|
Name |
Accession |
Description |
Interval |
E-value |
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
661-904 |
8.04e-102 |
|
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: 317.37 E-value: 8.04e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 661 GQDILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADgqfHAPKNPADFA 740
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRD---ITGLPPHRIA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 741 ALGLGRTFQIVQPFAAMTVEENIMVGAFYRHHH---------------EKDAREAARETAWRMGLGPLLGAEARGLTIGG 805
Cdd:COG0411 78 RLGIARTFQNPRLFPELTVLENVLVAAHARLGRgllaallrlprarreEREARERAEELLERVGLADRADEPAGNLSYGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 806 LKRLEVARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRD-SGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRP 884
Cdd:COG0411 158 QRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDeRGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTP 237
|
250 260
....*....|....*....|
gi 490819619 885 QDVVRDPQVVEAYLGKEFAH 904
Cdd:COG0411 238 AEVRADPRVIEAYLGEEAAA 257
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
665-893 |
5.31e-97 |
|
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: 303.59 E-value: 5.31e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 665 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGqfhAPKNPADFAALGL 744
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDI---TGLPPHEIARLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 745 GRTFQIVQPFAAMTVEENIMVGAFYRHHH----------EKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARV 814
Cdd:cd03219 78 GRTFQIPRLFPELTVLENVMVAAQARTGSglllararreEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490819619 815 MAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDPQV 893
Cdd:cd03219 158 LATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPRV 236
|
|
| LivH |
COG0559 |
Branched-chain amino acid ABC-type transport system, permease component [Amino acid transport ... |
1-286 |
1.00e-84 |
|
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: 273.09 E-value: 1.00e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 1 MTTFLQILLNGLMLGGLFAIVAVGLTLIFGIVKVVNFAHGEFLMAGMFVTWLITTKLGLHPYAAVIIVLPAMFILGALTQ 80
Cdd:COG0559 1 MDLFLQQLLNGLSLGSIYALIALGLTLIFGVMGVINFAHGEFVMLGAYVAYTLATLLGLPLWLALLLAVLVAALLGVLLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 81 RLLIQPLMASDDgHAQIFATVGLSTAMINLALLIFGADIANTPNFgLRTPIEIGPLRVLTGQVFIFLGAIVLVVALQLFL 160
Cdd:COG0559 81 RLVIRPLRGAPP-LALLLATIGLSLVLQGLVLLIFGADPRSFPAL-LSGSVELGGVSIPAYRLFIIVVALVLLAALWLFL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 161 KNSQTGRAIRAVAQHRSAAELMGVNVSRIYILCFGLGAACVGLAAVLIAPLYPTSSNIGTYFVLTAFVVVVLGGLGSIPG 240
Cdd:COG0559 159 RRTRLGLAMRAVAQNREAARLMGINVDRVIALTFALGAALAGLAGVLLAPIYSVSPTMGFLLGLKAFAAVVLGGLGSIPG 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 490819619 241 AFVGALIIGVIDTMSGYYIGSDLREAVVFGIFLLILILKPSGLFGK 286
Cdd:COG0559 239 AVVGGLLLGLAESLGAAYLPSGYKDVVAFVLLILVLLVRPQGLFGR 284
|
|
| TM_PBP1_LivH_like |
cd06582 |
Transmembrane subunit (TM) of Escherichia coli LivH and related proteins. LivH is one of two ... |
18-284 |
4.90e-79 |
|
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: 257.36 E-value: 4.90e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 18 FAIVAVGLTLIFGIVKVVNFAHGEFLMAGMFVTWLITTKLGLHPYAAVIIVLPAMFILGALTQRLLIQPLMasDDGHAQI 97
Cdd:cd06582 8 YALIALGLTLIFGVTGVINFAHGEFYMLGAYVAYTLLVALGLPFWLALLLALLVAALLGVLLERLVLRPLR--GAPLLTL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 98 FATVGLSTAMINLALLIFGADIANTPNFGLRTPIEIGPLRVLTGQVFIFLGAIVLVVALQLFLKNSQTGRAIRAVAQHRS 177
Cdd:cd06582 86 LITFGGLLILLQGLLLIFGGDPRVPPPPLLSGSVELGGVTIPPYRLFIIAVALVLLAALYLFLRRTRLGRAIRAVAQNPE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 178 AAELMGVNVSRIYILCFGLGAACVGLAAVLIAPLYPTSSNIGTYFVLTAFVVVVLGGLGSIPGAFVGALIIGVIDTMSGY 257
Cdd:cd06582 166 AARLLGINVRRVFALTFALGAALAGLAGVLLAPITGVSPTMGLLLLLKAFAAVVLGGLGSIPGAVVGGLLLGLAESLAAA 245
|
250 260
....*....|....*....|....*..
gi 490819619 258 YIGSDLREAVVFGIFLLILILKPSGLF 284
Cdd:cd06582 246 YLSSGYKDAVAFVLLILVLLVRPQGLF 272
|
|
| LivM |
COG4177 |
ABC-type branched-chain amino acid transport system, permease component [Amino acid transport ... |
338-627 |
3.02e-75 |
|
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: 247.69 E-value: 3.02e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 338 NAFVSHIFITICLFAALSTAWNIVGGFAGQMSLGHAVFYGIGGYTGVILF-NMGISPWFSMFIGAFIAALVGMVISYPCF 416
Cdd:COG4177 1 SPYYLSLLTLILIYAILALGLNLLLGYTGLLSLGHAAFFGIGAYAAALLTtHLGLPFWLALLLAGLVAALLGLLIGLPAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 417 RLKGPFYSLASIAFLEVFRVLALHFGWLTGGATGLMIQLKLGWVWMVFRERWPSLLIVFGMLLVTLAITWAVRRSRLGFY 496
Cdd:COG4177 81 RLRGDYLAIATLAFAEIVRLLALNLESLTGGADGLSGIPRPTLFGLDLGSPLAFYYLVLALLVLVLLLLRRLVRSRFGRA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 497 LVATRERESAARAAGVRTVRVRLIAVAISSALCAMLGTFHAMYLTFIEPaAMFSLAFSIQIAMFALIGGLGTVAGPLLGA 576
Cdd:COG4177 161 LRAIRENEIAAEALGINVTRYKLLAFVLSAALAGLAGALYAHYVGFVSP-ESFSFLLSIEILLMVVLGGLGSLLGPVLGA 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 490819619 577 VLLVPITEWARaslgaSALGLHGFVYGLVLILVVLFMPNGIMGAINRFVRK 627
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 ... |
348-619 |
9.74e-74 |
|
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: 243.12 E-value: 9.74e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 348 ICLFAALSTAWNIVGGFAGQMSLGHAVFYGIGGYTGVILFNM-GISPWFSMFIGAFIAALVGMVISYPCFRLKGPFYSLA 426
Cdd:cd06581 1 ILIYAILALGLNLLLGYAGQLSLGHAAFFGIGAYTAALLATRlGLPFWLALLAAGLVAALVGLLLGLPALRLRGVYFAIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 427 SIAFLEVFRVLALHFGWLTGGATGLMIQLKLGWVWMVFRERWPSLLIVFGMLLVTLAITWAVRRSRLGFYLVATRERESA 506
Cdd:cd06581 81 TLAFAEIVRLLALNWSSLTGGSNGLSGIPPPLLGGLLLSSPLAFYYLVLAVLLLVLLLLRRLVRSPFGRALRAIRENEVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 507 ARAAGVRTVRVRLIAVAISSALCAMLGTFHAMYLTFIEPaAMFSLAFSIQIAMFALIGGLGTVAGPLLGAVLLVPITEWA 586
Cdd:cd06581 161 AEALGINVTRYKLLAFALSAALAGLAGALYAHYLGFVSP-ESFGFALSIELLLMVVLGGLGSLLGPVLGAALLVLLPELL 239
|
250 260 270
....*....|....*....|....*....|...
gi 490819619 587 RASLGasalGLHGFVYGLVLILVVLFMPNGIMG 619
Cdd:cd06581 240 RSLGP----GLRLLVFGLLLILVVLFLPRGLVG 268
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
662-901 |
4.42e-59 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 202.53 E-value: 4.42e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 662 QDILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQFHAPKNPADFAA 741
Cdd:PRK11300 3 QPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILL---RGQHIEGLPGHQIAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 742 LGLGRTFQIVQPFAAMTVEENIMVgAFYRH----------------HHEKDAREAARETAWRMGLGPLLGAEARGLTIGG 805
Cdd:PRK11300 80 MGVVRTFQHVRLFREMTVIENLLV-AQHQQlktglfsgllktpafrRAESEALDRAATWLERVGLLEHANRQAGNLAYGQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 806 LKRLEVARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRDS-GVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRP 884
Cdd:PRK11300 159 QRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTP 238
|
250
....*....|....*..
gi 490819619 885 QDVVRDPQVVEAYLGKE 901
Cdd:PRK11300 239 EEIRNNPDVIKAYLGEA 255
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
664-902 |
1.44e-47 |
|
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: 169.38 E-value: 1.44e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 664 ILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQFHAPKNPADFAALG 743
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILI---DGQDITHLPMHERARLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 744 LGRTFQIVQPFAAMTVEENIMVGAFYRHHHEKDAREAARETAW-RMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRIL 822
Cdd:TIGR04406 78 IGYLPQEASIFRKLTVEENIMAVLEIRKDLDRAEREERLEALLeEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 823 LLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDPQVVEAYLGKEF 902
Cdd:TIGR04406 158 LLDEPFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEKVRRVYLGEQF 237
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
665-889 |
1.93e-47 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 169.09 E-value: 1.93e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 665 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADgqfhAPKNPADFAALgL 744
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGED----VARDPAEVRRR-I 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 745 GRTFQIVQPFAAMTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTiGGLK-RLEVARVMAMEPRILL 823
Cdd:COG1131 76 GYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLS-GGMKqRLGLALALLHDPELLI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490819619 824 LDEVMAGInqtDV--RRAI-DLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVR 889
Cdd:COG1131 155 LDEPTSGL---DPeaRRELwELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKA 220
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
664-904 |
1.38e-46 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 174.44 E-value: 1.38e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 664 ILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQFHAPKNPADFAALG 743
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILL---DGEPVRFRSPRDAQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 744 LGRTFQIVQPFAAMTVEENIMVGAFYRHH---HEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPR 820
Cdd:COG1129 81 IAIIHQELNLVPNLSVAENIFLGREPRRGgliDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 821 ILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDpQVVEAYLGK 900
Cdd:COG1129 161 VLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTED-ELVRLMVGR 239
|
....
gi 490819619 901 EFAH 904
Cdd:COG1129 240 ELED 243
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
664-899 |
2.61e-46 |
|
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: 2.61e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 664 ILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGAD--GqfhapKNPADFAA 741
Cdd:COG4674 10 ILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDltG-----LDEHEIAR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 742 LGLGRTFQIVQPFAAMTVEENIMVGA----------FYRHHHEKDAREAarETAWRMGLGPLLGAEARGLTIGGLKRLEV 811
Cdd:COG4674 85 LGIGRKFQKPTVFEELTVFENLELALkgdrgvfaslFARLTAEERDRIE--EVLETIGLTDKADRLAGLLSHGQKQWLEI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 812 ARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRdSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDP 891
Cdd:COG4674 163 GMLLAQDPKLLLLDEPVAGMTDAETERTAELLKSLA-GKHSVVVVEHDMEFVRQIARKVTVLHQGSVLAEGSLDEVQADP 241
|
....*...
gi 490819619 892 QVVEAYLG 899
Cdd:COG4674 242 RVIEVYLG 249
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
664-902 |
7.57e-46 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 164.82 E-value: 7.57e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 664 ILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQfhapknpaDF---- 739
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFL---DGE--------DIthlp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 740 ----AALGLGRTFQivQP--FAAMTVEENIMvgAFyRHHHEKDAREAARETAWRM---GLGPLlgAEARGLTI-GGLKR- 808
Cdd:COG1137 72 mhkrARLGIGYLPQ--EAsiFRKLTVEDNIL--AV-LELRKLSKKEREERLEELLeefGITHL--RKSKAYSLsGGERRr 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 809 LEVARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVV 888
Cdd:COG1137 145 VEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEIL 224
|
250
....*....|....
gi 490819619 889 RDPQVVEAYLGKEF 902
Cdd:COG1137 225 NNPLVRKVYLGEDF 238
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
664-899 |
6.33e-45 |
|
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: 161.69 E-value: 6.33e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 664 ILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADgqfHAPKNPADFAALG 743
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGED---ITGLPPHRIARLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 744 L-----GRtfQIvqpFAAMTVEENIMVGAFyrhhhekdAREAARETAWRMG--------LGPLLGAEARGLTiGGLKR-L 809
Cdd:COG0410 80 IgyvpeGR--RI---FPSLTVEENLLLGAY--------ARRDRAEVRADLErvyelfprLKERRRQRAGTLS-GGEQQmL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 810 EVARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVR 889
Cdd:COG0410 146 AIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLA 225
|
250
....*....|
gi 490819619 890 DPQVVEAYLG 899
Cdd:COG0410 226 DPEVREAYLG 235
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
665-899 |
8.39e-45 |
|
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: 161.56 E-value: 8.39e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 665 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQFHAPKNPADFAALGL 744
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILL---DGQDITKLPMHKRARLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 745 GRTFQIVQPFAAMTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLL 824
Cdd:cd03218 78 GYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490819619 825 DEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDPQVVEAYLG 899
Cdd:cd03218 158 DEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVRKVYLG 232
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
665-890 |
3.39e-44 |
|
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: 159.14 E-value: 3.39e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 665 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADgqfHAPKNPADFAALGL 744
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRD---ITGLPPHERARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 745 GRTFQIVQPFAAMTVEENIMVGAFYRHhheKDAREAARETAWRM--GLGPLLGAEARGLTIGGLKRLEVARVMAMEPRIL 822
Cdd:cd03224 78 GYVPEGRRIFPELTVEENLLLGAYARR---RAKRKARLERVYELfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490819619 823 LLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRD 890
Cdd:cd03224 155 LLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
665-887 |
8.32e-44 |
|
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: 158.87 E-value: 8.32e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 665 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKNPADFAALGL 744
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 745 GRTFqivqpFAAMTVEENI-MVGAFYRHHHEkDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILL 823
Cdd:COG4555 82 ERGL-----YDRLTVRENIrYFAELYGLFDE-ELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490819619 824 LDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDV 887
Cdd:COG4555 156 LDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
665-896 |
3.29e-41 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 150.95 E-value: 3.29e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 665 LRVQNLN-KHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADgqfHAPKNPADFAAL- 742
Cdd:COG1122 1 IELENLSfSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKD---ITKKNLRELRRKv 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 743 GLgrTFQivQP---FAAMTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEP 819
Cdd:COG1122 78 GL--VFQ--NPddqLFAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEP 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490819619 820 RILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDPQVVEA 896
Cdd:COG1122 154 EVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYELLEE 230
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
637-892 |
4.69e-39 |
|
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: 152.75 E-value: 4.69e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 637 ARTEPIAAVPA-RAIKAPSPDRAGIGQDILRVQNLNKHF-----GGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMI 710
Cdd:COG1123 232 AAPQALAAVPRlGAARGRAAPAAAAAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 711 SGFLAPDEGTVNLCGADGQFHAPKNPADFAalglgRTFQIV-Q-PFAA----MTVEENIMVGAfyRHHHEKDAREAARET 784
Cdd:COG1123 312 LGLLRPTSGSILFDGKDLTKLSRRSLRELR-----RRVQMVfQdPYSSlnprMTVGDIIAEPL--RLHGLLSRAERRERV 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 785 AW---RMGLGP-LLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGINQTdVRRAI-DLMLSIRDS-GVSIIAIEH 858
Cdd:COG1123 385 AElleRVGLPPdLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVS-VQAQIlNLLRDLQRElGLTYLFISH 463
|
250 260 270
....*....|....*....|....*....|....
gi 490819619 859 VMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDPQ 892
Cdd:COG1123 464 DLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQ 497
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
665-878 |
7.16e-39 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 142.15 E-value: 7.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 665 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKNPADFAALgl 744
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 745 grtFQIVQPFAAMTVEENIMvgafyrhhhekdareaaretawrmglgpllgaeargLTIGGLKRLEVARVMAMEPRILLL 824
Cdd:cd03230 79 ---PEEPSLYENLTVRENLK------------------------------------LSGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490819619 825 DEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEV 878
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
664-887 |
5.37e-38 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 149.41 E-value: 5.37e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 664 ILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQFHAPKNPADFAALG 743
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILI---DGKPVRIRSPRDAIALG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 744 LGRTFQIVQPFAAMTVEENIMVGA---FYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPR 820
Cdd:COG3845 82 IGMVHQHFMLVPNLTVAENIVLGLeptKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGAR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490819619 821 ILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDV 887
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 ... |
681-877 |
1.86e-37 |
|
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: 139.52 E-value: 1.86e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 681 RNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKNPADFAALglgrTFQivQP---FAAM 757
Cdd:cd03225 18 DDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL----VFQ--NPddqFFGP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 758 TVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGINQTDVR 837
Cdd:cd03225 92 TVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRR 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490819619 838 RAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGE 877
Cdd:cd03225 172 ELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
664-898 |
1.97e-37 |
|
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: 140.50 E-value: 1.97e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 664 ILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQfhapknpaDFAALG 743
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILV---DGQ--------DITGLS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 744 LGRTFQIVQP----------FAAMTVEENImvgAF--YRHHH--EKDAREAARETAWRMGLGpllGAEAR------Glti 803
Cdd:COG1127 74 EKELYELRRRigmlfqggalFDSLTVFENV---AFplREHTDlsEAEIRELVLEKLELVGLP---GAADKmpselsG--- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 804 GGLKRLEVARVMAMEPRILLLDE-------VMAginqtdvrRAID-LMLSIRDS-GVSIIAIEHVMQAVMSLSDRVIVLA 874
Cdd:COG1127 145 GMRKRVALARALALDPEILLYDEptagldpITS--------AVIDeLIRELRDElGLTSVVVTHDLDSAFAIADRVAVLA 216
|
250 260
....*....|....*....|....*
gi 490819619 875 SGEVIAQGRPQDVVR-DPQVVEAYL 898
Cdd:COG1127 217 DGKIIAEGTPEELLAsDDPWVRQFL 241
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
665-893 |
5.82e-37 |
|
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: 139.17 E-value: 5.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 665 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQFHAPKNPADFAALGL 744
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLI---DGEDISGLSEAELYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 745 --GRTFQIVQPFAAMTVEENImvgAFYRHHH----EKDAREAARETAWRMGLGP---LLGAEARGltiGGLKRLEVARVM 815
Cdd:cd03261 78 rmGMLFQSGALFDSLTVFENV---AFPLREHtrlsEEEIREIVLEKLEAVGLRGaedLYPAELSG---GMKKRVALARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 816 AMEPRILLLDEVMAG---INQTDVrraIDLMLSIRDS-GVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVR-- 889
Cdd:cd03261 152 ALDPELLLYDEPTAGldpIASGVI---DDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRAsd 228
|
....
gi 490819619 890 DPQV 893
Cdd:cd03261 229 DPLV 232
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
665-881 |
8.71e-37 |
|
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: 136.02 E-value: 8.71e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 665 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQFHAPKNPADFAALGL 744
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILV---DGKEVSFASPRDARRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 745 GRTFQivqpfaamtveenimvgafyrhhhekdareaaretawrmglgpllgaeargLTIGGLKRLEVARVMAMEPRILLL 824
Cdd:cd03216 78 AMVYQ---------------------------------------------------LSVGERQMVEIARALARNARLLIL 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490819619 825 DEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQ 881
Cdd:cd03216 107 DEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
664-907 |
1.93e-36 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 137.91 E-value: 1.93e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 664 ILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKnpadfaaLG 743
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR-------IG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 744 -------LGRTFQIvqpfaamTVEENIMVGaFYRHH-----HEKDAREAARETAWRMGLGPLlgaeaRGLTIGGL----- 806
Cdd:COG1121 79 yvpqraeVDWDFPI-------TVRDVVLMG-RYGRRglfrrPSRADREAVDEALERVGLEDL-----ADRPIGELsggqq 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 807 KRLEVARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLAsGEVIAQGRPQD 886
Cdd:COG1121 146 QRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLN-RGLVAHGPPEE 224
|
250 260
....*....|....*....|.
gi 490819619 887 VVRDPQVVEAYLGKEFAHAHA 907
Cdd:COG1121 225 VLTPENLSRAYGGPVALLAHG 245
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
665-882 |
2.97e-36 |
|
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: 136.11 E-value: 2.97e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 665 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPknpadfAALGL 744
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPP------ERRNI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 745 GRTFQIVQPFAAMTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLL 824
Cdd:cd03259 75 GMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 825 DEVMAGINQtDVRRAIDLMLS--IRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQG 882
Cdd:cd03259 155 DEPLSALDA-KLREELREELKelQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
664-896 |
2.31e-35 |
|
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: 135.17 E-value: 2.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 664 ILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADgqfHAPKNPADFAALg 743
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRD---LASLSRRELARR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 744 LGRTFQIVQPFAAMTVEENIMVGafyRHHH--------EKDaREAARETAWRMGLGPLlgAEARGLTI-GG-LKRLEVAR 813
Cdd:COG1120 77 IAYVPQEPPAPFGLTVRELVALG---RYPHlglfgrpsAED-REAVEEALERTGLEHL--ADRPVDELsGGeRQRVLIAR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 814 VMAMEPRILLLDEVMAGInqtDVRRAIDLMLSIRD----SGVSIIAIEH-VMQAVMsLSDRVIVLASGEVIAQGRPQDVV 888
Cdd:COG1120 151 ALAQEPPLLLLDEPTSHL---DLAHQLEVLELLRRlareRGRTVVMVLHdLNLAAR-YADRLVLLKDGRIVAQGPPEEVL 226
|
....*...
gi 490819619 889 rDPQVVEA 896
Cdd:COG1120 227 -TPELLEE 233
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
665-901 |
1.11e-34 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 132.46 E-value: 1.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 665 LRVQNLNKHFGGLHVtRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKNpadfaalgl 744
Cdd:cd03299 1 LKVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 745 gRTFQIVQP----FAAMTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPR 820
Cdd:cd03299 71 -RDISYVPQnyalFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 821 ILLLDEVMAGINQTDVRRAIDLMLSIRDS-GVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDPQ--VVEAY 897
Cdd:cd03299 150 ILLLDEPFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKneFVAEF 229
|
....
gi 490819619 898 LGKE 901
Cdd:cd03299 230 LGFN 233
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
664-902 |
1.23e-34 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 132.71 E-value: 1.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 664 ILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQ---FHAPknpadfA 740
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllpLHAR------A 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 741 ALGLGRTFQIVQPFAAMTVEENIMVGAFYRHHHEKDAREA-ARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEP 819
Cdd:PRK10895 77 RRGIGYLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDrANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 820 RILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDPQVVEAYLG 899
Cdd:PRK10895 157 KFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVYLG 236
|
...
gi 490819619 900 KEF 902
Cdd:PRK10895 237 EDF 239
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
664-887 |
3.61e-34 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 132.93 E-value: 3.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 664 ILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQFHAPKNPADFAAL- 742
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLW---DGEPLDPEDRRRIGYLp 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 743 ---GLgrtfqivqpFAAMTVEENIMvgafY----RHHHEKDAREAAREtaW--RMGLGPLLGAEARGLTIGGLKRLEVAR 813
Cdd:COG4152 78 eerGL---------YPKMKVGEQLV----YlarlKGLSKAEAKRRADE--WleRLGLGDRANKKVEELSKGNQQKVQLIA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490819619 814 VMAMEPRILLLDEVMAG---INQTDVRraiDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDV 887
Cdd:COG4152 143 ALLHDPELLILDEPFSGldpVNVELLK---DVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
665-885 |
3.80e-34 |
|
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: 130.32 E-value: 3.80e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 665 LRVQNLNKHFGGL--HVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKnpadfAAL 742
Cdd:cd03263 1 LQIRNLTKTYKKGtkPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKA-----ARQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 743 GLGRTFQIVQPFAAMTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRIL 822
Cdd:cd03263 76 SLGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490819619 823 LLDEVMAGInqtDV--RRAI-DLMLSIRdSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQ 885
Cdd:cd03263 156 LLDEPTSGL---DPasRRAIwDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQ 217
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
664-882 |
1.32e-33 |
|
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: 128.64 E-value: 1.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 664 ILRVQNLNKHF----GGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADgqfhAPKNPADf 739
Cdd:cd03266 1 MITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFD----VVKEPAE- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 740 AALGLGRTFQIVQPFAAMTVEENimVGAFYRHHHEKDAREAAR--ETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAM 817
Cdd:cd03266 76 ARRRLGFVSDSTGLYDRLTAREN--LEYFAGLYGLKGDELTARleELADRLGMEELLDRRVGGFSTGMRQKVAIARALVH 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490819619 818 EPRILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQG 882
Cdd:cd03266 154 DPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| BPD_transp_2 |
pfam02653 |
Branched-chain amino acid transport system / permease component; This is a large family mainly ... |
18-278 |
3.31e-33 |
|
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: 129.30 E-value: 3.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 18 FAIVAVGLTLIFGIVKVVNFAHGEFLMAGMFVTWLITTKLGLHPYAAVII----VLPAMFILGALTQRLLIQPLMAsddg 93
Cdd:pfam02653 12 YAIAALGLTLIYGIAGVINLGHGGFMMLGAYVAAMLLNLLGPGLWLALPVgilvGAAVGLLIGILTLRLKINEVII---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 94 haqifaTVGLSTAMINLALLIFGADIANTPNFGLRT-PIEIGPLRVLTGQVFIFLGAIVLVVALQLFLKNSQTGRAIRAV 172
Cdd:pfam02653 88 ------TLLLNLAALGLALFLVTGILGGEGGTSGITgPSGFPGAFLSFAFAFIFLLALLLVLALWLLLYRTKFGRALRAV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 173 AQHRSAAELMGVNVSRIYILCFGLGAACVGLAAVLIAPLY--PTSSNIGTYFVLTAFVVVVLGGLGSIPGAFVGALIIGV 250
Cdd:pfam02653 162 GENEEAARAAGINVKKLKLLTFVISGALAGLAGALLALYTgvVPPSNFGVGLGLDAIAAVVLGGAGSPIGVVIGSLIIGL 241
|
250 260
....*....|....*....|....*...
gi 490819619 251 IDTMSGYYIGSDLREAVVFGIFLLILIL 278
Cdd:pfam02653 242 VQSLGLGALGSPPELSLLVLGALLILVL 269
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
664-892 |
3.45e-33 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 131.76 E-value: 3.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 664 ILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQfhapknpaDFAAL- 742
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILL---DGR--------DVTGLp 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 743 ----GLGrtfqIV-QPFAA---MTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTiGGLK-RLEVAR 813
Cdd:COG3842 74 pekrNVG----MVfQDYALfphLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLS-GGQQqRVALAR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 814 VMAMEPRILLLDEVMAGInqtDVRRAIDLMLSIRD----SGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVR 889
Cdd:COG3842 149 ALAPEPRVLLLDEPLSAL---DAKLREEMREELRRlqreLGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYE 225
|
...
gi 490819619 890 DPQ 892
Cdd:COG3842 226 RPA 228
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
665-887 |
5.70e-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: 127.30 E-value: 5.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 665 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFL-----APDEGTVNLCGADgqfhAPKNPADF 739
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKD----IYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 740 AAL--GLGRTFQIVQPFaAMTVEENIMVGAfyRHHHEKDAREAARETAW---RMGLGPLLG--AEARGLTIGGLKRLEVA 812
Cdd:cd03260 77 LELrrRVGMVFQKPNPF-PGSIYDNVAYGL--RLHGIKLKEELDERVEEalrKAALWDEVKdrLHALGLSGGQQQRLCLA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490819619 813 RVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRDSgVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDV 887
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
663-889 |
1.23e-32 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 126.73 E-value: 1.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 663 DILRVQNLNKHF----------------------GGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGT 720
Cdd:COG1134 3 SMIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 721 VNLcgaDGQFHAPknpadfaaLGLGRTFQivqpfAAMTVEENI-MVGAFYRhHHEKDAREAARETAWRMGLGPLLGAEAR 799
Cdd:COG1134 83 VEV---NGRVSAL--------LELGAGFH-----PELTGRENIyLNGRLLG-LSRKEIDEKFDEIVEFAELGDFIDQPVK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 800 GLTIGGLKRLEVARVMAMEPRILLLDEVMAGinqTDV---RRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASG 876
Cdd:COG1134 146 TYSSGMRARLAFAVATAVDPDILLVDEVLAV---GDAafqKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKG 222
|
250
....*....|...
gi 490819619 877 EVIAQGRPQDVVR 889
Cdd:COG1134 223 RLVMDGDPEEVIA 235
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
665-878 |
1.57e-32 |
|
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: 125.68 E-value: 1.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 665 LRVQNLNKHFGG----LHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKNPADFA 740
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 741 ALGLGRTFQ----IvqPFaaMTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMA 816
Cdd:cd03255 81 RRHIGFVFQsfnlL--PD--LTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490819619 817 MEPRILLLDEVMAGINQTDVRRAIDLMLSI-RDSGVSIIAIEHVMQAVmSLSDRVIVLASGEV 878
Cdd:cd03255 157 NDPKIILADEPTGNLDSETGKEVMELLRELnKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
664-882 |
2.95e-32 |
|
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: 125.31 E-value: 2.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 664 ILRVQNLNKHF--GGLHVT--RNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGqfhaPKNPADF 739
Cdd:cd03257 1 LLEVKNLSVSFptGGGSVKalDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDL----LKLSRRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 740 AALgLGRTFQIV-Q-PFAA----MTVEENIMVGafYRHHHEKDAREAARETAW--RMGLGP---LLGAEARGLTIGGLKR 808
Cdd:cd03257 77 RKI-RRKEIQMVfQdPMSSlnprMTIGEQIAEP--LRIHGKLSKKEARKEAVLllLVGVGLpeeVLNRYPHELSGGQRQR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490819619 809 LEVARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRDS-GVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQG 882
Cdd:cd03257 154 VAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
665-897 |
4.16e-32 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 125.61 E-value: 4.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 665 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGadgqfhapKNPADFAALGL 744
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNG--------RPLAAWSPWEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 745 GR-----------TFqivqPFaamTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTiGGLK-RLEVA 812
Cdd:COG4559 74 ARrravlpqhsslAF----PF---TVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLS-GGEQqRVQLA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 813 RVMA-------MEPRILLLDEVMAGInqtDVRRAIDLMLSIRD---SGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQG 882
Cdd:COG4559 146 RVLAqlwepvdGGPRWLFLDEPTSAL---DLAHQHAVLRLARQlarRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQG 222
|
250
....*....|....*
gi 490819619 883 RPQDVVRDPQVVEAY 897
Cdd:COG4559 223 TPEEVLTDELLERVY 237
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
665-881 |
6.33e-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: 124.12 E-value: 6.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 665 LRVQNLNKHFGG----LHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKnpadfa 740
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 741 algLGRTFQivQP--FAAMTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTiGGLK-RLEVARVMAM 817
Cdd:cd03293 75 ---RGYVFQ--QDalLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLS-GGMRqRVALARALAV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 818 EPRILLLDEVMAGIN-QTdvRRAI-DLMLSI-RDSGVSIIAIEH-VMQAVMsLSDRVIVLAS--GEVIAQ 881
Cdd:cd03293 149 DPDVLLLDEPFSALDaLT--REQLqEELLDIwRETGKTVLLVTHdIDEAVF-LADRVVVLSArpGRIVAE 215
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
665-892 |
9.69e-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: 123.89 E-value: 9.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 665 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQfhaPKNPADFAALGL 744
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILL---DGK---DITNLPPHKRPV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 745 GRTFQIVQPFAAMTVEENImvgAFYRHHHEKDAREAARETAWRMGLGPLLGAEAR---GLTIGGLKRLEVARVMAMEPRI 821
Cdd:cd03300 75 NTVFQNYALFPHLTVFENI---AFGLRLKKLPKAEIKERVAEALDLVQLEGYANRkpsQLSGGQQQRVAIARALVNEPKV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490819619 822 LLLDEVMAGInqtDVRRAIDLMLSI----RDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDPQ 892
Cdd:cd03300 152 LLLDEPLGAL---DLKLRKDMQLELkrlqKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
665-877 |
1.29e-31 |
|
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: 121.53 E-value: 1.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 665 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKNPADFAALGL 744
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 745 grTFQIVQPFAAMTVEENIMVgafyrhhhekdareaaretawrmglgpllgaearGLTIGGLKRLEVARVMAMEPRILLL 824
Cdd:cd03229 81 --VFQDFALFPHLTVLENIAL----------------------------------GLSGGQQQRVALARALAMDPDVLLL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490819619 825 DEVMAGINQTDVRRAIDLMLSIRD-SGVSIIAIEHVMQAVMSLSDRVIVLASGE 877
Cdd:cd03229 125 DEPTSALDPITRREVRALLKSLQAqLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
681-826 |
5.50e-31 |
|
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: 118.90 E-value: 5.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 681 RNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQFHAPKNPADFAAlGLGRTFQIVQPFAAMTVE 760
Cdd:pfam00005 2 KNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILL---DGQDLTDDERKSLRK-EIGYVFQDPQLFPRLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490819619 761 ENIMVGA--FYRHHHEKDAR-EAAREtawRMGLGPL----LGAEARGLTIGGLKRLEVARVMAMEPRILLLDE 826
Cdd:pfam00005 78 ENLRLGLllKGLSKREKDARaEEALE---KLGLGDLadrpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDE 147
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
648-895 |
1.77e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 123.04 E-value: 1.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 648 RAIKAPSPDRAGIgqdILRVQNLNKHFGG-----LHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVN 722
Cdd:PRK13631 8 KKLKVPNPLSDDI---ILRVKNLYCVFDEkqeneLVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 723 L----CGADGQF------HAPKNPADFAALGlgRTFQIVQPFAAM-----TVEENIMVGAFYRHHHEKDAREAARETAWR 787
Cdd:PRK13631 85 VgdiyIGDKKNNhelitnPYSKKIKNFKELR--RRVSMVFQFPEYqlfkdTIEKDIMFGPVALGVKKSEAKKLAKFYLNK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 788 MGLG-PLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSL 866
Cdd:PRK13631 163 MGLDdSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEV 242
|
250 260
....*....|....*....|....*....
gi 490819619 867 SDRVIVLASGEVIAQGRPQDVVRDPQVVE 895
Cdd:PRK13631 243 ADEVIVMDKGKILKTGTPYEIFTDQHIIN 271
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
665-882 |
1.87e-30 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 119.31 E-value: 1.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 665 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFhAPKNpaDFAAL-- 742
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI-AARN--RIGYLpe 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 743 --GLGRTfqivqpfaaMTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPR 820
Cdd:cd03269 78 erGLYPK---------MKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490819619 821 ILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQG 882
Cdd:cd03269 149 LLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
665-874 |
3.19e-30 |
|
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: 118.74 E-value: 3.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 665 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKNPADFAALG- 743
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLGh 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 744 -LGrtfqivqPFAAMTVEENImvgAFYRH-HHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRI 821
Cdd:COG4133 83 aDG-------LKPELTVRENL---RFWAAlYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490819619 822 LLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHvmQAVMSLSDRVIVLA 874
Cdd:COG4133 153 WLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTH--QPLELAAARVLDLG 203
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
665-899 |
3.56e-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: 119.75 E-value: 3.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 665 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKNPadfaalGL 744
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQER------NV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 745 GRTFQIVQPFAAMTVEENIMVGAFYRHHHEKDAREAARETAWR-MGLGPLLGAEAR---GLTIGGLKRLEVARVMAMEPR 820
Cdd:cd03296 77 GFVFQHYALFRHMTVFDNVAFGLRVKPRSERPPEAEIRAKVHElLKLVQLDWLADRypaQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 821 ILLLDEVMAGINqTDVRRaiDLMLSIR----DSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDPQ--VV 894
Cdd:cd03296 157 VLLLDEPFGALD-AKVRK--ELRRWLRrlhdELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPAspFV 233
|
....*
gi 490819619 895 EAYLG 899
Cdd:cd03296 234 YSFLG 238
|
|
| PRK10740 |
PRK10740 |
high-affinity branched-chain amino acid ABC transporter permease LivH; |
4-286 |
1.02e-29 |
|
high-affinity branched-chain amino acid ABC transporter permease LivH;
Pssm-ID: 182689 [Multi-domain] Cd Length: 308 Bit Score: 120.41 E-value: 1.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 4 FLQILLNGLMLGGLFAIVAVGLTLIFGIVKVVNFAHGEFLMAGMFVTWLITTKLGLHPYAAVIIVLPAMFIL-------- 75
Cdd:PRK10740 8 FLQQMFNGVTLGSTYALIAIGYTMVYGIIGMINFAHGEVYMIGSYVSFMIIAALMMMGIDTSWLLVAAGFVGaiviasay 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 76 GALTQRLLIQPLMASDDGHAQIFAtVGLSTAMINLALLIFGADIANTPNFgLRTPIEIG-----PLRVLTGQVFIFLGAI 150
Cdd:PRK10740 88 GWSIERVAYRPVRNSKRLIALISA-IGMSIFLQNYVSLTEGSRDVALPSL-FNGQWVVGhsenfSASITTMQAVIWIVTF 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 151 VLVVALQLFLKNSQTGRAIRAVAQHRSAAELMGVNVSRIYILCFGLGAACVGLAAVLIAPLYPT-SSNIGTYFVLTAFVV 229
Cdd:PRK10740 166 LAMLALTIFIRYSRMGRACRACAEDLKMASLLGINTDRVIALTFVIGAAMAAVAGVLLGQFYGViNPYIGFMAGMKAFTA 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 490819619 230 VVLGGLGSIPGAFVGALIIGVIDTMSGYYIGSDLREAVVFGIFLLILILKPSGLFGK 286
Cdd:PRK10740 246 AVLGGIGSIPGAMIGGLILGIAEALSSAYLSTEYKDVVSFALLILVLLVMPTGILGR 302
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
666-882 |
1.04e-29 |
|
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: 117.25 E-value: 1.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 666 RVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGadgqFHAPKNPADFA----A 741
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG----KPLEKERKRIGyvpqR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 742 LGLGRTFQIvqpfaamTVEENIMVGAFYR----HHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAM 817
Cdd:cd03235 77 RSIDRDFPI-------SVRDVVLMGLYGHkglfRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQ 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490819619 818 EPRILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLAsGEVIAQG 882
Cdd:cd03235 150 DPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLN-RTVVASG 213
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
665-897 |
1.90e-29 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 117.95 E-value: 1.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 665 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGadgqfhapKNPADFAALGL 744
Cdd:PRK13548 3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNG--------RPLADWSPAEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 745 GR-----------TFqivqPFaamTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTiGGLK-RLEVA 812
Cdd:PRK13548 75 ARrravlpqhsslSF----PF---TVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLS-GGEQqRVQLA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 813 RVMA------MEPRILLLDEVMAGInqtDVRRAIDLMLSIRD----SGVSIIAIEH-VMQAVMsLSDRVIVLASGEVIAQ 881
Cdd:PRK13548 147 RVLAqlwepdGPPRWLLLDEPTSAL---DLAHQHHVLRLARQlaheRGLAVIVVLHdLNLAAR-YADRIVLLHQGRLVAD 222
|
250
....*....|....*.
gi 490819619 882 GRPQDVVRDPQVVEAY 897
Cdd:PRK13548 223 GTPAEVLTPETLRRVY 238
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
665-878 |
2.00e-29 |
|
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: 116.48 E-value: 2.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 665 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQfHAPKNPADFAAL-- 742
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIII---DGL-KLTDDKKNINELrq 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 743 GLGRTFQIVQPFAAMTVEENIMVGAFYRHHHEKD-AREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRI 821
Cdd:cd03262 77 KVGMVFQQFNLFPHLTVLENITLAPIKVKGMSKAeAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490819619 822 LLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEV 878
Cdd:cd03262 157 MLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
667-884 |
4.23e-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: 4.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 667 VQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADgqfhAPKNPADFAAlGLGR 746
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHD----VVREPREVRR-RIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 747 TFQIVQPFAAMTVEENI-MVGAFYRHHHEKdAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLD 825
Cdd:cd03265 78 VFQDLSVDDELTGWENLyIHARLYGVPGAE-RRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490819619 826 EVMAGIN---QTDVRRAIDLMLsiRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRP 884
Cdd:cd03265 157 EPTIGLDpqtRAHVWEYIEKLK--EEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTP 216
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
665-882 |
4.76e-29 |
|
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: 115.39 E-value: 4.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 665 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQfhapKNPADFAALGL 744
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ----KNIEALRRIGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 745 GRTFQIVqpFAAMTVEENIMVGAFYRHHHEKDAREAAREtawrMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLL 824
Cdd:cd03268 77 LIEAPGF--YPNLTARENLRLLARLLGIRKKRIDEVLDV----VGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLIL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490819619 825 DEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQG 882
Cdd:cd03268 151 DEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
662-896 |
5.23e-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: 122.32 E-value: 5.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 662 QDILRVQNLNKHF--GGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPD---EGTVNLCGADgqfhAPKNP 736
Cdd:COG1123 2 TPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRD----LLELS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 737 ADFAALGLGRTFQivQPFAAM---TVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVAR 813
Cdd:COG1123 78 EALRGRRIGMVFQ--DPMTQLnpvTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 814 VMAMEPRILLLDEVMAGINQTDVRRAIDLMLSI-RDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDPQ 892
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
....
gi 490819619 893 VVEA 896
Cdd:COG1123 236 ALAA 239
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
666-882 |
7.17e-29 |
|
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: 113.68 E-value: 7.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 666 RVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGadgqfhapknpadfaalglg 745
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDG-------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 746 rtfqivQPFAAMtveenimvgafyrhhhekDAREAARETAW------RMGLGPLLGAEARGLTIGGLKRLEVARVMAMEP 819
Cdd:cd03214 61 ------KDLASL------------------SPKELARKIAYvpqaleLLGLAHLADRPFNELSGGERQRVLLARALAQEP 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490819619 820 RILLLDEVMAGInqtDVRRAIDLMLSIRD----SGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQG 882
Cdd:cd03214 117 PILLLDEPTSHL---DIAHQIELLELLRRlareRGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
664-892 |
1.63e-28 |
|
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: 114.60 E-value: 1.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 664 ILRVQNLNKHFGG----LHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKNPADF 739
Cdd:cd03258 1 MIELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 740 AAlGLGRTFQIVQPFAAMTVEENIMVgAFYRHHHEKDAREA-ARETAWRMGLGPLLGAEARGLTiGGLK-RLEVARVMAM 817
Cdd:cd03258 81 RR-RIGMIFQHFNLLSSRTVFENVAL-PLEIAGVPKAEIEErVLELLELVGLEDKADAYPAQLS-GGQKqRVGIARALAN 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490819619 818 EPRILLLDEVMAGINQTDVRRAIDLMLSI-RDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDPQ 892
Cdd:cd03258 158 NPKVLLCDEATSALDPETTQSILALLRDInRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
665-901 |
2.97e-28 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 119.89 E-value: 2.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 665 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQFHAPKNPADFAALGL 744
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITI---NNINYNKLDHKLAAQLGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 745 GRTFQIVQPFAAMTVEENIMVGafyRHHHEK----------DAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARV 814
Cdd:PRK09700 83 GIIYQELSVIDELTVLENLYIG---RHLTKKvcgvniidwrEMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 815 MAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDpQVV 894
Cdd:PRK09700 160 LMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSND-DIV 238
|
....*..
gi 490819619 895 EAYLGKE 901
Cdd:PRK09700 239 RLMVGRE 245
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
662-892 |
7.30e-28 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 113.48 E-value: 7.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 662 QDILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHapknpaDFAA 741
Cdd:PRK11701 4 QPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLR------DLYA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 742 LG------LGRT-FQIVQPFAA----MTVE------ENIM-VGAfyRHHheKDAREAARETAWRMGLGPLLGAEARGLTI 803
Cdd:PRK11701 78 LSeaerrrLLRTeWGFVHQHPRdglrMQVSaggnigERLMaVGA--RHY--GDIRATAGDWLERVEIDAARIDDLPTTFS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 804 GGLK-RLEVARVMAMEPRILLLDEVMAGInqtDVR---RAIDLMLS-IRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEV 878
Cdd:PRK11701 154 GGMQqRLQIARNLVTHPRLVFMDEPTGGL---DVSvqaRLLDLLRGlVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRV 230
|
250
....*....|....
gi 490819619 879 IAQGRPQDVVRDPQ 892
Cdd:PRK11701 231 VESGLTDQVLDDPQ 244
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
678-882 |
8.96e-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: 112.24 E-value: 8.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 678 HVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQFHAPknpadfaaLGLGRTFQivqpfAAM 757
Cdd:cd03220 36 WALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTV---RGRVSSL--------LGLGGGFN-----PEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 758 TVEENI-MVGAFYRhHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGINQTDV 836
Cdd:cd03220 100 TGRENIyLNGRLLG-LSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQ 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490819619 837 RRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQG 882
Cdd:cd03220 179 EKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
664-894 |
2.57e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 112.63 E-value: 2.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 664 ILRVQNLNKHFG-GLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQfhapknPADFAAL 742
Cdd:PRK13636 5 ILKVEELNYNYSdGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILF---DGK------PIDYSRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 743 GL-------GRTFQIV--QPFAAmTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVAR 813
Cdd:PRK13636 76 GLmklresvGMVFQDPdnQLFSA-SVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 814 VMAMEPRILLLDEVMAGINQTDVRRAIDLMLSI-RDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDPQ 892
Cdd:PRK13636 155 VLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMqKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKE 234
|
..
gi 490819619 893 VV 894
Cdd:PRK13636 235 ML 236
|
|
| urea_t_UrtB_arc |
TIGR03622 |
urea ABC transporter, permease protein UrtB; Members of this protein family are ABC ... |
19-285 |
3.32e-27 |
|
urea ABC transporter, permease protein UrtB; Members of this protein family are ABC transporter permease subunits restricted to the Archaea. Several lines of evidence suggest this protein is functionally analogous, as well as homologous, to the UrtB subunit of the Corynebacterium glutamicum urea transporter. All members of the operon show sequence similarity to urea transport subunits, the gene is located near the urease structural subunits in two of three species, and partial phylogenetic profiling identifies this permease subunit as closely matching the profile of urea utilization.
Pssm-ID: 132661 Cd Length: 283 Bit Score: 112.26 E-value: 3.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 19 AIVAVGLTLIFGIVKVVNFAHGEFLMAGMFVTWLITTKLGLHPYAAVIIVLPAMFILGALTQRLLIQPLMasDDGHAQIF 98
Cdd:TIGR03622 15 VLAAVGLAVIFGMMGVINLAHGEFILVGAYGTTLTYHQAGLPLPVAMVSGVVMTVIFGIIVERLIIQHLY--DRLLDSMV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 99 ATVGLSTAMINLALLIFGADIAN--TPnFGlrtPIEIGPLRVLTGQVFIFLGAIVLVVALQLFLKNSQTGRAIRAVAQHR 176
Cdd:TIGR03622 93 ATFGLALILTQGLRITFGNSLDSisTP-FG---NVAYGPYTYSTYRVFLPLVAIGVLVGLYVLFTRTEFGVRARATIQDP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 177 SAAELMGVNVSRIYILCFGLGAACVGLAAVLIAPLYPTSSNIGTYFVLTAFVVVVLGGLGSIPGAFVGALIIGVIDTMSG 256
Cdd:TIGR03622 169 ETARAMGVDTDRMYVTTFAIGSGLAGLTGALYAPIGAITPDRGSIFLVEAFVAVVVGGPSVVLGTALAGGLLGFINAVFS 248
|
250 260
....*....|....*....|....*....
gi 490819619 257 YYIGSDLREAVVFGIFLLILILKPSGLFG 285
Cdd:TIGR03622 249 NLYGTFVGLIALLIVAIIALRVLPDGITG 277
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
665-901 |
4.77e-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: 110.47 E-value: 4.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 665 LRVQNLNKHFGGLH-VTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGadgqfhapKNPADFAALG 743
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDG--------EDIREQDPVE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 744 L----GRTFQIVQPFAAMTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGP--LLGAEARGLTIGGLKRLEVARVMAM 817
Cdd:cd03295 73 LrrkiGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPaeFADRYPHELSGGQQQRVGVARALAA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 818 EPRILLLDEVMAGINQTDVRRAIDLMLSI-RDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDP--QVV 894
Cdd:cd03295 153 DPPLLLMDEPFGALDPITRDQLQEEFKRLqQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPanDFV 232
|
....*..
gi 490819619 895 EAYLGKE 901
Cdd:cd03295 233 AEFVGAD 239
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
666-877 |
5.33e-27 |
|
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: 107.72 E-value: 5.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 666 RVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADgqfhapknpadfaalglg 745
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKD------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 746 rtfqivqpfaamtveenimvgafyrhHHEKDAREAARETAWRMGLGpllgaeargltiGGLK-RLEVARVMAMEPRILLL 824
Cdd:cd00267 63 --------------------------IAKLPLEELRRRIGYVPQLS------------GGQRqRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490819619 825 DEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGE 877
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
665-887 |
8.15e-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: 109.97 E-value: 8.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 665 LRVQNLNKHFG-GLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKNPADFAAlg 743
Cdd:cd03256 1 IEVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 744 lgRTFQIVQPFA---AMTVEENIMVGAFYRHH---------HEKDaREAARETAWRMGLGPLLGAEARGLTIGGLKRLEV 811
Cdd:cd03256 79 --QIGMIFQQFNlieRLSVLENVLSGRLGRRStwrslfglfPKEE-KQRALAALERVGLLDKAYQRADQLSGGQQQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490819619 812 ARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSI-RDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDV 887
Cdd:cd03256 156 ARALMQQPKLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
665-891 |
1.22e-26 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 112.47 E-value: 1.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 665 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKNPadfaalGL 744
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDR------NI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 745 GRTFQ--IVQPFaaMTVEENImvgAFY---RHHHEKDAREAARETAWRMGLGPLLGAEARGLTiGGLK-RLEVARVMAME 818
Cdd:COG3839 78 AMVFQsyALYPH--MTVYENI---AFPlklRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLS-GGQRqRVALGRALVRE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 819 PRILLLDEVMAGInqtDVRRAIDLMLSI----RDSGVSII-----AIEhvmqaVMSLSDRVIVLASGEVIAQGRPQDVVR 889
Cdd:COG3839 152 PKVFLLDEPLSNL---DAKLRVEMRAEIkrlhRRLGTTTIyvthdQVE-----AMTLADRIAVMNDGRIQQVGTPEELYD 223
|
..
gi 490819619 890 DP 891
Cdd:COG3839 224 RP 225
|
|
| urea_trans_UrtC |
TIGR03408 |
urea ABC transporter, permease protein UrtC; Members of this protein family are ABC ... |
351-619 |
1.93e-26 |
|
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: 110.82 E-value: 1.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 351 FAALSTAWNIVGGFAGQMSLGHAVFYGIGGY---------------TGVILFnMGI--------------SPWFSMFIGA 401
Cdd:TIGR03408 18 YAIVALGIDLIWGYTGILSLGQGVFFGLGGYamamylklqasgegtTGLPDF-MLWngvtelpwfwqpfaSFPFALLAVV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 402 FIAALVGMVISYPCF--RLKGPFYSLASIAFLEVFRVLALHFGWLTGGATGLM-IQLKLGWVWMVFRERWPSLLIVFGML 478
Cdd:TIGR03408 97 LVPGLLAFLLGYFVFrsRIKGVYFSIITQALALALALLFVGQQTGTGGTNGLTdFKTLLGFDLSSDSTKRALYFLTAALL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 479 LVTLAITWAVRRSRLGFYLVATRERESAARAAGVRTVRVRLIAVAISSALCAMLGTFHAMYLTFIEPaAMFSLAFSIQIA 558
Cdd:TIGR03408 177 ALAFLLCRWLVRSRFGRVLIAIRDAENRVRFLGYDPANYKVFVFVLSAGIAGIAGALYVPQVGIISP-SEMGIVPSIEMV 255
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490819619 559 MFALIGGLGTVAGPLLGAVLlvpiTEWARASLGASALGLHGFVYGLVLILVVLFMPNGIMG 619
Cdd:TIGR03408 256 IWVAVGGRGTLIGAVLGALL----VNYAKTFFSEAFPEAWLYILGALFVVVVLFLPKGLAG 312
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
681-895 |
2.04e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 109.70 E-value: 2.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 681 RNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCG----ADGQFHAPKNpadfaalgLGRTFQivQP--- 753
Cdd:PRK13632 26 KNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGitisKENLKEIRKK--------IGIIFQ--NPdnq 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 754 FAAMTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGINQ 833
Cdd:PRK13632 96 FIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDP 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490819619 834 TDVRRAIDLMLSIRDSGV-SIIAIEHVMQAVMsLSDRVIVLASGEVIAQGRPQDVVRDPQVVE 895
Cdd:PRK13632 176 KGKREIKKIMVDLRKTRKkTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEILNNKEILE 237
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
649-899 |
5.23e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 110.31 E-value: 5.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 649 AIKAPSPDRAGIGQDILRVqnlNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADg 728
Cdd:PRK13536 29 AKASIPGSMSTVAIDLAGV---SKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVP- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 729 qfhAPKNpADFAALGLGRTFQIVQPFAAMTVEENIMV-GAFYRHHhekdAREAarETAwrmgLGPLL-------GAEAR- 799
Cdd:PRK13536 105 ---VPAR-ARLARARIGVVPQFDNLDLEFTVRENLLVfGRYFGMS----TREI--EAV----IPSLLefarlesKADARv 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 800 GLTIGGLKR-LEVARVMAMEPRILLLDEVMAGINqTDVRRAI-DLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGE 877
Cdd:PRK13536 171 SDLSGGMKRrLTLARALINDPQLLILDEPTTGLD-PHARHLIwERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGR 249
|
250 260
....*....|....*....|....*
gi 490819619 878 VIAQGRPQDVVRDP---QVVEAYLG 899
Cdd:PRK13536 250 KIAEGRPHALIDEHigcQVIEIYGG 274
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
665-882 |
9.46e-26 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 105.74 E-value: 9.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 665 LRVQNLNKHFGGLHVTRNVSFTLREGeVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADgqfhAPKNPADFAALgL 744
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQD----VLKQPQKLRRR-I 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 745 GRTFQIVQPFAAMTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLL 824
Cdd:cd03264 75 GYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 825 DEVMAGInqtDVRRAIDL--MLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQG 882
Cdd:cd03264 155 DEPTAGL---DPEERIRFrnLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
664-897 |
1.40e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 108.35 E-value: 1.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 664 ILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKNPadfAALG 743
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHAR---QRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 744 LGRTFQIVQPfaAMTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILL 823
Cdd:PRK13537 84 VVPQFDNLDP--DFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490819619 824 LDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDP---QVVEAY 897
Cdd:PRK13537 162 LDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESEigcDVIEIY 238
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
665-899 |
1.48e-25 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 105.99 E-value: 1.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 665 LRVQNLNKHFGGLHVtrNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADgqfHAPKNPAD--FAAL 742
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQD---LTALPPAErpVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 743 glgrtFQIVQPFAAMTVEENIMVGafyRHHHEK---DAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEP 819
Cdd:COG3840 77 -----FQENNLFPHLTVAQNIGLG---LRPGLKltaEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 820 RILLLDEVMAginqtdvrrAID--L---MLSI-----RDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVV- 888
Cdd:COG3840 149 PILLLDEPFS---------ALDpaLrqeMLDLvdelcRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLd 219
|
250
....*....|..
gi 490819619 889 -RDPQVVEAYLG 899
Cdd:COG3840 220 gEPPPALAAYLG 231
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
665-882 |
1.99e-25 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 104.88 E-value: 1.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 665 LRVQNLNKHFgglhvtrnvSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADgqfHAPKNPADFAALGL 744
Cdd:cd03298 8 FSYGEQPMHF---------DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVD---VTAAPPADRPVSML 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 745 grtFQIVQPFAAMTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLL 824
Cdd:cd03298 76 ---FQENNLFAHLTVEQNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490819619 825 DEVMAGINQTDVRRAIDLMLSI-RDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQG 882
Cdd:cd03298 153 DEPFAALDPALRAEMLDLVLDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
664-895 |
2.12e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 106.70 E-value: 2.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 664 ILRVQNLN-KHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGadgqfhapkNPADFAAL 742
Cdd:PRK13639 1 ILETRDLKySYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKG---------EPIKYDKK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 743 GLGRTFQIV---------QPFAAmTVEENIMVGAFYRHHHEKDAREAARETAWRMGLgplLGAEARG---LTIGGLKRLE 810
Cdd:PRK13639 72 SLLEVRKTVgivfqnpddQLFAP-TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGM---EGFENKPphhLSGGQKKRVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 811 VARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRD 890
Cdd:PRK13639 148 IAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSD 227
|
....*
gi 490819619 891 PQVVE 895
Cdd:PRK13639 228 IETIR 232
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
648-880 |
3.32e-25 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 110.49 E-value: 3.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 648 RAIKAPSPDRAG-IGQDILRVQNLNKHfgglHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcga 726
Cdd:COG1129 239 RELEDLFPKRAAaPGEVVLEVEGLSVG----GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRL--- 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 727 DGQFHAPKNPADFAALGLG------RTFQIVQPfaaMTVEENIMVGAFYRHHH-----EKDAREAARETAWRMGL-GPLL 794
Cdd:COG1129 312 DGKPVRIRSPRDAIRAGIAyvpedrKGEGLVLD---LSIRENITLASLDRLSRgglldRRRERALAEEYIKRLRIkTPSP 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 795 GAEARGLTiGG------LkrlevARVMAMEPRILLLDEVMAGInqtDV--RRAI-DLMLSIRDSGVSIIAI--EhvMQAV 863
Cdd:COG1129 389 EQPVGNLS-GGnqqkvvL-----AKWLATDPKVLILDEPTRGI---DVgaKAEIyRLIRELAAEGKAVIVIssE--LPEL 457
|
250
....*....|....*..
gi 490819619 864 MSLSDRVIVLASGEVIA 880
Cdd:COG1129 458 LGLSDRILVMREGRIVG 474
|
|
| TM_PBP1_LivM_like |
cd06581 |
Transmembrane subunit (TM) of Escherichia coli LivM and related proteins. LivM is one of two ... |
18-285 |
6.37e-25 |
|
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: 105.22 E-value: 6.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 18 FAIVAVGLTLIFGIVKVVNFAHGEFLMAGMFVTWLITTKLGLHPY----AAVIIVLPAMFILGALTQRLliqplmasdDG 93
Cdd:cd06581 4 YAILALGLNLLLGYAGQLSLGHAAFFGIGAYTAALLATRLGLPFWlallAAGLVAALVGLLLGLPALRL---------RG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 94 HAQIFATVGLSTAMInlALLIFGADIANTPN-FGLRTPIEIGPLRVLTGQVFIFLGAIVLVVALQLF--LKNSQTGRAIR 170
Cdd:cd06581 75 VYFAIATLAFAEIVR--LLALNWSSLTGGSNgLSGIPPPLLGGLLLSSPLAFYYLVLAVLLLVLLLLrrLVRSPFGRALR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 171 AVAQHRSAAELMGVNVSRIYILCFGLGAACVGLAAVLIAPL--YPTSSNIGTYFVLTAFVVVVLGGLGSIPGAFVGALII 248
Cdd:cd06581 153 AIRENEVAAEALGINVTRYKLLAFALSAALAGLAGALYAHYlgFVSPESFGFALSIELLLMVVLGGLGSLLGPVLGAALL 232
|
250 260 270
....*....|....*....|....*....|....*..
gi 490819619 249 GVIDTMSGYYiGSDLREAVVFGIFLLILILKPSGLFG 285
Cdd:cd06581 233 VLLPELLRSL-GPGLRLLVFGLLLILVVLFLPRGLVG 268
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
649-891 |
9.07e-25 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 107.23 E-value: 9.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 649 AIKAPSPDRAGIGQDILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADG 728
Cdd:PRK11607 4 AIPRPQAKTRKALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 729 QFHAP-KNPADFaalglgrTFQIVQPFAAMTVEENIMVGAfyrhHHEKDAR-EAARETAWRMGLGPLLGAEARG---LTI 803
Cdd:PRK11607 84 SHVPPyQRPINM-------MFQSYALFPHMTVEQNIAFGL----KQDKLPKaEIASRVNEMLGLVHMQEFAKRKphqLSG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 804 GGLKRLEVARVMAMEPRILLLDEVMAGINQT-DVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQG 882
Cdd:PRK11607 153 GQRQRVALARSLAKRPKLLLLDEPMGALDKKlRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIG 232
|
....*....
gi 490819619 883 RPQDVVRDP 891
Cdd:PRK11607 233 EPEEIYEHP 241
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
681-882 |
1.06e-24 |
|
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: 103.57 E-value: 1.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 681 RNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKNPADFAALgLGRTFQIVQPFAAMTve 760
Cdd:cd03267 38 KGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVV-FGQKTQLWWDLPVID-- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 761 enimvgAFYRHHH-----EKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGIN--- 832
Cdd:cd03267 115 ------SFYLLAAiydlpPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDvva 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490819619 833 QTDVRRAIDLMlsIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQG 882
Cdd:cd03267 189 QENIRNFLKEY--NRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
665-901 |
1.15e-24 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 108.85 E-value: 1.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 665 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQFHAPKNPADFAALGL 744
Cdd:PRK11288 5 LSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILI---DGQEMRFASTTAALAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 745 GRTFQIVQPFAAMTVEENIMVGAFYRHH---HEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRI 821
Cdd:PRK11288 82 AIIYQELHLVPEMTVAENLYLGQLPHKGgivNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 822 LLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRP-QDVVRDpQVVEAYLGK 900
Cdd:PRK11288 162 IAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVATFDDmAQVDRD-QLVQAMVGR 240
|
.
gi 490819619 901 E 901
Cdd:PRK11288 241 E 241
|
|
| BPD_transp_2 |
pfam02653 |
Branched-chain amino acid transport system / permease component; This is a large family mainly ... |
344-610 |
1.91e-24 |
|
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: 103.88 E-value: 1.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 344 IFITICLFAALSTAWNIVGGFAGQMSLGHAVFYGIGGYTGVILFNMGIS-PWFSMFIGAFIAALVGMVISYPCFRLKGPF 422
Cdd:pfam02653 5 ILTLASIYAIAALGLTLIYGIAGVINLGHGGFMMLGAYVAAMLLNLLGPgLWLALPVGILVGAAVGLLIGILTLRLKINE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 423 YSLASIAFLEVFRVLALHFGWLTGGATGLMIQLKLGWVWMVFRERWPSLLIVFGmLLVTLAITWAVRRSRLGFYLVATRE 502
Cdd:pfam02653 85 VIITLLLNLAALGLALFLVTGILGGEGGTSGITGPSGFPGAFLSFAFAFIFLLA-LLLVLALWLLLYRTKFGRALRAVGE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 503 RESAARAAGVRTVRVRLIAVAISSALCAMLGTFHAMYLTFIEPAAmFSLAFSIQIAMFALIGGLGTVAGPLLGAVLLVPI 582
Cdd:pfam02653 164 NEEAARAAGINVKKLKLLTFVISGALAGLAGALLALYTGVVPPSN-FGVGLGLDAIAAVVLGGAGSPIGVVIGSLIIGLV 242
|
250 260
....*....|....*....|....*...
gi 490819619 583 TEWARASLGASALgLHGFVYGLVLILVV 610
Cdd:pfam02653 243 QSLGLGALGSPPE-LSLLVLGALLILVL 269
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
682-896 |
6.35e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 102.79 E-value: 6.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 682 NVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgADGQFHAPKNPADFAAL--GLGRTFQIV--QPFAAm 757
Cdd:PRK13634 25 DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI--GERVITAGKKNKKLKPLrkKVGIVFQFPehQLFEE- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 758 TVEENIMVGAFYRHHHEKDAREAARETAWRMGLGP-LLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGINQTDV 836
Cdd:PRK13634 102 TVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGR 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490819619 837 RRAIDLMLSI-RDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDPQVVEA 896
Cdd:PRK13634 182 KEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDELEA 242
|
|
| LivM |
COG4177 |
ABC-type branched-chain amino acid transport system, permease component [Amino acid transport ... |
18-285 |
6.99e-24 |
|
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: 102.47 E-value: 6.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 18 FAIVAVGLTLIFGIVKVVNFAHGEFLMAGMFVTWLITTKLGLHPYAAVII--VLPAMF--ILGALTQRLliqplmasdDG 93
Cdd:COG4177 14 YAILALGLNLLLGYTGLLSLGHAAFFGIGAYAAALLTTHLGLPFWLALLLagLVAALLglLIGLPALRL---------RG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 94 HAQIFATVGLS----TAMINLALLIFGAD-IANTPnfglrtPIEIGPLRVLTGQVFIFLGAIVLVVA--LQLFLKNSQTG 166
Cdd:COG4177 85 DYLAIATLAFAeivrLLALNLESLTGGADgLSGIP------RPTLFGLDLGSPLAFYYLVLALLVLVllLLRRLVRSRFG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 167 RAIRAVAQHRSAAELMGVNVSRIYILCFGLGAACVGLAAVLIAPLYPTSSNIGTYFVLTAFVV--VVLGGLGSIPGAFVG 244
Cdd:COG4177 159 RALRAIRENEIAAEALGINVTRYKLLAFVLSAALAGLAGALYAHYVGFVSPESFSFLLSIEILlmVVLGGLGSLLGPVLG 238
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 490819619 245 ALIIGVIDTMSGYYigSDLREAVVFGIFLLILILKPSGLFG 285
Cdd:COG4177 239 AVLLVLLPELLRSL--PEYRLLIFGLLLILVVLFRPRGLAG 277
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
664-892 |
8.59e-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: 8.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 664 ILRVQNLNKHF----GGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAP---DEGTVNLCGADgqfHAPKNP 736
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGED---LLKLSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 737 ADFAALgLGRTFQIV-Q-PFAA----MTVEENIMVGafYRHHH---EKDAREAARETAWRMGLGPllgAEARgltI---- 803
Cdd:COG0444 78 KELRKI-RGREIQMIfQdPMTSlnpvMTVGDQIAEP--LRIHGglsKAEARERAIELLERVGLPD---PERR---Ldryp 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 804 ----GGLK-RLEVARVMAMEPRILLLDE--------VMAGInqtdvrraIDLMLSIRDS-GVSIIAIEHVMQAVMSLSDR 869
Cdd:COG0444 149 helsGGMRqRVMIARALALEPKLLIADEpttaldvtIQAQI--------LNLLKDLQRElGLAILFITHDLGVVAEIADR 220
|
250 260
....*....|....*....|...
gi 490819619 870 VIVLASGEVIAQGRPQDVVRDPQ 892
Cdd:COG0444 221 VAVMYAGRIVEEGPVEELFENPR 243
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
665-878 |
8.60e-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: 8.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 665 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKNPadfaalGL 744
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDR------DI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 745 GRTFQIVQPFAAMTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLL 824
Cdd:cd03301 75 AMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLM 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490819619 825 DEVMAGINqTDVRRAIDLMLS--IRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEV 878
Cdd:cd03301 155 DEPLSNLD-AKLRVQMRAELKrlQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
664-896 |
1.17e-23 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 105.90 E-value: 1.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 664 ILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQFHAPKNPADFAALG 743
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEI---GGNPCARLTPAKAHQLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 744 LGRTFQIVQPFAAMTVEENIMVGAfyrHHHEKDAREAARETAwRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILL 823
Cdd:PRK15439 88 IYLVPQEPLLFPNLSVKENILFGL---PKRQASMQKMKQLLA-ALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490819619 824 LDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGrPQDVVRDPQVVEA 896
Cdd:PRK15439 164 LDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSG-KTADLSTDDIIQA 235
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
665-892 |
1.24e-23 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 101.20 E-value: 1.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 665 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCG--------ADGQFHApknp 736
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlvrdKDGQLKV---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 737 ADFAALGLGRT-----FQIVQPFAAMTVEENIMVGAFYRHHHEK-DAREAARETAWRMGLGpllgAEARG-----LTIGG 805
Cdd:PRK10619 82 ADKNQLRLLRTrltmvFQHFNLWSHMTVLENVMEAPIQVLGLSKqEARERAVKYLAKVGID----ERAQGkypvhLSGGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 806 LKRLEVARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQ 885
Cdd:PRK10619 158 QQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPE 237
|
....*..
gi 490819619 886 DVVRDPQ 892
Cdd:PRK10619 238 QLFGNPQ 244
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
682-895 |
2.47e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 101.06 E-value: 2.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 682 NVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGadgqFHAPKNPADFA------ALGLGRTFQIVQPFA 755
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAG----YHITPETGNKNlkklrkKVSLVFQFPEAQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 756 AmTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGP-LLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGINQT 834
Cdd:PRK13641 101 N-TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEdLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPE 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490819619 835 DVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDPQVVE 895
Cdd:PRK13641 180 GRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKEWLK 240
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
664-879 |
2.87e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 100.16 E-value: 2.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 664 ILRVQNLNKHFG-GL----HVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADgqfhAPKNPAD 738
Cdd:COG1101 1 MLELKNLSKTFNpGTvnekRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKD----VTKLPEY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 739 FAALGLGRTFQivQPFA----AMTVEENIMVgAFYRHH-------HEKDAREAARETAWRMGLGpL---LGAEArGLTIG 804
Cdd:COG1101 77 KRAKYIGRVFQ--DPMMgtapSMTIEENLAL-AYRRGKrrglrrgLTKKRRELFRELLATLGLG-LenrLDTKV-GLLSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 805 GlKRLEVARVMAM--EPRILLLDEVMAGInqtDVRRAIDLM-LS---IRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEV 878
Cdd:COG1101 152 G-QRQALSLLMATltKPKLLLLDEHTAAL---DPKTAALVLeLTekiVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
.
gi 490819619 879 I 879
Cdd:COG1101 228 I 228
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
669-891 |
1.08e-22 |
|
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: 100.56 E-value: 1.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 669 NLNKHFGGLHVtrNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCG------ADGQFHAP-KNPadfaa 741
Cdd:COG4148 6 DFRLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlqdsARGIFLPPhRRR----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 742 lgLGRTFQIVQPFAAMTVEENIMVGAfyrhhheKDAREAARETAW-----RMGLGPLLGAEARGLTiGGLK-RLEVARVM 815
Cdd:COG4148 79 --IGYVFQEARLFPHLSVRGNLLYGR-------KRAPRAERRISFdevveLLGIGHLLDRRPATLS-GGERqRVAIGRAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490819619 816 AMEPRILLLDEVMAGINQTdvRRA--IDLMLSIRDS-GVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDP 891
Cdd:COG4148 149 LSSPRLLLMDEPLAALDLA--RKAeiLPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
661-878 |
1.19e-22 |
|
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: 95.96 E-value: 1.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 661 GQDILRVQNLNKHfgglHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADgqfHAPKNPADFA 740
Cdd:cd03215 1 GEPVLEVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKP---VTRRSPRDAI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 741 ALGLG------RTFQIVQPfaaMTVEENIMVGAFyrhhhekdareaaretawrmglgpLLGaeargltiGGLKRLEVARV 814
Cdd:cd03215 74 RAGIAyvpedrKREGLVLD---LSVAENIALSSL------------------------LSG--------GNQQKVVLARW 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490819619 815 MAMEPRILLLDEVMAGInqtDV--RRAI-DLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEV 878
Cdd:cd03215 119 LARDPRVLILDEPTRGV---DVgaKAEIyRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
664-899 |
1.37e-22 |
|
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: 1.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 664 ILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGAD-GQFHAPK-NPADFAA 741
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDiTDWQTAKiMREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 742 LGLGRtfqivQPFAAMTVEENIMVGAFYrhhheKDAREAARETAWRMGLGPLL---GAEARGLTIGGLKR-LEVARVMAM 817
Cdd:PRK11614 85 VPEGR-----RVFSRMTVEENLAMGGFF-----AERDQFQERIKWVYELFPRLherRIQRAGTMSGGEQQmLAIGRALMS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 818 EPRILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDPQVVEAY 897
Cdd:PRK11614 155 QPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVRSAY 234
|
..
gi 490819619 898 LG 899
Cdd:PRK11614 235 LG 236
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
666-891 |
1.53e-22 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 97.85 E-value: 1.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 666 RVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGqfhapKNPADFAALGLG 745
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLV---DG-----LDVATTPSRELA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 746 RTFQIVQ---PFAA-MTVEENIMVGAFyRHHH----EKDaREAARETAWRMGLGPLlgaEARGLT--IGGLK-RLEVARV 814
Cdd:COG4604 75 KRLAILRqenHINSrLTVRELVAFGRF-PYSKgrltAED-REIIDEAIAYLDLEDL---ADRYLDelSGGQRqRAFIAMV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 815 MAMEPRILLLDEVMagiNQTDVRRAIDLMLSIR----DSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRD 890
Cdd:COG4604 150 LAQDTDYVLLDEPL---NNLDMKHSVQMMKLLRrladELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITP 226
|
.
gi 490819619 891 P 891
Cdd:COG4604 227 E 227
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
588-888 |
1.75e-22 |
|
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: 103.38 E-value: 1.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 588 ASLGASALGLHGFVYGLVLILVVLFMPNG----------------IMGAINRFVRKPQDSEETATA--RTEPIAAVPARA 649
Cdd:COG2274 379 NLLSTLSGLLQQLATVALLWLGAYLVIDGqltlgqliafnilsgrFLAPVAQLIGLLQRFQDAKIAleRLDDILDLPPER 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 650 IKAPSPDRAGIGQDILRVQNLNKHFGGLH--VTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGAD 727
Cdd:COG2274 459 EEGRSKLSLPRLKGDIELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGID 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 728 -GQFhapkNPADFAALgLGRTFQIVQPFAAmTVEENIMVGAfyRHHHEKDAREAARET-------AWRMGLGPLLGAEAR 799
Cdd:COG2274 539 lRQI----DPASLRRQ-IGVVLQDVFLFSG-TIRENITLGD--PDATDEEIIEAARLAglhdfieALPMGYDTVVGEGGS 610
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 800 GLTIGGLKRLEVARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRdSGVSIIAIEHVMqAVMSLSDRVIVLASGEVI 879
Cdd:COG2274 611 NLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRL-STIRLADRIIVLDKGRIV 688
|
....*....
gi 490819619 880 AQGRPQDVV 888
Cdd:COG2274 689 EDGTHEELL 697
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
665-890 |
4.18e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 97.85 E-value: 4.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 665 LRVQNLNKHFGG-----LHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHapKNPADF 739
Cdd:PRK13651 3 IKVKNIVKIFNKklpteLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNK--KKTKEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 740 AALG----------------------LGRTFQIV--QPFAAmTVEENIMVGAFYRHHHEKDAREAARETAWRMGLgPL-- 793
Cdd:PRK13651 81 EKVLeklviqktrfkkikkikeirrrVGVVFQFAeyQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGL-DEsy 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 794 LGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVL 873
Cdd:PRK13651 159 LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFF 238
|
250
....*....|....*..
gi 490819619 874 ASGEVIAQGRPQDVVRD 890
Cdd:PRK13651 239 KDGKIIKDGDTYDILSD 255
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
642-897 |
4.24e-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: 4.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 642 IAAVPARAiKAPSPDRAGIgqdILRVQNLNKHF-----------GGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMI 710
Cdd:COG4172 257 LAAEPRGD-PRPVPPDAPP---LLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLAL 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 711 SGfLAPDEGTVNLCGADGQfhapknPADFAAL-GLGRTFQIV-Q-PFAA----MTVEENIMVGaFYRHHHEKDA---REA 780
Cdd:COG4172 333 LR-LIPSEGEIRFDGQDLD------GLSRRALrPLRRRMQVVfQdPFGSlsprMTVGQIIAEG-LRVHGPGLSAaerRAR 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 781 ARETAWRMGLGPllgaEAR--------GltiGGLKRLEVARVMAMEPRILLLDE--------VMAGInqtdvrraIDLML 844
Cdd:COG4172 405 VAEALEEVGLDP----AARhryphefsG---GQRQRIAIARALILEPKLLVLDEptsaldvsVQAQI--------LDLLR 469
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 490819619 845 SI-RDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDPQvvEAY 897
Cdd:COG4172 470 DLqREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQ--HPY 521
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
665-897 |
4.30e-22 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 99.92 E-value: 4.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 665 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADgqfhapknPADFAALGL 744
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDD--------VEALSARAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 745 GRTFQIVQPFAAM----TVEENIMVGafyRHHH-------EKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVAR 813
Cdd:PRK09536 76 SRRVASVPQDTSLsfefDVRQVVEMG---RTPHrsrfdtwTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLAR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 814 VMAMEPRILLLDEVMAGInqtDVRRAIDLMLSIR---DSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRD 890
Cdd:PRK09536 153 ALAQATPVLLLDEPTASL---DINHQVRTLELVRrlvDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTA 229
|
....*..
gi 490819619 891 PQVVEAY 897
Cdd:PRK09536 230 DTLRAAF 236
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
664-891 |
5.72e-22 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 98.87 E-value: 5.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 664 ILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGAD-GQFHAPKNPadfaal 742
Cdd:PRK09452 14 LVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDiTHVPAENRH------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 743 gLGRTFQIVQPFAAMTVEENIMVGAFYRHHHEKDAREAAREtAWRM-GLGPLLGAEARGLTIGGLKRLEVARVMAMEPRI 821
Cdd:PRK09452 88 -VNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVME-ALRMvQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKV 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490819619 822 LLLDEVMAGINQTdVRRAIDLMLSI--RDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDP 891
Cdd:PRK09452 166 LLLDESLSALDYK-LRKQMQNELKAlqRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEP 236
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
665-888 |
7.62e-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: 7.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 665 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGF--LAPDEGT----VNLCGADGQFHAP----- 733
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRiiyhVALCEKCGYVERPskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 734 ----------KNPADF--------------AALGLGRTFQIvqpFAAMTVEENIMVGAFYRHHHEKDAREAARETAWRMG 789
Cdd:TIGR03269 81 pcpvcggtlePEEVDFwnlsdklrrrirkrIAIMLQRTFAL---YGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 790 LGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGIN-QTD--VRRAidLMLSIRDSGVSIIAIEHVMQAVMSL 866
Cdd:TIGR03269 158 LSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDpQTAklVHNA--LEEAVKASGISMVLTSHWPEVIEDL 235
|
250 260
....*....|....*....|..
gi 490819619 867 SDRVIVLASGEVIAQGRPQDVV 888
Cdd:TIGR03269 236 SDKAIWLENGEIKEEGTPDEVV 257
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
662-892 |
9.36e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 95.61 E-value: 9.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 662 QDILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMIS--GFLAPD---EGTVNLCGADgqFHAPKnp 736
Cdd:PRK14239 3 EPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPEvtiTGSIVYNGHN--IYSPR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 737 ADFAAL--GLGRTFQIVQPFAaMTVEENIMVGAFYRHHHEKDAREAARETAWRMG-----LGPLLGAEARGLTIGGLKRL 809
Cdd:PRK14239 79 TDTVDLrkEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQVLDEAVEKSLKGAsiwdeVKDRLHDSALGLSGGQQQRV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 810 EVARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRDSgVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVR 889
Cdd:PRK14239 158 CIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFM 236
|
...
gi 490819619 890 DPQ 892
Cdd:PRK14239 237 NPK 239
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
662-897 |
9.83e-22 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 95.54 E-value: 9.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 662 QDILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEG-TVNLCGADgqfhapknpadfa 740
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGER------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 741 algLGRT--FQI------VQPF------AAMTVEENIMVGAF-----YRHHHEKDaREAARETAWRMGLGPLLGAEARGL 801
Cdd:COG1119 68 ---RGGEdvWELrkriglVSPAlqlrfpRDETVLDVVLSGFFdsiglYREPTDEQ-RERARELLELLGLAHLADRPFGTL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 802 TIGGLKRLEVARVMAMEPRILLLDEVMAG---INQTDVRRAIDLMlsIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEV 878
Cdd:COG1119 144 SQGEQRRVLIARALVKDPELLILDEPTAGldlGARELLLALLDKL--AAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRV 221
|
250
....*....|....*....
gi 490819619 879 IAQGRPQDVVRDPQVVEAY 897
Cdd:COG1119 222 VAAGPKEEVLTSENLSEAF 240
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
667-891 |
1.16e-21 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 97.46 E-value: 1.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 667 VQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGAD-GQFHAPKNPADFaalglg 745
Cdd:PRK10851 5 IANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDvSRLHARDRKVGF------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 746 rTFQIVQPFAAMTVEENIMVGAFYRHHHEKDAREAARETAWRM----GLGPLLGAEARGLTIGGLKRLEVARVMAMEPRI 821
Cdd:PRK10851 79 -VFQHYALFRHMTVFDNIAFGLTVLPRRERPNAAAIKAKVTQLlemvQLAHLADRYPAQLSGGQKQRVALARALAVEPQI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490819619 822 LLLDEVMAGIN---QTDVRRAI-DLMLSIRDSGVsiiAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDP 891
Cdd:PRK10851 158 LLLDEPFGALDaqvRKELRRWLrQLHEELKFTSV---FVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREP 228
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
664-898 |
1.69e-21 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 95.10 E-value: 1.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 664 ILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTL---FN----MISGFLApdEGTVNLCGADgqFHAPKnp 736
Cdd:COG1117 11 KIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLlrcLNrmndLIPGARV--EGEILLDGED--IYDPD-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 737 ADFAALglgRT-----FQIVQPFaAMTVEENIMVGAfyRHHHEKDAREAAR--ETA------W-----RmglgplLGAEA 798
Cdd:COG1117 85 VDVVEL---RRrvgmvFQKPNPF-PKSIYDNVAYGL--RLHGIKSKSELDEivEESlrkaalWdevkdR------LKKSA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 799 RGLTIGGLKRLEVARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRDSgVSIIAIEHVMQAVMSLSDRVIVLASGEV 878
Cdd:COG1117 153 LGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQAARVSDYTAFFYLGEL 231
|
250 260
....*....|....*....|..
gi 490819619 879 IAQGRPQDVVRDP--QVVEAYL 898
Cdd:COG1117 232 VEFGPTEQIFTNPkdKRTEDYI 253
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
640-886 |
1.74e-21 |
|
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: 99.45 E-value: 1.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 640 EPIAAVPARAIKAPSPDRAGIgqdilRVQNLN-KHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDE 718
Cdd:COG4988 317 APEPAAPAGTAPLPAAGPPSI-----ELEDVSfSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYS 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 719 GTVNLCGADgqfhapknPADFAALGLGRTFQIV--QPF-AAMTVEENImvgAFYRHHHEKDA-REAARET-AWRM----- 788
Cdd:COG4988 392 GSILINGVD--------LSDLDPASWRRQIAWVpqNPYlFAGTIRENL---RLGRPDASDEElEAALEAAgLDEFvaalp 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 789 -GLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGInqtDVRRAIDLMLSIRD--SGVSIIAIEHVMqAVMS 865
Cdd:COG4988 461 dGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHL---DAETEAEILQALRRlaKGRTVILITHRL-ALLA 536
|
250 260
....*....|....*....|.
gi 490819619 866 LSDRVIVLASGEVIAQGRPQD 886
Cdd:COG4988 537 QADRILVLDDGRIVEQGTHEE 557
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
664-879 |
2.12e-21 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 93.58 E-value: 2.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 664 ILRVQNLNKHF-GGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQfHAPKNpaDFAAL 742
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLS-RLKRR--EIPYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 743 --GLGRTFQIVQPFAAMTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPR 820
Cdd:COG2884 78 rrRIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490819619 821 ILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVI 879
Cdd:COG2884 158 LLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLV 216
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
678-882 |
3.03e-21 |
|
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: 93.04 E-value: 3.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 678 HVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGAD-GQFHapknPADFAAlGLGRTFQIVQPFAA 756
Cdd:cd03245 18 PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDiRQLD----PADLRR-NIGYVPQDVTLFYG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 757 mTVEENIMVGAfyRHHHEKDAREAAR-----ETAWR--MGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMA 829
Cdd:cd03245 93 -TLRDNITLGA--PLADDERILRAAElagvtDFVNKhpNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490819619 830 GINQTDVRRAID-LMLSIRDSgvSIIAIEHVMqAVMSLSDRVIVLASGEVIAQG 882
Cdd:cd03245 170 AMDMNSEERLKErLRQLLGDK--TLIIITHRP-SLLDLVDRIIVMDSGRIVADG 220
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
667-826 |
6.30e-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: 6.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 667 VQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGA--------DGQFHAPKNPAD 738
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGlrigylpqEPPLDDDLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 739 FAALGLGRTFQIVQPFAAM-----TVEENIM----VGAFYRHHHEKDAREAARETAWRMGLGP-LLGAEARGLTiGGLK- 807
Cdd:COG0488 81 TVLDGDAELRALEAELEELeaklaEPDEDLErlaeLQEEFEALGGWEAEARAEEILSGLGFPEeDLDRPVSELS-GGWRr 159
|
170
....*....|....*....
gi 490819619 808 RLEVARVMAMEPRILLLDE 826
Cdd:COG0488 160 RVALARALLSEPDLLLLDE 178
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
665-882 |
9.17e-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: 91.59 E-value: 9.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 665 LRVQnLNKHFGGLHVtrNVSFTLrEGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQ--FHAPKN---PADF 739
Cdd:cd03297 2 LCVD-IEKRLPDFTL--KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVL---NGTvlFDSRKKinlPPQQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 740 AALGLgrTFQIVQPFAAMTVEENIMVGafYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEP 819
Cdd:cd03297 75 RKIGL--VFQQYALFPHLNVRENLAFG--LKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490819619 820 RILLLDEVMAGInqtDVRRAIDLMLSIRDS----GVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQG 882
Cdd:cd03297 151 ELLLLDEPFSAL---DRALRLQLLPELKQIkknlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
667-892 |
1.03e-20 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 92.51 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 667 VQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNL--CGADGQFHAPKNPADFAAL-- 742
Cdd:PRK11264 6 VKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgdITIDTARSLSQQKGLIRQLrq 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 743 GLGRTFQIVQPFAAMTVEENIMVGAFYRHHHEKDAREA-ARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRI 821
Cdd:PRK11264 86 HVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATArARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEV 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490819619 822 LLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDPQ 892
Cdd:PRK11264 166 ILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQ 236
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
664-899 |
1.32e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 92.74 E-value: 1.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 664 ILRVQNLNKHF-GGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGqfhapknpADFAAL 742
Cdd:PRK13644 1 MIRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDT--------GDFSKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 743 -GLGRTFQIV-----QPFAAMTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMA 816
Cdd:PRK13644 73 qGIRKLVGIVfqnpeTQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 817 MEPRILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAvMSLSDRVIVLASGEVIAQGRPQDVVRDPQVveA 896
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVSL--Q 229
|
...
gi 490819619 897 YLG 899
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 ... |
660-890 |
1.74e-20 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 96.02 E-value: 1.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 660 IGQDILRVQNLNKHF-----GGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPK 734
Cdd:TIGR03269 275 VGEPIIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWVDMTK 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 735 NPADF---AALGLGRTFQIVQPFAAMTVEENIMvgafyrhhhEKDAREAARETAWRMGLGPLLGA-----EARG------ 800
Cdd:TIGR03269 355 PGPDGrgrAKRYIGILHQEYDLYPHRTVLDNLT---------EAIGLELPDELARMKAVITLKMVgfdeeKAEEildkyp 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 801 --LTIGGLKRLEVARVMAMEPRILLLDE---VMAGINQTDVRRAIdlMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLAS 875
Cdd:TIGR03269 426 deLSEGERHRVALAQVLIKEPRIVILDEptgTMDPITKVDVTHSI--LKAREEMEQTFIIVSHDMDFVLDVCDRAALMRD 503
|
250
....*....|....*
gi 490819619 876 GEVIAQGRPQDVVRD 890
Cdd:TIGR03269 504 GKIVKIGDPEEIVEE 518
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
650-826 |
4.35e-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: 4.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 650 IKAPSPDRagIGQDILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNlcgadgq 729
Cdd:COG0488 303 IRFPPPER--LGKKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVK------- 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 730 fhapknpadfaalgLGRTFQIVQpFA--------AMTVEENImvgafyrhhheKDAREAARETAWRMGLGPLL--GAEAR 799
Cdd:COG0488 374 --------------LGETVKIGY-FDqhqeeldpDKTVLDEL-----------RDGAPGGTEQEVRGYLGRFLfsGDDAF 427
|
170 180 190
....*....|....*....|....*....|..
gi 490819619 800 GLtIGGL-----KRLEVARVMAMEPRILLLDE 826
Cdd:COG0488 428 KP-VGVLsggekARLALAKLLLSPPNVLLLDE 458
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
668-891 |
4.68e-20 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 90.15 E-value: 4.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 668 QNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMI-------SGFLAPDEGTVNlcgadgqfhAPKNPADFA 740
Cdd:PRK09493 5 KNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCInkleeitSGDLIVDGLKVN---------DPKVDERLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 741 ALGLGRTFQIVQPFAAMTVEENIMVGAFY-RHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEP 819
Cdd:PRK09493 76 RQEAGMVFQQFYLFPHLTALENVMFGPLRvRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490819619 820 RILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDP 891
Cdd:PRK09493 156 KLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNP 227
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
679-889 |
5.61e-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: 89.85 E-value: 5.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 679 VTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQFHAPKNPADFAAlGLGRTFQIVQPFAAmT 758
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLV---DGHDLALADPAWLRR-QVGVVLQENVLFNR-S 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 759 VEENIMVG--AFYRHHHEKDAREA-ARETAWRM--GLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGINQ 833
Cdd:cd03252 92 IRDNIALAdpGMSMERVIEAAKLAgAHDFISELpeGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDY 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490819619 834 TDVRRAIDLMLSIRDsGVSIIAIEHVMQAVMSlSDRVIVLASGEVIAQGRPQDVVR 889
Cdd:cd03252 172 ESEHAIMRNMHDICA-GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLA 225
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
665-877 |
1.03e-19 |
|
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: 87.05 E-value: 1.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 665 LRVQNLNKHFGG--LHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKNPADFAAL 742
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 743 glgrTFQIVQPFaAMTVEENIMVGafyrhhhekdareaaretawrmglgpllgaeargltiGGLKRLEVARVMAMEPRIL 822
Cdd:cd03228 81 ----VPQDPFLF-SGTIRENILSG-------------------------------------GQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490819619 823 LLDEVMAGI---NQTDVRRAIDLMLsirdSGVSIIAIEHVMQAVMsLSDRVIVLASGE 877
Cdd:cd03228 119 ILDEATSALdpeTEALILEALRALA----KGKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
665-898 |
1.25e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 89.52 E-value: 1.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 665 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFL-----APDEGTVNLCGADgqFHAPKNPADF 739
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLelneeARVEGEVRLFGRN--IYSPDVDPIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 740 AALGLGRTFQIVQPFAAMTVEENIMVGAFYrHHHEKDAREAARETAWRMGLGPL-------LGAEARGLTIGGLKRLEVA 812
Cdd:PRK14267 83 VRREVGMVFQYPNPFPHLTIYDNVAIGVKL-NGLVKSKKELDERVEWALKKAALwdevkdrLNDYPSNLSGGQRQRLVIA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 813 RVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRDSgVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDP- 891
Cdd:PRK14267 162 RALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPe 240
|
....*...
gi 490819619 892 -QVVEAYL 898
Cdd:PRK14267 241 hELTEKYV 248
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
665-899 |
1.46e-19 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 89.66 E-value: 1.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 665 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKNpadfAALGL 744
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKE----VARRI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 745 GRTFQIVQPFAAMTVEENIMVGAF--------YRHHHEKDAREAARETawrmGLGPLLGAEARGLTIGGLKRLEVARVMA 816
Cdd:PRK10253 84 GLLAQNATTPGDITVQELVARGRYphqplftrWRKEDEEAVTKAMQAT----GITHLADQSVDTLSGGQRQRAWIAMVLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 817 MEPRILLLDEVMAGInqtDVRRAIDLMLSI----RDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVrDPQ 892
Cdd:PRK10253 160 QETAIMLLDEPTTWL---DISHQIDLLELLselnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIV-TAE 235
|
....*..
gi 490819619 893 VVEAYLG 899
Cdd:PRK10253 236 LIERIYG 242
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
644-887 |
2.24e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 92.40 E-value: 2.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 644 AVPARAIKAPSPDragiGQDILRVQNLN-KHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVN 722
Cdd:COG3845 241 EVLLRVEKAPAEP----GEVVLEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIR 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 723 LCGADgqfHAPKNPADFAALGLGR------TFQIVqpfAAMTVEENIMVGAFYRHH-------HEKDAREAARETAWRMG 789
Cdd:COG3845 317 LDGED---ITGLSPRERRRLGVAYipedrlGRGLV---PDMSVAENLILGRYRRPPfsrggflDRKAIRAFAEELIEEFD 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 790 L-GPLLGAEARGLTIGGLKRLEVARVMAMEPRILL-------LDeVMAgINQtdVRRAIdlmLSIRDSGVSIIAI----- 856
Cdd:COG3845 391 VrTPGPDTPARSLSGGNQQKVILARELSRDPKLLIaaqptrgLD-VGA-IEF--IHQRL---LELRDAGAAVLLIsedld 463
|
250 260 270
....*....|....*....|....*....|.
gi 490819619 857 EhvmqaVMSLSDRVIVLASGEVIAQGRPQDV 887
Cdd:COG3845 464 E-----ILALSDRIAVMYEGRIVGEVPAAEA 489
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
664-894 |
3.06e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 88.71 E-value: 3.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 664 ILRVQNLNKHF-GGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKNPADFAAL 742
Cdd:PRK13652 3 LIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 743 GLGRT-FQIVQPfaamTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRI 821
Cdd:PRK13652 83 VFQNPdDQIFSP----TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490819619 822 LLLDEVMAGINQTDVRRAIDLMLSIRDS-GVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDPQVV 894
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPDLL 232
|
|
| TM_PBP1_LivH_like |
cd06582 |
Transmembrane subunit (TM) of Escherichia coli LivH and related proteins. LivH is one of two ... |
349-618 |
3.50e-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: 88.64 E-value: 3.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 349 CLFAALSTAWNIVGGFAGQMSLGHAVFYGIGGYTGVILFN-MGISPWFSMFIGAFIAALVGMVISYPCFRL---KGPFYS 424
Cdd:cd06582 6 AIYALIALGLTLIFGVTGVINFAHGEFYMLGAYVAYTLLVaLGLPFWLALLLALLVAALLGVLLERLVLRPlrgAPLLTL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 425 LASIAFLEVFRVLALHFGWLTGGATGLMIqLKLGWVWMVFRERWPSLLIVFGMLLVTLAITWAVRRSRLGFYLVATRERE 504
Cdd:cd06582 86 LITFGGLLILLQGLLLIFGGDPRVPPPPL-LSGSVELGGVTIPPYRLFIIAVALVLLAALYLFLRRTRLGRAIRAVAQNP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 505 SAARAAGVRTVRVRLIAVAISSALCAMLGTFHAMYlTFIEPAAMFSLAFSIQIAmfALIGGLGTVAGPLLGAVLLVPITE 584
Cdd:cd06582 165 EAARLLGINVRRVFALTFALGAALAGLAGVLLAPI-TGVSPTMGLLLLLKAFAA--VVLGGLGSIPGAVVGGLLLGLAES 241
|
250 260 270
....*....|....*....|....*....|....
gi 490819619 585 WARASLGASALGLHGFVyglVLILVVLFMPNGIM 618
Cdd:cd06582 242 LAAAYLSSGYKDAVAFV---LLILVLLVRPQGLF 272
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
460-889 |
4.79e-19 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 91.76 E-value: 4.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 460 VWMVFRERWPSLLIVFGMLLVTLAITWAVRRSRLGFYLVATRERESAARA----AGVRTVRvrlIAVAISSALCAMLGTF 535
Cdd:COG1132 154 VVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLqeslSGIRVVK---AFGREERELERFREAN 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 536 HAMYLTFIEPAAMFSLAFSIqiamFALIGGLGTVAGPLLGAVLlvpiteWARASLGASALGLhgfvygLVLILVVLFMP- 614
Cdd:COG1132 231 EELRRANLRAARLSALFFPL----MELLGNLGLALVLLVGGLL------VLSGSLTVGDLVA------FILYLLRLFGPl 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 615 NGIMGAINRFVRkpqdsEETATARTEPIAAVPARAIKAPSPDRAGIGQDILRVQNLnkHF---GGLHVTRNVSFTLREGE 691
Cdd:COG1132 295 RQLANVLNQLQR-----ALASAERIFELLDEPPEIPDPPGAVPLPPVRGEIEFENV--SFsypGDRPVLKDISLTIPPGE 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 692 VLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQfhapkNPADFAALGLGRTFQIV--QPF-AAMTVEENIMVGAf 768
Cdd:COG1132 368 TVALVGPSGSGKSTLVNLLLRFYDPTSGRILI---DGV-----DIRDLTLESLRRQIGVVpqDTFlFSGTIRENIRYGR- 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 769 yRHHHEKDAREAARET-AWRM------GLGPLLGaeARGLTI-GGLK-RLEVARVMAMEPRILLLDEVMAGI-NQTD--V 836
Cdd:COG1132 439 -PDATDEEVEEAAKAAqAHEFiealpdGYDTVVG--ERGVNLsGGQRqRIAIARALLKDPPILILDEATSALdTETEalI 515
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 490819619 837 RRAID-LMlsirdSGVSIIAIEH----VMQAvmslsDRVIVLASGEVIAQGRPQDVVR 889
Cdd:COG1132 516 QEALErLM-----KGRTTIVIAHrlstIRNA-----DRILVLDDGRIVEQGTHEELLA 563
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
665-858 |
4.84e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 86.47 E-value: 4.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 665 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGqfHAPKNPADFAALGL 744
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI--DDPDVAEACHYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 745 GRTFQivqpfAAMTVEENIMVGAFYRHHHEKDAREAARetawRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLL 824
Cdd:PRK13539 81 RNAMK-----PALTVAENLEFWAAFLGGEELDIAAALE----AVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWIL 151
|
170 180 190
....*....|....*....|....*....|....
gi 490819619 825 DEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEH 858
Cdd:PRK13539 152 DEPTAALDAAAVALFAELIRAHLAQGGIVIAATH 185
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
679-888 |
4.95e-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: 87.29 E-value: 4.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 679 VTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADgqfhapknPADFAALGLGRTFQIVQPFAAM- 757
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHD--------VRDYTLASLRRQIGLVSQDVFLf 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 758 --TVEENIMVGAfyRHHHEKDAREAAR-----ETAWRM--GLGPLLGaeARGLTI-GGLK-RLEVARVMAMEPRILLLDE 826
Cdd:cd03251 89 ndTVAENIAYGR--PGATREEVEEAARaanahEFIMELpeGYDTVIG--ERGVKLsGGQRqRIAIARALLKDPPILILDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490819619 827 VMAGI-NQTD--VRRAIDLMLSIRDSgvsiIAIEHVMQAVMSlSDRVIVLASGEVIAQGRPQDVV 888
Cdd:cd03251 165 ATSALdTESErlVQAALERLMKNRTT----FVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEELL 224
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
662-889 |
7.23e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 87.76 E-value: 7.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 662 QDILRVQNLNKHFGGL--HVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQFHAPKNPADF 739
Cdd:PRK13635 3 EEIIRVEHISFRYPDAatYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITV---GGMVLSEETVWDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 740 AALgLGRTFQivQP---FAAMTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMA 816
Cdd:PRK13635 80 RRQ-VGMVFQ--NPdnqFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490819619 817 MEPRILLLDEVMAGInqtDVRRAIDLMLSIRD----SGVSIIAIEHVMQAVMSlSDRVIVLASGEVIAQGRPQDVVR 889
Cdd:PRK13635 157 LQPDIIILDEATSML---DPRGRREVLETVRQlkeqKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFK 229
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
682-897 |
1.03e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 87.48 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 682 NVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKNPADFAALGLGRTFQIVQP-FAAMTVE 760
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQFPESqLFEETVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 761 ENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEAR-GLTIGGLKRLEVARVMAMEPRILLLDEVMAGINQTDVRRA 839
Cdd:PRK13643 104 KDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPfELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEM 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490819619 840 IDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDPQVVEAY 897
Cdd:PRK13643 184 MQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEVDFLKAH 241
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
668-878 |
1.06e-18 |
|
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: 85.54 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 668 QNLNKHFGGLHVT-RNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQfHAPKNPADFAALGLGR 746
Cdd:cd03292 4 INVTKTYPNGTAAlDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVS-DLRGRAIPYLRRKIGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 747 TFQIVQPFAAMTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDE 826
Cdd:cd03292 83 VFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490819619 827 VMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEV 878
Cdd:cd03292 163 PTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
682-895 |
1.10e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 87.11 E-value: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 682 NVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKNPADFAALGLGRTFQI--VQPFAAmTV 759
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIRKKVGLVFQFpeSQLFEE-TV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 760 EENIMVGAFYRHHHEKDAREAARETAWRMGLGP-LLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGINQTDVRR 838
Cdd:PRK13649 104 LKDVAFGPQNFGVSQEEAEALAREKLALVGISEsLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKE 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490819619 839 AIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDPQVVE 895
Cdd:PRK13649 184 LMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQDVDFLE 240
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
682-887 |
1.33e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 87.09 E-value: 1.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 682 NVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQFHAPKNPADFAALgLGRTFQivQP---FAAMT 758
Cdd:PRK13650 25 DVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIII---DGDLLTEENVWDIRHK-IGMVFQ--NPdnqFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 759 VEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGINQTDVRR 838
Cdd:PRK13650 99 VEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490819619 839 AIDLMLSIRDS-GVSIIAIEHVMQAVmSLSDRVIVLASGEVIAQGRPQDV 887
Cdd:PRK13650 179 LIKTIKGIRDDyQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPREL 227
|
|
| livM |
PRK11301 |
leucine/isoleucine/valine transporter permease subunit; Provisional |
359-618 |
1.40e-18 |
|
leucine/isoleucine/valine transporter permease subunit; Provisional
Pssm-ID: 236896 [Multi-domain] Cd Length: 419 Bit Score: 89.26 E-value: 1.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 359 NIVGGFAGQMSLGHAVFYGIGGYTGVILFN-MGISPWFSMFIGAFIAALVGMVISYPCFRLKGPFYSLASIAFLEVFRVL 437
Cdd:PRK11301 129 NVVVGLAGLLDLGYVGFYAVGAYTYALLNHyYGLGFWECLPIAGLMAALFGFLLGFPVLRLRGDYLAIVTLGFGEIIRIL 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 438 ALHFGWLTGGATGLMIQLKLGWVWMVFRER-----WPSLLIVFGM------------------LLVTLAITWAVRRSRLG 494
Cdd:PRK11301 209 LLNNTEITGGPNGISQIPKPTLFGLEFSRTareggWDTFHEFFGLkydpsdrviflylvalllVVLTLFVINRLLRMPLG 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 495 FYLVATRERESAARAAGVRTVRVRLIAVAISSALCAMLGTFHAMYLTFIEPAAmFSLAFSIQIAMFALIGGLGTVAGPLL 574
Cdd:PRK11301 289 RAWEALREDEIACRSLGLNPTRIKLSAFTIGAAFAGFAGTFFAARQGFVSPES-FTFIESAFILAIVVLGGMGSQFGVIL 367
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 490819619 575 GAVLLVPITEWARASLGASALglhgfVYGLVLILVVLFMPNGIM 618
Cdd:PRK11301 368 AAILLVVLPELMRDFNEYRML-----MFGLLMVLMMIWRPQGLL 406
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
679-895 |
1.55e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 86.78 E-value: 1.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 679 VTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKNPADFAAlGLGRTFQivQP---FA 755
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKTVWDIRE-KVGIVFQ--NPdnqFV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 756 AMTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGINQTD 835
Cdd:PRK13640 99 GATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAG 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490819619 836 VRRAIDLMLSI-RDSGVSIIAIEH-VMQAVMslSDRVIVLASGEVIAQGRPQDVVRDPQVVE 895
Cdd:PRK13640 179 KEQILKLIRKLkKKNNLTVISITHdIDEANM--ADQVLVLDDGKLLAQGSPVEIFSKVEMLK 238
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
664-879 |
1.61e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 87.45 E-value: 1.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 664 ILRVQNLNKHF----------GGL-----------HVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVN 722
Cdd:COG4586 1 IIEVENLSKTYrvyekepglkGALkglfrreyrevEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 723 LCGadgqfHAP-KNPADFAalglgRTFQIV-----QPFAAMTVEENimvgaFYRHHH-----EKDAREAARETAWRMGLG 791
Cdd:COG4586 81 VLG-----YVPfKRRKEFA-----RRIGVVfgqrsQLWWDLPAIDS-----FRLLKAiyripDAEYKKRLDELVELLDLG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 792 PLLGAEARGLTIGGLKRLEVArvMAM--EPRILLLDE------VMAginQTDVRRAIDLMlsIRDSGVSIIAIEHVMQAV 863
Cdd:COG4586 146 ELLDTPVRQLSLGQRMRCELA--AALlhRPKILFLDEptigldVVS---KEAIREFLKEY--NRERGTTILLTSHDMDDI 218
|
250
....*....|....*.
gi 490819619 864 MSLSDRVIVLASGEVI 879
Cdd:COG4586 219 EALCDRVIVIDHGRII 234
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
664-892 |
1.90e-18 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 87.83 E-value: 1.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 664 ILRVQNLNKHF----GGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQfhapknpaDF 739
Cdd:COG1135 1 MIELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLV---DGV--------DL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 740 AAL---GLgRTFQ-----IVQPFAAM---TVEENImvgAF--YRHHHEKDAREA-AREtawrmgLGPLLGAEARG----- 800
Cdd:COG1135 70 TALserEL-RAARrkigmIFQHFNLLssrTVAENV---ALplEIAGVPKAEIRKrVAE------LLELVGLSDKAdayps 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 801 -LTiGGLK-RLEVARVMAMEPRILLLDEVMAGIN-QTDvrRAI-DLMLSIRDS-GVSIIAIEHVMQAVMSLSDRVIVLAS 875
Cdd:COG1135 140 qLS-GGQKqRVGIARALANNPKVLLCDEATSALDpETT--RSIlDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLEN 216
|
250
....*....|....*..
gi 490819619 876 GEVIAQGRPQDVVRDPQ 892
Cdd:COG1135 217 GRIVEQGPVLDVFANPQ 233
|
|
| LivH |
COG0559 |
Branched-chain amino acid ABC-type transport system, permease component [Amino acid transport ... |
370-619 |
2.52e-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: 86.27 E-value: 2.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 370 LGHAVFYGIGGYTGVILFN-MGISPWFSMFIGAFIAALVGMVISYPCFRlkgPFYS-------LASIAFLEVFRVLALhf 441
Cdd:COG0559 37 FAHGEFVMLGAYVAYTLATlLGLPLWLALLLAVLVAALLGVLLERLVIR---PLRGapplallLATIGLSLVLQGLVL-- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 442 gwLTGGATGLMIQLKLGWVWMVFRERWPS--LLIVFGMLLVTLAITWAVRRSRLGFYLVATRERESAARAAGVRTVRVRL 519
Cdd:COG0559 112 --LIFGADPRSFPALLSGSVELGGVSIPAyrLFIIVVALVLLAALWLFLRRTRLGLAMRAVAQNREAARLMGINVDRVIA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 520 IAVAISSALCAMLGTFHAMYlTFIEPAAMFSLAFSIQIAmfALIGGLGTVAGPLLGAVLLVPITEWARASLGASALGLHG 599
Cdd:COG0559 190 LTFALGAALAGLAGVLLAPI-YSVSPTMGFLLGLKAFAA--VVLGGLGSIPGAVVGGLLLGLAESLGAAYLPSGYKDVVA 266
|
250 260
....*....|....*....|
gi 490819619 600 FVyglVLILVVLFMPNGIMG 619
Cdd:COG0559 267 FV---LLILVLLVRPQGLFG 283
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
664-892 |
3.31e-18 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 85.61 E-value: 3.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 664 ILRVQNLNKHF---GGL----HV--TRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQfhaPK 734
Cdd:PRK15112 4 LLEVRNLSKTFryrTGWfrrqTVeaVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLI---DDH---PL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 735 NPADFAALGlGRTFQIVQ-PFAAMTVEENI--MVGAFYRHHHEKD--AREAARETAWRM-GLGP-LLGAEARGLTIGGLK 807
Cdd:PRK15112 78 HFGDYSYRS-QRIRMIFQdPSTSLNPRQRIsqILDFPLRLNTDLEpeQREKQIIETLRQvGLLPdHASYYPHMLAPGQKQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 808 RLEVARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRDS-GVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQD 886
Cdd:PRK15112 157 RLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTAD 236
|
....*.
gi 490819619 887 VVRDPQ 892
Cdd:PRK15112 237 VLASPL 242
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
665-882 |
3.73e-18 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 84.68 E-value: 3.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 665 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKNPADFAAL-- 742
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTPSDKAIRELrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 743 GLGRTFQIVQPFAAMTVEENIM------VGAfyrhhHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMA 816
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNLIeapcrvLGL-----SKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490819619 817 MEPRILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQG 882
Cdd:PRK11124 158 MEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQG 223
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
681-882 |
7.77e-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: 82.60 E-value: 7.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 681 RNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAP--DEGTVNLCGadgqfhAPKNPADFAALgLGRTFQIVQPFAAMT 758
Cdd:cd03213 26 KNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLING------RPLDKRSFRKI-IGYVPQDDILHPTLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 759 VEENIMVgafyrhhhekdareaaretawrmglgpllGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGInqtDVRR 838
Cdd:cd03213 99 VRETLMF-----------------------------AAKLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGL---DSSS 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490819619 839 AIDLMLSIR---DSGVSIIAIEHVMQAVM-SLSDRVIVLASGEVIAQG 882
Cdd:cd03213 147 ALQVMSLLRrlaDTGRTIICSIHQPSSEIfELFDKLLLLSQGRVIYFG 194
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
682-901 |
8.43e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 84.75 E-value: 8.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 682 NVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQ---------------FHAPKNpadfaalglgr 746
Cdd:PRK13633 28 DVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSdeenlwdirnkagmvFQNPDN----------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 747 tfQIVqpfaAMTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDE 826
Cdd:PRK13633 97 --QIV----ATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 827 VMAGINQTDVRRAIDLMLSI-RDSGVSIIAIEHVMQAVMSlSDRVIVLASGEVIAQGRPQDVVRD-----------PQVV 894
Cdd:PRK13633 171 PTAMLDPSGRREVVNTIKELnKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKEvemmkkigldvPQVT 249
|
....*....
gi 490819619 895 E-AY-LGKE 901
Cdd:PRK13633 250 ElAYeLKKE 258
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
682-895 |
8.45e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 84.71 E-value: 8.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 682 NVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADgqFHAPKNPADFAALGLGRTFQI--VQPFAAmTV 759
Cdd:PRK13637 25 NVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVD--ITDKKVKLSDIRKKVGLVFQYpeYQLFEE-TI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 760 EENIMVGAFYRHHHEKDAREAARETAWRMGLG--PLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGInqtDVR 837
Cdd:PRK13637 102 EKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGL---DPK 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490819619 838 RAIDLMLSIRD----SGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDPQVVE 895
Cdd:PRK13637 179 GRDEILNKIKElhkeYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEVETLE 240
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
662-885 |
1.02e-17 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 83.91 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 662 QDILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPD---EGTVNLCGADGQfHAPKNPAD 738
Cdd:PRK09984 2 QTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDksaGSHIELLGRTVQ-REGRLARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 739 F--AALGLGRTFQIVQPFAAMTVEENIMVGA-----FYR---HHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKR 808
Cdd:PRK09984 81 IrkSRANTGYIFQQFNLVNRLSVLENVLIGAlgstpFWRtcfSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490819619 809 LEVARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSI-RDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQ 885
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQ 238
|
|
| AraH |
COG1172 |
Ribose/xylose/arabinose/galactoside ABC-type transport system, permease component ... |
44-278 |
1.04e-17 |
|
Ribose/xylose/arabinose/galactoside ABC-type transport system, permease component [Carbohydrate transport and metabolism];
Pssm-ID: 440785 Cd Length: 322 Bit Score: 85.16 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 44 MAGMFVTWLITtKLGLHPYAAVIIVLPAMFILGA----LTQRLLIQPLMAsddghaqifaTVGLSTAMINLALLIFGADI 119
Cdd:COG1172 81 LSGVVAALLLV-ALGLPILLAILLALLVGALLGLlnglLVAKLRIPPFIV----------TLGTMFIARGLALLLTGGRP 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 120 ANTPNFGLRtpiEIGPLRVLTGQVFIFLgAIVLVVALQLFLKNSQTGRAIRAVAQHRSAAELMGVNVSRIYILCFGLGAA 199
Cdd:COG1172 150 ISGLPDAFR---ALGQGSLLGIPVPVLI-ALVVALVAWFLLRRTRFGRYIYAVGGNEEAARLSGINVRRVKILAYVLSGL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 200 CVGLAAVLIAPLYPT-SSNIGTYFVLTAFVVVVLG------GLGSIPGAFVGALIIGVIDTMSGYY-IGSDLREAVVFGI 271
Cdd:COG1172 226 LAGLAGILLAARLGSaQPNAGSGYELDAIAAVVIGgtsltgGRGSVLGTLLGALILGVLNNGLNLLgVSSYWQQIVKGAI 305
|
....*..
gi 490819619 272 FLLILIL 278
Cdd:COG1172 306 ILLAVLL 312
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
664-896 |
1.11e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 84.02 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 664 ILRVQNLnkHF---GGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGadgQFHAPKNPADFA 740
Cdd:PRK13647 4 IIEVEDL--HFrykDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMG---REVNAENEKWVR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 741 ALgLGRTFQIV--QPFAaMTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAME 818
Cdd:PRK13647 79 SK-VGLVFQDPddQVFS-STVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490819619 819 PRILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQdVVRDPQVVEA 896
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 ... |
666-879 |
1.88e-17 |
|
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: 81.92 E-value: 1.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 666 RVQNLN-KHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGadgqfhapknpADFAALGL 744
Cdd:cd03226 1 RIENISfSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG-----------KPIKAKER 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 745 GRTFQIV------QPFAAmTVEENIMVGAfyrhhHEKDAREAARETAWR-MGLGPLLGAEARGLTIGGLKRLEVARVMAM 817
Cdd:cd03226 70 RKSIGYVmqdvdyQLFTD-SVREELLLGL-----KELDAGNEQAETVLKdLDLYALKERHPLSLSGGQKQRLAIAAALLS 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490819619 818 EPRILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVI 879
Cdd:cd03226 144 GKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
664-899 |
2.08e-17 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 83.34 E-value: 2.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 664 ILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLaPDEGTVNLCGADGQFHAPKNP-ADFAAL 742
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDL-TGGGAPRGARVTGDVTLNGEPlAAIDAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 743 GLGRTF----QIVQPFAAMTVEENIMVGafyRHHHEKDAREAARET---AW----RMGLGPLLGAEARGLTIGGLKRLEV 811
Cdd:PRK13547 80 RLARLRavlpQAAQPAFAFSAREIVLLG---RYPHARRAGALTHRDgeiAWqalaLAGATALVGRDVTTLSGGELARVQF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 812 ARVMAM---------EPRILLLDEVMAGINQTDVRRAIDLMLSI-RDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQ 881
Cdd:PRK13547 157 ARVLAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLaRDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAH 236
|
250
....*....|....*...
gi 490819619 882 GRPQDVVRdPQVVEAYLG 899
Cdd:PRK13547 237 GAPADVLT-PAHIARCYG 253
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
664-876 |
3.13e-17 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 82.44 E-value: 3.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 664 ILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGadgqfhapkNPADFAALG 743
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDG---------KPVEGPGAE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 744 LGRTFQIVQPFAAMTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGpllGAEAR---GLTIGGLKRLEVARVMAMEPR 820
Cdd:PRK11248 72 RGVVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLE---GAEKRyiwQLSGGQRQRVGIARALAANPQ 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490819619 821 ILLLDEVMAGINQTDVRRAIDLMLSI-RDSGVSIIAIEHVMQAVMSLSDRVIVLASG 876
Cdd:PRK11248 149 LLLLDEPFGALDAFTREQMQTLLLKLwQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
664-901 |
3.83e-17 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 85.37 E-value: 3.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 664 ILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGfLAPD---EGTVNLCGADGQFHapkNPADFA 740
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHgtyEGEIIFEGEELQAS---NIRDTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 741 ALGLGRTFQIVQPFAAMTVEENIMVGAFYRHHHEKD-AREAARETAW--RMGLGPLLGAEARGLTIGGLKRLEVARVMAM 817
Cdd:PRK13549 81 RAGIAIIHQELALVKELSVLENIFLGNEITPGGIMDyDAMYLRAQKLlaQLKLDINPATPVGNLGLGQQQLVEIAKALNK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 818 EPRILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQgRPQDVVRDPQVVEAY 897
Cdd:PRK13549 161 QARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGT-RPAAGMTEDDIITMM 239
|
....
gi 490819619 898 LGKE 901
Cdd:PRK13549 240 VGRE 243
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
667-884 |
5.53e-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: 5.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 667 VQNLNKHF--GGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQfhapkNPADFAALGL 744
Cdd:TIGR01257 931 VKNLVKIFepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIE-----TNLDAVRQSL 1005
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 745 GRTFQIVQPFAAMTVEENIMvgaFYRHHHEKDAREAARETAWRM---GLGPLLGAEARGLTIGGLKRLEVARVMAMEPRI 821
Cdd:TIGR01257 1006 GMCPQHNILFHHLTVAEHIL---FYAQLKGRSWEEAQLEMEAMLedtGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKV 1082
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490819619 822 LLLDEVMAGINQTDVRRAIDLMLSIRdSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRP 884
Cdd:TIGR01257 1083 VVLDEPTSGVDPYSRRSIWDLLLKYR-SGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
662-861 |
6.05e-17 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 80.98 E-value: 6.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 662 QDILRVQNLNKHFGG----LHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKNPA 737
Cdd:PRK10584 4 ENIVEVHHLKKSVGQgeheLSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 738 DFAALGLGRTFQIVQPFAAMTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAM 817
Cdd:PRK10584 84 KLRAKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNG 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490819619 818 EPRILLLDEVMAGINQTDVRRAIDLMLSI-RDSGVSIIAIEHVMQ 861
Cdd:PRK10584 164 RPDVLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHDLQ 208
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
662-900 |
6.59e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 84.67 E-value: 6.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 662 QDILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKnpaDFAA 741
Cdd:PRK10762 2 QALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPK---SSQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 742 LGLGRTFQIVQPFAAMTVEENIMVG-----AFYRHHHEKDAREAARETAwRMGLG----PLLGAeargLTIGGLKRLEVA 812
Cdd:PRK10762 79 AGIGIIHQELNLIPQLTIAENIFLGrefvnRFGRIDWKKMYAEADKLLA-RLNLRfssdKLVGE----LSIGEQQMVEIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 813 RVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDpQ 892
Cdd:PRK10762 154 KVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLTED-S 232
|
....*...
gi 490819619 893 VVEAYLGK 900
Cdd:PRK10762 233 LIEMMVGR 240
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
662-898 |
6.83e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 81.50 E-value: 6.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 662 QDILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGF--LAPD---EGTVNLCGADgqfhAPKNP 736
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLieLYPEarvSGEVYLDGQD----IFKMD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 737 ADFAALGLGRTFQIVQPFAAMTVEENIMVGaFYRHHHEKDAREAARETAWRMGLGPL-------LGAEARGLTIGGLKRL 809
Cdd:PRK14247 77 VIELRRRVQMVFQIPNPIPNLSIFENVALG-LKLNRLVKSKKELQERVRWALEKAQLwdevkdrLDAPAGKLSGGQQQRL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 810 EVARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRDSgVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVR 889
Cdd:PRK14247 156 CIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFT 234
|
250
....*....|.
gi 490819619 890 DP--QVVEAYL 898
Cdd:PRK14247 235 NPrhELTEKYV 245
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
664-879 |
7.34e-17 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 84.46 E-value: 7.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 664 ILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGfLAPD---EGTVNLCGADGQFhapKNPADFA 740
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG-VYPHgsyEGEILFDGEVCRF---KDIRDSE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 741 ALGlgrtfqIV---QPFA---AMTVEENIMVGafyrHHHEK----DAREAARETA---WRMGLGPLLGAEARGLTIGGLK 807
Cdd:NF040905 77 ALG------IViihQELAlipYLSIAENIFLG----NERAKrgviDWNETNRRARellAKVGLDESPDTLVTDIGVGKQQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490819619 808 RLEVARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVI 879
Cdd:NF040905 147 LVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTI 218
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
665-878 |
7.53e-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: 79.18 E-value: 7.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 665 LRVQNLNKHFGGLH--VTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKNPADFaal 742
Cdd:cd03246 1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDH--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 743 gLGRTFQIVQPFAAmTVEENIMVGafyrhhhekdareaaretawrmglgpllgaeargltiGGLKRLEVARVMAMEPRIL 822
Cdd:cd03246 78 -VGYLPQDDELFSG-SIAENILSG-------------------------------------GQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490819619 823 LLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMqAVMSLSDRVIVLASGEV 878
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
633-898 |
1.12e-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: 84.11 E-value: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 633 ETATARTEP--IAAVPARAIKAPSPDRA-GIGQDILRVQNLNK-HFGGLHVTR--NVSFTLREGEVLGLIGPNGAGKTTL 706
Cdd:TIGR02633 223 KDMSTMSEDdiITMMVGREITSLYPHEPhEIGDVILEARNLTCwDVINPHRKRvdDVSFSLRRGEILGVAGLVGAGRTEL 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 707 FNMISG-FLAPDEGTVNLcgaDGQFHAPKNPADFAALGLG-----RTFQIVQPfaAMTVEENIMVGAFYRHHHEKDAREA 780
Cdd:TIGR02633 303 VQALFGaYPGKFEGNVFI---NGKPVDIRNPAQAIRAGIAmvpedRKRHGIVP--ILGVGKNITLSVLKSFCFKMRIDAA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 781 ARETAWRMGLGPL-LGAEARGLTIGGL-----KRLEVARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSII 854
Cdd:TIGR02633 378 AELQIIGSAIQRLkVKTASPFLPIGRLsggnqQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAII 457
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 490819619 855 AIEHVMQAVMSLSDRVIVLASGEVIAqgrpqDVVRD----PQVVEAYL 898
Cdd:TIGR02633 458 VVSSELAEVLGLSDRVLVIGEGKLKG-----DFVNHaltqEQVLAAAL 500
|
|
| TM_PBP1_transp_AraH_like |
cd06579 |
Transmembrane subunit (TM) of Escherichia coli AraH and related proteins. E. coli AraH is the ... |
44-253 |
1.28e-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: 80.92 E-value: 1.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 44 MAGMFVTWLITTkLGLHPYAAVIIVLPAMFILGA----LTQRLLIQPLMAsddghaqifaTVGLSTAMINLALLIFGADI 119
Cdd:cd06579 30 LSAVVAALLLVN-AGLPIPLAILAALAVGALIGLlnglLVAYLRIPPFIV----------TLGTMFILRGLALLITGGRP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 120 ANTPNFGLRTPIEIGPLRVLTGQVFIFlgaIVLVVALQLFLKNSQTGRAIRAVAQHRSAAELMGVNVSRIYILCFGLGAA 199
Cdd:cd06579 99 ISGLPPLFSFFLGGGLILGIPVPVLIA---LAVALVAWFLLRRTRFGRYLYAVGGNPEAARLSGINVRRVKILAYVLSGL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490819619 200 CVGLAAVLIAPLYPT-SSNIGTYFVLTAFVVVVLGGL------GSIPGAFVGALIIGVIDT 253
Cdd:cd06579 176 LAGLAGILLAARLGSaQPTAGNGYELDAIAAVVLGGTsltggrGSVLGTLLGALLLGVLNN 236
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
661-898 |
1.32e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 80.48 E-value: 1.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 661 GQDILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQ-FHAPKNPADF 739
Cdd:PRK14246 7 AEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKV---DGKvLYFGKDIFQI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 740 AALGL----GRTFQIVQPFAAMTVEENIMVGafYRHHHEKDAREAAR---ETAWRMGLGP----LLGAEARGLTIGGLKR 808
Cdd:PRK14246 84 DAIKLrkevGMVFQQPNPFPHLSIYDNIAYP--LKSHGIKEKREIKKiveECLRKVGLWKevydRLNSPASQLSGGQQQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 809 LEVARVMAMEPRILLLDEVMAGINQTDvRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVV 888
Cdd:PRK14246 162 LTIARALALKPKVLLMDEPTSMIDIVN-SQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIF 240
|
250
....*....|..
gi 490819619 889 RDP--QVVEAYL 898
Cdd:PRK14246 241 TSPknELTEKYV 252
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
664-887 |
2.32e-16 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 79.67 E-value: 2.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 664 ILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVnlcgadgqFHAPKNPADFAALG 743
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTV--------FLGDKPISMLSSRQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 744 LGRTF-----QIVQPfAAMTVEENIMVG-AFYRHHHEKDAREAARETAWRM---GLGPLLGAEARGLTIGGLKRLEVARV 814
Cdd:PRK11231 74 LARRLallpqHHLTP-EGITVRELVAYGrSPWLSLWGRLSAEDNARVNQAMeqtRINHLADRRLTDLSGGQRQRAFLAMV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490819619 815 MAMEPRILLLDEVMAGInqtDVRRAIDLMLSIR---DSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDV 887
Cdd:PRK11231 153 LAQDTPVVLLDEPTTYL---DINHQVELMRLMRelnTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEV 225
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
665-874 |
4.19e-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: 77.92 E-value: 4.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 665 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKNPADFAALGL 744
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 745 GRTFQivqpfAAMTVEENImvgAFYRHHHEKDAREAAREtawRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLL 824
Cdd:cd03231 81 APGIK-----TTLSVLENL---RFWHADHSDEQVEEALA---RVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWIL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490819619 825 DEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLA 874
Cdd:cd03231 150 DEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGARELDLG 199
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
678-888 |
4.22e-16 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 78.47 E-value: 4.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 678 HVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADgqfHAPKNPADFAALGLgrtFQIVQPFAAM 757
Cdd:PRK10771 13 HLPMRFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD---HTTTPPSRRPVSML---FQENNLFSHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 758 TVEENIMVGAF--YRHHHEKdaREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGINQTD 835
Cdd:PRK10771 87 TVAQNIGLGLNpgLKLNAAQ--REKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPAL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490819619 836 VRRAIDLMLSI-RDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVV 888
Cdd:PRK10771 165 RQEMLTLVSQVcQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELL 218
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
683-899 |
4.99e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 79.06 E-value: 4.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 683 VSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQFHAPKNPADFAAlGLGRTFQIVQPFAAMTVEEN 762
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILL---DAQPLESWSSKAFAR-KVAYLPQQLPAAEGMTVREL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 763 IMVGAFYRH----HHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGIN---QTD 835
Cdd:PRK10575 106 VAIGRYPWHgalgRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDiahQVD 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490819619 836 VRRAIDLMLSIRdsGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRdPQVVEAYLG 899
Cdd:PRK10575 186 VLALVHRLSQER--GLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMR-GETLEQIYG 246
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
638-892 |
5.10e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 82.60 E-value: 5.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 638 RTEPIAAVPARAIKAPSPDRAGI--GQDILRVQNLNKHF---GGL--------HVTRNVSFTLREGEVLGLIGPNGAGKT 704
Cdd:PRK10261 285 RRFPLISLEHPAKQEPPIEQDTVvdGEPILQVRNLVTRFplrSGLlnrvtrevHAVEKVSFDLWPGETLSLVGESGSGKS 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 705 TLFNMISGFLAPDEGTVNLCG------ADGQFHAPKNPADFaalglgrTFQivQPFAAM----TVEENIMvgAFYRHHHE 774
Cdd:PRK10261 365 TTGRALLRLVESQGGEIIFNGqridtlSPGKLQALRRDIQF-------IFQ--DPYASLdprqTVGDSIM--EPLRVHGL 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 775 KDAREAARETAW---RMGLGPLLGAEARGLTIGGLK-RLEVARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSI-RDS 849
Cdd:PRK10261 434 LPGKAAAARVAWlleRVGLLPEHAWRYPHEFSGGQRqRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLqRDF 513
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 490819619 850 GVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDPQ 892
Cdd:PRK10261 514 GIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQ 556
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
683-897 |
5.23e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 78.73 E-value: 5.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 683 VSFTLREGEVLGLIGPNGAGKTTLFNMISGfLAPDEGTVNLCGadgqfhapKNPADFAALGLGR-----TFQIVQPFaAM 757
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLNG--------RPLSDWSAAELARhraylSQQQSPPF-AM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 758 TVEENImvgAFYRHHHEKDA--REAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAM-------EPRILLLDEVM 828
Cdd:COG4138 85 PVFQYL---ALHQPAGASSEavEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490819619 829 AGInqtDVR--RAIDLMLS-IRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDPQVVEAY 897
Cdd:COG4138 162 NSL---DVAqqAALDRLLReLCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPENLSEVF 230
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
660-901 |
5.70e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 81.90 E-value: 5.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 660 IGQDILRVQNLNK-HFGGLHVTR--NVSFTLREGEVLGLIGPNGAGKTTLFNMISG-FLAPDEGTVNLcgaDGQFHAPKN 735
Cdd:PRK13549 255 IGEVILEVRNLTAwDPVNPHIKRvdDVSFSLRRGEILGIAGLVGAGRTELVQCLFGaYPGRWEGEIFI---DGKPVKIRN 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 736 PADFAALGLG------RTFQIVqpfAAMTVEENIMVGA---FYRHHHEKDARE--AARETAWRMGL---GPLLgAEARgL 801
Cdd:PRK13549 332 PQQAIAQGIAmvpedrKRDGIV---PVMGVGKNITLAAldrFTGGSRIDDAAElkTILESIQRLKVktaSPEL-AIAR-L 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 802 TIGGLKRLEVARVMAMEPRILLLDEVMAGInqtDV--RRAI-DLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEV 878
Cdd:PRK13549 407 SGGNQQKAVLAKCLLLNPKILILDEPTRGI---DVgaKYEIyKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
250 260
....*....|....*....|....*..
gi 490819619 879 ----IAQGRPQDvvrdpQVVEAYLGKE 901
Cdd:PRK13549 484 kgdlINHNLTQE-----QVMEAALRSE 505
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
634-873 |
5.89e-16 |
|
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: 81.95 E-value: 5.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 634 TATARTEPIAAVPARAiKAPSPDRAGIGQD---ILRVQNLNKHFGG-LHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNM 709
Cdd:TIGR02857 289 DGVAAAEALFAVLDAA-PRPLAGKAPVTAApasSLEFSGVSVAYPGrRPALRPVSFTVPPGERVALVGPSGAGKSTLLNL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 710 ISGFLAPDEGTVNLcgaDGQFHAPKNPADFAAlGLGRTFQIVQPFAAmTVEENImvgAFYRhhheKDAREAA-RETAWRM 788
Cdd:TIGR02857 368 LLGFVDPTEGSIAV---NGVPLADADADSWRD-QIAWVPQHPFLFAG-TIAENI---RLAR----PDASDAEiREALERA 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 789 GLGPL-----------LGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRdSGVSIIAIE 857
Cdd:TIGR02857 436 GLDEFvaalpqgldtpIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVT 514
|
250
....*....|....*.
gi 490819619 858 HvMQAVMSLSDRVIVL 873
Cdd:TIGR02857 515 H-RLALAALADRIVVL 529
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
675-887 |
6.31e-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: 78.04 E-value: 6.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 675 GGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQfhaPKNPADFAAL--GLGRTFQIVQ 752
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILI---DGI---DIRDISRKSLrsMIGVVLQDTF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 753 PFAAmTVEENIMVGAFYrhHHEKDAREAARETAWRM-------GLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLD 825
Cdd:cd03254 88 LFSG-TIMENIRLGRPN--ATDEEVIEAAKEAGAHDfimklpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490819619 826 EVMAGIN---QTDVRRAidlMLSIRDSGVSIIaIEHVMQAVMSlSDRVIVLASGEVIAQGRPQDV 887
Cdd:cd03254 165 EATSNIDtetEKLIQEA---LEKLMKGRTSII-IAHRLSTIKN-ADKILVLDDGKIIEEGTHDEL 224
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
683-897 |
6.45e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 78.44 E-value: 6.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 683 VSFTLREGEVLGLIGPNGAGKTTLFNMISGFLaPDEGTVNLCGAD-GQFHAPKnpadfaaLGLGRTF--QIVQPFAAMTV 759
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPlEAWSAAE-------LARHRAYlsQQQTPPFAMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 760 EENImvgAFYRHH--HEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKR-------LEVARVMAMEPRILLLDEVMAG 830
Cdd:PRK03695 87 FQYL---TLHQPDktRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRvrlaavvLQVWPDINPAGQLLLLDEPMNS 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 831 InqtDV--RRAIDLMLS-IRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDPQVVEAY 897
Cdd:PRK03695 164 L---DVaqQAALDRLLSeLCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVF 230
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
665-890 |
8.20e-16 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 76.80 E-value: 8.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 665 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFlaPD----EGTVNLcgaDGQFHAPKNPADFA 740
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH--PKyevtEGEILF---KGEDITDLPPEERA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 741 ALGLGRTFQIVQPFAAMTVEEnimvgaFYRHHHEkdareaaretawrmglgpllgaearGLTIGGLKRLEVARVMAMEPR 820
Cdd:cd03217 76 RLGIFLAFQYPPEIPGVKNAD------FLRYVNE-------------------------GFSGGEKKRNEILQLLLLEPD 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490819619 821 ILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQ-AVMSLSDRVIVLASGEVIAQGrPQDVVRD 890
Cdd:cd03217 125 LAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRlLDYIKPDRVHVLYDGRIVKSG-DKELALE 194
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
679-886 |
8.64e-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: 77.58 E-value: 8.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 679 VTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQfhapkNPADFAALGLGRTFQIVQ--P--F 754
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILL---DGV-----DIRDLNLRWLRSQIGLVSqePvlF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 755 aAMTVEENIMVGAFYRhhHEKDAREAARE-------TAWRMGLGPLLGaeARGLTI-GGLK-RLEVARVMAMEPRILLLD 825
Cdd:cd03249 90 -DGTIAENIRYGKPDA--TDEEVEEAAKKanihdfiMSLPDGYDTLVG--ERGSQLsGGQKqRIAIARALLRNPKILLLD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490819619 826 EVMAGI-NQTD--VRRAID-LMLsirdsGVSIIAIEHVMQAVMSlSDRVIVLASGEVIAQGRPQD 886
Cdd:cd03249 165 EATSALdAESEklVQEALDrAMK-----GRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDE 223
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
682-888 |
9.01e-16 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 81.48 E-value: 9.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 682 NVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgadgqfhapKNPADFAALGLGRTFQivqpfaaMTVEE 761
Cdd:PRK13545 42 NISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDI----------KGSAALIAISSGLNGQ-------LTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 762 NIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGINQTDVRRAID 841
Cdd:PRK13545 105 NIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLD 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490819619 842 LMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVV 888
Cdd:PRK13545 185 KMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVV 231
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
665-721 |
9.05e-16 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 75.18 E-value: 9.05e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 490819619 665 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTV 721
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV 57
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
664-901 |
1.04e-15 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 81.02 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 664 ILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGflapdegtVNLCGA-DGQFHAPKNP------ 736
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG--------VYPHGTwDGEIYWSGSPlkasni 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 737 ADFAALGLGRTFQIVQPFAAMTVEENIMVGAFYRHHHEKDAREA----ARETAWRMGLGPLLGAEARGLTIGGLKRL-EV 811
Cdd:TIGR02633 73 RDTERAGIVIIHQELTLVPELSVAENIFLGNEITLPGGRMAYNAmylrAKNLLRELQLDADNVTRPVGDYGGGQQQLvEI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 812 ARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQgRPQDVVRDP 891
Cdd:TIGR02633 153 AKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVAT-KDMSTMSED 231
|
250
....*....|
gi 490819619 892 QVVEAYLGKE 901
Cdd:TIGR02633 232 DIITMMVGRE 241
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
666-892 |
1.71e-15 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 78.69 E-value: 1.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 666 RVQNLNKHFGG----LHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQfhapknpaDFAA 741
Cdd:PRK11153 3 ELKNISKVFPQggrtIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLV---DGQ--------DLTA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 742 L---GLGRTFQ----IVQPF---AAMTVEENImvgAFYRHHHEKDAREAARETAwrmglgPLLgaEARGLT--------- 802
Cdd:PRK11153 72 LsekELRKARRqigmIFQHFnllSSRTVFDNV---ALPLELAGTPKAEIKARVT------ELL--ELVGLSdkadrypaq 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 803 -IGGLK-RLEVARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSI-RDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVI 879
Cdd:PRK11153 141 lSGGQKqRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDInRELGLTIVLITHEMDVVKRICDRVAVIDAGRLV 220
|
250
....*....|...
gi 490819619 880 AQGRPQDVVRDPQ 892
Cdd:PRK11153 221 EQGTVSEVFSHPK 233
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
664-887 |
1.99e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 77.44 E-value: 1.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 664 ILRVQNLNKHF---GGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQFHAPKNPADFA 740
Cdd:PRK13642 4 ILEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKI---DGELLTAENVWNLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 741 AlGLGRTFQivQP---FAAMTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAM 817
Cdd:PRK13642 81 R-KIGMVFQ--NPdnqFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490819619 818 EPRILLLDEVMAGINQTDVRRAIDLMLSIRDS-GVSIIAIEHVMQAVMSlSDRVIVLASGEVIAQGRPQDV 887
Cdd:PRK13642 158 RPEIIILDESTSMLDPTGRQEIMRVIHEIKEKyQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSEL 227
|
|
| TM_PBP1_branched-chain-AA_like |
cd06574 |
Transmembrane subunit (TM) of Periplasmic Binding Protein (PBP)-dependent ATP-Binding Cassette ... |
18-276 |
2.36e-15 |
|
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: 76.93 E-value: 2.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 18 FAIVAVGLTLIFGIVKVVNFAHGEFLMAGMFVTwLITTKLGLHPYAAVIIVLPAMFILGALT----QRLLIQPLMASddg 93
Cdd:cd06574 4 YAILALGVYIVFRILGFPDLTVDGSFPLGAAVA-AILIVAGYNPWLALIAAILAGAAAGLVTgflhTRLKINGLLAG--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 94 haqIFATVGLSTAMINLALLIFGADIANTPNFGLrtPIEIGPLRVLTGQVFIFLGAIVLVVALQLFLKnSQTGRAIRAVA 173
Cdd:cd06574 80 ---ILIMIGLYSINLRIMGGPNIPLGTRDTLLGL--LLLFGISGTLSIPVVLLLIVLLVLFLVIWFLR-TKLGLAMRATG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 174 QHRSAAELMGVNVSRIYILCFGLGAACVGLAAVLIAPLYPTSS-NIGTYFVLTAFVVVVLGG--------LGSIPGAFVG 244
Cdd:cd06574 154 DNPDMARSLGINVDRTRILGLVISNALAALGGALYAQYQGFADvNMGIGTGVIGLAAVIIGGaivgrrtiKASILGVIIG 233
|
250 260 270
....*....|....*....|....*....|...
gi 490819619 245 ALIIGVIDT-MSGYYIGSDLREAVVFGIFLLIL 276
Cdd:cd06574 234 AILYRIALAlALGSGLIPSDLKLITAGVIVLVL 266
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
682-882 |
4.22e-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: 75.39 E-value: 4.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 682 NVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLapdEGTVNLCGA---DGQfhaPKNPADFA-ALGLGRTFQIVQPFaaM 757
Cdd:cd03234 25 DVSLHVESGQVMAILGSSGSGKTTLLDAISGRV---EGGGTTSGQilfNGQ---PRKPDQFQkCVAYVRQDDILLPG--L 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 758 TVEENIMVGAFYR-HHHEKDAREAARETAWRM---GLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGInq 833
Cdd:cd03234 97 TVRETLTYTAILRlPRKSSDAIRKKRVEDVLLrdlALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGL-- 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490819619 834 tDVRRAIDLMLSIRDSGVS----IIAIEHVMQAVMSLSDRVIVLASGEVIAQG 882
Cdd:cd03234 175 -DSFTALNLVSTLSQLARRnrivILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
664-892 |
6.40e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 78.59 E-value: 6.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 664 ILRVQNLNKHF---GGL--------HVTRNVSFTLREGEVLGLIGPNGAGKTT----LFNMIsgflaPDEGTVNLCGADG 728
Cdd:PRK15134 275 LLDVEQLQVAFpirKGIlkrtvdhnVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 729 QFHAPKnpadfAALGLGRTFQIV--QPFAA----MTVEENIMVGafYRHHH------EKDAR--EAAREtawrMGLGPLL 794
Cdd:PRK15134 350 HNLNRR-----QLLPVRHRIQVVfqDPNSSlnprLNVLQIIEEG--LRVHQptlsaaQREQQviAVMEE----VGLDPET 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 795 ----GAEARGltiGGLKRLEVARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRDS-GVSIIAIEHVMQAVMSLSDR 869
Cdd:PRK15134 419 rhryPAEFSG---GQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQ 495
|
250 260
....*....|....*....|...
gi 490819619 870 VIVLASGEVIAQGRPQDVVRDPQ 892
Cdd:PRK15134 496 VIVLRQGEVVEQGDCERVFAAPQ 518
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
654-877 |
8.08e-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: 8.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 654 SPDRAGIGQDILRVQNLNKHFGG--LHVTRNvsfTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgadgqfh 731
Cdd:COG1245 331 APRREKEEETLVEYPDLTKSYGGfsLEVEGG---EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDE-------- 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 732 apknpadfaALGLGRTFQIVQPFAAMTVEENImvgafyrhhheKDAREAARETAW-------RMGLGPLLGAEARGLTIG 804
Cdd:COG1245 400 ---------DLKISYKPQYISPDYDGTVEEFL-----------RSANTDDFGSSYykteiikPLGLEKLLDKNVKDLSGG 459
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490819619 805 GLKRLEVARVMAMEPRILLLDEVMAGInqtDV--R----RAIDLMlsIRDSGVSIIAIEHVMQAVMSLSDRVIVLaSGE 877
Cdd:COG1245 460 ELQRVAIAACLSRDADLYLLDEPSAHL---DVeqRlavaKAIRRF--AENRGKTAMVVDHDIYLIDYISDRLMVF-EGE 532
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
650-723 |
9.15e-15 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 78.24 E-value: 9.15e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490819619 650 IKAPSPDRagIGQDILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNL 723
Cdd:PRK11819 312 IFIPPGPR--LGDKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI 383
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
643-889 |
1.35e-14 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 77.87 E-value: 1.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 643 AAVPARAIKAPSPDRAGIgqdiLRVQNLNKHFGG--LHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGT 720
Cdd:COG4618 313 AAVPAEPERMPLPRPKGR----LSVENLTVVPPGskRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGS 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 721 VNLCGAD-GQFhapkNPADfaalgLGRTF----QIVQPFAAmTVEENImvgafyrhhhekdAR----------EAAR--- 782
Cdd:COG4618 389 VRLDGADlSQW----DREE-----LGRHIgylpQDVELFDG-TIAENI-------------ARfgdadpekvvAAAKlag 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 783 --ETAWRM--GLGPLLGAEARGLTiGGLK-RLEVARVMAMEPRILLLDEVMAGINQT---DVRRAIDLMlsiRDSGVSII 854
Cdd:COG4618 446 vhEMILRLpdGYDTRIGEGGARLS-GGQRqRIGLARALYGDPRLVVLDEPNSNLDDEgeaALAAAIRAL---KARGATVV 521
|
250 260 270
....*....|....*....|....*....|....*
gi 490819619 855 AIEHVMqAVMSLSDRVIVLASGEVIAQGRPQDVVR 889
Cdd:COG4618 522 VITHRP-SLLAAVDKLLVLRDGRVQAFGPRDEVLA 555
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
665-858 |
1.48e-14 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 73.16 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 665 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKNPADFAALGL 744
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 745 GRTFQivqpfAAMTVEENImvgAFYRHHHeKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLL 824
Cdd:TIGR01189 81 LPGLK-----PELSALENL---HFWAAIH-GGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWIL 151
|
170 180 190
....*....|....*....|....*....|....
gi 490819619 825 DEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEH 858
Cdd:TIGR01189 152 DEPTTALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
468-858 |
1.51e-14 |
|
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: 77.40 E-value: 1.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 468 WPSLLIVFGMLLVTLAIT-----WAVR---------RSRLGFYLVATRERESAARAAG--------VRTVRVRLIAVAIS 525
Cdd:TIGR02868 153 VPAALILAAGLLLAGFVAplvslRAARaaeqalarlRGELAAQLTDALDGAAELVASGalpaalaqVEEADRELTRAERR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 526 SALCAMLGtfhamyltfiepAAMFSLAFSIQIAMFALIGGLGTVAGPLLGAVLLVpitewaraslgasalglhgfvygLV 605
Cdd:TIGR02868 233 AAAATALG------------AALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAV-----------------------LV 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 606 LILVVLFMPNGIMGAINRFVRKPQDSEETATARTEpiAAVPARAIKAPSPDRAGIGQDILRVQNLNKHF-GGLHVTRNVS 684
Cdd:TIGR02868 278 LLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVLD--AAGPVAEGSAPAAGAVGLGKPTLELRDLSAGYpGAPPVLDGVS 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 685 FTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGAdgqfHAPKNPADFAALGLGRTFQIVQPFAAmTVEENIM 764
Cdd:TIGR02868 356 LDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGV----PVSSLDQDEVRRRVSVCAQDAHLFDT-TVRENLR 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 765 VGAfyrhhheKDAREAARETAWRM------------GLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGIN 832
Cdd:TIGR02868 431 LAR-------PDATDEELWAALERvgladwlralpdGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLD 503
|
410 420
....*....|....*....|....*.
gi 490819619 833 QTDVRRAIDLMLSIrDSGVSIIAIEH 858
Cdd:TIGR02868 504 AETADELLEDLLAA-LSGRTVVLITH 528
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
679-895 |
1.68e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 74.66 E-value: 1.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 679 VTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGadgqfhapkNPADFAALGLGRTFQIV------- 751
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQG---------KPLDYSKRGLLALRQQVatvfqdp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 752 -QPFAAMTVEENImvgAFYRHHHEKDAREAARETAWRMGLgpllgAEARG--------LTIGGLKRLEVARVMAMEPRIL 822
Cdd:PRK13638 87 eQQIFYTDIDSDI---AFSLRNLGVPEAEITRRVDEALTL-----VDAQHfrhqpiqcLSHGQKKRVAIAGALVLQARYL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490819619 823 LLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDPQVVE 895
Cdd:PRK13638 159 LLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTEAME 231
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
654-877 |
1.82e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 77.54 E-value: 1.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 654 SPDRAGIGQDILRVQNLNKHFGG--LHVTrnvSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNlcgadgqfh 731
Cdd:PRK13409 330 PPRDESERETLVEYPDLTKKLGDfsLEVE---GGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD--------- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 732 apknpadfAALGLGRTFQIVQPFAAMTVEENIM-VGAFYRHHHEKDareaarETAWRMGLGPLLGAEARGLTIGGLKRLE 810
Cdd:PRK13409 398 --------PELKISYKPQYIKPDYDGTVEDLLRsITDDLGSSYYKS------EIIKPLQLERLLDKNVKDLSGGELQRVA 463
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 811 VARVMAMEPRILLLDEVMAGIN---QTDVRRAIDLMlsIRDSGVSIIAIEHVMQAVMSLSDRVIVLaSGE 877
Cdd:PRK13409 464 IAACLSRDADLYLLDEPSAHLDveqRLAVAKAIRRI--AEEREATALVVDHDIYMIDYISDRLMVF-EGE 530
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
663-894 |
1.90e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 73.99 E-value: 1.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 663 DILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNlcgadgqfHAPKnpadfaaL 742
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK--------RNGK-------L 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 743 GLGRTFQIVQPFAAMTveenIMVGAFYRHH---HEKDAREAARetawRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEP 819
Cdd:PRK09544 68 RIGYVPQKLYLDTTLP----LTVNRFLRLRpgtKKEDILPALK----RVQAGHLIDAPMQKLSGGETQRVLLARALLNRP 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490819619 820 RILLLDEVMAGINQTDVRRAIDLMLSIRDS-GVSIIAIEHVMQAVMSLSDRVIVLaSGEVIAQGRPQDVVRDPQVV 894
Cdd:PRK09544 140 QLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGTPEVVSLHPEFI 214
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
679-884 |
2.15e-14 |
|
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: 72.83 E-value: 2.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 679 VTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQfhapknpaDFAALGLG---RTFQIV--QP 753
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEI---DGI--------DISTIPLEdlrSSLTIIpqDP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 754 FAAM-TVEENIMVgafYRHHHEKDAREAARETawrmGLGPLLGAEARGLtigglkrLEVARVMAMEPRILLLDEVMAGIN 832
Cdd:cd03369 92 TLFSgTIRSNLDP---FDEYSDEEIYGALRVS----EGGLNLSQGQRQL-------LCLARALLKRPRVLVLDEATASID 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490819619 833 -QTDVRraidLMLSIRD--SGVSIIAIEHVMQAVMSLsDRVIVLASGEVIAQGRP 884
Cdd:cd03369 158 yATDAL----IQKTIREefTNSTILTIAHRLRTIIDY-DKILVMDAGEVKEYDHP 207
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
662-891 |
2.21e-14 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 75.53 E-value: 2.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 662 QDILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKNpADFAA 741
Cdd:PRK11432 4 KNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ-RDICM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 742 LglgrtFQIVQPFAAMTVEENIMVGAFYRHHHEKDAREAARETawrMGLGPLLGAEAR---GLTIGGLKRLEVARVMAME 818
Cdd:PRK11432 83 V-----FQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEA---LELVDLAGFEDRyvdQISGGQQQRVALARALILK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 819 PRILLLDEVMAGINqTDVRRaidlmlSIRDS--------GVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRD 890
Cdd:PRK11432 155 PKVLLFDEPLSNLD-ANLRR------SMREKirelqqqfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
|
.
gi 490819619 891 P 891
Cdd:PRK11432 228 P 228
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
681-891 |
2.69e-14 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 75.84 E-value: 2.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 681 RNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADgqfHAPKNPADFAALGLGRTFQIVQPFAA---M 757
Cdd:PRK10070 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVD---IAKISDAELREVRRKKIAMVFQSFALmphM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 758 TVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGINQTDVR 837
Cdd:PRK10070 122 TVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490819619 838 RAIDLMLSIR-DSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDP 891
Cdd:PRK10070 202 EMQDELVKLQaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNP 256
|
|
| TM_PBP1_transp_AraH_like |
cd06579 |
Transmembrane subunit (TM) of Escherichia coli AraH and related proteins. E. coli AraH is the ... |
382-612 |
5.56e-14 |
|
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: 72.83 E-value: 5.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 382 TGVILFNMGISPWFSMFIGAFIAALVGMVISYPCFRLKGPFYsLASIAFLEVFRVLALhfgWLTGGATGLMIQLKLGWVW 461
Cdd:cd06579 35 AALLLVNAGLPIPLAILAALAVGALIGLLNGLLVAYLRIPPF-IVTLGTMFILRGLAL---LITGGRPISGLPPLFSFFL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 462 MVFRERWPSLLIVFgMLLVTLAITWAVRRSRLGFYLVATRERESAARAAGVRTVRVRLIAVAISSALCAMLGTFHAMYLT 541
Cdd:cd06579 111 GGGLILGIPVPVLI-ALAVALVAWFLLRRTRFGRYLYAVGGNPEAARLSGINVRRVKILAYVLSGLLAGLAGILLAARLG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 542 FIEPAAMFSLAFSIQIAMF----ALIGGLGTVAGPLLGAVLLvpitewaraSLGASALGLHG-------FVYGLVLILVV 610
Cdd:cd06579 190 SAQPTAGNGYELDAIAAVVlggtSLTGGRGSVLGTLLGALLL---------GVLNNGLNLLGvssfwqqIVKGAILLLAV 260
|
..
gi 490819619 611 LF 612
Cdd:cd06579 261 AL 262
|
|
| AraH |
COG1172 |
Ribose/xylose/arabinose/galactoside ABC-type transport system, permease component ... |
382-612 |
6.07e-14 |
|
Ribose/xylose/arabinose/galactoside ABC-type transport system, permease component [Carbohydrate transport and metabolism];
Pssm-ID: 440785 Cd Length: 322 Bit Score: 73.99 E-value: 6.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 382 TGVILFNMGISPWFSMFIGAFIAALVGMVISYPCFRLKGP-FysLASIAFLEVFRVLALhfgWLTGGATglmIQLKLGWV 460
Cdd:COG1172 86 AALLLVALGLPILLAILLALLVGALLGLLNGLLVAKLRIPpF--IVTLGTMFIARGLAL---LLTGGRP---ISGLPDAF 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 461 WMVFRERWPSL-LIVFGMLLVTLAITWAVRRSRLGFYLVATRERESAARAAGVRTVRVRLIAVAISSALCAMLGTFHAMY 539
Cdd:COG1172 158 RALGQGSLLGIpVPVLIALVVALVAWFLLRRTRFGRYIYAVGGNEEAARLSGINVRRVKILAYVLSGLLAGLAGILLAAR 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 540 LTFIEPAAMFSLAFSIQIAMF----ALIGGLGTVAGPLLGAVLLvpitewaraSLGASALGLHG-------FVYGLVLIL 608
Cdd:COG1172 238 LGSAQPNAGSGYELDAIAAVViggtSLTGGRGSVLGTLLGALIL---------GVLNNGLNLLGvssywqqIVKGAIILL 308
|
....
gi 490819619 609 VVLF 612
Cdd:COG1172 309 AVLL 312
|
|
| TM_PBP1_branched-chain-AA_like |
cd06574 |
Transmembrane subunit (TM) of Periplasmic Binding Protein (PBP)-dependent ATP-Binding Cassette ... |
359-580 |
8.01e-14 |
|
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: 72.70 E-value: 8.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 359 NIVGGFAGQMSLGHAVFYGIGGYTGVILFNMGISPWFSMFIGAFIAALVGMVISYPCFRLKGPfYSLASIAFLEVFRVLA 438
Cdd:cd06574 12 YIVFRILGFPDLTVDGSFPLGAAVAAILIVAGYNPWLALIAAILAGAAAGLVTGFLHTRLKIN-GLLAGILIMIGLYSIN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 439 LHFGWLTGGATGLMIQLKLGWVWMVFRERWPSLLIVFGMLLVTLAITWAVRRSRLGFYLVATRERESAARAAGVRTVRVR 518
Cdd:cd06574 91 LRIMGGPNIPLGTRDTLLGLLLLFGISGTLSIPVVLLLIVLLVLFLVIWFLRTKLGLAMRATGDNPDMARSLGINVDRTR 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490819619 519 LIAVAISSALCAMLGTFHAMYLTFIEP-----AAMFSLAfSIQI--AMFALIGGLGTVAGPLLGAVLLV 580
Cdd:cd06574 171 ILGLVISNALAALGGALYAQYQGFADVnmgigTGVIGLA-AVIIggAIVGRRTIKASILGVIIGAILYR 238
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
650-723 |
1.06e-13 |
|
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: 1.06e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490819619 650 IKAPSPDRagIGQDILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNL 723
Cdd:TIGR03719 310 IYIPPGPR--LGDKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI 381
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
681-897 |
1.08e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 72.50 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 681 RNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgADGQFHAPKNPADFAAL--GLGRTFQI--VQPFAA 756
Cdd:PRK13646 24 HDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTV--DDITITHKTKDKYIRPVrkRIGMVFQFpeSQLFED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 757 mTVEENIMVGAfyrhHHEKDAREAARETAWR--MGLG---PLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGI 831
Cdd:PRK13646 102 -TVEREIIFGP----KNFKMNLDEVKNYAHRllMDLGfsrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490819619 832 NQTDVRRAIDLMLSIR-DSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDPQVVEAY 897
Cdd:PRK13646 177 DPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKKKLADW 243
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
679-878 |
1.20e-13 |
|
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: 71.35 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 679 VTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGqfhapKNPADFAALGLGRTFQIV--QP-FA 755
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLL---DG-----KPISQYEHKYLHSKVSLVgqEPvLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 756 AMTVEENIMVGAFYRHHHE-KDAREAARETAWRMGL--GPLLGAEARG--LTIGGLKRLEVARVMAMEPRILLLDEVMAG 830
Cdd:cd03248 101 ARSLQDNIAYGLQSCSFECvKEAAQKAHAHSFISELasGYDTEVGEKGsqLSGGQKQRVAIARALIRNPQVLILDEATSA 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490819619 831 INqTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSlSDRVIVLASGEV 878
Cdd:cd03248 181 LD-AESEQQVQQALYDWPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
664-892 |
1.30e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 72.82 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 664 ILRVQNLNKHFG-------------GLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGAD--- 727
Cdd:PRK15079 8 LLEVADLKVHFDikdgkqwfwqppkTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDllg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 728 ---GQFHAPKNPadfaalgLGRTFQivQPFAA----MTVEENIM--VGAFYRHHHEKDAREAARETAWRMGLGP-LLGAE 797
Cdd:PRK15079 88 mkdDEWRAVRSD-------IQMIFQ--DPLASlnprMTIGEIIAepLRTYHPKLSRQEVKDRVKAMMLKVGLLPnLINRY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 798 ARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSI-RDSGVSIIAIEHVMQAVMSLSDRVIVLASG 876
Cdd:PRK15079 159 PHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVMYLG 238
|
250
....*....|....*.
gi 490819619 877 EVIAQGRPQDVVRDPQ 892
Cdd:PRK15079 239 HAVELGTYDEVYHNPL 254
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
669-892 |
1.54e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 73.14 E-value: 1.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 669 NLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQFHAPKNPADfaaLGLGRTF 748
Cdd:PRK11000 8 NVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFI---GEKRMNDVPPAE---RGVGMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 749 QIVQPFAAMTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVM 828
Cdd:PRK11000 82 QSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490819619 829 AGINQT-DVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDPQ 892
Cdd:PRK11000 162 SNLDAAlRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPA 226
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
678-888 |
1.64e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 74.31 E-value: 1.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 678 HVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPD---EGTVNLCGAdgqfhaPKNPADFAAL-GLGRTFQIVQP 753
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGM------PIDAKEMRAIsAYVQQDDLFIP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 754 faAMTVEENIMVGAFYR---HHHEKDAREAARETAWRMGLGP----LLGAEAR--GLTIGGLKRLEVARVMAMEPRILLL 824
Cdd:TIGR00955 113 --TLTVREHLMFQAHLRmprRVTKKEKRERVDEVLQALGLRKcantRIGVPGRvkGLSGGERKRLAFASELLTDPPLLFC 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490819619 825 DEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQA-VMSLSDRVIVLASGEVIAQGRPQDVV 888
Cdd:TIGR00955 191 DEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSeLFELFDKIILMAEGRVAYLGSPDQAV 255
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
669-904 |
1.75e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 74.00 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 669 NLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKNpadfaAL--GLGR 746
Cdd:PRK10982 3 NISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKE-----ALenGISM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 747 TFQIVQPFAAMTVEENIMVGAFYRHHHEKDAREAARET-AWRMGLGPLLGAEARG--LTIGGLKRLEVARVMAMEPRILL 823
Cdd:PRK10982 78 VHQELNLVLQRSVMDNMWLGRYPTKGMFVDQDKMYRDTkAIFDELDIDIDPRAKVatLSVSQMQMIEIAKAFSYNAKIVI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 824 LDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDpQVVEAYLGKEFA 903
Cdd:PRK10982 158 MDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMD-KIIAMMVGRSLT 236
|
.
gi 490819619 904 H 904
Cdd:PRK10982 237 Q 237
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
671-884 |
3.22e-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: 70.34 E-value: 3.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 671 NKHFG---GLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQfhaPKNPADFAAL--GLG 745
Cdd:cd03253 5 NVTFAydpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILI---DGQ---DIREVTLDSLrrAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 746 RTFQIVQPFAAmTVEENIMVG---AfyrhhHEKDAREAARE-------TAWRMGLGPLLGAeaRGLTI-GGLK-RLEVAR 813
Cdd:cd03253 79 VVPQDTVLFND-TIGYNIRYGrpdA-----TDEEVIEAAKAaqihdkiMRFPDGYDTIVGE--RGLKLsGGEKqRVAIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490819619 814 VMAMEPRILLLDEVMAGINqTDVRRAIdlMLSIRD--SGVSIIAIEHVMQAVMSlSDRVIVLASGEVIAQGRP 884
Cdd:cd03253 151 AILKNPPILLLDEATSALD-THTEREI--QAALRDvsKGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTH 219
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
682-894 |
3.55e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 71.19 E-value: 3.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 682 NVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgadGQFHAPKNPADFAA-------LGLGRTFQIVQPF 754
Cdd:PRK13645 29 NTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIV----GDYAIPANLKKIKEvkrlrkeIGLVFQFPEYQLF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 755 AAmTVEENIMVGAFyrhHHEKDAREAARETAWRMGLGPLLGAEAR----GLTIGGLKRLEVARVMAMEPRILLLDEVMAG 830
Cdd:PRK13645 105 QE-TIEKDIAFGPV---NLGENKQEAYKKVPELLKLVQLPEDYVKrspfELSGGQKRRVALAGIIAMDGNTLVLDEPTGG 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490819619 831 INQTDVRRAIDLMLSI-RDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDPQVV 894
Cdd:PRK13645 181 LDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQELL 245
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
661-878 |
3.97e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 72.73 E-value: 3.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 661 GQDILRVQNLNkhfgGLHVtRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQFHAPKNPADFA 740
Cdd:PRK10762 254 GEVRLKVDNLS----GPGV-NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTL---DGHEVVTRSPQDGL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 741 ALG--------------LGrtfqivqpfaaMTVEENIMVGAF---------YRHHHEKDA----------REAARETAwr 787
Cdd:PRK10762 326 ANGivyisedrkrdglvLG-----------MSVKENMSLTALryfsraggsLKHADEQQAvsdfirlfniKTPSMEQA-- 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 788 mgLGPLLGaeargltiGGLKRLEVARVMAMEPRILLLDEVMAGInqtDV--RRAI-DLMLSIRDSGVSIIAIEHVMQAVM 864
Cdd:PRK10762 393 --IGLLSG--------GNQQKVAIARGLMTRPKVLILDEPTRGV---DVgaKKEIyQLINQFKAEGLSIILVSSEMPEVL 459
|
250
....*....|....
gi 490819619 865 SLSDRVIVLASGEV 878
Cdd:PRK10762 460 GMSDRILVMHEGRI 473
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
664-879 |
5.69e-13 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 70.10 E-value: 5.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 664 ILRVQNLNKHFGG---------LHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGAD-GQFhap 733
Cdd:PRK10419 3 LLNVSGLSHHYAHgglsgkhqhQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPlAKL--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 734 kNPADFAAlgLGRTFQIV--QPFAAMTVEENI--MVGAFYRH--HHEKDAREA-ARETAWRMGLGPLLGAEARGLTIGG- 805
Cdd:PRK10419 80 -NRAQRKA--FRRDIQMVfqDSISAVNPRKTVreIIREPLRHllSLDKAERLArASEMLRAVDLDDSVLDKRPPQLSGGq 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490819619 806 LKRLEVARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRD-SGVSIIAIEHVMQAVMSLSDRVIVLASGEVI 879
Cdd:PRK10419 157 LQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQqFGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
682-893 |
8.62e-13 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 69.41 E-value: 8.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 682 NVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQfhapknpaDFAALGLGR----------TFQIV 751
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILF---DGE--------NIPAMSRSRlytvrkrmsmLFQSG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 752 QPFAAMTVEENImvgAFYRHHHEKDAREAARETAWR-------MGLGPLLGAEARGltiGGLKRLEVARVMAMEPRILLL 824
Cdd:PRK11831 94 ALFTDMNVFDNV---AYPLREHTQLPAPLLHSTVMMkleavglRGAAKLMPSELSG---GMARRAALARAIALEPDLIMF 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490819619 825 DEVMAGINQTDVRRAIDLMLSIRDS-GVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVR--DPQV 893
Cdd:PRK11831 168 DEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQAnpDPRV 239
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
665-882 |
1.82e-12 |
|
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: 66.57 E-value: 1.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 665 LRVQNLNKHFGG--LHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGadgqfhapKNPADFAAL 742
Cdd:cd03247 1 LSINNVSFSYPEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDG--------VPVSDLEKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 743 gLGRTFQIV--QPFA-AMTVEENimvgafyrhhhekdareaaretawrmglgplLGAEARGltiGGLKRLEVARVMAMEP 819
Cdd:cd03247 73 -LSSLISVLnqRPYLfDTTLRNN-------------------------------LGRRFSG---GERQRLALARILLQDA 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490819619 820 RILLLDEVMAGINQTDVRRAIDLMLSIRDsGVSIIAIEHVMQAvMSLSDRVIVLASGEVIAQG 882
Cdd:cd03247 118 PIVLLDEPTVGLDPITERQLLSLIFEVLK-DKTLIWITHHLTG-IEHMDKILFLENGKIIMQG 178
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
660-878 |
3.80e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 69.55 E-value: 3.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 660 IGQDILRVQNLNkhfgGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKN---- 735
Cdd:PRK11288 253 LGEVRLRLDGLK----GPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDaira 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 736 -----PADFAALGlgrtfqIVqpfAAMTVEENIMVGAfYRHH-------HEKDAREAARETAWRMGL-GPLLGAEARGLT 802
Cdd:PRK11288 329 gimlcPEDRKAEG------II---PVHSVADNINISA-RRHHlragcliNNRWEAENADRFIRSLNIkTPSREQLIMNLS 398
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490819619 803 IGGLKRLEVARVMAMEPRILLLDEVMAGInqtDV--RRAI-DLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEV 878
Cdd:PRK11288 399 GGNQQKAILGRWLSEDMKVILLDEPTRGI---DVgaKHEIyNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
661-883 |
5.65e-12 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 68.22 E-value: 5.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 661 GQDILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAG--KTTLFNMISGflaPDEGtvnlcgadgqfhapKNPAD 738
Cdd:NF000106 10 ARNAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAG--------------RRPWR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 739 FAAL-----GLGRTFQIVQPF-----AAMTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKR 808
Cdd:NF000106 73 F*TWcanrrALRRTIG*HRPVr*grrESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490819619 809 LEVARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGR 883
Cdd:NF000106 153 LDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGK 227
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
681-882 |
6.60e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 66.83 E-value: 6.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 681 RNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKNPADFAAlglgRTFQIVQPFAAMtVE 760
Cdd:PRK15056 24 RDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVP----QSEEVDWSFPVL-VE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 761 ENIMVG-----AFYRHHHEKDaREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGINQTD 835
Cdd:PRK15056 99 DVVMMGryghmGWLRRAKKRD-RQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKT 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490819619 836 VRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRViVLASGEVIAQG 882
Cdd:PRK15056 178 EARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYT-VMVKGTVLASG 223
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
664-868 |
7.39e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 66.73 E-value: 7.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 664 ILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTL---FN----MISGFLApdEGTVNLCGADgqFHAPK-N 735
Cdd:PRK14243 10 VLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTIlrcFNrlndLIPGFRV--EGKVTFHGKN--LYAPDvD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 736 PADFAALgLGRTFQIVQPFAAmTVEENIMVGAF---YRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVA 812
Cdd:PRK14243 86 PVEVRRR-IGMVFQKPNPFPK-SIYDNIAYGARingYKGDMDELVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490819619 813 RVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRDSgVSIIAIEHVMQAVMSLSD 868
Cdd:PRK14243 164 RAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAARVSD 218
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
668-889 |
1.10e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 69.00 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 668 QNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGAdgqfhaPKNPADFAalglgrT 747
Cdd:NF033858 270 RGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQ------PVDAGDIA------T 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 748 FQIV----QPF---AAMTVEENIMVGAfyRHHHEKDAREAAR--ETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAME 818
Cdd:NF033858 338 RRRVgymsQAFslyGELTVRQNLELHA--RLFHLPAAEIAARvaEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHK 415
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490819619 819 PRILLLDEVMAGInqtD-VRR------AIDLMlsiRDSGVSIIAIEHVMQAVMsLSDRVIVLASGEVIAQGRPQDVVR 889
Cdd:NF033858 416 PELLILDEPTSGV---DpVARdmfwrlLIELS---REDGVTIFISTHFMNEAE-RCDRISLMHAGRVLASDTPAALVA 486
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
662-870 |
1.11e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 65.61 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 662 QDILRVQNLNKHF--GGLH--VTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKNPA 737
Cdd:PRK11629 3 KILLQCDNLCKRYqeGSVQtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 738 DFAALGLGRTFQIVQPFAAMTVEENIMVGAFYRHHHEKDAREAARETAWRMGLgpllgaEARG------LTIGGLKRLEV 811
Cdd:PRK11629 83 ELRNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGL------EHRAnhrpseLSGGERQRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 812 ARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSI-RDSGVSIIAIEHVMQAVMSLSDRV 870
Cdd:PRK11629 157 ARALVNNPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKRMSRQL 216
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
631-878 |
1.66e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 67.77 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 631 SEETATART-EPIAAVPARAIKAPSPD-------------RAGIGQDILRVQNLN-KHFgglhvtRNVSFTLREGEVLGL 695
Cdd:PRK15439 221 SGKTADLSTdDIIQAITPAAREKSLSAsqklwlelpgnrrQQAAGAPVLTVEDLTgEGF------RNISLEVRAGEILGL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 696 IGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKN---------PADFAALGLGRTFQIVQPFAAMTVEENimvG 766
Cdd:PRK15439 295 AGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrlarglvylPEDRQSSGLYLDAPLAWNVCALTHNRR---G 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 767 AFYRhhhekDAREAARETAWRMGLG-PLLGAE--ARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGInqtDV--RRAI- 840
Cdd:PRK15439 372 FWIK-----PARENAVLERYRRALNiKFNHAEqaARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGV---DVsaRNDIy 443
|
250 260 270
....*....|....*....|....*....|....*...
gi 490819619 841 DLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEV 878
Cdd:PRK15439 444 QLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
679-885 |
2.50e-11 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 67.44 E-value: 2.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 679 VTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADgqfHAPKNPADFAAL---GLGRTFQIVQPFA 755
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQD---VATLDADALAQLrreHFGFIFQRYHLLS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 756 AMTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGINQTD 835
Cdd:PRK10535 100 HLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHS 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490819619 836 VRRAIDLMLSIRDSGVSIIAIEHVMQaVMSLSDRVIVLASGEVIAQGRPQ 885
Cdd:PRK10535 180 GEEVMAILHQLRDRGHTVIIVTHDPQ-VAAQAERVIEIRDGEIVRNPPAQ 228
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
661-878 |
3.31e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 66.73 E-value: 3.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 661 GQDILRVQNLNKHFGGLhvTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADgqfHAPKNPADFA 740
Cdd:PRK09700 262 HETVFEVRNVTSRDRKK--VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKD---ISPRSPLDAV 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 741 ALGLG------------RTFQIVQpfaAMTVEENIMVGAF------YRHHHEKDAREAARE------TAWRMGLGPLLGA 796
Cdd:PRK09700 337 KKGMAyitesrrdngffPNFSIAQ---NMAISRSLKDGGYkgamglFHEVDEQRTAENQREllalkcHSVNQNITELSGG 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 797 EARGLTIGglkrlevaRVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASG 876
Cdd:PRK09700 414 NQQKVLIS--------KWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEG 485
|
..
gi 490819619 877 EV 878
Cdd:PRK09700 486 RL 487
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
681-826 |
3.96e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 63.28 E-value: 3.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 681 RNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCG-----ADGQFHapknpADFAALG--LGrtfqiVQP 753
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGepirrQRDEYH-----QDLLYLGhqPG-----IKT 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490819619 754 faAMTVEENImvgAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDE 826
Cdd:PRK13538 88 --ELTALENL---RFYQRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDE 155
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
682-891 |
4.09e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 66.79 E-value: 4.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 682 NVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLaPDEG--TVNlcgadGQFHAPKNPADF----AALGlgrtfQIVQPFA 755
Cdd:PRK11174 368 PLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGslKIN-----GIELRELDPESWrkhlSWVG-----QNPQLPH 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 756 AmTVEENIMVGafyRHHHEKDAREAARETAW--------RMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDE- 826
Cdd:PRK11174 437 G-TLRDNVLLG---NPDASDEQLQQALENAWvseflpllPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEp 512
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490819619 827 -----------VMAGINQTdVRRAIDLMLSIRdsgvsiiaIEHVMQAvmslsDRVIVLASGEVIAQGRPQDVVRDP 891
Cdd:PRK11174 513 tasldahseqlVMQALNAA-SRRQTTLMVTHQ--------LEDLAQW-----DQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
682-892 |
5.03e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 64.39 E-value: 5.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 682 NVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTV---NLcgadgqfhaPKNPADFAAL--GLGRTFQivQP--- 753
Cdd:PRK13648 27 DVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynNQ---------AITDDNFEKLrkHIGIVFQ--NPdnq 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 754 FAAMTVE-------ENIMVGafyrhhHEKDAREAArETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDE 826
Cdd:PRK13648 96 FVGSIVKydvafglENHAVP------YDEMHRRVS-EALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDE 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490819619 827 VMAGINQTDVRRAIDLMLSIR-DSGVSIIAIEHVMQAVMSlSDRVIVLASGEVIAQGRPQDVVRDPQ 892
Cdd:PRK13648 169 ATSMLDPDARQNLLDLVRKVKsEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHAE 234
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
662-902 |
5.34e-11 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 64.07 E-value: 5.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 662 QDILRVQNLNKHFGGLHvtrNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGAdgqfhapknpADFAA 741
Cdd:PRK13546 25 KDALIPKHKNKTFFALD---DISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE----------VSVIA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 742 LGLGRTFQivqpfaaMTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRI 821
Cdd:PRK13546 92 ISAGLSGQ-------LTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 822 LLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDpqvVEAYLgKE 901
Cdd:PRK13546 165 LVIDEALSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPK---YEAFL-ND 240
|
.
gi 490819619 902 F 902
Cdd:PRK13546 241 F 241
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
584-885 |
8.59e-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: 8.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 584 EWARASLGASALGLHGFVYGLVLILVVLFMpngimgAINRFVRKPqdSEETATARTEPIAAVPARAIKApspdraGIGQD 663
Cdd:TIGR01257 1871 QWDLIGKNLVAMAVEGVVYFLLTLLIQHHF------FLSRWIAEP--AKEPIFDEDDDVAEERQRIISG------GNKTD 1936
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 664 ILRVQNLNKHFGGLH--VTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADgqfhAPKNPADF-A 740
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKS----ILTNISDVhQ 2012
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 741 ALGLGRTFQIVQPFaaMTVEENIMVGAFYRHhheKDAREAARETAWRM-GLGPLLGAEA-RGLTIGGLKR-LEVARVMAM 817
Cdd:TIGR01257 2013 NMGYCPQFDAIDDL--LTGREHLYLYARLRG---VPAEEIEKVANWSIqSLGLSLYADRlAGTYSGGNKRkLSTAIALIG 2087
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490819619 818 EPRILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQ 885
Cdd:TIGR01257 2088 CPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQ 2155
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
647-895 |
1.12e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 63.19 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 647 ARAIKAPSPDRAGIgqdilrvqNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLF-------NMISGFLApdEG 719
Cdd:PRK14271 12 AADVDAAAPAMAAV--------NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLrtlnrmnDKVSGYRY--SG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 720 TVnLCGADGQFHApKNPADFAALgLGRTFQIVQPFaAMTVEENIMVGAfyRHHH---EKDAREAARETAWRMGL----GP 792
Cdd:PRK14271 82 DV-LLGGRSIFNY-RDVLEFRRR-VGMLFQRPNPF-PMSIMDNVLAGV--RAHKlvpRKEFRGVAQARLTEVGLwdavKD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 793 LLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRDSgVSIIAIEHVMQAVMSLSDRVIV 872
Cdd:PRK14271 156 RLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAAL 234
|
250 260
....*....|....*....|...
gi 490819619 873 LASGEVIAQGRPQDVVRDPQVVE 895
Cdd:PRK14271 235 FFDGRLVEEGPTEQLFSSPKHAE 257
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
686-885 |
1.96e-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: 1.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 686 TLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFhapkNPadfaalglgrtfQIVQPFAAMTVEENIM- 764
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSY----KP------------QYIKADYEGTVRDLLSs 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 765 -VGAFYRHHHEKDareaarETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGIN---QTDVRRAI 840
Cdd:cd03237 85 iTKDFYTHPYFKT------EIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDveqRLMASKVI 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490819619 841 DLMLSIRDSGVSIiaIEHVMQAVMSLSDRVIVLaSGEVIAQGR---PQ 885
Cdd:cd03237 159 RRFAENNEKTAFV--VEHDIIMIDYLADRLIVF-EGEPSVNGVanpPQ 203
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
669-887 |
2.09e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 63.35 E-value: 2.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 669 NLNKHFGGLHVTRNVsfTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCG-----ADGQFHAPKNPAdfaalG 743
Cdd:PRK11144 5 NFKQQLGDLCLTVNL--TLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdAEKGICLPPEKR-----R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 744 LGRTFQIVQPFAAMTVEENIMVGAfyrhhHEKDAREAARETAWrMGLGPLLGAEARGLTiGGLK-RLEVARVMAMEPRIL 822
Cdd:PRK11144 78 IGYVFQDARLFPHYKVRGNLRYGM-----AKSMVAQFDKIVAL-LGIEPLLDRYPGSLS-GGEKqRVAIGRALLTAPELL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 823 LLDEVMAGInqtDVRRAIDLM-----LSiRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDV 887
Cdd:PRK11144 151 LMDEPLASL---DLPRKRELLpylerLA-REINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEV 216
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
679-884 |
3.68e-10 |
|
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: 60.97 E-value: 3.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 679 VTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQfhapknpaDFAALGLG--RTF-----QIV 751
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILI---DGV--------DISKIGLHdlRSRisiipQDP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 752 QPFAAmTVEENImvGAFyrHHHEKDAREAAREtawRMGLGPLLGAEARGL----TIGGL-----KR--LEVARVMAMEPR 820
Cdd:cd03244 88 VLFSG-TIRSNL--DPF--GEYSDEELWQALE---RVGLKEFVESLPGGLdtvvEEGGEnlsvgQRqlLCLARALLRKSK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490819619 821 ILLLDEVMAGI-NQTDvrRAIDLMLSIRDSGVSIIAIEHVMQAVMSlSDRVIVLASGEVIAQGRP 884
Cdd:cd03244 160 ILVLDEATASVdPETD--ALIQKTIREAFKDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFDSP 221
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
664-875 |
6.02e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 60.11 E-value: 6.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 664 ILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAP---------- 733
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPeiyrqqvsyc 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 734 -KNPADFAAlglgrtfqivqpfaamTVEENIMVGAFYRHHHeKDAREAARETAwRMGLgP--LLGAEARGLTIGGLKRLE 810
Cdd:PRK10247 87 aQTPTLFGD----------------TVYDNLIFPWQIRNQQ-PDPAIFLDDLE-RFAL-PdtILTKNIAELSGGEKQRIS 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490819619 811 VARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLS-IRDSGVSIIAIEHVMQAVmSLSDRVIVLAS 875
Cdd:PRK10247 148 LIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRyVREQNIAVLWVTHDKDEI-NHADKVITLQP 212
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
665-721 |
8.86e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 62.22 E-value: 8.86e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 490819619 665 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTV 721
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
681-885 |
2.09e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 61.27 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 681 RNVSFTLREGEV--------------LGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQfhaPKNPADFAALGLGr 746
Cdd:PRK10790 344 DNVSFAYRDDNLvlqninlsvpsrgfVALVGHTGSGKSTLASLLMGYYPLTEGEIRL---DGR---PLSSLSHSVLRQG- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 747 tFQIVQ--PFA-AMTVEENIMVGAFYRHHHEKDAREAAR--ETAWRM--GLGPLLGAEARGLTIGGLKRLEVARVMAMEP 819
Cdd:PRK10790 417 -VAMVQqdPVVlADTFLANVTLGRDISEEQVWQALETVQlaELARSLpdGLYTPLGEQGNNLSVGQKQLLALARVLVQTP 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490819619 820 RILLLDEVMAGINqTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSlSDRVIVLASGEVIAQGRPQ 885
Cdd:PRK10790 496 QILILDEATANID-SGTEQAIQQALAAVREHTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQ 559
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
681-888 |
2.18e-09 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 61.13 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 681 RNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADgqfhapKNPADFAAL--GLGRTFQIVQPFAaMT 758
Cdd:PRK13657 352 EDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTD------IRTVTRASLrrNIAVVFQDAGLFN-RS 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 759 VEENIMVG---AFYRHHHEKDAREAARETAWR--MGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGIN- 832
Cdd:PRK13657 425 IEDNIRVGrpdATDEEMRAAAERAQAHDFIERkpDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDv 504
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490819619 833 --QTDVRRAIDLMLSIRDSGVsiiaIEHVMQAVMSlSDRVIVLASGEVIAQGRPQDVV 888
Cdd:PRK13657 505 etEAKVKAALDELMKGRTTFI----IAHRLSTVRN-ADRILVFDNGRVVESGSFDELV 557
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
665-877 |
8.30e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 57.35 E-value: 8.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 665 LRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGfLAPDEGTVNLCGADGQFHAPKNPADFAALGL 744
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNR-MNELESEVRVEGRVEFFNQNIYERRVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 745 GRTFQIVQP---FAAMTVEENIMVGAFYRHHHEKDAREAARETAWRMG-----LGPLLGAEARGLTIGGLKRLEVARVMA 816
Cdd:PRK14258 87 RRQVSMVHPkpnLFPMSVYDNVAYGVKIVGWRPKLEIDDIVESALKDAdlwdeIKHKIHKSALDLSGGQQQRLCIARALA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490819619 817 MEPRILLLDEVMAGINQTDVRRAIDLMLSIR-DSGVSIIAIEHVMQAVMSLSDRVIVLASGE 877
Cdd:PRK14258 167 VKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLHQVSRLSDFTAFFKGNE 228
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
679-893 |
9.48e-09 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 59.35 E-value: 9.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 679 VTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQfhapknP-ADFAALGLGRTFQIVQP---F 754
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLL---DGV------PlVQYDHHYLHRQVALVGQepvL 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 755 AAMTVEENIMVGafYRHHHEKDAREAARE-------TAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEV 827
Cdd:TIGR00958 567 FSGSVRENIAYG--LTDTPDEEIMAAAKAanahdfiMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEA 644
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490819619 828 MAGInqtDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSlSDRVIVLASGEVIAQGRPQDVVRDPQV 893
Cdd:TIGR00958 645 TSAL---DAECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQGC 706
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
664-892 |
1.08e-08 |
|
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: 58.54 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 664 ILRVQNLNKHFGG----LHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPD----EGTVNLCGADGqFHAPkn 735
Cdd:COG4172 6 LLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPaahpSGSILFDGQDL-LGLS-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 736 PADFAAL---GLGRTFQivQPFAA----MTVEENIM-VGAFYRHHHEKDAREAARETAWRMGLgPllGAEARgLTI---- 803
Cdd:COG4172 83 ERELRRIrgnRIAMIFQ--EPMTSlnplHTIGKQIAeVLRLHRGLSGAAARARALELLERVGI-P--DPERR-LDAyphq 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 804 --GGLKRlevaRVM-AM----EPRILLLDE--------VMAGInqtdvrraIDLMLSI-RDSGVSIIAIEHVMQAVMSLS 867
Cdd:COG4172 157 lsGGQRQ----RVMiAMalanEPDLLIADEpttaldvtVQAQI--------LDLLKDLqRELGMALLLITHDLGVVRRFA 224
|
250 260
....*....|....*....|....*
gi 490819619 868 DRVIVLASGEVIAQGRPQDVVRDPQ 892
Cdd:COG4172 225 DRVAVMRQGEIVEQGPTAELFAAPQ 249
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
664-878 |
1.65e-08 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 56.04 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 664 ILRVQNLNK-HFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGAD-GQFHAPKNPadFAA 741
Cdd:PRK10908 1 MIRFEHVSKaYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDiTRLKNREVP--FLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 742 LGLGRTFQIVQPFAAMTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRI 821
Cdd:PRK10908 79 RQIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490819619 822 LLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSDRVIVLASGEV 878
Cdd:PRK10908 159 LLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
681-882 |
2.24e-08 |
|
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: 55.35 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 681 RNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPD---EGTVNLCGADGQFHAPKNPADfaalglgrtfqivqpfAAM 757
Cdd:cd03233 24 KDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGE----------------IIY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 758 TVEENImvgafyrHHHEKDARE----AARetawrmglgpLLGAE-ARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGIn 832
Cdd:cd03233 88 VSEEDV-------HFPTLTVREtldfALR----------CKGNEfVRGISGGERKRVSIAEALVSRASVLCWDNSTRGL- 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490819619 833 qtDVRRAIDLMLSIRD----SGVSIIAIehVMQA---VMSLSDRVIVLASGEVIAQG 882
Cdd:cd03233 150 --DSSTALEILKCIRTmadvLKTTTFVS--LYQAsdeIYDLFDKVLVLYEGRQIYYG 202
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
662-892 |
2.56e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 57.56 E-value: 2.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 662 QDILRVQNLNKHF----GGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNlCG------------ 725
Cdd:PRK10261 10 RDVLAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQ-CDkmllrrrsrqvi 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 726 -----ADGQFHAPKNpADFAALglgrtFQivQPFAAM----TVEENImvgAFYRHHHEKDAREAARETAWRM-------G 789
Cdd:PRK10261 89 elseqSAAQMRHVRG-ADMAMI-----FQ--EPMTSLnpvfTVGEQI---AESIRLHQGASREEAMVEAKRMldqvripE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 790 LGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSI-RDSGVSIIAIEHVMQAVMSLSD 868
Cdd:PRK10261 158 AQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLqKEMSMGVIFITHDMGVVAEIAD 237
|
250 260
....*....|....*....|....
gi 490819619 869 RVIVLASGEVIAQGRPQDVVRDPQ 892
Cdd:PRK10261 238 RVLVMYQGEAVETGSVEQIFHAPQ 261
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
686-877 |
2.71e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.51 E-value: 2.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 686 TLREGEVLGLIGPNGAGKTTLFNMISGFLAPdegtvNLCGADgqfhapkNPAD-------FAALGLGRTFQ--------- 749
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIP-----NLGDYE-------EEPSwdevlkrFRGTELQNYFKklyngeikv 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 750 IVQP----FAAM----TVEENIMvgafyrhhhEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRI 821
Cdd:PRK13409 163 VHKPqyvdLIPKvfkgKVRELLK---------KVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADF 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490819619 822 LLLDEVMagiNQTDVRRAIDLMLSIRD--SGVSIIAIEHVMqAVMS-LSDrVIVLASGE 877
Cdd:PRK13409 234 YFFDEPT---SYLDIRQRLNVARLIRElaEGKYVLVVEHDL-AVLDyLAD-NVHIAYGE 287
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
788-882 |
3.75e-08 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 53.87 E-value: 3.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 788 MGLGPL-LGAEARGLTIGGLKRLEVARVMAMEPR--ILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHvMQAVM 864
Cdd:cd03238 74 VGLGYLtLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEH-NLDVL 152
|
90 100
....*....|....*....|....
gi 490819619 865 SLSDRVIVLA------SGEVIAQG 882
Cdd:cd03238 153 SSADWIIDFGpgsgksGGKVVFSG 176
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
664-892 |
5.01e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 55.90 E-value: 5.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 664 ILRVQNLNKHFGG----LHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGflapdegtvnLCGADGQFHAPK---NP 736
Cdd:PRK11022 3 LLNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMG----------LIDYPGRVMAEKlefNG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 737 ADFAALGLGRTFQIVQPFAAM-------------TVEENIMVGAfyrHHHEKDAREAARETAwrMGLGPLLG---AEAR- 799
Cdd:PRK11022 73 QDLQRISEKERRNLVGAEVAMifqdpmtslnpcyTVGFQIMEAI---KVHQGGNKKTRRQRA--IDLLNQVGipdPASRl 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 800 -----GLTIGGLKRLEVARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSI-RDSGVSIIAIEHVMQAVMSLSDRVIVL 873
Cdd:PRK11022 148 dvyphQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqQKENMALVLITHDLALVAEAAHKIIVM 227
|
250
....*....|....*....
gi 490819619 874 ASGEVIAQGRPQDVVRDPQ 892
Cdd:PRK11022 228 YAGQVVETGKAHDIFRAPR 246
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
686-877 |
5.22e-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: 5.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 686 TLREGEVLGLIGPNGAGKTTLFNMISGFLAPdegtvNLcgadGQFHapkNPAD-------FAALGLGRTFQIVqpfaamt 758
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGELKP-----NL----GDYD---EEPSwdevlkrFRGTELQDYFKKL------- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 759 VEENI-------MVGAFYRHHH-------EK-DAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILL 823
Cdd:COG1245 156 ANGEIkvahkpqYVDLIPKVFKgtvrellEKvDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYF 235
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490819619 824 LDEVmaginqT---DVRRAIDLMLSIRD---SGVSIIAIEHVMqAVMS-LSDrVIVLASGE 877
Cdd:COG1245 236 FDEP------SsylDIYQRLNVARLIRElaeEGKYVLVVEHDL-AILDyLAD-YVHILYGE 288
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
679-888 |
6.38e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 56.91 E-value: 6.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 679 VTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADgqfhapknPADFAALGLGRTFQIVQPFAAM- 757
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCD--------VAKFGLTDLRRVLSIIPQSPVLf 1322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 758 --TVEENImvgAFYRHHHEKDAREAARETAWR-------MGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVM 828
Cdd:PLN03232 1323 sgTVRFNI---DPFSEHNDADLWEALERAHIKdvidrnpFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEAT 1399
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490819619 829 AGInqtDVRRAIDLMLSIRDS--GVSIIAIEHVMQAVMSlSDRVIVLASGEVIAQGRPQDVV 888
Cdd:PLN03232 1400 ASV---DVRTDSLIQRTIREEfkSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELL 1457
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
682-876 |
8.04e-08 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 53.40 E-value: 8.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 682 NVSFTLREGEVLGLIGPNGAGKTTLFNMISG--FLAPDEGTVNLCGadgqfhapknpadfaaLGLGRTFQIVQPFaamtV 759
Cdd:cd03232 25 NISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILING----------------RPLDKNFQRSTGY----V 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 760 EENimvgafYRHHHEKDAREAARETAWrmglgpllgaeARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGInqtDVRRA 839
Cdd:cd03232 85 EQQ------DVHSPNLTVREALRFSAL-----------LRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGL---DSQAA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 490819619 840 IDLMLSIR---DSGVSII-AIEHVMQAVMSLSDRVIVLASG 876
Cdd:cd03232 145 YNIVRFLKklaDSGQAILcTIHQPSASIFEKFDRLLLLKRG 185
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
666-879 |
9.46e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 53.81 E-value: 9.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 666 RVQNLNKHFG------GLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFL--APDEGTVNLcgadgqfhaPKNPA 737
Cdd:COG2401 26 RVAIVLEAFGvelrvvERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDV---------PDNQF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 738 DfaalglgrtfqivqpfaamtvEENIMVGAFYRHHHEKDAREAARetawRMGLG--PLLGAEARGLTIGGLKRLEVARVM 815
Cdd:COG2401 97 G---------------------REASLIDAIGRKGDFKDAVELLN----AVGLSdaVLWLRRFKELSTGQKFRFRLALLL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490819619 816 AMEPRILLLDEVMAGIN-QTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLS-DRVIVLASGEVI 879
Cdd:COG2401 152 AERPKLLVIDEFCSHLDrQTAKRVARNLQKLARRAGITLVVATHHYDVIDDLQpDLLIFVGYGGVP 217
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
665-888 |
1.02e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 55.60 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 665 LRVQNLnkHFG----GLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGadgqfhapKNPADFA 740
Cdd:PRK11160 339 LTLNNV--SFTypdqPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNG--------QPIADYS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 741 ALGLGRTF----QIVQPFAAmTVEENIMVGAfyrhHHEKDarEAARETAWRMGLGPLL----------GAEARGLTIGGL 806
Cdd:PRK11160 409 EAALRQAIsvvsQRVHLFSA-TLRDNLLLAA----PNASD--EALIEVLQQVGLEKLLeddkglnawlGEGGRQLSGGEQ 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 807 KRLEVARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRdSGVSIIAIEHVMQAVMSLsDRVIVLASGEVIAQGRPQD 886
Cdd:PRK11160 482 RRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHA-QNKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQE 559
|
..
gi 490819619 887 VV 888
Cdd:PRK11160 560 LL 561
|
|
| TM_PBP1_transp_TpRbsC_like |
cd06580 |
Transmembrane subunit (TM) of Treponema pallidum (Tp) RbsC-1, RbsC-2 and related proteins. ... |
143-278 |
1.13e-07 |
|
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: 53.60 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 143 VFIFLGAIVLVVALQLFLKNSQTGRAIRAVAQHRSAAELMGVNVSRIYILCFGLGAACVGLAAVL--IAPLYPTSSNIGT 220
Cdd:cd06580 95 SYLLLLALLLVILVWLLLYRTRFGLRLRAVGENPRAARYAGINVKRVRLLAMLISGALAGLAGAYlvLGVQGRFTEGMSA 174
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 490819619 221 YFVLTAFVVVVLGGlGSIPGAFVGALIIGVIDTMSGYYIGSDLREAVVFGIFLLILIL 278
Cdd:cd06580 175 GYGFIAIAVALLGR-WNPLGILLAALLFGALEAGGIALQRSGGVPSELVQVLPGIIVL 231
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
664-858 |
1.49e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 52.64 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 664 ILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVnlcgadgQFHAPKNPADFAALG 743
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEI-------LFERQSIKKDLCTYQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 744 LGRTF----QIVQPFaaMTVEENimvgAFYRHHHEKDAREAArETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEP 819
Cdd:PRK13540 74 KQLCFvghrSGINPY--LTLREN----CLYDIHFSPGAVGIT-ELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKA 146
|
170 180 190
....*....|....*....|....*....|....*....
gi 490819619 820 RILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEH 858
Cdd:PRK13540 147 KLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSH 185
|
|
| BCA_ABC_TP_C |
pfam12399 |
Branched-chain amino acid ATP-binding cassette transporter; This domain family is found in ... |
877-901 |
1.65e-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: 48.02 E-value: 1.65e-07
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
661-725 |
2.15e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.57 E-value: 2.15e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490819619 661 GQDILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNlCG 725
Cdd:PRK11147 316 GKIVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIH-CG 379
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
690-888 |
2.40e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 54.50 E-value: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 690 GEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKnpadfaalgLGRTFQIVQP---FAAMTVEENIMVG 766
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANNRKPTKQI---------LKRTGFVTQDdilYPHLTVRETLVFC 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 767 AFYR---HHHEKDAREAARETAWRMGL----GPLLGAE-ARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGINQTDVRR 838
Cdd:PLN03211 165 SLLRlpkSLTKQEKILVAESVISELGLtkceNTIIGNSfIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYR 244
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490819619 839 AIDLMLSIRDSGVSIIAIEHVMQA-VMSLSDRVIVLASGEVIAQGRPQDVV 888
Cdd:PLN03211 245 LVLTLGSLAQKGKTIVTSMHQPSSrVYQMFDSVLVLSEGRCLFFGKGSDAM 295
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
681-883 |
2.45e-07 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 54.64 E-value: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 681 RNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQFHAPKNPADFAALglgrTFQIVQPFAAmTVE 760
Cdd:PRK11176 360 RNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVAL----VSQNVHLFND-TIA 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 761 ENImvgAFYRH-HHEKDAREAARETAWRM--------GLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGI 831
Cdd:PRK11176 435 NNI---AYARTeQYSREQIEEAARMAYAMdfinkmdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSAL 511
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490819619 832 NqTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSlSDRVIVLASGEVIAQGR 883
Cdd:PRK11176 512 D-TESERAIQAALDELQKNRTSLVIAHRLSTIEK-ADEILVVEDGEIVERGT 561
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
652-878 |
2.64e-07 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 52.76 E-value: 2.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 652 APSPDRAGIGQDILrVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVnLCGAdgqfh 731
Cdd:PRK11247 1 MMNTARLNQGTPLL-LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGT----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 732 APKNPA-DFAALglgrTFQIVQPFAAMTVEENIMVGAfyrhhhEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLE 810
Cdd:PRK11247 74 APLAEArEDTRL----MFQDARLLPWKKVIDNVGLGL------KGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 811 VARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSI-RDSGVSIIAIEH-VMQAVmSLSDRVIVLASGEV 878
Cdd:PRK11247 144 LARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHdVSEAV-AMADRVLLIEEGKI 212
|
|
| PRK10740 |
PRK10740 |
high-affinity branched-chain amino acid ABC transporter permease LivH; |
351-619 |
2.71e-07 |
|
high-affinity branched-chain amino acid ABC transporter permease LivH;
Pssm-ID: 182689 [Multi-domain] Cd Length: 308 Bit Score: 53.39 E-value: 2.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 351 FAALSTAWNIVGGFAGQMSLGHAVFYGIGGYTGVI----LFNMGISPWFSMFIGAFIAALVGMV--------ISYPCFRL 418
Cdd:PRK10740 22 YALIAIGYTMVYGIIGMINFAHGEVYMIGSYVSFMiiaaLMMMGIDTSWLLVAAGFVGAIVIASaygwsierVAYRPVRN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 419 KGPFYSLASIAFLEVFrvlALHFGWLTGGATGLMIQLKLGWVWMVFRERWPS-------LLIVFGMLLVTLAITWAVRRS 491
Cdd:PRK10740 102 SKRLIALISAIGMSIF---LQNYVSLTEGSRDVALPSLFNGQWVVGHSENFSasittmqAVIWIVTFLAMLALTIFIRYS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 492 RLGFYLVATRERESAARAAGVRTVRVRLIAVAISSALCAMLGTFHAMYLTFIEPAAMFSLAFSIQIAmfALIGGLGTVAG 571
Cdd:PRK10740 179 RMGRACRACAEDLKMASLLGINTDRVIALTFVIGAAMAAVAGVLLGQFYGVINPYIGFMAGMKAFTA--AVLGGIGSIPG 256
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 490819619 572 PLLGAVLLVPITEWARASLGASALGLHGFVyglVLILVVLFMPNGIMG 619
Cdd:PRK10740 257 AMIGGLILGIAEALSSAYLSTEYKDVVSFA---LLILVLLVMPTGILG 301
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
642-878 |
3.25e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.97 E-value: 3.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 642 IAAVPARAIKAPSPDRAGI-GQDILRVQNLNKHfgGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGT 720
Cdd:PRK10982 227 IAMMVGRSLTQRFPDKENKpGEVILEVRNLTSL--RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGT 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 721 VNLCGadgqfHAPKNPADFAALGLGrtFQIVQP-------FAAMTVEENIMVgAFYRHHHEK----DAREAARETAW--- 786
Cdd:PRK10982 305 ITLHG-----KKINNHNANEAINHG--FALVTEerrstgiYAYLDIGFNSLI-SNIRNYKNKvgllDNSRMKSDTQWvid 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 787 ---------RMGLGPLLGAEARGLTIGglkrlevaRVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIE 857
Cdd:PRK10982 377 smrvktpghRTQIGSLSGGNQQKVIIG--------RWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIIS 448
|
250 260
....*....|....*....|.
gi 490819619 858 HVMQAVMSLSDRVIVLASGEV 878
Cdd:PRK10982 449 SEMPELLGITDRILVMSNGLV 469
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
664-891 |
4.34e-07 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 52.88 E-value: 4.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 664 ILRVQNLNKHF----GGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGF---------------------LAPDE 718
Cdd:PRK15093 3 LLDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVtkdnwrvtadrmrfddidllrLSPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 719 GTvNLCGADGQ--FHAPKNPADFAAlGLGRtfQIVQPFAAMTVEenimvGAFYRHHHEKDAReaARETAWRMGLG---PL 793
Cdd:PRK15093 83 RR-KLVGHNVSmiFQEPQSCLDPSE-RVGR--QLMQNIPGWTYK-----GRWWQRFGWRKRR--AIELLHRVGIKdhkDA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 794 LGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSI-RDSGVSIIAIEHVMQAVMSLSDRVIV 872
Cdd:PRK15093 152 MRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADKINV 231
|
250
....*....|....*....
gi 490819619 873 LASGEVIAQGRPQDVVRDP 891
Cdd:PRK15093 232 LYCGQTVETAPSKELVTTP 250
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
665-891 |
5.03e-07 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 52.92 E-value: 5.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 665 LRVQNLNKHF-GGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQFHAPKNPADfaaLG 743
Cdd:PRK11650 4 LKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWI---GGRVVNELEPAD---RD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 744 LGRTFQIVQPFAAMTVEENIMVG----AFYRHHHEKDAREAARetawRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEP 819
Cdd:PRK11650 78 IAMVFQNYALYPHMSVRENMAYGlkirGMPKAEIEERVAEAAR----ILELEPLLDRKPRELSGGQRQRVAMGRAIVREP 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490819619 820 RILLLDEVMAGInqtDVRRAIDLMLSI----RDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDP 891
Cdd:PRK11650 154 AVFLFDEPLSNL---DAKLRVQMRLEIqrlhRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKP 226
|
|
| TM_PBP1_transp_TpRbsC_like |
cd06580 |
Transmembrane subunit (TM) of Treponema pallidum (Tp) RbsC-1, RbsC-2 and related proteins. ... |
347-541 |
6.28e-07 |
|
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: 51.29 E-value: 6.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 347 TICLFAALSTA-------WNIvgGFAGQMSLGhAVFYGIGGYTGVILFnmGISPWFSMFIGAFIAALVGMVISYPCFRLK 419
Cdd:cd06580 2 TPLILAALGVAisfragvFNI--GLEGQMLLG-AFAAALVALYLGLPA--TGSLPLGLLAAALAGALWALLPALLKAKLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 420 GPfyslasiaflEVFRVLALHFGwltggATGLMiqlklgwvwmvfrerwpSLLIVFGMLLVtLAITWAVRRSRLGFYLVA 499
Cdd:cd06580 77 VN----------EVISGLMLNYI-----ALGLT-----------------SYLLLLALLLV-ILVWLLLYRTRFGLRLRA 123
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490819619 500 TRERESAARAAGVRTVRVRLIAVAISSALCAMLGTFHAMYLT 541
Cdd:cd06580 124 VGENPRAARYAGINVKRVRLLAMLISGALAGLAGAYLVLGVQ 165
|
|
| COG4120 |
COG4120 |
ABC-type uncharacterized transport system, permease component [General function prediction ... |
18-209 |
6.30e-07 |
|
ABC-type uncharacterized transport system, permease component [General function prediction only];
Pssm-ID: 443296 Cd Length: 296 Bit Score: 52.04 E-value: 6.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 18 FAIVAVGLTLIFgivKVVNFA----HGEFLMAGMFVTWLITtkLGLHPYAAVIIVLPAMFILGALT----QRLLIQPLMA 89
Cdd:COG4120 16 YAIMALGVYITF---RILDFPdltvDGSFPLGAAVAAVLIV--AGVNPFLATLAAFLAGALAGLVTgllhTKLKIPPLLA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 90 SddghaqIFATVGLSTamINLalLIFGAdiANTPNFGLRT---PIEIGPLRVLTGQVFIFLGAIVLVVALQLFLKNSQTG 166
Cdd:COG4120 91 G------ILTMTALYS--INL--RIMGK--PNIPLLGEDTiftLLPDLGLPGDWAKLLVLLVIVLVIKLLLDWFLKTELG 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490819619 167 RAIRAVAQHRSAAELMGVNVSRIYILCFGLGAACVGLAAVLIA 209
Cdd:COG4120 159 LALRATGDNPQMARALGINTDRMKILGLALSNGLVALSGALVA 201
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
468-729 |
7.07e-07 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 52.88 E-value: 7.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 468 WPSLLIVFGMLLVTLAITWaVRRSRLGFYLVATRERE-------------------SAARAAGVRTVRVRLIAVAISSal 528
Cdd:COG4615 147 PPLFLLTLVLLGLGVAGYR-LLVRRARRHLRRAREAEdrlfkhfrallegfkelklNRRRRRAFFDEDLQPTAERYRD-- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 529 camlgtfhamylTFIEPAAMFSLAFS-IQIAMFALIGGLgtvagpllgaVLLVPITEWARASLgasalgLHGFVyglvli 607
Cdd:COG4615 224 ------------LRIRADTIFALANNwGNLLFFALIGLI----------LFLLPALGWADPAV------LSGFV------ 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 608 LVVLFM--P-NGIMGAINRFVRkpqdseetatartepiAAVPARAIKA--PSPDRAGIGQDILRVQNLNKHFGGLHVtRN 682
Cdd:COG4615 270 LVLLFLrgPlSQLVGALPTLSR----------------ANVALRKIEEleLALAAAEPAAADAAAPPAPADFQTLEL-RG 332
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490819619 683 VSF------------------TLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQ 729
Cdd:COG4615 333 VTYrypgedgdegftlgpidlTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILL---DGQ 394
|
|
| NupP |
COG4603 |
ABC-type guanosine uptake system NupNOPQ, permease component NupP [Nucleotide transport and ... |
146-249 |
1.27e-06 |
|
ABC-type guanosine uptake system NupNOPQ, permease component NupP [Nucleotide transport and metabolism];
Pssm-ID: 443653 [Multi-domain] Cd Length: 356 Bit Score: 51.66 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 146 FLGAIVLVVALQLFLKNSQTGRAIRAVAQHRSAAELMGVNVSRIYILCFGLGAACVGLAAV--LIAPLYPTSSNIGTYFV 223
Cdd:COG4603 200 LLIALLAAVLVWVLLNRTTLGYELRAVGLNPRAARYAGINVKRLIVLAMLISGALAGLAGAveVLGVQGRLTPGFSPGYG 279
|
90 100 110
....*....|....*....|....*....|
gi 490819619 224 LTAFVVVVLGG---LGSIPGA-FVGALIIG 249
Cdd:COG4603 280 FTGIAVALLGRnnpLGIILAAlLFGALYVG 309
|
|
| NupQ |
COG1079 |
ABC-type guanosine uptake system NupNOPQ, permease subunit NupQ [Nucleotide transport and ... |
110-255 |
1.48e-06 |
|
ABC-type guanosine uptake system NupNOPQ, permease subunit NupQ [Nucleotide transport and metabolism];
Pssm-ID: 440697 [Multi-domain] Cd Length: 309 Bit Score: 51.22 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 110 LALLIFGADiANTPNFGLRTPIEIGPL-------RVLTGQVFIFLGAIVLVVALQLFLKNSQTGRAIRAVAQHRSAAELM 182
Cdd:COG1079 109 LGRLLFGQG-GQTPSIPGLPPIPIPGLsdipvlgPLLFGQSPLVYLALLLVPLVWWVLYRTRFGLRLRAVGENPAAADAL 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 183 GVNVSRIYILCFGLGAACVGLAavliaplyptssniGTYFVLT----------------AFVVVVLGGlGSIPGAFVGAL 246
Cdd:COG1079 188 GINVYRIRYLAVLIGGALAGLG--------------GAYLSLGyvgsftegmtagrgfiALAAVIFGR-WRPLGALLAAL 252
|
....*....
gi 490819619 247 IIGVIDTMS 255
Cdd:COG1079 253 LFGFADALQ 261
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
824-902 |
1.76e-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: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 824 LDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAvMSLSDRVIVLA------SGEVIAQGRPQDVVRDPQ-VVEA 896
Cdd:TIGR00630 514 LDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDT-IRAADYVIDIGpgagehGGEVVASGTPEEILANPDsLTGQ 592
|
....*.
gi 490819619 897 YLGKEF 902
Cdd:TIGR00630 593 YLSGRK 598
|
|
| rbsC |
PRK09512 |
ribose ABC transporter permease protein; Reviewed |
133-258 |
1.80e-06 |
|
ribose ABC transporter permease protein; Reviewed
Pssm-ID: 181922 [Multi-domain] Cd Length: 320 Bit Score: 50.87 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 133 IGPLRVLTGQVFIFLGAIVLVVALQLfLKNSQTGRAIRAVAQHRSAAELMGVNVSRIYILCFGLGAACVGLAAVLI-APL 211
Cdd:PRK09512 163 FGIGRPLGIPTPVWIMAIVFLAAWYM-LHHTRLGRYIYALGGNEAATRLSGINVNKVKIIVYALCGLLAALAGIIEvARL 241
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 490819619 212 YPTSSNIGTYFVLTAFVVVVLGGL------GSIPGAFVGALIIGVIDT------MSGYY 258
Cdd:PRK09512 242 SSAQPTAGTGYELDAIAAVVLGGTslaggkGRIVGTLIGALILGFLNNglnllgVSSYY 300
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
679-888 |
2.67e-06 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 51.48 E-value: 2.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 679 VTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCG---ADGQFH--------APKNPADFAalglGRT 747
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGlniAKIGLHdlrfkitiIPQDPVLFS----GSL 1376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 748 FQIVQPFAAMTvEENIMVGAFYRHHHEKDAREAAretawrmGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEV 827
Cdd:TIGR00957 1377 RMNLDPFSQYS-DEEVWWALELAHLKTFVSALPD-------KLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEA 1448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490819619 828 MAGIN-QTDvrRAIDLMLSIRDSGVSIIAIEHVMQAVMSLSdRVIVLASGEVIAQGRPQDVV 888
Cdd:TIGR00957 1449 TAAVDlETD--NLIQSTIRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLL 1507
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
679-891 |
3.06e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 50.87 E-value: 3.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 679 VTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGtvnlcgaDGQFHAPKNPaDFAALGLGRTFQIVQ--PFA- 755
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEG-------DIRFHDIPLT-KLQLDSWRSRLAVVSqtPFLf 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 756 AMTVEENIMVG--AFYRHHHEKDAREAA-RETAWRMGLGPLLGAEARGLTI-GGLK-RLEVARVMAMEPRILLLDEVMAG 830
Cdd:PRK10789 402 SDTVANNIALGrpDATQQEIEHVARLASvHDDILRLPQGYDTEVGERGVMLsGGQKqRISIARALLLNAEILILDDALSA 481
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490819619 831 InqtDVRRAIDLMLSIRD--SGVSIIAIEHVMQAvMSLSDRVIVLASGEVIAQGRPQDVVRDP 891
Cdd:PRK10789 482 V---DGRTEHQILHNLRQwgEGRTVIISAHRLSA-LTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
688-873 |
3.89e-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: 3.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 688 REGEVLGLIGPNGAGKTTLFNMISGFLAPdegtvNLCGADGQ---------FHAPKNPADFAALGLGRTFQIVQP----- 753
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKP-----NLGKFDDPpdwdeildeFRGSELQNYFTKLLEGDVKVIVKPqyvdl 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 754 ---FAAMTVEENImvgafyrhhHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAG 830
Cdd:cd03236 99 ipkAVKGKVGELL---------KKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSY 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490819619 831 InqtDVRRAIDLMLSIR---DSGVSIIAIEHVMQAVMSLSDRVIVL 873
Cdd:cd03236 170 L---DIKQRLNAARLIRelaEDDNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
664-887 |
4.55e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 50.51 E-value: 4.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 664 ILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQfhapkNPADFAAL- 742
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMA-----DARHRRAVc 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 743 --------GLGRTFqivqpFAAMTVEENImvgAFYrhhhekdAR---EAARETAWRM-------GLGPLLGAEARGLTiG 804
Cdd:NF033858 76 priaympqGLGKNL-----YPTLSVFENL---DFF-------GRlfgQDAAERRRRIdellratGLAPFADRPAGKLS-G 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 805 GLKR---LEVARVmaMEPRILLLDEVMAGINQTDVRRAIDLMLSIRDS--GVSIIaiehVMQAVMSLSDR---VIVLASG 876
Cdd:NF033858 140 GMKQklgLCCALI--HDPDLLILDEPTTGVDPLSRRQFWELIDRIRAErpGMSVL----VATAYMEEAERfdwLVAMDAG 213
|
250
....*....|.
gi 490819619 877 EVIAQGRPQDV 887
Cdd:NF033858 214 RVLATGTPAEL 224
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
681-892 |
4.85e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 48.93 E-value: 4.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 681 RNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPdeGTVNLCG---ADGQfhaPKNPADFAalglGRT---------- 747
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPA--GVRQTAGrvlLDGK---PVAPCALR----GRKiatimqnprs 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 748 -FQIVQPFAAMTVEENIMVGafyRHHHEKDAREAAREtawrMGLGP---LLGAEARGLTIGGLKRLEVARVMAMEPRILL 823
Cdd:PRK10418 91 aFNPLHTMHTHARETCLALG---KPADDATLTAALEA----VGLENaarVLKLYPFEMSGGMLQRMMIALALLCEAPFII 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 824 LDEVMAGINQTDVRRAIDLMLSI-RDSGVSIIAIEHVMQAVMSLSDRVIVLASGEVIAQGRPQDVVRDPQ 892
Cdd:PRK10418 164 ADEPTTDLDVVAQARILDLLESIvQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPK 233
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
789-887 |
7.28e-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: 7.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 789 GLGPL-LGAEARGLTIGGLKRLEVARVM---AMEPRILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQaVM 864
Cdd:TIGR00630 817 GLGYIrLGQPATTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLD-VI 895
|
90 100
....*....|....*....|....*....
gi 490819619 865 SLSDRVIVL------ASGEVIAQGRPQDV 887
Cdd:TIGR00630 896 KTADYIIDLgpeggdGGGTVVASGTPEEV 924
|
|
| PRK11618 |
PRK11618 |
inner membrane ABC transporter permease protein YjfF; Provisional |
20-253 |
7.71e-06 |
|
inner membrane ABC transporter permease protein YjfF; Provisional
Pssm-ID: 183235 [Multi-domain] Cd Length: 317 Bit Score: 48.80 E-value: 7.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 20 IVAVGLTLI-------FGIVKVVNFAhgeflmaGMFVTWLITtKLGLHPYAAVIIVLP--AMF--ILGALTQRLLIQPLM 88
Cdd:PRK11618 47 IVAVGMTFVilsggidLSVGSVIAFT-------GVFLAKLIG-DYGWSPLLAFPLVLVmgAAFgaFMGALIHYLKLPAFI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 89 ASDDGhaqIFATVGLSTAMINLALLIFGADIANTPNFGLRTPiEIGPLRVLTGQVFIFLGAIVLVVALQLFlknsqtGRA 168
Cdd:PRK11618 119 VTLAG---MFLARGVSFLVSEESIPINHPFYDTLSSLAWKLP-GGGRLSAMALIMLAVVAIGIFLAHRTRF------GNN 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 169 IRAVAQHRSAAELMGVNVSRIYILCFGLGAACVGLAAVLIApLYpTSSNIGTYFV---LTAFVVVVL------GGLGSIP 239
Cdd:PRK11618 189 VYAIGGNATSANLMGIPVRRTTIRIYMLSGFLATLAGIVFS-LY-TSAGYALAAVgveLDAIAAVVIggtlltGGVGTVL 266
|
250
....*....|....
gi 490819619 240 GAFVGALIIGVIDT 253
Cdd:PRK11618 267 GTLFGVLIQGLIQT 280
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
677-858 |
1.17e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 49.46 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 677 LHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPD--EGTVNLCGadgqfhAPKNPADFAAL-GLGRTFQIVQP 753
Cdd:PLN03140 893 LQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISG------FPKKQETFARIsGYCEQNDIHSP 966
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 754 faAMTVEENIMVGAFYRHHHEKDAREAARETAWRMGLGPL--LGAEARGLT-IGGL-----KRLEVARVMAMEPRILLLD 825
Cdd:PLN03140 967 --QVTVRESLIYSAFLRLPKEVSKEEKMMFVDEVMELVELdnLKDAIVGLPgVTGLsteqrKRLTIAVELVANPSIIFMD 1044
|
170 180 190
....*....|....*....|....*....|....*.
gi 490819619 826 EVMAGInqtDVRRAIDLMLSIR---DSGVSIIAIEH 858
Cdd:PLN03140 1045 EPTSGL---DARAAAIVMRTVRntvDTGRTVVCTIH 1077
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
681-877 |
1.19e-05 |
|
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: 47.08 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 681 RNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGqfhapknpadFAAlglgrtfQivQPFA-AMTV 759
Cdd:cd03250 22 KDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIA----------YVS-------Q--EPWIqNGTI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 760 EENIMVGAFYRHHHEKDAREAAretawrmGLGPLL-----GAEA----RGLTI-GGLK-RLEVARVMAMEPRILLLDEVM 828
Cdd:cd03250 83 RENILFGKPFDEERYEKVIKAC-------ALEPDLeilpdGDLTeigeKGINLsGGQKqRISLARAVYSDADIYLLDDPL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490819619 829 AGINqTDVRRAI--DLMLSIRDSGVSIIAIEHVMQAVmSLSDRVIVLASGE 877
Cdd:cd03250 156 SAVD-AHVGRHIfeNCILGLLLNNKTRILVTHQLQLL-PHADQIVVLDNGR 204
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
661-725 |
1.37e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 49.14 E-value: 1.37e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490819619 661 GQDILRVQNLNKHfgGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCG 725
Cdd:TIGR01271 425 GDDGLFFSNFSLY--VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG 487
|
|
| PRK09699 |
PRK09699 |
D-allose ABC transporter permease; |
149-252 |
2.16e-05 |
|
D-allose ABC transporter permease;
Pssm-ID: 182035 [Multi-domain] Cd Length: 312 Bit Score: 47.46 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 149 AIVLVVALQLFLKNSQTGRAIRAVAQHRSAAELMGVNVSRIYILCFGLGAACVGLAAVL-IAPLYPTSSNIGTYFVLTAF 227
Cdd:PRK09699 169 SLIVALILWFLTTRMRLGRNIYALGGNKNSAFYSGIDVKFHILVVFIISGVCAGLAGVVsTARLGAAEPLAGMGFETYAI 248
|
90 100 110
....*....|....*....|....*....|.
gi 490819619 228 VVVVLGGL------GSIPGAFVGALIIGVID 252
Cdd:PRK09699 249 ASAIIGGTsffggkGRIFSVVIGGLIIGTIN 279
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
687-780 |
2.50e-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: 45.64 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 687 LREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGT--------------VNLCGADGQFHApknpadfAALGLGRT---FQ 749
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNdewdgitpvykpqyIDLSGGELQRVA-------IAAALLRNatfYL 94
|
90 100 110
....*....|....*....|....*....|.
gi 490819619 750 IVQPFAAMTVEENIMVGAFYRHHHEKDAREA 780
Cdd:cd03222 95 FDEPSAYLDIEQRLNAARAIRRLSEEGKKTA 125
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
681-858 |
2.55e-05 |
|
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: 45.61 E-value: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 681 RNVSFTLREGEVLGLIGPNGAGKTTLFNMISGfLAP-DEGTVNLCGADGQFHAPKNPadFAALGLGRTfQIVQPfaamtv 759
Cdd:cd03223 18 KDLSFEIKPGDRLLITGPSGTGKSSLFRALAG-LWPwGSGRIGMPEGEDLLFLPQRP--YLPLGTLRE-QLIYP------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 760 eenimvgafyrhhhekdareaaretaWRMGLGPllgaeargltiGGLKRLEVARVMAMEPRILLLDEVMAGINQTDVRRA 839
Cdd:cd03223 88 --------------------------WDDVLSG-----------GEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRL 130
|
170
....*....|....*....
gi 490819619 840 IDLmlsIRDSGVSIIAIEH 858
Cdd:cd03223 131 YQL---LKELGITVISVGH 146
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
664-712 |
3.55e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 46.17 E-value: 3.55e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 490819619 664 ILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISG 712
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG 55
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
682-858 |
3.63e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 47.64 E-value: 3.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 682 NVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVN----LCGADGQFHAPKNPA----DFAALGLGRTFQIVQP 753
Cdd:PRK11147 21 NAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIyeqdLIVARLQQDPPRNVEgtvyDFVAEGIEEQAEYLKR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 754 FAAMT--VEENIMvgafyrhhhEKDAREAAR-------ETAWRMG------LGPL-LGAEAR--GLTIGGLKRLEVARVM 815
Cdd:PRK11147 101 YHDIShlVETDPS---------EKNLNELAKlqeqldhHNLWQLEnrinevLAQLgLDPDAAlsSLSGGWLRKAALGRAL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490819619 816 AMEPRILLLDEvmaGINQTDVrRAID-LMLSIRDSGVSIIAIEH 858
Cdd:PRK11147 172 VSNPDVLLLDE---PTNHLDI-ETIEwLEGFLKTFQGSIIFISH 211
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
787-903 |
4.97e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.52 E-value: 4.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 787 RMGLGPLLGAEARGLTigglkrlevarvmamepriLLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQaVMSL 866
Cdd:PRK00635 484 RTALAKHLGAELIGIT-------------------YILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQ-MISL 543
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 490819619 867 SDRVIVLA------SGEVIAQGRPQDVVRDPQVVEA-YLGKEFA 903
Cdd:PRK00635 544 ADRIIDIGpgagifGGEVLFNGSPREFLAKSDSLTAkYLRQELT 587
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
674-832 |
5.44e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 45.22 E-value: 5.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 674 FGGLHvtrnvsFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQFHAPKNPADFAALgLGRTFQIVQP 753
Cdd:PRK13543 27 FGPLD------FHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQI---DGKTATRGDRSRFMAY-LGHLPGLKAD 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490819619 754 FAAMtveENIMvgaFYRHHHEKDAREAARETAWRMGLGPLLGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGIN 832
Cdd:PRK13543 97 LSTL---ENLH---FLCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
664-882 |
7.02e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 45.55 E-value: 7.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 664 ILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGF--LAPDEGTVNLCGADgqfHAPKNPADFAA 741
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKD---LLELSPEDRAG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 742 LGLGRTFQ--IVQPFAAMTVEENIMVGAF--YRHHHEKDAREAA-----RETAWRMGLGPLLGAEARGLTIGGLKRLEVA 812
Cdd:PRK09580 78 EGIFMAFQypVEIPGVSNQFFLQTALNAVrsYRGQEPLDRFDFQdlmeeKIALLKMPEDLLTRSVNVGFSGGEKKRNDIL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490819619 813 RVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQAVMSLS-DRVIVLASGEVIAQG 882
Cdd:PRK09580 158 QMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDYIKpDYVHVLYQGRIVKSG 228
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
661-725 |
7.06e-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: 7.06e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490819619 661 GQDILRVQNLNKHfgGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCG 725
Cdd:cd03291 36 DDNNLFFSNLCLV--GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG 98
|
|
| NupP |
COG4603 |
ABC-type guanosine uptake system NupNOPQ, permease component NupP [Nucleotide transport and ... |
474-538 |
1.18e-04 |
|
ABC-type guanosine uptake system NupNOPQ, permease component NupP [Nucleotide transport and metabolism];
Pssm-ID: 443653 [Multi-domain] Cd Length: 356 Bit Score: 45.50 E-value: 1.18e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490819619 474 VFGMLLVTLAITWAVRRSRLGFYLVATRERESAARAAGVRTVRVRLIAVAISSALCAMLGTFHAM 538
Cdd:COG4603 200 LLIALLAAVLVWVLLNRTTLGYELRAVGLNPRAARYAGINVKRLIVLAMLISGALAGLAGAVEVL 264
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
789-884 |
1.27e-04 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 44.53 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 789 GLGPL-LGAEARGLTIGGLKRLEVARVMAMEPR---ILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMQaVM 864
Cdd:cd03271 157 GLGYIkLGQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLD-VI 235
|
90 100
....*....|....*....|....*.
gi 490819619 865 SLSDRVIVL------ASGEVIAQGRP 884
Cdd:cd03271 236 KCADWIIDLgpeggdGGGQVVASGTP 261
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
789-882 |
1.50e-04 |
|
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: 44.17 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 789 GLGPL-LGAEARGLTIGGLKRLEVARVMAMEPR--ILLLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVmQAVMS 865
Cdd:cd03270 125 GLGYLtLSRSAPTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHD-EDTIR 203
|
90 100
....*....|....*....|...
gi 490819619 866 LSDRVIVLA------SGEVIAQG 882
Cdd:cd03270 204 AADHVIDIGpgagvhGGEIVAQG 226
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
683-858 |
2.06e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 44.96 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 683 VSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQFHAPKNPADFAALglgrtfqivqpFAAMTVEen 762
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILL---DGKPVTAEQPEDYRKL-----------FSAVFTD-- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 763 imvgaFYRHHH----EKDAREAARETAW--RMGLGPLLGAE-ARGLTI----GGLKRLEVARVMAMEPRILLLDEVMAgi 831
Cdd:PRK10522 406 -----FHLFDQllgpEGKPANPALVEKWleRLKMAHKLELEdGRISNLklskGQKKRLALLLALAEERDILLLDEWAA-- 478
|
170 180 190
....*....|....*....|....*....|
gi 490819619 832 NQTDVRRAI---DLMLSIRDSGVSIIAIEH 858
Cdd:PRK10522 479 DQDPHFRREfyqVLLPLLQEMGKTIFAISH 508
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
675-721 |
2.11e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 45.24 E-value: 2.11e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 490819619 675 GGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTV 721
Cdd:PLN03073 520 GGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV 566
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
664-723 |
3.01e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.39 E-value: 3.01e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 664 ILRVQNLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNL 723
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL 371
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
655-706 |
3.05e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.40 E-value: 3.05e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 490819619 655 PDR-AGIGQDILRVQNLNKH---FGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTL 706
Cdd:NF040905 247 PERtPKIGEVVFEVKNWTVYhplHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTEL 302
|
|
| PRK15432 |
PRK15432 |
autoinducer 2 ABC transporter permease LsrC; Provisional |
477-612 |
3.42e-04 |
|
autoinducer 2 ABC transporter permease LsrC; Provisional
Pssm-ID: 185330 [Multi-domain] Cd Length: 344 Bit Score: 43.95 E-value: 3.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 477 MLLVTLAITWAVRRSRLGFYLVATRERESAARAAGVRTVRVRLIAVAISSALCAMLGTFHAMYLTFIEPAA-----MFSL 551
Cdd:PRK15432 166 TLILILAMAWLLAKTAFGRSFYATGDNLQGARQLGVRTEAIRIVAFSLNGCMAALAGIVFASQIGFIPNQTgtgleMKAI 245
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490819619 552 AFSIqIAMFALIGGLGTVAGPLLGAVLLVPITewaraslgaSALGL-------HGFVYGLVLILVVLF 612
Cdd:PRK15432 246 AACV-LGGISLLGGSGTIIGAVLGAYFLTQID---------SVLVLlripawwNDFIAGLVLLGVLVF 303
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
771-888 |
4.16e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.43 E-value: 4.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 771 HHHEKdareaaRETAWRMGLGPL-LGAEARGLTIGGLKRLEVARVM---AMEPRILLLDEVMAGINQTDVRRAIDLMLSI 846
Cdd:PRK00635 785 SIHEK------IHALCSLGLDYLpLGRPLSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSL 858
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 490819619 847 RDSGVSIIAIEHVMQaVMSLSDRVIVLA------SGEVIAQGRPQDVV 888
Cdd:PRK00635 859 THQGHTVVIIEHNMH-VVKVADYVLELGpeggnlGGYLLASCSPEELI 905
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
594-725 |
6.66e-04 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 43.75 E-value: 6.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 594 ALGLHGFVYGLVLILVVLFMP---------------NGIMGAINR---FVRKPQDSEETaTARTEPIAAVPARAIKAPSP 655
Cdd:TIGR01271 1130 AIGTNQDGEGEVGIILTLAMNilstlqwavnssidvDGLMRSVSRvfkFIDLPQEEPRP-SGGGGKYQLSTVLVIENPHA 1208
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490819619 656 DRAGIGQDILRVQNLNKHF--GGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLfnmISGF--LAPDEGTVNLCG 725
Cdd:TIGR01271 1209 QKCWPSGGQMDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTL---LSALlrLLSTEGEIQIDG 1279
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
669-723 |
8.19e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 42.96 E-value: 8.19e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 490819619 669 NLNKHFGGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNL 723
Cdd:PRK15064 6 NITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSL 60
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
794-873 |
1.08e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 43.09 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 794 LGAEARGLTIGGLKRLEVARVMAMEPRILLLDEVMAGINQTDVRRAIDLMLSIRDSG-VSIIAIEHVMqAVMSLSDRVIV 872
Cdd:PTZ00265 1352 VGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRI-ASIKRSDKIVV 1430
|
.
gi 490819619 873 L 873
Cdd:PTZ00265 1431 F 1431
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
824-892 |
1.10e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 42.71 E-value: 1.10e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490819619 824 LDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEH---VMQAvmslSDRVIVL------ASGEVIAQGRPQDVVRDPQ 892
Cdd:COG0178 511 LDEPSIGLHQRDNDRLIETLKRLRDLGNTVIVVEHdedTIRA----ADYIIDIgpgageHGGEVVAQGTPEEILKNPD 584
|
|
| rbsC |
PRK09512 |
ribose ABC transporter permease protein; Reviewed |
474-579 |
1.14e-03 |
|
ribose ABC transporter permease protein; Reviewed
Pssm-ID: 181922 [Multi-domain] Cd Length: 320 Bit Score: 42.01 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 474 VFGMLLVTLAITWAVRRSRLGFYLVATRERESAARAAGVRTVRVRLIAVAISSALCAMLGTFHAMYLTFIEPAAMFSLAF 553
Cdd:PRK09512 175 VWIMAIVFLAAWYMLHHTRLGRYIYALGGNEAATRLSGINVNKVKIIVYALCGLLAALAGIIEVARLSSAQPTAGTGYEL 254
|
90 100 110
....*....|....*....|....*....|
gi 490819619 554 SIQIAMF----ALIGGLGTVAGPLLGAVLL 579
Cdd:PRK09512 255 DAIAAVVlggtSLAGGKGRIVGTLIGALIL 284
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
690-730 |
1.50e-03 |
|
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: 40.05 E-value: 1.50e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 490819619 690 GEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCGADGQF 730
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDIL 42
|
|
| PRK15432 |
PRK15432 |
autoinducer 2 ABC transporter permease LsrC; Provisional |
150-253 |
1.81e-03 |
|
autoinducer 2 ABC transporter permease LsrC; Provisional
Pssm-ID: 185330 [Multi-domain] Cd Length: 344 Bit Score: 41.64 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 150 IVLVVALQLFLKNSQTGRAIRAVAQHRSAAELMGVNVSRIYILCF---GLGAACVGLAAVLIAPLYPTSSNIGTYFVLTA 226
Cdd:PRK15432 167 LILILAMAWLLAKTAFGRSFYATGDNLQGARQLGVRTEAIRIVAFslnGCMAALAGIVFASQIGFIPNQTGTGLEMKAIA 246
|
90 100 110
....*....|....*....|....*....|.
gi 490819619 227 FVVV----VLGGLGSIPGAFVGALIIGVIDT 253
Cdd:PRK15432 247 ACVLggisLLGGSGTIIGAVLGAYFLTQIDS 277
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
662-721 |
3.16e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 41.55 E-value: 3.16e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490819619 662 QDILRVQ--NLNKHFG---GLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTV 721
Cdd:PTZ00265 378 KDIKKIQfkNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDI 442
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
681-826 |
3.62e-03 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 40.95 E-value: 3.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 681 RNVSFTLREGEVLGLIGPNGAGKTTLFNMISGfLAPD-EGTVNLCGADGQFHAPKNPadfaALGLGRTFQIVqpfaamtv 759
Cdd:COG4178 380 EDLSLSLKPGERLLITGPSGSGKSTLLRAIAG-LWPYgSGRIARPAGARVLFLPQRP----YLPLGTLREAL-------- 446
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490819619 760 eenimvgaFYRHHHEKDAREAARETAWRMGLGPL---LGAEA---RGLTIGGLKRLEVARVMAMEPRILLLDE 826
Cdd:COG4178 447 --------LYPATAEAFSDAELREALEAVGLGHLaerLDEEAdwdQVLSLGEQQRLAFARLLLHKPDWLFLDE 511
|
|
| livM |
PRK11301 |
leucine/isoleucine/valine transporter permease subunit; Provisional |
143-283 |
4.71e-03 |
|
leucine/isoleucine/valine transporter permease subunit; Provisional
Pssm-ID: 236896 [Multi-domain] Cd Length: 419 Bit Score: 40.34 E-value: 4.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 143 VFIFLGAIVLVVaLQLFLKNS----QTGRAIRAVAQHRSAAELMGVNVSRIYILCFGLGAACVGLAAVLIAPLYPTSSNI 218
Cdd:PRK11301 262 IFLYLVALLLVV-LTLFVINRllrmPLGRAWEALREDEIACRSLGLNPTRIKLSAFTIGAAFAGFAGTFFAARQGFVSPE 340
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490819619 219 GTYFVLTAFV--VVVLGGLGSIPGAFVGALIIGVI-DTMSGYyigSDLREAVVFGIFLLILILKPSGL 283
Cdd:PRK11301 341 SFTFIESAFIlaIVVLGGMGSQFGVILAAILLVVLpELMRDF---NEYRMLMFGLLMVLMMIWRPQGL 405
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
682-725 |
5.94e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 40.15 E-value: 5.94e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 490819619 682 NVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLCG 725
Cdd:PRK10636 19 NATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG 62
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
681-883 |
6.83e-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: 40.19 E-value: 6.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 681 RNVSFTLREGEVLGLIGPNGAGKTTLFNMISGFLAPDEGTVNLcgaDGQfhapkNPADFAALGLGRTFQIVqP-----FA 755
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILI---DGQ-----DIRDVTQASLRAAIGIV-PqdtvlFN 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 756 AmTVEENImvgAFYRHhhekDAREAARETAWRM------------GLGPLLGaEaRGLTI-GGLK-RLEVARVMAMEPRI 821
Cdd:COG5265 446 D-TIAYNI---AYGRP----DASEEEVEAAARAaqihdfieslpdGYDTRVG-E-RGLKLsGGEKqRVAIARTLLKNPPI 515
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490819619 822 LLLDEVMAGINqTDVRRAIDLMLSIRDSGVSIIAIEH----VMQAvmslsDRVIVLASGEVIAQGR 883
Cdd:COG5265 516 LIFDEATSALD-SRTERAIQAALREVARGRTTLVIAHrlstIVDA-----DEILVLEAGRIVERGT 575
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
823-892 |
8.71e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.01 E-value: 8.71e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490819619 823 LLDEVMAGINQTDVRRAIDLMLSIRDSGVSIIAIEHVMqAVMSLSDRVIVL------ASGEVIAQGRPQDVVRDPQ 892
Cdd:COG0178 852 ILDEPTTGLHFHDIRKLLEVLHRLVDKGNTVVVIEHNL-DVIKTADWIIDLgpeggdGGGEIVAEGTPEEVAKVKA 926
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
667-708 |
9.24e-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: 9.24e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 490819619 667 VQNLNKHF--GGLHVTRNVSFTLREGEVLGLIGPNGAGKTTLFN 708
Cdd:cd03289 5 VKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLS 48
|
|
| FepD |
COG0609 |
ABC-type Fe3+-siderophore transport system, permease component [Inorganic ion transport and ... |
380-530 |
9.86e-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: 9.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 380 GYTGVILFNMGISPWFSM---FIGAFIAALVGMVISYPCFRLKGPFYSLASIAFlevfrvlalhfGWLTGGATGLMI--- 453
Cdd:COG0609 79 GAVLAIVLGGGLSALGLPlaaFLGALLAALLVYLLARRGGGLSPLRLVLAGVAV-----------SALFSALTSLLLlla 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490819619 454 ---QLKLGWVWM---VFRERWPSLLIVFGMLLVTLAITWAVRRS----RLGfylvatrerESAARAAGVRTVRVRLIAVA 523
Cdd:COG0609 148 dpeQLRSIVFWLmgsLAGASWDDVLLLLPVLLIGLLLALLLARAlnalALG---------DETARSLGVNVERLRLLLLL 218
|
....*..
gi 490819619 524 ISSALCA 530
Cdd:COG0609 219 LAALLTG 225
|
|
| |
