEGFLKTFQGSIIFISH 211
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
366-414 |
2.18e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 46.17 E-value: 2.18e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 489057211 366 ILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISG 414
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG 55
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
376-534 |
2.81e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 45.61 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 376 FGGLHvtrnvsFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQFHAPKNPADFAALgLGRTFQIVQP 455
Cdd:PRK13543 27 FGPLD------FHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQI---DGKTATRGDRSRFMAY-LGHLPGLKAD 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489057211 456 FAAMtveENIMvgaFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGIN 534
Cdd:PRK13543 97 LSTL---ENLH---FLCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
489-605 |
2.92e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.52 E-value: 2.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 489 RMGLGPLLGAEARGLTigglkrlevarvmamepriLLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQaVMSL 568
Cdd:PRK00635 484 RTALAKHLGAELIGIT-------------------YILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQ-MISL 543
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 489057211 569 SDRVIVLA------SGEVIAQGRPQDVVRDPQVVEA-YLGKEFA 605
Cdd:PRK00635 544 ADRIIDIGpgagifGGEVLFNGSPREFLAKSDSLTAkYLRQELT 587
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
366-584 |
3.38e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 45.55 E-value: 3.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 366 ILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGF--LAPDEGTVNLCGADgqfHAPKNPADFAA 443
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKD---LLELSPEDRAG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 444 LGLGRTFQ--IVQPFAAMTVEENIMVGAF--YRHHHEKDAREAA-----RETAWRMGLGPLLGAEARGLTIGGLKRLEVA 514
Cdd:PRK09580 78 EGIFMAFQypVEIPGVSNQFFLQTALNAVrsYRGQEPLDRFDFQdlmeeKIALLKMPEDLLTRSVNVGFSGGEKKRNDIL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489057211 515 RVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLS-DRVIVLASGEVIAQG 584
Cdd:PRK09580 158 QMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDYIKpDYVHVLYQGRIVKSG 228
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
363-427 |
4.30e-05 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 45.62 E-value: 4.30e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489057211 363 GQDILRVQNLNKHfgGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCG 427
Cdd:cd03291 36 DDNNLFFSNLCLV--GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG 98
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
491-586 |
4.60e-05 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 45.30 E-value: 4.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 491 GLGPL-LGAEARGLTIGGLKRLEVARVMAMEPR---ILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQaVM 566
Cdd:cd03271 157 GLGYIkLGQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLD-VI 235
|
90 100
....*....|....*....|....*.
gi 489057211 567 SLSDRVIVL------ASGEVIAQGRP 586
Cdd:cd03271 236 KCADWIIDLgpeggdGGGQVVASGTP 261
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
385-560 |
5.20e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 46.12 E-value: 5.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 385 VSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQFHAPKNPADFAALglgrtfqivqpFAAMTVEen 464
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILL---DGKPVTAEQPEDYRKL-----------FSAVFTD-- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 465 imvgaFYRHHH----EKDAREAARETAW--RMGLGPLLGAE-ARGLTI----GGLKRLEVARVMAMEPRILLLDEVMAgi 533
Cdd:PRK10522 406 -----FHLFDQllgpEGKPANPALVEKWleRLKMAHKLELEdGRISNLklskGQKKRLALLLALAEERDILLLDEWAA-- 478
|
170 180 190
....*....|....*....|....*....|
gi 489057211 534 NQTDVRRAI---DLMLSIRDSGVSIIAIEH 560
Cdd:PRK10522 479 DQDPHFRREfyqVLLPLLQEMGKTIFAISH 508
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
491-584 |
5.69e-05 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 44.94 E-value: 5.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 491 GLGPL-LGAEARGLTIGGLKRLEVARVMAMEPR--ILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVmQAVMS 567
Cdd:cd03270 125 GLGYLtLSRSAPTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHD-EDTIR 203
|
90 100
....*....|....*....|...
gi 489057211 568 LSDRVIVLA------SGEVIAQG 584
Cdd:cd03270 204 AADHVIDIGpgagvhGGEIVAQG 226
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
386-560 |
7.38e-05 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 45.90 E-value: 7.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 386 SFTLREGEVLGLIGPNGAGKTTLFNMISGfLAPDEGTVNLCGADGQ-FHAPKNPadFAALGLGRTfQIVQPfaaMTVEEN 464
Cdd:TIGR00954 472 SFEVPSGNNLLICGPNGCGKSSLFRILGE-LWPVYGGRLTKPAKGKlFYVPQRP--YMTLGTLRD-QIIYP---DSSEDM 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 465 IMvgafyRHHHEKDAREAAREtawrMGLGPLL----GAEARG-----LTIGGLKRLEVARVMAMEPRILLLDEVMAGINq 535
Cdd:TIGR00954 545 KR-----RGLSDKDLEQILDN----VQLTHILeregGWSAVQdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVS- 614
|
170 180
....*....|....*....|....*
gi 489057211 536 TDVRRAIDLMLsiRDSGVSIIAIEH 560
Cdd:TIGR00954 615 VDVEGYMYRLC--REFGITLFSVSH 637
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
377-423 |
1.38e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.85 E-value: 1.38e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 489057211 377 GGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTV 423
Cdd:PLN03073 520 GGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV 566
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
357-408 |
1.61e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.40 E-value: 1.61e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 489057211 357 PDR-AGIGQDILRVQNLNKH---FGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTL 408
Cdd:NF040905 247 PERtPKIGEVVFEVKNWTVYhplHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTEL 302
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
366-425 |
1.80e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.39 E-value: 1.80e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 366 ILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNL 425
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL 371
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
473-590 |
2.47e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.43 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 473 HHHEKdareaaRETAWRMGLGPL-LGAEARGLTIGGLKRLEVARVM---AMEPRILLLDEVMAGINQTDVRRAIDLMLSI 548
Cdd:PRK00635 785 SIHEK------IHALCSLGLDYLpLGRPLSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSL 858
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 489057211 549 RDSGVSIIAIEHVMQaVMSLSDRVIVLA------SGEVIAQGRPQDVV 590
Cdd:PRK00635 859 THQGHTVVIIEHNMH-VVKVADYVLELGpeggnlGGYLLASCSPEELI 905
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
296-427 |
2.93e-04 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 44.13 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 296 ALGLHGFVYGLVLILVVLFMP---------------NGIMGAINR---FVRKPQDSEETaTARTEPIAAVPARAIKAPSP 357
Cdd:TIGR01271 1130 AIGTNQDGEGEVGIILTLAMNilstlqwavnssidvDGLMRSVSRvfkFIDLPQEEPRP-SGGGGKYQLSTVLVIENPHA 1208
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489057211 358 DRAGIGQDILRVQNLNKHF--GGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLfnmISGF--LAPDEGTVNLCG 427
Cdd:TIGR01271 1209 QKCWPSGGQMDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTL---LSALlrLLSTEGEIQIDG 1279
|
|
| PRK15432 |
PRK15432 |
autoinducer 2 ABC transporter permease LsrC; Provisional |
179-314 |
2.97e-04 |
|
autoinducer 2 ABC transporter permease LsrC; Provisional
Pssm-ID: 185330 [Multi-domain] Cd Length: 344 Bit Score: 43.18 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 179 MLLVTLAITWAARRSRLGFYLVATRERESAARAAGVRTVRVRLIAVAISSALCAMLGTFHAMYLTFIEPAA-----MFSL 253
Cdd:PRK15432 166 TLILILAMAWLLAKTAFGRSFYATGDNLQGARQLGVRTEAIRIVAFSLNGCMAALAGIVFASQIGFIPNQTgtgleMKAI 245
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489057211 254 AFSIqIAMFALNGGLGTVAGPLLGAVLLVPITewaraslgaSALGL-------HGFVYGLVLILVVLF 314
Cdd:PRK15432 246 AACV-LGGISLLGGSGTIIGAVLGAYFLTQID---------SVLVLlripawwNDFIAGLVLLGVLVF 303
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
392-432 |
4.13e-04 |
|
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: 41.20 E-value: 4.13e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 489057211 392 GEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQF 432
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDIL 42
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
371-425 |
5.33e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 42.96 E-value: 5.33e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 489057211 371 NLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNL 425
Cdd:PRK15064 6 NITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSL 60
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
526-594 |
5.35e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 43.09 E-value: 5.35e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489057211 526 LDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEH---VMQAvmslSDRVIVL------ASGEVIAQGRPQDVVRDPQ 594
Cdd:COG0178 511 LDEPSIGLHQRDNDRLIETLKRLRDLGNTVIVVEHdedTIRA----ADYIIDIgpgageHGGEVVAQGTPEEILKNPD 584
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
496-575 |
6.48e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 43.09 E-value: 6.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 496 LGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRDSG-VSIIAIEHVMqAVMSLSDRVIV 574
Cdd:PTZ00265 1352 VGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRI-ASIKRSDKIVV 1430
|
.
gi 489057211 575 L 575
Cdd:PTZ00265 1431 F 1431
|
|
| rbsC |
PRK09512 |
ribose ABC transporter permease protein; Reviewed |
176-281 |
7.45e-04 |
|
ribose ABC transporter permease protein; Reviewed
Pssm-ID: 181922 [Multi-domain] Cd Length: 320 Bit Score: 42.01 E-value: 7.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 176 VFGMLLVTLAITWAARRSRLGFYLVATRERESAARAAGVRTVRVRLIAVAISSALCAMLGTFHAMYLTFIEPAAMFSLAF 255
Cdd:PRK09512 175 VWIMAIVFLAAWYMLHHTRLGRYIYALGGNEAATRLSGINVNKVKIIVYALCGLLAALAGIIEVARLSSAQPTAGTGYEL 254
|
90 100 110
....*....|....*....|....*....|
gi 489057211 256 SIQIAMF----ALNGGLGTVAGPLLGAVLL 281
Cdd:PRK09512 255 DAIAAVVlggtSLAGGKGRIVGTLIGALIL 284
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
383-528 |
1.44e-03 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 41.72 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 383 RNVSFTLREGEVLGLIGPNGAGKTTLFNMISGfLAPD-EGTVNLCGADGQFHAPKNPadfaALGLGRTFQIVqpfaamtv 461
Cdd:COG4178 380 EDLSLSLKPGERLLITGPSGSGKSTLLRAIAG-LWPYgSGRIARPAGARVLFLPQRP----YLPLGTLREAL-------- 446
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489057211 462 eenimvgaFYRHHHEKDAREAARETAWRMGLGPL---LGAEA---RGLTIGGLKRLEVARVMAMEPRILLLDE 528
Cdd:COG4178 447 --------LYPATAEAFSDAELREALEAVGLGHLaerLDEEAdwdQVLSLGEQQRLAFARLLLHKPDWLFLDE 511
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
364-423 |
1.91e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 41.55 E-value: 1.91e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489057211 364 QDILRVQ--NLNKHFG---GLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTV 423
Cdd:PTZ00265 378 KDIKKIQfkNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDI 442
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
383-585 |
2.63e-03 |
|
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: 40.57 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 383 RNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQfhapkNPADFAALGLGRTFQIVqP-----FA 457
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILI---DGQ-----DIRDVTQASLRAAIGIV-PqdtvlFN 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 458 AmTVEENImvgAFYRHhhekDAREAARETAWRM------------GLGPLLGaEaRGLTI-GGLK-RLEVARVMAMEPRI 523
Cdd:COG5265 446 D-TIAYNI---AYGRP----DASEEEVEAAARAaqihdfieslpdGYDTRVG-E-RGLKLsGGEKqRVAIARTLLKNPPI 515
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489057211 524 LLLDEVMAGINqTDVRRAIDLMLSIRDSGVSIIAIEH----VMQAvmslsDRVIVLASGEVIAQGR 585
Cdd:COG5265 516 LIFDEATSALD-SRTERAIQAALREVARGRTTLVIAHrlstIVDA-----DEILVLEAGRIVERGT 575
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
384-427 |
3.61e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 40.15 E-value: 3.61e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 489057211 384 NVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCG 427
Cdd:PRK10636 19 NATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG 62
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
525-594 |
4.77e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.01 E-value: 4.77e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489057211 525 LLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMqAVMSLSDRVIVL------ASGEVIAQGRPQDVVRDPQ 594
Cdd:COG0178 852 ILDEPTTGLHFHDIRKLLEVLHRLVDKGNTVVVIEHNL-DVIKTADWIIDLgpeggdGGGEIVAEGTPEEVAKVKA 926
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
369-410 |
5.73e-03 |
|
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: 39.07 E-value: 5.73e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 489057211 369 VQNLNKHF--GGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFN 410
Cdd:cd03289 5 VKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLS 48
|
|
| FepD |
COG0609 |
ABC-type Fe3+-siderophore transport system, permease component [Inorganic ion transport and ... |
82-232 |
6.41e-03 |
|
ABC-type Fe3+-siderophore transport system, permease component [Inorganic ion transport and metabolism];
Pssm-ID: 440374 Cd Length: 306 Bit Score: 38.90 E-value: 6.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 82 GYTGVILFNMGISPWFSM---FIGTFIAALVGMVISYPCFRLKGPFYSLASIAFlevfrvlalhfGWLTGGATGLMI--- 155
Cdd:COG0609 79 GAVLAIVLGGGLSALGLPlaaFLGALLAALLVYLLARRGGGLSPLRLVLAGVAV-----------SALFSALTSLLLlla 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057211 156 ---QLKLGWVWM---VFRERWPSLLIVFGMLLVTLAITWAARRS----RLGfylvatrerESAARAAGVRTVRVRLIAVA 225
Cdd:COG0609 148 dpeQLRSIVFWLmgsLAGASWDDVLLLLPVLLIGLLLALLLARAlnalALG---------DETARSLGVNVERLRLLLLL 218
|
....*..
gi 489057211 226 ISSALCA 232
Cdd:COG0609 219 LAALLTG 225
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
367-410 |
7.03e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 38.25 E-value: 7.03e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 489057211 367 LRVQNLNKHfgglhvtRNVSFTLREGEVLgLIGPNGAGKTTLFN 410
Cdd:pfam13476 1 LTIENFRSF-------RDQTIDFSKGLTL-ITGPNGSGKTTILD 36
|
|
| |
