|
Name |
Accession |
Description |
Interval |
E-value |
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
307-562 |
7.46e-127 |
|
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: 373.60 E-value: 7.46e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 307 GETVVSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRVAAAG 386
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 387 VSRTFQHSKLFNRLSALENVLVGAHLVSRPTFLRRLLWLPSARRDERAALEHAARCLRRVGLGDLAGNRASSLSYGDQRR 466
Cdd:COG0411 81 IARTFQNPRLFPELTVLENVLVAAHARLGRGLLAALLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 467 LEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQG-GLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEI 545
Cdd:COG0411 161 LEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEV 240
|
250
....*....|....*..
gi 502712709 546 AADPAVIEAYLGTADDD 562
Cdd:COG0411 241 RADPRVIEAYLGEEAAA 257
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
315-551 |
1.15e-107 |
|
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: 323.62 E-value: 1.15e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 315 GLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRVAAAGVSRTFQHS 394
Cdd:cd03219 5 GLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRTFQIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 395 KLFNRLSALENVLVGAHLVSRPTFlrrllWLPSARRDERAALEHAARCLRRVGLGDLAGNRASSLSYGDQRRLEIARALA 474
Cdd:cd03219 85 RLFPELTVLENVMVAAQARTGSGL-----LLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502712709 475 AEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEIAADPAV 551
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPRV 236
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
308-559 |
2.18e-85 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 266.86 E-value: 2.18e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 308 ETVVSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRVAAAGV 387
Cdd:PRK11300 3 QPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 388 SRTFQHSKLFNRLSALENVLVGAHLVSRPTFLRRLLWLPSARRDERAALEHAARCLRRVGLGDLAGNRASSLSYGDQRRL 467
Cdd:PRK11300 83 VRTFQHVRLFREMTVIENLLVAQHQQLKTGLFSGLLKTPAFRRAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 468 EIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSL-AQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEIA 546
Cdd:PRK11300 163 EIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELrNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIR 242
|
250
....*....|...
gi 502712709 547 ADPAVIEAYLGTA 559
Cdd:PRK11300 243 NNPDVIKAYLGEA 255
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
311-547 |
6.55e-65 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 212.62 E-value: 6.55e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 311 VSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVH---RVAAAgv 387
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEvrrRIGYV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 388 srtFQHSKLFNRLSALENVlvgahlvsrpTFLRRLLWLPSARRDERAAlehaaRCLRRVGLGDLAGNRASSLSYGDQRRL 467
Cdd:COG1131 79 ---PQEPALYPDLTVRENL----------RFFARLYGLPRKEARERID-----ELLELFGLTDAADRKVGTLSGGMKQRL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 468 EIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEIAA 547
Cdd:COG1131 141 GLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKA 220
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
320-557 |
3.04e-63 |
|
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: 208.30 E-value: 3.04e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 320 YGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRVAAAGVSRTFQHSKLFNR 399
Cdd:COG0410 13 YGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGIGYVPEGRRIFPS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 400 LSALENVLVGAhlvsrptFLRRllwlpsARRDERAALEHAARCLRRvgLGDLAGNRASSLSYGDQRRLEIARALAAEPSL 479
Cdd:COG0410 93 LTVEENLLLGA-------YARR------DRAEVRADLERVYELFPR--LKERRRQRAGTLSGGEQQMLAIGRALMSRPKL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502712709 480 LILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEIAADPAVIEAYLG 557
Cdd:COG0410 158 LLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPEVREAYLG 235
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
312-557 |
7.89e-63 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 207.19 E-value: 7.89e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 312 SLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRVAAAGVSRTF 391
Cdd:COG1137 5 EAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLGIGYLP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 392 QHSKLFNRLSALENVLvgAHLVSRPtflrrllwLPSARRDERA-ALehaarcLRRVGLGDLAGNRASSLSYGDQRRLEIA 470
Cdd:COG1137 85 QEASIFRKLTVEDNIL--AVLELRK--------LSKKEREERLeEL------LEEFGITHLRKSKAYSLSGGERRRVEIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 471 RALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEIAADPA 550
Cdd:COG1137 149 RALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEILNNPL 228
|
....*..
gi 502712709 551 VIEAYLG 557
Cdd:COG1137 229 VRKVYLG 235
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
308-558 |
3.73e-62 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 206.12 E-value: 3.73e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 308 ETVVSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRVAAAGV 387
Cdd:COG4674 8 GPILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHEIARLGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 388 SRTFQHSKLFNRLSALENVLVGAhlvSRPTFLRRLLWlpsARRDeRAALEHAARCLRRVGLGDLAGNRASSLSYGDQRRL 467
Cdd:COG4674 88 GRKFQKPTVFEELTVFENLELAL---KGDRGVFASLF---ARLT-AEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 468 EIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAqGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEIAA 547
Cdd:COG4674 161 EIGMLLAQDPKLLLLDEPVAGMTDAETERTAELLKSLA-GKHSVVVVEHDMEFVRQIARKVTVLHQGSVLAEGSLDEVQA 239
|
250
....*....|.
gi 502712709 548 DPAVIEAYLGT 558
Cdd:COG4674 240 DPRVIEVYLGR 250
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
311-557 |
9.63e-61 |
|
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: 201.62 E-value: 9.63e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 311 VSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRVAAAGVSRT 390
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 391 FQHSKLFNRLSALENVLVGAhlvsrptflrRLLWLPSARRDERaaLEHAarcLRRVGLGDLAGNRASSLSYGDQRRLEIA 470
Cdd:cd03218 81 PQEASIFRKLTVEENILAVL----------EIRGLSKKEREEK--LEEL---LEEFHITHLRKSKASSLSGGERRRVEIA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 471 RALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEIAADPA 550
Cdd:cd03218 146 RALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
....*..
gi 502712709 551 VIEAYLG 557
Cdd:cd03218 226 VRKVYLG 232
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
312-548 |
5.58e-59 |
|
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: 196.50 E-value: 5.58e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 312 SLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRVAAAGVSRTF 391
Cdd:cd03224 2 EVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 392 QHSKLFNRLSALENVLVGAHlvsrptflrrllwlPSARRDERAALEHAARCLRRvgLGDLAGNRASSLSYGDQRRLEIAR 471
Cdd:cd03224 82 EGRRIFPELTVEENLLLGAY--------------ARRRAKRKARLERVYELFPR--LKERRKQLAGTLSGGEQQMLAIAR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502712709 472 ALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEIAAD 548
Cdd:cd03224 146 ALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
306-555 |
2.07e-58 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 195.69 E-value: 2.07e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 306 AGETVVSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPvHRVA-- 383
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRAR-RRIGyv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 384 --AAGVSRTFQhsklfnrLSALENVLVGahlvsrptFLRRLLWLPSARRDERAAlehAARCLRRVGLGDLAGNRASSLSY 461
Cdd:COG1121 81 pqRAEVDWDFP-------ITVRDVVLMG--------RYGRRGLFRRPSRADREA---VDEALERVGLEDLADRPIGELSG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 462 GDQRRLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDfGEVIASGT 541
Cdd:COG1121 143 GQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLN-RGLVAHGP 221
|
250
....*....|....
gi 502712709 542 PAEIAADPAVIEAY 555
Cdd:COG1121 222 PEEVLTPENLSRAY 235
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
315-557 |
2.93e-58 |
|
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: 195.19 E-value: 2.93e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 315 GLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRVAAAGVSRTFQHS 394
Cdd:TIGR04406 6 NLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLGIGYLPQEA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 395 KLFNRLSALENVLVgahlvsrptFLRRLLWLPSARRDERA-ALehaarcLRRVGLGDLAGNRASSLSYGDQRRLEIARAL 473
Cdd:TIGR04406 86 SIFRKLTVEENIMA---------VLEIRKDLDRAEREERLeAL------LEEFQISHLRDNKAMSLSGGERRRVEIARAL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 474 AAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEIAADPAVIE 553
Cdd:TIGR04406 151 ATNPKFILLDEPFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEKVRR 230
|
....
gi 502712709 554 AYLG 557
Cdd:TIGR04406 231 VYLG 234
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
309-562 |
1.67e-55 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 188.34 E-value: 1.67e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 309 TVVSLTGLAKEY-GGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRVAAAgv 387
Cdd:COG3638 1 PMLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 388 sRT-----FQHSKLFNRLSALENVLVGAhlVSRPTFLRRllWLPSARRDERAAlehAARCLRRVGLGDLAGNRASSLSYG 462
Cdd:COG3638 79 -RRrigmiFQQFNLVPRLSVLTNVLAGR--LGRTSTWRS--LLGLFPPEDRER---ALEALERVGLADKAYQRADQLSGG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 463 DQRRLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQ-GGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGT 541
Cdd:COG3638 151 QQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAReDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGP 230
|
250 260
....*....|....*....|.
gi 502712709 542 PAEIaaDPAVIEAYLGTADDD 562
Cdd:COG3638 231 PAEL--TDAVLREIYGGEAEE 249
|
|
| LivM |
COG4177 |
ABC-type branched-chain amino acid transport system, permease component [Amino acid transport ... |
5-245 |
1.37e-54 |
|
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: 187.21 E-value: 1.37e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 5 YATTLTFIALGAIFAYSFYAVL-IAGQLSLGQAGFASVAAFSAATLAPSGDdvgdVPALLtAVVIGMAVGAVASVVLGLP 83
Cdd:COG4177 4 YLSLLTLILIYAILALGLNLLLgYTGLLSLGHAAFFGIGAYAAALLTTHLG----LPFWL-ALLLAGLVAALLGLLIGLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 84 TMHLRGVFLAIATLGFAEAVRVVLLN-QEWTGGAQGLA-VPRILTVGM-----------AWTALAVVAYWFWRMGRSRYG 150
Cdd:COG4177 79 ALRLRGDYLAIATLAFAEIVRLLALNlESLTGGADGLSgIPRPTLFGLdlgsplafyylVLALLVLVLLLLRRLVRSRFG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 151 RALEAIREDELAARSMGIDVGRHRLAAFVTSGAVAGLYGVLFAYYVRLIAPSDFDFTAAVDGLVTAVVGGSTMFLGPILG 230
Cdd:COG4177 159 RALRAIRENEIAAEALGINVTRYKLLAFVLSAALAGLAGALYAHYVGFVSPESFSFLLSIEILLMVVLGGLGSLLGPVLG 238
|
250
....*....|....*
gi 502712709 231 SGFQTMIPEIQRAVG 245
Cdd:COG4177 239 AVLLVLLPELLRSLP 253
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
295-549 |
8.42e-53 |
|
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: 188.96 E-value: 8.42e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 295 APRLAARAHPAAGETVVSLTGLAKEY-----GGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATV 369
Cdd:COG1123 245 AARGRAAPAAAAAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILF 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 370 LGTTIGRTPVHRVAAAG--VSRTFQH--SKLFNRLSALEnvlvgahLVSRPtfLRRLLWLPSARRDERaalehAARCLRR 445
Cdd:COG1123 325 DGKDLTKLSRRSLRELRrrVQMVFQDpySSLNPRMTVGD-------IIAEP--LRLHGLLSRAERRER-----VAELLER 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 446 VGLG-DLAGNRASSLSYGDQRRLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSL-AQGGLTILFIEHNVGMVLE 523
Cdd:COG1123 391 VGLPpDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLqRELGLTYLFISHDLAVVRY 470
|
250 260
....*....|....*....|....*.
gi 502712709 524 TCTRVVVLDFGEVIASGTPAEIAADP 549
Cdd:COG1123 471 IADRVAVMYDGRIVEDGPTEEVFANP 496
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
313-548 |
1.41e-52 |
|
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: 180.07 E-value: 1.41e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 313 LTGLAKEYG-GVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIG-------RTPVHRVAA 384
Cdd:cd03256 3 VENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINklkgkalRQLRRQIGM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 385 agvsrTFQHSKLFNRLSALENVLVGAhlVSRPTFLRRLLWLPSaRRDERAALEhaarCLRRVGLGDLAGNRASSLSYGDQ 464
Cdd:cd03256 83 -----IFQQFNLIERLSVLENVLSGR--LGRRSTWRSLFGLFP-KEEKQRALA----ALERVGLLDKAYQRADQLSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 465 RRLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQG-GLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPA 543
Cdd:cd03256 151 QRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPA 230
|
....*
gi 502712709 544 EIAAD 548
Cdd:cd03256 231 ELTDE 235
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
311-554 |
1.49e-52 |
|
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: 179.84 E-value: 1.49e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 311 VSLTGLAKEY-GGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRVAA-AGVs 388
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRkVGL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 389 rTFQH--SKLFNRlSALENVLVGahlvsrptfLRRlLWLPSARRDERaalehAARCLRRVGLGDLAGNRASSLSYGDQRR 466
Cdd:COG1122 80 -VFQNpdDQLFAP-TVEEDVAFG---------PEN-LGLPREEIRER-----VEEALELVGLEHLADRPPHELSGGQKQR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 467 LEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEIA 546
Cdd:COG1122 143 VAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVF 222
|
....*...
gi 502712709 547 ADPAVIEA 554
Cdd:COG1122 223 SDYELLEE 230
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
312-540 |
2.61e-52 |
|
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: 178.50 E-value: 2.61e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 312 SLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPvHRVA----AAGV 387
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKER-KRIGyvpqRRSI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 388 SRTFqhsklfnRLSALENVLVGahlvsrptFLRRLLWLPSARRDERAALEHAarcLRRVGLGDLAGNRASSLSYGDQRRL 467
Cdd:cd03235 80 DRDF-------PISVRDVVLMG--------LYGHKGLFRRLSKADKAKVDEA---LERVGLSELADRQIGELSGGQQQRV 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502712709 468 EIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDfGEVIASG 540
Cdd:cd03235 142 LLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLN-RTVVASG 213
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
313-547 |
6.58e-52 |
|
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: 178.51 E-value: 6.58e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 313 LTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRVAAAGVSRTFQ 392
Cdd:COG4555 4 VENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLPDER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 393 HskLFNRLSALENVLvgahlvsrptFLRRLLWLPSARRDERaalehAARCLRRVGLGDLAGNRASSLSYGDQRRLEIARA 472
Cdd:COG4555 84 G--LYDRLTVRENIR----------YFAELYGLFDEELKKR-----IEELIELLGLEEFLDRRVGELSTGMKKKVALARA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502712709 473 LAAEPSLLILDEPAAGMNhVEAA-QLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEIAA 547
Cdd:COG4555 147 LVHDPKVLLLDEPTNGLD-VMARrLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELRE 221
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
306-556 |
3.33e-51 |
|
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: 176.32 E-value: 3.33e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 306 AGETVVSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRVAAA 385
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 386 ----GVSrtFQHSKLFNRLSALENVLVGahlvsrptfLRRLLWLPSARRDERAALehaarCLRRVGLGDLAGNRASSLSY 461
Cdd:COG1127 81 rrriGML--FQGGALFDSLTVFENVAFP---------LREHTDLSEAEIRELVLE-----KLELVGLPGAADKMPSELSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 462 GDQRRLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQG-GLTILFIEHNVGMVLETCTRVVVLDFGEVIASG 540
Cdd:COG1127 145 GMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEG 224
|
250
....*....|....*..
gi 502712709 541 TPAEI-AADPAVIEAYL 556
Cdd:COG1127 225 TPEELlASDDPWVRQFL 241
|
|
| TM_PBP1_LivM_like |
cd06581 |
Transmembrane subunit (TM) of Escherichia coli LivM and related proteins. LivM is one of two ... |
12-251 |
2.99e-50 |
|
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: 174.94 E-value: 2.99e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 12 IALGAIFAYSFYAVL-IAGQLSLGQAGFASVAAFSAATLAPsgddVGDVPALLtAVVIGMAVGAVASVVLGLPTMHLRGV 90
Cdd:cd06581 1 ILIYAILALGLNLLLgYAGQLSLGHAAFFGIGAYTAALLAT----RLGLPFWL-ALLAAGLVAALVGLLLGLPALRLRGV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 91 FLAIATLGFAEAVRVVLLN-QEWTGGAQGLAVPRILTVGMAWT-----------ALAVVAYWF-WRMGRSRYGRALEAIR 157
Cdd:cd06581 76 YFAIATLAFAEIVRLLALNwSSLTGGSNGLSGIPPPLLGGLLLssplafyylvlAVLLLVLLLlRRLVRSPFGRALRAIR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 158 EDELAARSMGIDVGRHRLAAFVTSGAVAGLYGVLFAYYVRLIAPSDFDFTAAVDGLVTAVVGGSTMFLGPILGSGFQTMI 237
Cdd:cd06581 156 ENEVAAEALGINVTRYKLLAFALSAALAGLAGALYAHYLGFVSPESFGFALSIELLLMVVLGGLGSLLGPVLGAALLVLL 235
|
250
....*....|....
gi 502712709 238 PEIQRAVGVEAGWI 251
Cdd:cd06581 236 PELLRSLGPGLRLL 249
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
315-545 |
1.77e-49 |
|
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: 171.40 E-value: 1.77e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 315 GLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRVAAAGVsrTFQHS 394
Cdd:cd03265 5 NLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGI--VFQDL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 395 KLFNRLSALENVLVGAhlvsrptflrRLLWLPSARRDERaalehAARCLRRVGLGDLAGNRASSLSYGDQRRLEIARALA 474
Cdd:cd03265 83 SVDDELTGWENLYIHA----------RLYGVPGAERRER-----IDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502712709 475 AEPSLLILDEPAAGMNHVEAAQLSELIRSL-AQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEI 545
Cdd:cd03265 148 HRPEVLFLDEPTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
308-557 |
4.31e-49 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 178.29 E-value: 4.31e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 308 ETVVSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRVAAAGV 387
Cdd:COG1129 2 EPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 388 SRTFQHSKLFNRLSALENVLVGAHLVSRPTFlrrllwlpsarrDERAALEHAARCLRRVGLGDLAGNRASSLSYGDQRRL 467
Cdd:COG1129 82 AIIHQELNLVPNLSVAENIFLGREPRRGGLI------------DWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 468 EIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEIAA 547
Cdd:COG1129 150 EIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTE 229
|
250
....*....|
gi 502712709 548 DpAVIEAYLG 557
Cdd:COG1129 230 D-ELVRLMVG 238
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
311-551 |
3.12e-48 |
|
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: 168.45 E-value: 3.12e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 311 VSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVH--RVAAAGVS 388
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAelYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 389 RTFQHSKLFNRLSALENVLVgahlvsrptFLRRLLWLPSARRDERAALehaarCLRRVGLGDLAGNRASSLSYGDQRRLE 468
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAF---------PLREHTRLSEEEIREIVLE-----KLEAVGLRGAEDLYPAELSGGMKKRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 469 IARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQ-GGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEIAA 547
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKeLGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
....*.
gi 502712709 548 --DPAV 551
Cdd:cd03261 227 sdDPLV 232
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
311-536 |
3.58e-48 |
|
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: 166.03 E-value: 3.58e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 311 VSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPV---HRVAAAgv 387
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEevkRRIGYL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 388 srtFQHSKLFNRLSALENVlvgahlvsrptflrrllwlpsarrderaalehaarclrrvglgdlagnrasSLSYGDQRRL 467
Cdd:cd03230 79 ---PEEPSLYENLTVRENL---------------------------------------------------KLSGGMKQRL 104
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502712709 468 EIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEV 536
Cdd:cd03230 105 ALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
310-549 |
4.33e-48 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 168.25 E-value: 4.33e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 310 VVSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRVAAagvsR 389
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKL----R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 390 T-----FQHSKLFNRLSALENVLVGahlvsrptfLRRLLwlpsaRRDERAALEHAARCLRRVGLGDLAGNRASSLSYGDQ 464
Cdd:COG1126 77 RkvgmvFQQFNLFPHLTVLENVTLA---------PIKVK-----KMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 465 RRLEIARALAAEPSLLILDEPAagmnhveaaqlS-----------ELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDF 533
Cdd:COG1126 143 QRVAIARALAMEPKVMLFDEPT-----------SaldpelvgevlDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDG 211
|
250
....*....|....*.
gi 502712709 534 GEVIASGTPAEIAADP 549
Cdd:COG1126 212 GRIVEEGPPEEFFENP 227
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
311-536 |
2.17e-47 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 165.36 E-value: 2.17e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 311 VSLTGLAKEYGG----VHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRVAA-- 384
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAfr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 385 -AGVSRTFQHSKLFNRLSALENVLVGAHLVSRptflrrllwlPSARRDERaalehAARCLRRVGLGDLAGNRASSLSYGD 463
Cdd:cd03255 81 rRHIGFVFQSFNLLPDLTALENVELPLLLAGV----------PKKERRER-----AEELLERVGLGDRLNHYPSELSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502712709 464 QRRLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLA-QGGLTILFIEHNVGMVlETCTRVVVLDFGEV 536
Cdd:cd03255 146 QQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNkEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
311-540 |
4.89e-46 |
|
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: 161.62 E-value: 4.89e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 311 VSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRT--PVHRVAAAGVS 388
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNieALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 389 RTFqhsklFNRLSALENVLVGAhlvsrptflrRLLWLPSARRDEraalehaarCLRRVGLGDLAGNRASSLSYGDQRRLE 468
Cdd:cd03268 81 PGF-----YPNLTARENLRLLA----------RLLGIRKKRIDE---------VLDVVGLKDSAKKKVKGFSLGMKQRLG 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502712709 469 IARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASG 540
Cdd:cd03268 137 IALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
316-557 |
6.08e-46 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 162.37 E-value: 6.08e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 316 LAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRVAAAGVSRTFQHSK 395
Cdd:PRK10895 9 LAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYLPQEAS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 396 LFNRLSALENVLvgAHLVSRPTflrrllwLPSARRDERAAlehaaRCLRRVGLGDLAGNRASSLSYGDQRRLEIARALAA 475
Cdd:PRK10895 89 IFRRLSVYDNLM--AVLQIRDD-------LSAEQREDRAN-----ELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 476 EPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEIAADPAVIEAY 555
Cdd:PRK10895 155 NPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVY 234
|
..
gi 502712709 556 LG 557
Cdd:PRK10895 235 LG 236
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
306-544 |
6.77e-46 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 169.44 E-value: 6.77e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 306 AGETVVSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGttigrTPVH----R 381
Cdd:COG3845 1 MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG-----KPVRirspR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 382 VA-AAGVSRTFQHSKLFNRLSALENVLVGAhlvsRPTFLRRLlwlpsarrDERAALEHAARCLRRVGLG-DLAgNRASSL 459
Cdd:COG3845 76 DAiALGIGMVHQHFMLVPNLTVAENIVLGL----EPTKGGRL--------DRKAARARIRELSERYGLDvDPD-AKVEDL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 460 SYGDQRRLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIAS 539
Cdd:COG3845 143 SVGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGT 222
|
....*
gi 502712709 540 GTPAE 544
Cdd:COG3845 223 VDTAE 227
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
308-538 |
7.42e-46 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 161.75 E-value: 7.42e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 308 ETVVSLTGLAKEYG----GVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRVA 383
Cdd:COG1136 2 SPLLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 384 AagVSRT-----FQHSKLFNRLSALENVLVGAHLvsrptflrrllwlpsARRDERAALEHAARCLRRVGLGDLAGNRASS 458
Cdd:COG1136 82 R--LRRRhigfvFQFFNLLPELTALENVALPLLL---------------AGVSRKERRERARELLERVGLGDRLDHRPSQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 459 LSYGDQRRLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLA-QGGLTILFIEHNVGmVLETCTRVVVLDFGEVI 537
Cdd:COG1136 145 LSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNrELGTTIVMVTHDPE-LAARADRVIRLRDGRIV 223
|
.
gi 502712709 538 A 538
Cdd:COG1136 224 S 224
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
308-555 |
7.89e-46 |
|
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: 162.18 E-value: 7.89e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 308 ETVVSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSG-SATVLGTTIGRTPVHRVAAA- 385
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 386 GVSRTFQHSKLFNRLSALENVLVGAH----LVSRPTflrrllwlpsarrdeRAALEHAARCLRRVGLGDLAGNRASSLSY 461
Cdd:COG1119 81 GLVSPALQLRFPRDETVLDVVLSGFFdsigLYREPT---------------DEQRERARELLELLGLAHLADRPFGTLSQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 462 GDQRRLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQ-GGLTILFIEHNVGMVLETCTRVVVLDFGEVIASG 540
Cdd:COG1119 146 GEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAeGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAG 225
|
250
....*....|....*
gi 502712709 541 TPAEIAADPAVIEAY 555
Cdd:COG1119 226 PKEEVLTSENLSEAF 240
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
310-554 |
1.11e-45 |
|
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: 162.14 E-value: 1.11e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 310 VVSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGttigrTPVHRVAAAGVSR 389
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDG-----RDLASLSRRELAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 390 T----FQHSKLFNRLSALENVLVGahlvsrptflrRLLWLPSARRDERAALEHAARCLRRVGLGDLAGNRASSLSYGDQR 465
Cdd:COG1120 76 RiayvPQEPPAPFGLTVRELVALG-----------RYPHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 466 RLEIARALAAEPSLLILDEPAAG--MNHveAAQLSELIRSLAQG-GLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTP 542
Cdd:COG1120 145 RVLIARALAQEPPLLLLDEPTSHldLAH--QLEVLELLRRLARErGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPP 222
|
250
....*....|..
gi 502712709 543 AEIaADPAVIEA 554
Cdd:COG1120 223 EEV-LTPELLEE 233
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
311-545 |
2.44e-44 |
|
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: 157.28 E-value: 2.44e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 311 VSLTGLAKEYGG--VHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRVAAAGVS 388
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 389 rtFQHSKLFNRLSALEnvlvgaHLvsrpTFLRRLLWLPSARRDERAALEhaarcLRRVGLGDLAGNRASSLSYGDQRRLE 468
Cdd:cd03263 81 --PQFDALFDELTVRE------HL----RFYARLKGLPKSEIKEEVELL-----LRVLGLTDKANKRARTLSGGMKRKLS 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502712709 469 IARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLaQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEI 545
Cdd:cd03263 144 LAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
310-549 |
2.86e-44 |
|
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: 157.74 E-value: 2.86e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 310 VVSLTGLAKEYGG----VHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVH--RVA 383
Cdd:cd03258 1 MIELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKelRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 384 AAGVSRTFQHSKLFNRLSALENVlvgahlvsrpTFLRRLLWLPSARRDERaalehAARCLRRVGLGDLAGNRASSLSYGD 463
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENV----------ALPLEIAGVPKAEIEER-----VLELLELVGLEDKADAYPAQLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 464 QRRLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQG-GLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTP 542
Cdd:cd03258 146 KQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTV 225
|
....*..
gi 502712709 543 AEIAADP 549
Cdd:cd03258 226 EEVFANP 232
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
311-599 |
5.79e-44 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 160.26 E-value: 5.79e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 311 VSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHR-----Vaaa 385
Cdd:COG3842 6 LELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKrnvgmV--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 386 gvsrtFQHSKLFNRLSALENVLVGahlvsrptfLRRLlWLPSARRDERAAlehaaRCLRRVGLGDLAGNRASSLSYGDQR 465
Cdd:COG3842 83 -----FQDYALFPHLTVAENVAFG---------LRMR-GVPKAEIRARVA-----ELLELVGLEGLADRYPHQLSGGQQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 466 RLEIARALAAEPSLLILDEPAAGMNhveaAQL-----SELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASG 540
Cdd:COG3842 143 RVALARALAPEPRVLLLDEPLSALD----AKLreemrEELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVG 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502712709 541 TPAEIAADPA------------VIEAYLgtADDDPGGSSVADGTLADPTGGSGAPT--------PDAVTNVDPSAAGTL 599
Cdd:COG3842 219 TPEEIYERPAtrfvadfigeanLLPGTV--LGDEGGGVRTGGRTLEVPADAGLAAGgpvtvairPEDIRLSPEGPENGL 295
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
305-551 |
1.02e-43 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 156.79 E-value: 1.02e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 305 AAGETVVSLTGLAKEY----GGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRtPVH 380
Cdd:COG1116 2 SAAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-PGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 381 RVAAAgvsrtFQHSKLFNRLSALENVLVGAhlvsrptflrRLLWLPSARRDERAalEHAarcLRRVGLGDLAGNRASSLS 460
Cdd:COG1116 81 DRGVV-----FQEPALLPWLTVLDNVALGL----------ELRGVPKAERRERA--REL---LELVGLAGFEDAYPHQLS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 461 YGDQRRLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSL-AQGGLTILFIEHNVGMVLETCTRVVVLdfgeviaS 539
Cdd:COG1116 141 GGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLwQETGKTVLFVTHDVDEAVFLADRVVVL-------S 213
|
250
....*....|..
gi 502712709 540 GTPAEIAADPAV 551
Cdd:COG1116 214 ARPGRIVEEIDV 225
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
311-540 |
2.46e-43 |
|
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: 154.21 E-value: 2.46e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 311 VSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRvaaAGVSRT 390
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER---RNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 391 FQHSKLFNRLSALENVLVGahlvsrptfLRRLLWlpsaRRDERAALEHAArcLRRVGLGDLAGNRASSLSYGDQRRLEIA 470
Cdd:cd03259 78 FQDYALFPHLTVAENIAFG---------LKLRGV----PKAEIRARVREL--LELVGLEGLLNRYPHELSGGQQQRVALA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502712709 471 RALAAEPSLLILDEPAAGMN-HVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASG 540
Cdd:cd03259 143 RALAREPSLLLLDEPLSALDaKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
310-545 |
4.29e-43 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 156.42 E-value: 4.29e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 310 VVSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRVA----AA 385
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRIGylpeER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 386 GvsrtfqhskLFNRLSalenvlVGAHLVsrptFLRRLLWLPSArrderAALEHAARCLRRVGLGDLAGNRASSLSYGDQR 465
Cdd:COG4152 81 G---------LYPKMK------VGEQLV----YLARLKGLSKA-----EAKRRADEWLERLGLGDRANKKVEELSKGNQQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 466 RLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEI 545
Cdd:COG4152 137 KVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
311-548 |
4.60e-43 |
|
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: 153.78 E-value: 4.60e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 311 VSLTGLAKEYGG----VHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRvaaaG 386
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDR----G 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 387 VsrTFQHSKLFNRLSALENVLVGahlvsrptflrrllwLPSARRDERAALEHAARCLRRVGLGDLAGNRASSLSYGDQRR 466
Cdd:cd03293 77 Y--VFQQDALLPWLTVLDNVALG---------------LELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 467 LEIARALAAEPSLLILDEPAAGMNHVEAAQL-SELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLdfgeviaSGTPAEI 545
Cdd:cd03293 140 VALARALAVDPDVLLLDEPFSALDALTREQLqEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL-------SARPGRI 212
|
...
gi 502712709 546 AAD 548
Cdd:cd03293 213 VAE 215
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
311-536 |
6.27e-42 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 150.37 E-value: 6.27e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 311 VSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIG--RTPVHRVaAAGVS 388
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTddKKNINEL-RQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 389 RTFQHSKLFNRLSALENVLVGahlvsrPTFLRrllwlpsaRRDERAALEHAARCLRRVGLGDLAGNRASSLSYGDQRRLE 468
Cdd:cd03262 80 MVFQQFNLFPHLTVLENITLA------PIKVK--------GMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502712709 469 IARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEV 536
Cdd:cd03262 146 IARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
320-556 |
1.13e-41 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 150.37 E-value: 1.13e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 320 YGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRVAAAGVSRTFQHSKLFNR 399
Cdd:TIGR03410 10 YGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAGIAYVPQGREIFPR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 400 LSALENVLVGahlvsrptflrrllwLPSARRDERAALEHAARcLRRVgLGDLAGNRASSLSYGDQRRLEIARALAAEPSL 479
Cdd:TIGR03410 90 LTVEENLLTG---------------LAALPRRSRKIPDEIYE-LFPV-LKEMLGRRGGDLSGGQQQQLAIARALVTRPKL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502712709 480 LILDEPAAGMNHVEAAQLSELIRSLA-QGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEIaaDPAVIEAYL 556
Cdd:TIGR03410 153 LLLDEPTEGIQPSIIKDIGRVIRRLRaEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL--DEDKVRRYL 228
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
311-550 |
2.78e-41 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 152.99 E-value: 2.78e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 311 VSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIG-RTPVH-RvaaaGVS 388
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFtNLPPReR----RVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 389 RTFQHSKLFNRLSALENVLVGahlvsrptflrrllwLPSARRDERAALEHAARCLRRVGLGDLAGNRASSLSYGDQRRLE 468
Cdd:COG1118 79 FVFQHYALFPHMTVAENIAFG---------------LRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 469 IARALAAEPSLLILDEP-AAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEIAA 547
Cdd:COG1118 144 LARALAVEPEVLLLDEPfGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYD 223
|
...
gi 502712709 548 DPA 550
Cdd:COG1118 224 RPA 226
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
311-539 |
4.08e-41 |
|
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: 146.42 E-value: 4.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 311 VSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRVAAAGVSRT 390
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 391 FQhsklfnrlsalenvlvgahlvsrptflrrllwlpsarrderaalehaarclrrvglgdlagnrassLSYGDQRRLEIA 470
Cdd:cd03216 81 YQ------------------------------------------------------------------LSVGERQMVEIA 94
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502712709 471 RALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIAS 539
Cdd:cd03216 95 RALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
311-550 |
8.48e-41 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 148.15 E-value: 8.48e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 311 VSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRvaaAGVSRT 390
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHK---RPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 391 FQHSKLFNRLSALENVLVGahlvsrptfLRRllwlpsARRDERAALEHAARCLRRVGLGDLAGNRASSLSYGDQRRLEIA 470
Cdd:cd03300 78 FQNYALFPHLTVFENIAFG---------LRL------KKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 471 RALAAEPSLLILDEPAAGMN-------HVEaaqLSELIRSLaqgGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPA 543
Cdd:cd03300 143 RALVNEPKVLLLDEPLGALDlklrkdmQLE---LKRLQKEL---GITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPE 216
|
....*..
gi 502712709 544 EIAADPA 550
Cdd:cd03300 217 EIYEEPA 223
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
325-535 |
1.24e-40 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 146.84 E-value: 1.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 325 AVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRVAA-AGVsrTFQH--SKLFNrLS 401
Cdd:cd03225 16 ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRkVGL--VFQNpdDQFFG-PT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 402 ALENVLVGahlvsrptfLRRLLwLPSARRDERAAlehaaRCLRRVGLGDLAGNRASSLSYGDQRRLEIARALAAEPSLLI 481
Cdd:cd03225 93 VEEEVAFG---------LENLG-LPEEEIEERVE-----EALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502712709 482 LDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGE 535
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
311-579 |
3.11e-40 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 149.84 E-value: 3.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 311 VSLTGLAKEY----GGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRVAAA- 385
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 386 -GVSRTFQHSKLFNRLSALENV---LvgahlvsrptflrRLLWLPSARRDERAA-LehaarcLRRVGLGDLAGNRASSLS 460
Cdd:COG1135 82 rKIGMIFQHFNLLSSRTVAENValpL-------------EIAGVPKAEIRKRVAeL------LELVGLSDKADAYPSQLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 461 YGDQRRLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSL-AQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIAS 539
Cdd:COG1135 143 GGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDInRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQ 222
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 502712709 540 GTPAEIAADP--AVIEAYLGTADDDPGGSSVADGTLADPTGG 579
Cdd:COG1135 223 GPVLDVFANPqsELTRRFLPTVLNDELPEELLARLREAAGGG 264
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
308-554 |
7.79e-40 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 152.75 E-value: 7.79e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 308 ETVVSLTGLAKEY--GGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPS---SGSATVLGTTIGRTPVhRV 382
Cdd:COG1123 2 TPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSE-AL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 383 AAAGVSRTFQhsklfNRLSALENVLVGAHLVsrptFLRRLLWLPSARRDERAAlehaaRCLRRVGLGDLAGNRASSLSYG 462
Cdd:COG1123 81 RGRRIGMVFQ-----DPMTQLNPVTVGDQIA----EALENLGLSRAEARARVL-----ELLEAVGLERRLDRYPHQLSGG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 463 DQRRLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSL-AQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGT 541
Cdd:COG1123 147 QRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGP 226
|
250
....*....|...
gi 502712709 542 PAEIAADPAVIEA 554
Cdd:COG1123 227 PEEILAAPQALAA 239
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
311-549 |
1.28e-39 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 145.33 E-value: 1.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 311 VSLTGLAKEYG----GVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRtPVHRVAAAG 386
Cdd:COG1124 2 LEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTR-RRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 387 VSRTFQHSklfnrLSALEnvlvgahlvsrPTF-LRRLLWLPSARRDERAALEHAARCLRRVGLG-DLAGNRASSLSYGDQ 464
Cdd:COG1124 81 VQMVFQDP-----YASLH-----------PRHtVDRILAEPLRIHGLPDREERIAELLEQVGLPpSFLDRYPHQLSGGQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 465 RRLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSL-AQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPA 543
Cdd:COG1124 145 QRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVA 224
|
....*.
gi 502712709 544 EIAADP 549
Cdd:COG1124 225 DLLAGP 230
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
311-545 |
8.18e-39 |
|
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: 142.32 E-value: 8.18e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 311 VSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTL---VNMISGLVP--PSSGSATVLGTTIGRTPVHRVAA- 384
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLlrlLNRLNDLIPgaPDEGEVLLDGKDIYDLDVDVLELr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 385 AGVSRTFQHSKLFnRLSALENVLVGahlvsrptfLRRLLWLPSARRDERaalehAARCLRRVGLGDLAGNR--ASSLSYG 462
Cdd:cd03260 81 RRVGMVFQKPNPF-PGSIYDNVAYG---------LRLHGIKLKEELDER-----VEEALRKAALWDEVKDRlhALGLSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 463 DQRRLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQgGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTP 542
Cdd:cd03260 146 QQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKK-EYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPT 224
|
...
gi 502712709 543 AEI 545
Cdd:cd03260 225 EQI 227
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
311-540 |
3.93e-38 |
|
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: 140.20 E-value: 3.93e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 311 VSLTGLAKEY----GGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPvhRVAAAG 386
Cdd:cd03266 2 ITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEP--AEARRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 387 VSRTFQHSKLFNRLSALENVLV--GAHLVSRPTFLRRLLWLPSarrderaalehaarclrRVGLGDLAGNRASSLSYGDQ 464
Cdd:cd03266 80 LGFVSDSTGLYDRLTARENLEYfaGLYGLKGDELTARLEELAD-----------------RLGMEELLDRRVGGFSTGMR 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502712709 465 RRLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASG 540
Cdd:cd03266 143 QKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
310-540 |
4.51e-38 |
|
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: 140.33 E-value: 4.51e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 310 VVSLTGLAKEY----GGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRVAAA 385
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 386 G--VSRTFQHSklfnrLSALENVL-VGAHlvsrptfLRRLLWLPSARRDERAALEHAARCLRRVGLGDLAGNR-ASSLSY 461
Cdd:cd03257 81 RkeIQMVFQDP-----MSSLNPRMtIGEQ-------IAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRyPHELSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 462 GDQRRLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQG-GLTILFIEHNVGMVLETCTRVVVLDFGEVIASG 540
Cdd:cd03257 149 GQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
312-540 |
1.08e-37 |
|
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: 137.57 E-value: 1.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 312 SLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRVAaagvsrtf 391
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELA-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 392 qhsklfnrlsalenvlvgahlvsrptflRRLLWLPSArrderaalehaarcLRRVGLGDLAGNRASSLSYGDQRRLEIAR 471
Cdd:cd03214 73 ----------------------------RKIAYVPQA--------------LELLGLAHLADRPFNELSGGERQRVLLAR 110
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502712709 472 ALAAEPSLLILDEPAAG--MNHveAAQLSELIRSLA-QGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASG 540
Cdd:cd03214 111 ALAQEPPILLLDEPTSHldIAH--QIELLELLRRLArERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
308-551 |
1.59e-37 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 146.08 E-value: 1.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 308 ETVVSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPvHRVAAA-G 386
Cdd:PRK09700 3 TPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLD-HKLAAQlG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 387 VSRTFQHSKLFNRLSALENVLVGAHLVsrptflRRLLWLPSArrDERAALEHAARCLRRVGLGDLAGNRASSLSYGDQRR 466
Cdd:PRK09700 82 IGIIYQELSVIDELTVLENLYIGRHLT------KKVCGVNII--DWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 467 LEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEIA 546
Cdd:PRK09700 154 LEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVS 233
|
....*
gi 502712709 547 ADPAV 551
Cdd:PRK09700 234 NDDIV 238
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
326-487 |
1.94e-37 |
|
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: 135.85 E-value: 1.94e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 326 VRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIgRTPVHRVAAAGVSRTFQHSKLFNRLSALEN 405
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDL-TDDERKSLRKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 406 VLVGAHLvsrptflrrllwlpsARRDERAALEHAARCLRRVGLGDLA----GNRASSLSYGDQRRLEIARALAAEPSLLI 481
Cdd:pfam00005 80 LRLGLLL---------------KGLSKREKDARAEEALEKLGLGDLAdrpvGERPGTLSGGQRQRVAIARALLTKPKLLL 144
|
....*.
gi 502712709 482 LDEPAA 487
Cdd:pfam00005 145 LDEPTA 150
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
312-535 |
1.95e-37 |
|
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: 136.22 E-value: 1.95e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 312 SLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRVaaagvsrtf 391
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEEL--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 392 qhsklfnrlsalenvlvgahlvsrptfLRRLLWLPSarrderaalehaarclrrvglgdlagnrassLSYGDQRRLEIAR 471
Cdd:cd00267 72 ---------------------------RRRIGYVPQ-------------------------------LSGGQRQRVALAR 93
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502712709 472 ALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGE 535
Cdd:cd00267 94 ALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
313-535 |
2.29e-37 |
|
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: 136.93 E-value: 2.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 313 LTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGR----TPVHRVAAAGVs 388
Cdd:cd03229 3 LKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDledeLPPLRRRIGMV- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 389 rtFQHSKLFNRLSALENVLVGahlvsrptflrrllwlpsarrderaalehaarclrrvglgdlagnrassLSYGDQRRLE 468
Cdd:cd03229 82 --FQDFALFPHLTVLENIALG-------------------------------------------------LSGGQQQRVA 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502712709 469 IARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSL-AQGGLTILFIEHNVGMVLETCTRVVVLDFGE 535
Cdd:cd03229 111 LARALAMDPDVLLLDEPTSALDPITRREVRALLKSLqAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
310-544 |
3.23e-37 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 137.88 E-value: 3.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 310 VVSLTGLAKEY-GGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRVAAA--- 385
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 386 -GVSrtFQHSKLFNRLSALENVLvgahLVsrptfLRrllwlpSARRDERAALEHAARCLRRVGLGDLAGNRASSLSYGDQ 464
Cdd:COG2884 81 iGVV--FQDFRLLPDRTVYENVA----LP-----LR------VTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 465 RRLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAE 544
Cdd:COG2884 144 QRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEARGV 223
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
315-550 |
4.97e-37 |
|
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: 137.86 E-value: 4.97e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 315 GLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRvaaAGVSRTFQHS 394
Cdd:cd03296 7 NVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE---RNVGFVFQHY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 395 KLFNRLSALENVLVGahLVSRPTFLRRllwlPSARRDERaalehAARCLRRVGLGDLAGNRASSLSYGDQRRLEIARALA 474
Cdd:cd03296 84 ALFRHMTVFDNVAFG--LRVKPRSERP----PEAEIRAK-----VHELLKLVQLDWLADRYPAQLSGGQRQRVALARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502712709 475 AEPSLLILDEPAAGMNHVEAAQLSELIRSLA-QGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEIAADPA 550
Cdd:cd03296 153 VEPKVLLLDEPFGALDAKVRKELRRWLRRLHdELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPA 229
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
308-541 |
5.07e-37 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 138.61 E-value: 5.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 308 ETVVSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSAT---VLGTTI---GRTPVH- 380
Cdd:PRK09984 2 QTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGShieLLGRTVqreGRLARDi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 381 RVAAAGVSRTFQHSKLFNRLSALENVLVGAhLVSRPtflrrlLWLPSARRDERAALEHAARCLRRVGLGDLAGNRASSLS 460
Cdd:PRK09984 82 RKSRANTGYIFQQFNLVNRLSVLENVLIGA-LGSTP------FWRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 461 YGDQRRLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQG-GLTILFIEHNVGMVLETCTRVVVLDFGEVIAS 539
Cdd:PRK09984 155 GGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQGHVFYD 234
|
..
gi 502712709 540 GT 541
Cdd:PRK09984 235 GS 236
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
311-540 |
6.23e-37 |
|
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: 136.55 E-value: 6.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 311 VSLTGLAKEYGGVHAVRGVDLEIRSGeVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTP--VHRVaaagVS 388
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPqkLRRR----IG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 389 RTFQHSKLFNRLSALEnvlvgahlvsrptFLRRLLWL---PSARRDERAAlehaaRCLRRVGLGDLAGNRASSLSYGDQR 465
Cdd:cd03264 76 YLPQEFGVYPNFTVRE-------------FLDYIAWLkgiPSKEVKARVD-----EVLELVNLGDRAKKKIGSLSGGMRR 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502712709 466 RLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILfIEHNVGMVLETCTRVVVLDFGEVIASG 540
Cdd:cd03264 138 RVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVIL-STHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
310-512 |
1.23e-36 |
|
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: 135.68 E-value: 1.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 310 VVSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVH---RVAAAG 386
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDyrrRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 387 vsrtfQHSKLFNRLSALENVlvgahlvsrpTFLRRLLWLPSARRDERAALEhaarclrRVGLGDLAGNRASSLSYGDQRR 466
Cdd:COG4133 82 -----HADGLKPELTVRENL----------RFWAALYGLRADREAIDEALE-------AVGLAGLADLPVRQLSAGQKRR 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 502712709 467 LEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRS-LAQGGLTIL 512
Cdd:COG4133 140 VALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAhLARGGAVLL 186
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
311-540 |
1.23e-36 |
|
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: 135.87 E-value: 1.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 311 VSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRVAAAGVSRt 390
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIGYLPEER- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 391 fqhsKLFNRLSALENVLvgahlvsrptFLRRLLWLPsarrdERAALEHAARCLRRVGLGDLAGNRASSLSYGDQRRLEIA 470
Cdd:cd03269 80 ----GLYPKMKVIDQLV----------YLAQLKGLK-----KEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFI 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 471 RALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASG 540
Cdd:cd03269 141 AAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
320-554 |
9.49e-36 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 134.99 E-value: 9.49e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 320 YGG----VHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGttigrtpvHRVAAAGVSR--TFQH 393
Cdd:COG4525 13 YPGggqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDG--------VPVTGPGADRgvVFQK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 394 SKLFNRLSALENVLVGAhlvsrptflrRLLWLPSARRDERAAlehaaRCLRRVGLGDLAGNRASSLSYGDQRRLEIARAL 473
Cdd:COG4525 85 DALLPWLNVLDNVAFGL----------RLRGVPKAERRARAE-----ELLALVGLADFARRRIWQLSGGMRQRVGIARAL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 474 AAEPSLLILDEPAAGMNHVEAAQLSELIRSL-AQGGLTILFIEHNVGMVLETCTRVVV-------------LDFGEVIAS 539
Cdd:COG4525 150 AADPRFLLMDEPFGALDALTREQMQELLLDVwQRTGKGVFLITHSVEEALFLATRLVVmspgpgriverleLDFSRRFLA 229
|
250
....*....|....*.
gi 502712709 540 GTPA-EIAADPAVIEA 554
Cdd:COG4525 230 GEDArAIKSDPAFIAL 245
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
304-544 |
1.29e-35 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 133.71 E-value: 1.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 304 PAAGETVVSLTGLAKEYGG----VHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGR--- 376
Cdd:COG4181 2 SSSSAPIIELRGLTKTVGTgageLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAlde 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 377 TPVHRVAAAGVSRTFQHSKLFNRLSALENVLvgahlvsrptflrrllwLPSARRDERAALEHAARCLRRVGLGDLAGNRA 456
Cdd:COG4181 82 DARARLRARHVGFVFQSFQLLPTLTALENVM-----------------LPLELAGRRDARARARALLERVGLGHRLDHYP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 457 SSLSYGDQRRLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSL-AQGGLTILFIEHNVGMvLETCTRVVVLDFGE 535
Cdd:COG4181 145 AQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELnRERGTTLVLVTHDPAL-AARCDRVLRLRAGR 223
|
....*....
gi 502712709 536 VIASGTPAE 544
Cdd:COG4181 224 LVEDTAATA 232
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
330-558 |
1.32e-35 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 133.73 E-value: 1.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 330 DLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPvhrVAAAGVSRTFQHSKLFNRLSALENVLVG 409
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALP---PAERPVSMLFQENNLFPHLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 410 AHlvsrptflrrllwlPSAR--RDERAALEHAarcLRRVGLGDLAGNRASSLSYGDQRRLEIARALAAEPSLLILDEPAA 487
Cdd:COG3840 96 LR--------------PGLKltAEQRAQVEQA---LERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502712709 488 GMNHVEAAQLSELIRSLAQG-GLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEIAA--DPAVIEAYLGT 558
Cdd:COG3840 159 ALDPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDgePPPALAAYLGI 232
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
310-549 |
2.04e-35 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 133.68 E-value: 2.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 310 VVSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTI--GRTPVH--RVAAA 385
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndPKVDERliRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 386 GVsrtFQHSKLFNRLSALENVLVGahlvsrPTFLRRLlwlpsarrDERAALEHAARCLRRVGLGDLAGNRASSLSYGDQR 465
Cdd:PRK09493 81 MV---FQQFYLFPHLTALENVMFG------PLRVRGA--------SKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 466 RLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEI 545
Cdd:PRK09493 144 RVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVL 223
|
....
gi 502712709 546 AADP 549
Cdd:PRK09493 224 IKNP 227
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
311-550 |
5.85e-35 |
|
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: 132.42 E-value: 5.85e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 311 VSLTGLAKEYGGVH-AVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRVAAAgVSR 389
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRK-IGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 390 TFQHSKLFNRLSALENV-LVgahlvsrPTFLRrllWlPSARRDERaalehAARCLRRVGLGD--LAGNRASSLSYGDQRR 466
Cdd:cd03295 80 VIQQIGLFPHMTVEENIaLV-------PKLLK---W-PKEKIRER-----ADELLALVGLDPaeFADRYPHELSGGQQQR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 467 LEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQG-GLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEI 545
Cdd:cd03295 144 VGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
....*
gi 502712709 546 AADPA 550
Cdd:cd03295 224 LRSPA 228
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
310-557 |
3.45e-34 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 130.00 E-value: 3.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 310 VVSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRVAAAGVSR 389
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 390 TFQHSKLFNRLSALENVLVGAHLVSRPTFLRRLLWLPS--ARRDERAAlehaarclrrvglgdlagNRASSLSYGDQRRL 467
Cdd:PRK11614 85 VPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYElfPRLHERRI------------------QRAGTMSGGEQQML 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 468 EIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEIAA 547
Cdd:PRK11614 147 AIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLA 226
|
250
....*....|
gi 502712709 548 DPAVIEAYLG 557
Cdd:PRK11614 227 NEAVRSAYLG 236
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
320-555 |
4.23e-34 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 130.24 E-value: 4.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 320 YGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRVAAA-GVSRtfQHSKL-F 397
Cdd:COG4559 11 LGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRrAVLP--QHSSLaF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 398 NrLSALENVLVGahlvsrptflrRLLWLPSARRDERAALEhaarCLRRVGLGDLAGNRASSLSYGDQRRLEIARALA--- 474
Cdd:COG4559 89 P-FTVEEVVALG-----------RAPHGSSAAQDRQIVRE----ALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlw 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 475 ----AEPSLLILDEPAAGMN--HveaaQLS--ELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEIA 546
Cdd:COG4559 153 epvdGGPRWLFLDEPTSALDlaH----QHAvlRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVL 228
|
....*....
gi 502712709 547 ADPAVIEAY 555
Cdd:COG4559 229 TDELLERVY 237
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
318-550 |
1.28e-33 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 129.30 E-value: 1.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 318 KEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLG---TTIGRTPVHRVAAAGVSRTFQHS 394
Cdd:cd03294 32 KKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGqdiAAMSRKELRELRRKKISMVFQSF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 395 KLFNRLSALENVLVGAHLVSRPtflrrllwlpsarRDERaaLEHAARCLRRVGLGDLAGNRASSLSYGDQRRLEIARALA 474
Cdd:cd03294 112 ALLPHRTVLENVAFGLEVQGVP-------------RAER--EERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALA 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502712709 475 AEPSLLILDEPAAGMNHVEAAQL-SELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEIAADPA 550
Cdd:cd03294 177 VDPDILLMDEAFSALDPLIRREMqDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPA 253
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
312-540 |
1.30e-33 |
|
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: 128.22 E-value: 1.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 312 SLTGLAK-EYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRVAAAGVsrT 390
Cdd:cd03267 22 SLKSLFKrKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGV--V 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 391 F-QHSKLFNRLSALENVLvgahlvsrptFLRRLLWLPSARRDERaaLEHAARCLRrvgLGDLAGNRASSLSYGDQRRLEI 469
Cdd:cd03267 100 FgQKTQLWWDLPVIDSFY----------LLAAIYDLPPARFKKR--LDELSELLD---LEELLDTPVRQLSLGQRMRAEI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502712709 470 ARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSL-AQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASG 540
Cdd:cd03267 165 AAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
311-550 |
1.67e-33 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 131.35 E-value: 1.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 311 VSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGsaTVLgttIGRTPVHRVAAA--GVS 388
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSG--EIL---IGGRDVTDLPPKdrNIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 389 RTFQHSKLFNRLSALENVLVGAHlvsrptfLRRllwLPSARRDERAalEHAArclRRVGLGDLAGNRASSLSYGDQRRLE 468
Cdd:COG3839 79 MVFQSYALYPHMTVYENIAFPLK-------LRK---VPKAEIDRRV--REAA---ELLGLEDLLDRKPKQLSGGQRQRVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 469 IARALAAEPSLLILDEP-----AAGMNHVEaAQLSELIRSLaqgGLTILFIEHN-V-GMVLetCTRVVVLDFGEVIASGT 541
Cdd:COG3839 144 LGRALVREPKVFLLDEPlsnldAKLRVEMR-AEIKRLHRRL---GTTTIYVTHDqVeAMTL--ADRIAVMNDGRIQQVGT 217
|
....*....
gi 502712709 542 PAEIAADPA 550
Cdd:COG3839 218 PEELYDRPA 226
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
310-550 |
2.91e-32 |
|
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: 126.71 E-value: 2.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 310 VVSLTGLAKEY----GGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPP---SSGSATVLGTTIGRTP---V 379
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSekeL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 380 HRVAAAGVSRTFQHSklfnrLSALENVL-VGAHLvSRPTFLRRLLwlpsarrDERAALEHAARCLRRVGLGDlAGNRASS 458
Cdd:COG0444 81 RKIRGREIQMIFQDP-----MTSLNPVMtVGDQI-AEPLRIHGGL-------SKAEARERAIELLERVGLPD-PERRLDR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 459 ----LSYGDQRRLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSL-AQGGLTILFIEHNVGMVLETCTRVVVLDF 533
Cdd:COG0444 147 ypheLSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLqRELGLAILFITHDLGVVAEIADRVAVMYA 226
|
250
....*....|....*..
gi 502712709 534 GEVIASGTPAEIAADPA 550
Cdd:COG0444 227 GRIVEEGPVEELFENPR 243
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
302-550 |
9.14e-32 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 126.99 E-value: 9.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 302 AHPAAGETVVSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPV-H 380
Cdd:PRK09452 6 KQPSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAeN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 381 RvaaaGVSRTFQHSKLFNRLSALENVLVGAhlvsrptflrRLLWLPSARRDERaaLEHAarcLRRVGLGDLAGNRASSLS 460
Cdd:PRK09452 86 R----HVNTVFQSYALFPHMTVFENVAFGL----------RMQKTPAAEITPR--VMEA---LRMVQLEEFAQRKPHQLS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 461 YGDQRRLEIARALAAEPSLLILDEPAAGMNHVEAAQL-SELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIAS 539
Cdd:PRK09452 147 GGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMqNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQD 226
|
250
....*....|.
gi 502712709 540 GTPAEIAADPA 550
Cdd:PRK09452 227 GTPREIYEEPK 237
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
329-579 |
1.55e-31 |
|
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: 125.60 E-value: 1.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 329 VDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTI--GRT----PVHRVAAAGVsrtFQHSKLFNRLSA 402
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdSARgiflPPHRRRIGYV---FQEARLFPHLSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 403 LENVLVGahlvsrptfLRRllwlpSARRDERAALEHAARCLrrvGLGDLAGNRASSLSYGDQRRLEIARALAAEPSLLIL 482
Cdd:COG4148 95 RGNLLYG---------RKR-----APRAERRISFDEVVELL---GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 483 DEPAAGMNHVEAAQLSELIRSLAQ-GGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEIAADPAvieayLGTADD 561
Cdd:COG4148 158 DEPLAALDLARKAEILPYLERLRDeLDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPD-----LLPLAG 232
|
250 260
....*....|....*....|
gi 502712709 562 DPGGSSVADGTLA--DPTGG 579
Cdd:COG4148 233 GEEAGSVLEATVAahDPDYG 252
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
325-547 |
2.15e-31 |
|
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: 129.95 E-value: 2.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 325 AVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSatVLgttIGRTPVHRVAAAGVSRTF----QHSKLFNRl 400
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGR--IL---IDGIDLRQIDPASLRRQIgvvlQDVFLFSG- 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 401 SALENVLVGahlvsrptflrrllwlpsarrDERAALEHAARCLRRVGLGDLA-----------GNRASSLSYGDQRRLEI 469
Cdd:COG2274 564 TIRENITLG---------------------DPDATDEEIIEAARLAGLHDFIealpmgydtvvGEGGSNLSGGQRQRLAI 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 470 ARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQgGLTILFIEHNvgmvLET---CTRVVVLDFGEVIASGTPAEIA 546
Cdd:COG2274 623 ARALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHR----LSTirlADRIIVLDKGRIVEDGTHEELL 697
|
.
gi 502712709 547 A 547
Cdd:COG2274 698 A 698
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
312-545 |
5.33e-31 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 123.27 E-value: 5.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 312 SLTGLAK-EYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGttigRTPV-HRVAAA---G 386
Cdd:COG4586 23 ALKGLFRrEYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG----YVPFkRRKEFArriG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 387 VsrTF-QHSKLFNRLSALEnvlvgahlvsrpTF--LRRLLWLPSARRDERaaLEHAARCLrrvGLGDLAGNRASSLSYGd 463
Cdd:COG4586 99 V--VFgQRSQLWWDLPAID------------SFrlLKAIYRIPDAEYKKR--LDELVELL---DLGELLDTPVRQLSLG- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 464 QR-RLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSL-AQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGT 541
Cdd:COG4586 159 QRmRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGS 238
|
....
gi 502712709 542 PAEI 545
Cdd:COG4586 239 LEEL 242
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
309-557 |
6.10e-31 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 123.79 E-value: 6.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 309 TVVSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPvhRVAAAGVS 388
Cdd:PRK13536 40 VAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARA--RLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 389 RTFQHSKLFNRLSALENVLVgahlvsrptfLRRLLWLpSARRDERA--ALEHAARclrrvgLGDLAGNRASSLSYGDQRR 466
Cdd:PRK13536 118 VVPQFDNLDLEFTVRENLLV----------FGRYFGM-STREIEAVipSLLEFAR------LESKADARVSDLSGGMKRR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 467 LEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEIA 546
Cdd:PRK13536 181 LTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALI 260
|
250
....*....|....
gi 502712709 547 ADP---AVIEAYLG 557
Cdd:PRK13536 261 DEHigcQVIEIYGG 274
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
290-547 |
2.58e-30 |
|
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: 125.64 E-value: 2.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 290 SAADPAPRLAARAHPAAGETVVSLTGLAKEY-GGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSAt 368
Cdd:COG4988 316 DAPEPAAPAGTAPLPAAGPPSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSI- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 369 vlgtTIGRTPVHRVAAAGVSRTF----QHSKLFNrLSALENVLVGAHLVSrptflrrllwlpsarrdeRAALEHAarcLR 444
Cdd:COG4988 395 ----LINGVDLSDLDPASWRRQIawvpQNPYLFA-GTIRENLRLGRPDAS------------------DEELEAA---LE 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 445 RVGLGDLA-----------GNRASSLSYGDQRRLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQgGLTILF 513
Cdd:COG4988 449 AAGLDEFVaalpdgldtplGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVIL 527
|
250 260 270
....*....|....*....|....*....|....
gi 502712709 514 IEHNVGMVLEtCTRVVVLDFGEVIASGTPAEIAA 547
Cdd:COG4988 528 ITHRLALLAQ-ADRILVLDDGRIVEQGTHEELLA 560
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
318-556 |
2.64e-30 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 119.03 E-value: 2.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 318 KEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGttigrtpvhRVAA-----AGvsrtFQ 392
Cdd:COG1134 34 TRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG---------RVSAllelgAG----FH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 393 HSklfnrLSALENVLVGAhlvsrptflrRLLWLPSARRDERAA--LEHAarclrrvGLGDLAGNRASSLSYGDQRRLEIA 470
Cdd:COG1134 101 PE-----LTGRENIYLNG----------RLLGLSRKEIDEKFDeiVEFA-------ELGDFIDQPVKTYSSGMRARLAFA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 471 RALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEiaadpa 550
Cdd:COG1134 159 VATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEE------ 232
|
....*.
gi 502712709 551 VIEAYL 556
Cdd:COG1134 233 VIAAYE 238
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
311-557 |
2.76e-30 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 122.11 E-value: 2.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 311 VSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRtpVHrVAAAGVSRT 390
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSR--LH-ARDRKVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 391 FQHSKLFNRLSALENVLVGahlvsrptflrrLLWLPSARRDERAALEH-AARCLRRVGLGDLAGNRASSLSYGDQRRLEI 469
Cdd:PRK10851 80 FQHYALFRHMTVFDNIAFG------------LTVLPRRERPNAAAIKAkVTQLLEMVQLAHLADRYPAQLSGGQKQRVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 470 ARALAAEPSLLILDEPAAGMNhveaAQL-SELIRSLAQ----GGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAE 544
Cdd:PRK10851 148 ARALAVEPQILLLDEPFGALD----AQVrKELRRWLRQlheeLKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQ 223
|
250
....*....|....*.
gi 502712709 545 IAADPA---VIEaYLG 557
Cdd:PRK10851 224 VWREPAtrfVLE-FMG 238
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
308-552 |
5.76e-30 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 123.89 E-value: 5.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 308 ETVVSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVL--GTTIGRTPVHRVAAA 385
Cdd:PRK13549 3 EYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTYEGEIIfeGEELQASNIRDTERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 386 GVSRTFQHSKLFNRLSALENVLVGAHlvsrptflrrllWLPSARRDERAALEHAARCLRRVGLGDLAGNRASSLSYGDQR 465
Cdd:PRK13549 83 GIAIIHQELALVKELSVLENIFLGNE------------ITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 466 RLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASgTPAEI 545
Cdd:PRK13549 151 LVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGT-RPAAG 229
|
....*..
gi 502712709 546 AADPAVI 552
Cdd:PRK13549 230 MTEDDII 236
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
291-550 |
5.98e-30 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 124.49 E-value: 5.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 291 AADPAPRLAARAHPAAGETVVSLTGLAKEY--GGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSAT 368
Cdd:COG4987 314 DAPPAVTEPAEPAPAPGGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSIT 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 369 VLGTtigrtPVHRVAAAGVSRTF----QHSKLFNRlSALENVLVGAhlvsrptflrrllwlPSARRDEraaLEHAarcLR 444
Cdd:COG4987 394 LGGV-----DLRDLDEDDLRRRIavvpQRPHLFDT-TLRENLRLAR---------------PDATDEE---LWAA---LE 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 445 RVGLGDLA-----------GNRASSLSYGDQRRLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGlTILF 513
Cdd:COG4987 447 RVGLGDWLaalpdgldtwlGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR-TVLL 525
|
250 260 270
....*....|....*....|....*....|....*..
gi 502712709 514 IEHNVgMVLETCTRVVVLDFGEVIASGTPAEIAADPA 550
Cdd:COG4987 526 ITHRL-AGLERMDRILVLEDGRIVEQGTHEELLAQNG 561
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
309-544 |
8.73e-30 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 117.95 E-value: 8.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 309 TVVSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRVAAA-GV 387
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRrAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 388 SRtfQHSKLFNRLSALENVLVGahlvsrptflrRLLWLPSARRDERAalehAARCLRRVGLGDLAGNRASSLSYGDQRRL 467
Cdd:PRK13548 81 LP--QHSSLSFPFTVEEVVAMG-----------RAPHGLSRAEDDAL----VAAALAQVDLAHLAGRDYPQLSGGEQQRV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 468 EIARALA------AEPSLLILDEPAAGMN--HVEaaQLSELIRSLA-QGGLTILFIEHNVGMVLETCTRVVVLDFGEVIA 538
Cdd:PRK13548 144 QLARVLAqlwepdGPPRWLLLDEPTSALDlaHQH--HVLRLARQLAhERGLAVIVVLHDLNLAARYADRIVLLHQGRLVA 221
|
....*.
gi 502712709 539 SGTPAE 544
Cdd:PRK13548 222 DGTPAE 227
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
310-557 |
1.14e-29 |
|
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: 123.01 E-value: 1.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 310 VVSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVL--GTTIGRTPVHRVAAAGV 387
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEIYwsGSPLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 388 SRTFQHSKLFNRLSALENVLVGAHLVsrptflrrllwLPSARRDERAALEHAARCLRRVGLGDLAGNRA-SSLSYGDQRR 466
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGNEIT-----------LPGGRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 467 LEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASgTPAEIA 546
Cdd:TIGR02633 150 VEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVAT-KDMSTM 228
|
250
....*....|.
gi 502712709 547 ADPAVIEAYLG 557
Cdd:TIGR02633 229 SEDDIITMMVG 239
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
308-549 |
2.16e-29 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 116.99 E-value: 2.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 308 ETVVSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTI-------GRTPVH 380
Cdd:PRK10619 3 ENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdGQLKVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 381 -----RVAAAGVSRTFQHSKLFNRLSALENVLvgahlvSRPTflrRLLWLPSARRDERAAlehaaRCLRRVGLGDLA-GN 454
Cdd:PRK10619 83 dknqlRLLRTRLTMVFQHFNLWSHMTVLENVM------EAPI---QVLGLSKQEARERAV-----KYLAKVGIDERAqGK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 455 RASSLSYGDQRRLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFG 534
Cdd:PRK10619 149 YPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQG 228
|
250
....*....|....*
gi 502712709 535 EVIASGTPAEIAADP 549
Cdd:PRK10619 229 KIEEEGAPEQLFGNP 243
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
311-549 |
2.24e-29 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 116.65 E-value: 2.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 311 VSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTT--IGRTPVHRVAAA--- 385
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQfdFSQKPSEKAIRLlrq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 386 GVSRTFQHSKLFNRLSALENvlvgahLVSRPTflrRLLWLPSArrderAALEHAARCLRRVGLGDLAGNRASSLSYGDQR 465
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMEN------LIEAPC---KVLGLSKE-----QAREKAMKLLARLRLTDKADRFPLHLSGGQQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 466 RLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTpAEI 545
Cdd:COG4161 149 RVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD-ASH 227
|
....
gi 502712709 546 AADP 549
Cdd:COG4161 228 FTQP 231
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
309-549 |
2.38e-29 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 116.77 E-value: 2.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 309 TVVSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTI-GRTPVH------R 381
Cdd:PRK11264 2 SAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdTARSLSqqkgliR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 382 VAAAGVSRTFQHSKLFNRLSALENVLVGAHLVSrptflrrllwlpsaRRDERAALEHAARCLRRVGLGDLAGNRASSLSY 461
Cdd:PRK11264 82 QLRQHVGFVFQNFNLFPHRTVLENIIEGPVIVK--------------GEPKEEATARARELLAKVGLAGKETSYPRRLSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 462 GDQRRLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGT 541
Cdd:PRK11264 148 GQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGP 227
|
....*...
gi 502712709 542 PAEIAADP 549
Cdd:PRK11264 228 AKALFADP 235
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
305-554 |
4.13e-29 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 121.31 E-value: 4.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 305 AAGETVVSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGR-TPVHrVA 383
Cdd:PRK15439 6 TTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARlTPAK-AH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 384 AAGVSRTFQHSKLFNRLSALENVLVGahlvsrptflrrllwLPSARRDER--AALEHAARCLRrvglgDLAGNrASSLSY 461
Cdd:PRK15439 85 QLGIYLVPQEPLLFPNLSVKENILFG---------------LPKRQASMQkmKQLLAALGCQL-----DLDSS-AGSLEV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 462 GDQRRLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGT 541
Cdd:PRK15439 144 ADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGK 223
|
250
....*....|...
gi 502712709 542 PAEIAADpAVIEA 554
Cdd:PRK15439 224 TADLSTD-DIIQA 235
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
322-552 |
5.76e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 116.49 E-value: 5.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 322 GVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTI--GRTPVHRVAAAgVSRTFQHSklfnr 399
Cdd:PRK13636 18 GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdySRKGLMKLRES-VGMVFQDP----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 400 lsalENVLVGAHLVSRPTFLRRLLWLPSARRDERaaLEHAarcLRRVGLGDLAGNRASSLSYGDQRRLEIARALAAEPSL 479
Cdd:PRK13636 92 ----DNQLFSASVYQDVSFGAVNLKLPEDEVRKR--VDNA---LKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502712709 480 LILDEPAAGMNHVEAAQLSELIRSLAQG-GLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEIAADPAVI 552
Cdd:PRK13636 163 LVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKEML 236
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
311-540 |
1.27e-28 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 113.78 E-value: 1.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 311 VSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTtigrtpVHRVAAAGVSrt 390
Cdd:cd03220 23 LGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR------VSSLLGLGGG-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 391 FQhsklfNRLSALENVLVGAhlvsrptflrRLLWLpsaRRDERAALEHaaRCLRRVGLGDLAGNRASSLSYGDQRRLEIA 470
Cdd:cd03220 95 FN-----PELTGRENIYLNG----------RLLGL---SRKEIDEKID--EIIEFSELGDFIDLPVKTYSSGMKARLAFA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502712709 471 RALAAEPSLLILDEP-AAGMNH-VEAAQlsELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASG 540
Cdd:cd03220 155 IATALEPDILLIDEVlAVGDAAfQEKCQ--RRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
313-553 |
1.56e-28 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 114.41 E-value: 1.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 313 LTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTtigrtpvhRVAAAGVSR--T 390
Cdd:PRK11248 4 ISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGK--------PVEGPGAERgvV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 391 FQHSKLFNRLSALENVLVGahlvsrptflrrlLWLPSARRDERAALehAARCLRRVGLGDLAGNRASSLSYGDQRRLEIA 470
Cdd:PRK11248 76 FQNEGLLPWRNVQDNVAFG-------------LQLAGVEKMQRLEI--AHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 471 RALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQG-GLTILFIEHNV-----------------GMVLETCTrvvvLD 532
Cdd:PRK11248 141 RALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQEtGKQVLLITHDIeeavfmatelvllspgpGRVVERLP----LN 216
|
250 260
....*....|....*....|..
gi 502712709 533 FGEVIASGTPAE-IAADPAVIE 553
Cdd:PRK11248 217 FARRFVAGESSRsIKSDPQFIA 238
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
310-549 |
1.84e-28 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 116.44 E-value: 1.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 310 VVSLTGLAKEYGG----VHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLG---TTIGRTPVhRV 382
Cdd:PRK11153 1 MIELKNISKVFPQggrtIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGqdlTALSEKEL-RK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 383 AAAGVSRTFQHsklFNRLS---ALENVlvgahlvsrpTFLRRLLWLPSARRDERaalehAARCLRRVGLGDLAGNRASSL 459
Cdd:PRK11153 80 ARRQIGMIFQH---FNLLSsrtVFDNV----------ALPLELAGTPKAEIKAR-----VTELLELVGLSDKADRYPAQL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 460 SYGDQRRLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSL-AQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIA 538
Cdd:PRK11153 142 SGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDInRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVE 221
|
250
....*....|.
gi 502712709 539 SGTPAEIAADP 549
Cdd:PRK11153 222 QGTVSEVFSHP 232
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
311-541 |
3.73e-28 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 113.19 E-value: 3.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 311 VSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATV------LGTTIGRTPVhRVAA 384
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIagnhfdFSKTPSDKAI-RELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 385 AGVSRTFQHSKLFNRLSALENvlvgahLVSRPTflrRLLWLpsarrDERAALEHAARCLRRVGLGDLAGNRASSLSYGDQ 464
Cdd:PRK11124 82 RNVGMVFQQYNLWPHLTVQQN------LIEAPC---RVLGL-----SKDQALARAEKLLERLRLKPYADRFPLHLSGGQQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502712709 465 RRLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGT 541
Cdd:PRK11124 148 QRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD 224
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
308-555 |
3.88e-28 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 114.90 E-value: 3.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 308 ETVVSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTI-GRTPVHRVAAAG 386
Cdd:PRK13537 5 VAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVpSRARHARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 387 VSrtfQHSKLFNRLSALENVLVgahlvsrptfLRRLLWLPSARRDERAA--LEHAArclrrvgLGDLAGNRASSLSYGDQ 464
Cdd:PRK13537 85 VP---QFDNLDPDFTVRENLLV----------FGRYFGLSAAAARALVPplLEFAK-------LENKADAKVGELSGGMK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 465 RRLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTP-- 542
Cdd:PRK13537 145 RRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPha 224
|
250
....*....|....*.
gi 502712709 543 ---AEIAADpaVIEAY 555
Cdd:PRK13537 225 lieSEIGCD--VIEIY 238
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
313-537 |
3.99e-28 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 118.63 E-value: 3.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 313 LTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVL-GTTIGRTPvhrvaaagvsrtf 391
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPkGLRIGYLP------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 392 QHSKLFNRLSALENVLVGAH----LVSRPTFLRRLLWLPSARRDERAALEH-------------AARCLRRVGLGDLAGN 454
Cdd:COG0488 68 QEPPLDDDLTVLDTVLDGDAelraLEAELEELEAKLAEPDEDLERLAELQEefealggweaearAEEILSGLGFPEEDLD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 455 RA-SSLSYGDQRRLEIARALAAEPSLLILDEPAagmNH--VEAAQ-LSELIRSLaQGglTILFIEHNVGMVLETCTRVVV 530
Cdd:COG0488 148 RPvSELSGGWRRRVALARALLSEPDLLLLDEPT---NHldLESIEwLEEFLKNY-PG--TVLVVSHDRYFLDRVATRILE 221
|
....*..
gi 502712709 531 LDFGEVI 537
Cdd:COG0488 222 LDRGKLT 228
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
318-536 |
9.05e-28 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 110.96 E-value: 9.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 318 KEY-GGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRVA----AAGVsrTFQ 392
Cdd:cd03292 8 KTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPylrrKIGV--VFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 393 HSKLFNRLSALENVLVGAHLVSRPtflrrllwlpsarrdERAALEHAARCLRRVGLGDLAGNRASSLSYGDQRRLEIARA 472
Cdd:cd03292 86 DFRLLPDRNVYENVAFALEVTGVP---------------PREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502712709 473 LAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEV 536
Cdd:cd03292 151 IVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
296-557 |
1.33e-27 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 116.66 E-value: 1.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 296 PRLAARAHPAAGETVVSLTGL-AKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTI 374
Cdd:COG3845 243 LLRVEKAPAEPGEVVLEVENLsVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDI 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 375 GRTPVHRVAAAGVS-----RtfQHSKLFNRLSALENVLVGAHlvSRPTFLRRlLWLpsarrDERAALEHAARCLRR--VG 447
Cdd:COG3845 323 TGLSPRERRRLGVAyipedR--LGRGLVPDMSVAENLILGRY--RRPPFSRG-GFL-----DRKAIRAFAEELIEEfdVR 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 448 LGDlAGNRASSLSYGDQRRLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTR 527
Cdd:COG3845 393 TPG-PDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDR 471
|
250 260 270
....*....|....*....|....*....|
gi 502712709 528 VVVLDFGEVIASGTPAEiaADPAVIEAYLG 557
Cdd:COG3845 472 IAVMYEGRIVGEVPAAE--ATREEIGLLMA 499
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
326-534 |
1.57e-27 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 111.02 E-value: 1.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 326 VRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRVAaagvsrTFQHSKLFNRLSALEN 405
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMV------VFQNYSLLPWLTVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 406 VLVGAHLVsrptflrrllwLPSARRDERAAL--EHaarcLRRVGLGDLAGNRASSLSYGDQRRLEIARALAAEPSLLILD 483
Cdd:TIGR01184 75 IALAVDRV-----------LPDLSKSERRAIveEH----IALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLD 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 502712709 484 EPAAGMNHVEAAQLSE-LIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFG 534
Cdd:TIGR01184 140 EPFGALDALTRGNLQEeLMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
322-553 |
1.73e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 112.09 E-value: 1.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 322 GVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRVAA-AGVSRTFQHS--KLFN 398
Cdd:PRK13639 14 GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEVrKTVGIVFQNPddQLFA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 399 RlSALENVLVGahlvsrPTFLRrllwLPSARRDERAAlehaaRCLRRVGLGDLAGNRASSLSYGDQRRLEIARALAAEPS 478
Cdd:PRK13639 94 P-TVEEDVAFG------PLNLG----LSKEEVEKRVK-----EALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502712709 479 LLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEIAADPAVIE 553
Cdd:PRK13639 158 IIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETIR 232
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
311-554 |
1.84e-27 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 111.33 E-value: 1.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 311 VSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRVAaagvsrt 390
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELA------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 391 fqhsklfNRLSAL--ENvlvgaHLVSRPT------FLR------RLlwlpsARRDEraalEHAARCLRRVGLGDLAGNRA 456
Cdd:COG4604 75 -------KRLAILrqEN-----HINSRLTvrelvaFGRfpyskgRL-----TAEDR----EIIDEAIAYLDLEDLADRYL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 457 SSLSyGDQR-RLEIARALAAEPSLLILDEP--AAGMNHveAAQLSELIRSLAQG-GLTILFIEHNVGMVLETCTRVVVLD 532
Cdd:COG4604 134 DELS-GGQRqRAFIAMVLAQDTDYVLLDEPlnNLDMKH--SVQMMKLLRRLADElGKTVVIVLHDINFASCYADHIVAMK 210
|
250 260
....*....|....*....|..
gi 502712709 533 FGEVIASGTPAEIaADPAVIEA 554
Cdd:COG4604 211 DGRVVAQGTPEEI-ITPEVLSD 231
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
311-536 |
2.92e-27 |
|
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: 109.65 E-value: 2.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 311 VSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTI-GRTPVHRvaaaGVSR 389
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVtDLPPKDR----DIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 390 TFQHSKLFNRLSALENVLVGAHLVSRPtflrrllwlpsaRRDERAALEHAARCLrrvGLGDLAGNRASSLSYGDQRRLEI 469
Cdd:cd03301 77 VFQNYALYPHMTVYDNIAFGLKLRKVP------------KDEIDERVREVAELL---QIEHLLDRKPKQLSGGQRQRVAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502712709 470 ARALAAEPSLLILDEPAAGMN-HVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEV 536
Cdd:cd03301 142 GRAIVREPKVFLMDEPLSNLDaKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
311-598 |
4.03e-27 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 113.78 E-value: 4.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 311 VSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGttigrTPVHRVAAAGVSR- 389
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAG-----DDVEALSARAASRr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 390 ---TFQHSKLFNRLSALENVLVGAHlvsrPTFLRRLLWLPSARRDERAALEhaarclrRVGLGDLAGNRASSLSYGDQRR 466
Cdd:PRK09536 79 vasVPQDTSLSFEFDVRQVVEMGRT----PHRSRFDTWTETDRAAVERAME-------RTGVAQFADRPVTSLSGGERQR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 467 LEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEIA 546
Cdd:PRK09536 148 VLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVL 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 502712709 547 ADPAVIEAYlgtadddpgGSSVADGTlaDPTGGSGAPTPDAVTNVDPSAAGT 598
Cdd:PRK09536 228 TADTLRAAF---------DARTAVGT--DPATGAPTVTPLPDPDRTEAAADT 268
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
330-540 |
4.21e-27 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 109.12 E-value: 4.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 330 DLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPvhrVAAAGVSRTFQHSKLFNRLSALENVLVG 409
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAP---PADRPVSMLFQENNLFAHLTVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 410 ahlvsRPTFLRrllwlpsARRDERAALEHAarcLRRVGLGDLAGNRASSLSYGDQRRLEIARALAAEPSLLILDEPAAGM 489
Cdd:cd03298 95 -----LSPGLK-------LTAEDRQAIEVA---LARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 502712709 490 NHVEAAQLSELIRSL-AQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASG 540
Cdd:cd03298 160 DPALRAEMLDLVLDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| BPD_transp_2 |
pfam02653 |
Branched-chain amino acid transport system / permease component; This is a large family mainly ... |
1-231 |
7.40e-27 |
|
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: 110.04 E-value: 7.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 1 MLAQYATTLTFIALGAIFAYSfyavlIAGQLSLGQAGFASVAAFSAATLApsgddVGDVPALLTAVVIGMAVGAVASVVL 80
Cdd:pfam02653 4 NILTLASIYAIAALGLTLIYG-----IAGVINLGHGGFMMLGAYVAAMLL-----NLLGPGLWLALPVGILVGAAVGLLI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 81 GLPTMHLRGVFLAIATLGFAEAVRVVL-LNQEWTGGAQGLA------------VPRILTVGMAWTALAVVAYWfWRMGRS 147
Cdd:pfam02653 74 GILTLRLKINEVIITLLLNLAALGLALfLVTGILGGEGGTSgitgpsgfpgafLSFAFAFIFLLALLLVLALW-LLLYRT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 148 RYGRALEAIREDELAARSMGIDVGRHRLAAFVTSGAVAGLYGVLFAYYVRLIAPSDFDFTAAVDGLVTAVVGGSTMFLGP 227
Cdd:pfam02653 153 KFGRALRAVGENEEAARAAGINVKKLKLLTFVISGALAGLAGALLALYTGVVPPSNFGVGLGLDAIAAVVLGGAGSPIGV 232
|
....
gi 502712709 228 ILGS 231
Cdd:pfam02653 233 VIGS 236
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
318-537 |
9.56e-27 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 107.73 E-value: 9.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 318 KEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTpvHRVAAAG-VSRTFQHsKL 396
Cdd:cd03226 8 SYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAK--ERRKSIGyVMQDVDY-QL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 397 FnRLSALENVLVGAHLVSrptflrrllwlpsarrderAALEHAARCLRRVGLGDLAGNRASSLSYGDQRRLEIARALAAE 476
Cdd:cd03226 85 F-TDSVREELLLGLKELD-------------------AGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSG 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502712709 477 PSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEVI 537
Cdd:cd03226 145 KDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
293-537 |
3.02e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 112.85 E-value: 3.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 293 DPAPRLAARAHPAAGETVVSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATvLGT 372
Cdd:COG0488 298 DKTVEIRFPPPERLGKKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVK-LGE 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 373 TIgrtpvhRVAaagvsrTF-QHSKLFN-RLSALENVlvgahlvsrptflrrllwlpsARRDERAALEHAARCLRRVGL-G 449
Cdd:COG0488 377 TV------KIG------YFdQHQEELDpDKTVLDEL---------------------RDGAPGGTEQEVRGYLGRFLFsG 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 450 DLAGNRASSLSYGDQRRLEIARALAAEPSLLILDEPaagMNHVEAAQLSELIRSLA--QGglTILFIEHNVGMVLETCTR 527
Cdd:COG0488 424 DDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEP---TNHLDIETLEALEEALDdfPG--TVLLVSHDRYFLDRVATR 498
|
250
....*....|
gi 502712709 528 VVVLDFGEVI 537
Cdd:COG0488 499 ILEFEDGGVR 508
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
308-545 |
3.20e-26 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 108.56 E-value: 3.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 308 ETVVSLTGLAKEYGGV--HAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRVAAA 385
Cdd:PRK13635 3 EEIIRVEHISFRYPDAatYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 386 gVSRTFQHSklfnrlsalENVLVGA------------HLVSRPTFLRRLLWlpsarrderaalehaarCLRRVGLGDLAG 453
Cdd:PRK13635 83 -VGMVFQNP---------DNQFVGAtvqddvafglenIGVPREEMVERVDQ-----------------ALRQVGMEDFLN 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 454 NRASSLSYGDQRRLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSL-AQGGLTILFIEHNVGMVLETcTRVVVLD 532
Cdd:PRK13635 136 REPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLkEQKGITVLSITHDLDEAAQA-DRVIVMN 214
|
250
....*....|...
gi 502712709 533 FGEVIASGTPAEI 545
Cdd:PRK13635 215 KGEILEEGTPEEI 227
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
308-557 |
3.38e-26 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 112.40 E-value: 3.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 308 ETVVSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRVAAAGV 387
Cdd:PRK10762 2 QALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 388 SRTFQHSKLFNRLSALENVLVGAHLVSRptfLRRLLWlpsarrdeRAALEHAARCLRRVGLGDLAGNRASSLSYGDQRRL 467
Cdd:PRK10762 82 GIIHQELNLIPQLTIAENIFLGREFVNR---FGRIDW--------KKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 468 EIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEIAA 547
Cdd:PRK10762 151 EIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLTE 230
|
250
....*....|
gi 502712709 548 DpAVIEAYLG 557
Cdd:PRK10762 231 D-SLIEMMVG 239
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
304-550 |
3.59e-26 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 109.44 E-value: 3.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 304 PAAGETVVSLTGLAKEY-----------GGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGT 372
Cdd:COG4608 1 AAMAEPLLEVRDLKKHFpvrgglfgrtvGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 373 TIGRTPVHRVAA--AGVSRTFQ--HSKLFNRLSalenvlVGAhLVSRPTFLRRLLwlPSARRDERAAlehaaRCLRRVGL 448
Cdd:COG4608 81 DITGLSGRELRPlrRRMQMVFQdpYASLNPRMT------VGD-IIAEPLRIHGLA--SKAERRERVA-----ELLELVGL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 449 GDLAGNRasslsY-----GDQR-RLEIARALAAEPSLLILDEPaagmnhVEA------AQLSELIRSL-AQGGLTILFIE 515
Cdd:COG4608 147 RPEHADR-----YphefsGGQRqRIGIARALALNPKLIVCDEP------VSAldvsiqAQVLNLLEDLqDELGLTYLFIS 215
|
250 260 270
....*....|....*....|....*....|....*
gi 502712709 516 HNVGMVLETCTRVVVLDFGEVIASGTPAEIAADPA 550
Cdd:COG4608 216 HDLSVVRHISDRVAVMYLGKIVEIAPRDELYARPL 250
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
296-549 |
7.02e-26 |
|
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: 111.70 E-value: 7.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 296 PRLAARAHPAAGETVVSLTGLAKEY-----------GGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPpSS 364
Cdd:COG4172 261 PRGDPRPVPPDAPPLLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 365 GSATVLGTTIgrtpvhrvaaAGVSRT------------FQ--HSKLFNRLSALENVLVGAHLVSRPtflrrllwLPSARR 430
Cdd:COG4172 340 GEIRFDGQDL----------DGLSRRalrplrrrmqvvFQdpFGSLSPRMTVGQIIAEGLRVHGPG--------LSAAER 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 431 DERAAlehaaRCLRRVGLGDLAGNRasslsY-----GDQR-RLEIARALAAEPSLLILDEPaagmnhVEA------AQLS 498
Cdd:COG4172 402 RARVA-----EALEEVGLDPAARHR-----YphefsGGQRqRIAIARALILEPKLLVLDEP------TSAldvsvqAQIL 465
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 502712709 499 ELIRSL-AQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEIAADP 549
Cdd:COG4172 466 DLLRDLqREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAP 517
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
321-535 |
7.15e-26 |
|
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: 104.39 E-value: 7.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 321 GGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRVAAAgVSRTFQHSKLFNRl 400
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKN-IAYVPQDPFLFSG- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 401 SALENVLVGahlvsrptflrrllwlpsarrderaalehaarclrrvglgdlagnrasslsyGDQRRLEIARALAAEPSLL 480
Cdd:cd03228 91 TIRENILSG----------------------------------------------------GQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502712709 481 ILDEPAAGMNHVEAAQLSELIRSLAQgGLTILFIEHNVGMVLEtCTRVVVLDFGE 535
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAK-GKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
309-537 |
1.16e-25 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 106.69 E-value: 1.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 309 TVVSLTGLAKEYG-----GVHA----VRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRtpV 379
Cdd:PRK10419 2 TLLNVSGLSHHYAhgglsGKHQhqtvLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAK--L 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 380 HRVAAAGVSRT----FQHSklfnrLSALENVLVGAHLVSRPtfLRRLLWLPSARRDERaalehAARCLRRVGLGD-LAGN 454
Cdd:PRK10419 80 NRAQRKAFRRDiqmvFQDS-----ISAVNPRKTVREIIREP--LRHLLSLDKAERLAR-----ASEMLRAVDLDDsVLDK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 455 RASSLSYGDQRRLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSL-AQGGLTILFIEHNVGMVLETCTRVVVLDF 533
Cdd:PRK10419 148 RPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLqQQFGTACLFITHDLRLVERFCQRVMVMDN 227
|
....
gi 502712709 534 GEVI 537
Cdd:PRK10419 228 GQIV 231
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
323-537 |
1.38e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 106.32 E-value: 1.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 323 VHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRVAAAgVSRTFQHSKL--FNRL 400
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKY-IGRVFQDPMMgtAPSM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 401 SALENVLvgahLVSRPTFLRRLLW-LPSARRDERAALehaarcLRRVGLG--DLAGNRASSLSyGDQRrleiaRALA--- 474
Cdd:COG1101 98 TIEENLA----LAYRRGKRRGLRRgLTKKRRELFREL------LATLGLGleNRLDTKVGLLS-GGQR-----QALSllm 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502712709 475 ---AEPSLLILDEPAAGMNHVEAAQLSELIRSL-AQGGLTILFIEHNVGMVLETCTRVVVLDFGEVI 537
Cdd:COG1101 162 atlTKPKLLLLDEHTAALDPKTAALVLELTEKIvEENNLTTLMVTHNMEQALDYGNRLIMMHEGRII 228
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
301-545 |
2.71e-25 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 109.72 E-value: 2.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 301 RAHPAAGETVVSLTGLakeyGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTI-GRTPV 379
Cdd:COG1129 247 KRAAAPGEVVLEVEGL----SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVrIRSPR 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 380 HRVaAAGV-----SRtfQHSKLFNRLSALENVLVgAHLVSrptfLRRLLWLPsaRRDERAALEHAARCLR-RVGLGDLAg 453
Cdd:COG1129 323 DAI-RAGIayvpeDR--KGEGLVLDLSIRENITL-ASLDR----LSRGGLLD--RRRERALAEEYIKRLRiKTPSPEQP- 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 454 nrASSLSYGDQRRLEIARALAAEPSLLILDEPAAGMNhVEA-AQLSELIRSLAQGGLTILFI-----EhnvgmVLETCTR 527
Cdd:COG1129 392 --VGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGID-VGAkAEIYRLIRELAAEGKAVIVIsselpE-----LLGLSDR 463
|
250
....*....|....*...
gi 502712709 528 VVVLDFGEVIASGTPAEI 545
Cdd:COG1129 464 ILVMREGRIVGELDREEA 481
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
321-544 |
2.79e-25 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 110.25 E-value: 2.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 321 GGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSatVLgttIGRTPVHRVAAAGVSRT----FQHSKL 396
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGR--IL---IDGVDIRDLTLESLRRQigvvPQDTFL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 397 FNRlSALENVLVGAhlvsrptflrrllwlPSARRDE-RAALEhAARCLRRV-----GLGDLAGNRASSLSyGDQR-RLEI 469
Cdd:COG1132 426 FSG-TIRENIRYGR---------------PDATDEEvEEAAK-AAQAHEFIealpdGYDTVVGERGVNLS-GGQRqRIAI 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502712709 470 ARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQgGLTILFIEHNVGMVlETCTRVVVLDFGEVIASGTPAE 544
Cdd:COG1132 488 ARALLKDPPILILDEATSALDTETEALIQEALERLMK-GRTTIVIAHRLSTI-RNADRILVLDDGRIVEQGTHEE 560
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
329-549 |
3.05e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 106.07 E-value: 3.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 329 VDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTI----GRTPVHRVAAAgVSRTFQ--HSKLFNRlSA 402
Cdd:PRK13641 26 ISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetGNKNLKKLRKK-VSLVFQfpEAQLFEN-TV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 403 LENVLVGahlvsrPTFLrrllwlpSARRDEraALEHAARCLRRVGLG-DLAGNRASSLSYGDQRRLEIARALAAEPSLLI 481
Cdd:PRK13641 104 LKDVEFG------PKNF-------GFSEDE--AKEKALKWLKKVGLSeDLISKSPFELSGGQMRRVAIAGVMAYEPEILC 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502712709 482 LDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEIAADP 549
Cdd:PRK13641 169 LDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
307-548 |
3.98e-25 |
|
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: 109.51 E-value: 3.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 307 GETVVSLTGLAKEY-----GGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLgttIG------ 375
Cdd:TIGR03269 276 GEPIIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVR---VGdewvdm 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 376 --RTPVHRVAAAG-VSRTFQHSKLFNRLSALENVL--VGAHLVSRPTFLRRLLWLPSARRDEraalEHAARCLRRVglgd 450
Cdd:TIGR03269 353 tkPGPDGRGRAKRyIGILHQEYDLYPHRTVLDNLTeaIGLELPDELARMKAVITLKMVGFDE----EKAEEILDKY---- 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 451 lagnrASSLSYGDQRRLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELI-RSLAQGGLTILFIEHNVGMVLETCTRVV 529
Cdd:TIGR03269 425 -----PDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlKAREEMEQTFIIVSHDMDFVLDVCDRAA 499
|
250
....*....|....*....
gi 502712709 530 VLDFGEVIASGTPAEIAAD 548
Cdd:TIGR03269 500 LMRDGKIVKIGDPEEIVEE 518
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
322-554 |
9.94e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 104.05 E-value: 9.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 322 GVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRVAAAgVSRTFQH--SKLFNr 399
Cdd:PRK13647 17 GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSK-VGLVFQDpdDQVFS- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 400 LSALENVLVGahlvsrPTFLRrllwlpsARRDEraALEHAARCLRRVGLGDLAGNRASSLSYGDQRRLEIARALAAEPSL 479
Cdd:PRK13647 95 STVWDDVAFG------PVNMG-------LDKDE--VERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502712709 480 LILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPaEIAADPAVIEA 554
Cdd:PRK13647 160 IVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK-SLLTDEDIVEQ 233
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
329-540 |
1.02e-24 |
|
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: 102.37 E-value: 1.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 329 VDLEIrSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRT------PVHRvaaAGVSRTFQHSKLFNRLSA 402
Cdd:cd03297 17 IDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSrkkinlPPQQ---RKIGLVFQQYALFPHLNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 403 LENVLVGahlvsrptfLRRLLwlPSARRDERAALehaarcLRRVGLGDLAGNRASSLSYGDQRRLEIARALAAEPSLLIL 482
Cdd:cd03297 93 RENLAFG---------LKRKR--NREDRISVDEL------LDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502712709 483 DEPAAGMNHVEAAQL-SELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASG 540
Cdd:cd03297 156 DEPFSALDRALRLQLlPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
321-544 |
1.21e-24 |
|
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: 102.69 E-value: 1.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 321 GGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRVaAAGVSRTFQHSKLFNRl 400
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSL-RSMIGVVLQDTFLFSG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 401 SALENVLVGAhlvsrptflrrllwlPSARRDE--RAALE-HAARCLRRV--GLGDLAGNRASSLSYGDQRRLEIARALAA 475
Cdd:cd03254 92 TIMENIRLGR---------------PNATDEEviEAAKEaGAHDFIMKLpnGYDTVLGENGGNLSQGERQLLAIARAMLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502712709 476 EPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGlTILFIEHNVGMVLETcTRVVVLDFGEVIASGTPAE 544
Cdd:cd03254 157 DPKILILDEATSNIDTETEKLIQEALEKLMKGR-TSIIIAHRLSTIKNA-DKILVLDDGKIIEEGTHDE 223
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
312-539 |
1.25e-24 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 107.69 E-value: 1.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 312 SLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRVAAAGVSRTF 391
Cdd:PRK11288 6 SFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAGVAIIY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 392 QHSKLFNRLSALENVLVGaHLVSRPTFLrrllwlpsarrDERAALEHAARCLRRVGLGDLAGNRASSLSYGDQRRLEIAR 471
Cdd:PRK11288 86 QELHLVPEMTVAENLYLG-QLPHKGGIV-----------NRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAK 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502712709 472 ALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIAS 539
Cdd:PRK11288 154 ALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVAT 221
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
325-553 |
1.48e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 103.67 E-value: 1.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 325 AVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHR-----VAAAGVSRTFQHSKLFNR 399
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKdikqiRKKVGLVFQFPESQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 400 lSALENVLVGAHLVSrptflrrllwlPSARRDERAALEHaarcLRRVGLG-DLAGNRASSLSYGDQRRLEIARALAAEPS 478
Cdd:PRK13649 102 -TVLKDVAFGPQNFG-----------VSQEEAEALAREK----LALVGISeSLFEKNPFELSGGQMRRVAIAGILAMEPK 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502712709 479 LLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEIAADPAVIE 553
Cdd:PRK13649 166 ILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQDVDFLE 240
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
321-549 |
1.51e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 103.73 E-value: 1.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 321 GGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRVAAAgVSRTFQHS--KLFN 398
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKF-VGLVFQNPddQIFS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 399 rlsalenvlvgahlvsrPTFLRRLLWLPSARRDERAALEH-AARCLRRVGLGDLAGNRASSLSYGDQRRLEIARALAAEP 477
Cdd:PRK13652 94 -----------------PTVEQDIAFGPINLGLDEETVAHrVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502712709 478 SLLILDEPAAGMNHVEAAQLSELIRSLAQG-GLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEIAADP 549
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
328-540 |
3.62e-24 |
|
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: 101.19 E-value: 3.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 328 GVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPpsSGSATVLGTTIGRTPVHRvaaAGVSRTFQHSKLFNRLsaLENVL 407
Cdd:cd03234 25 DVSLHVESGQVMAILGSSGSGKTTLLDAISGRVE--GGGTTSGQILFNGQPRKP---DQFQKCVAYVRQDDIL--LPGLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 408 VGAHLVSRPTF-LRRLLwlPSARRDERAALEHaarcLRRVGLGDLAGNRASSLSYGDQRRLEIARALAAEPSLLILDEPA 486
Cdd:cd03234 98 VRETLTYTAILrLPRKS--SDAIRKKRVEDVL----LRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502712709 487 AGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGM-VLETCTRVVVLDFGEVIASG 540
Cdd:cd03234 172 SGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSdLFRLFDRILLLSSGEIVYSG 226
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
311-550 |
4.89e-24 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 103.96 E-value: 4.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 311 VSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSatvlgTTIGRTPVHRVAAA--GVS 388
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGD-----LFIGEKRMNDVPPAerGVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 389 RTFQHSKLFNRLSALENVLVGahlvsrptflrrlLWLPSARRDERAA-LEHAARCLRrvgLGDLAGNRASSLSYGDQRRL 467
Cdd:PRK11000 79 MVFQSYALYPHLSVAENMSFG-------------LKLAGAKKEEINQrVNQVAEVLQ---LAHLLDRKPKALSGGQRQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 468 EIARALAAEPSLLILDEPaagMNHVEAA-------QLSELIRSLaqgGLTILFIEHNVGMVLETCTRVVVLDFGEVIASG 540
Cdd:PRK11000 143 AIGRTLVAEPSVFLLDEP---LSNLDAAlrvqmriEISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
|
250
....*....|
gi 502712709 541 TPAEIAADPA 550
Cdd:PRK11000 217 KPLELYHYPA 226
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
323-540 |
7.84e-24 |
|
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: 99.97 E-value: 7.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 323 VHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPvHRVAAAGVSRTFQHSKLFNRlSA 402
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLD-PADLRRNIGYVPQDVTLFYG-TL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 403 LENVLVGAHLVSRptflRRLLwlpsaRRDERAALEHAARCLRRvGLGDLAGNRASSLSYGDQRRLEIARALAAEPSLLIL 482
Cdd:cd03245 95 RDNITLGAPLADD----ERIL-----RAAELAGVTDFVNKHPN-GLDLQIGERGRGLSGGQRQAVALARALLNDPPILLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502712709 483 DEPAAGMNHVEAAQLSELIRSLAqGGLTILFIEHNVGMvLETCTRVVVLDFGEVIASG 540
Cdd:cd03245 165 DEPTSAMDMNSEERLKERLRQLL-GDKTLIIITHRPSL-LDLVDRIIVMDSGRIVADG 220
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
320-545 |
1.07e-23 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 100.47 E-value: 1.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 320 YGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGrtpvhrvaaagvsrTFQHSKLFNR 399
Cdd:PRK11231 12 YGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPIS--------------MLSSRQLARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 400 LSALENVlvgaHLVSRPTFLRRL----------LWLPSARRDEraalEHAARCLRRVGLGDLAGNRASSLSYGDQRRLEI 469
Cdd:PRK11231 78 LALLPQH----HLTPEGITVRELvaygrspwlsLWGRLSAEDN----ARVNQAMEQTRINHLADRRLTDLSGGQRQRAFL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502712709 470 ARALAAEPSLLILDEPAA--GMNHveAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEI 545
Cdd:PRK11231 150 AMVLAQDTPVVLLDEPTTylDINH--QVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEV 225
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
307-536 |
1.85e-23 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 97.89 E-value: 1.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 307 GETVVSLTGLakeyGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRVAAAG 386
Cdd:cd03215 1 GEPVLEVRGL----SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 387 VS-----RtfQHSKLFNRLSALENVLVGAHlvsrptflrrllwlpsarrderaalehaarclrrvglgdlagnrassLSY 461
Cdd:cd03215 77 IAyvpedR--KREGLVLDLSVAENIALSSL-----------------------------------------------LSG 107
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502712709 462 GDQRRLEIARALAAEPSLLILDEPAAGMNhVEA-AQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEV 536
Cdd:cd03215 108 GNQQKVVLARWLARDPRVLILDEPTRGVD-VGAkAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
302-517 |
2.89e-23 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 99.34 E-value: 2.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 302 AHPAAGETVVSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLV---NMISGLVPPS--SGSATVLGTTI-- 374
Cdd:COG1117 3 APASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLrclNRMNDLIPGArvEGEILLDGEDIyd 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 375 GRTPVHRVaaagvsRT-----FQHSKLFNrLSALENVLVGahlvsrptfLRRLLWLPSARRDERAalEhaaRCLRRVGLG 449
Cdd:COG1117 83 PDVDVVEL------RRrvgmvFQKPNPFP-KSIYDNVAYG---------LRLHGIKSKSELDEIV--E---ESLRKAALW 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502712709 450 DLAGNR----ASSLSYGDQRRLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQgGLTILFIEHN 517
Cdd:COG1117 142 DEVKDRlkksALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKK-DYTIVIVTHN 212
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
293-550 |
3.11e-23 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 101.84 E-value: 3.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 293 DPAPRLAARAHPAAgETVVSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGT 372
Cdd:PRK11607 3 DAIPRPQAKTRKAL-TPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 373 TIGRTPVHRVAaagVSRTFQHSKLFNRLSALENVLVGahlvsrptflrrllwlpsARRDERAALEHAARC---LRRVGLG 449
Cdd:PRK11607 82 DLSHVPPYQRP---INMMFQSYALFPHMTVEQNIAFG------------------LKQDKLPKAEIASRVnemLGLVHMQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 450 DLAGNRASSLSYGDQRRLEIARALAAEPSLLILDEPAAGMNHV--EAAQLsELIRSLAQGGLTILFIEHNVGMVLETCTR 527
Cdd:PRK11607 141 EFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKlrDRMQL-EVVDILERVGVTCVMVTHDQEEAMTMAGR 219
|
250 260
....*....|....*....|...
gi 502712709 528 VVVLDFGEVIASGTPAEIAADPA 550
Cdd:PRK11607 220 IAIMNRGKFVQIGEPEEIYEHPT 242
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
315-549 |
3.45e-23 |
|
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: 98.56 E-value: 3.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 315 GLAKEYGGVHaVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRvaaAGVSRTFQHS 394
Cdd:cd03299 5 NLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK---RDISYVPQNY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 395 KLFNRLSALENVLVGAHLVSRPTflrrllwlpsaRRDERAALEHAarclRRVGLGDLAGNRASSLSYGDQRRLEIARALA 474
Cdd:cd03299 81 ALFPHMTVYKNIAYGLKKRKVDK-----------KEIERKVLEIA----EMLGIDHLLNRKPETLSGGEQQRVAIARALV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 475 AEPSLLILDEPAAGMNhveaAQLSELIRSL-----AQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEIAADP 549
Cdd:cd03299 146 VNPKILLLDEPFSALD----VRTKEKLREElkkirKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKP 221
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
301-585 |
6.60e-23 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 103.67 E-value: 6.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 301 RAHPAAGETVVSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPV- 379
Cdd:NF033858 257 RPADDDDEPAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIa 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 380 --HRVaaaG-VSRTFQhskLFNRLSALENVLVGAhlvsrptflrRLLWLPSARRDERaalehAARCLRRVGLGDLAGNRA 456
Cdd:NF033858 337 trRRV---GyMSQAFS---LYGELTVRQNLELHA----------RLFHLPAAEIAAR-----VAEMLERFDLADVADALP 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 457 SSLSYGDQRRLEIARALAAEPSLLILDEPAAGMNHVeA-----AQLSELIRslaQGGLTIlFIE-H--NVGmvlETCTRV 528
Cdd:NF033858 396 DSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPV-ArdmfwRLLIELSR---EDGVTI-FIStHfmNEA---ERCDRI 467
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502712709 529 VVLDFGEVIASGTPAEIAA-------DPAVIeAYLGTADDDPGGSSVADGTLADPTGGSGAPTP 585
Cdd:NF033858 468 SLMHAGRVLASDTPAALVAargaatlEEAFI-AYLEEAAGAAAAPAAAAAPAAAAAAPAAPAPA 530
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
325-570 |
9.91e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 98.65 E-value: 9.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 325 AVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRT-------PVHRvaAAGVSRTFQHSKLF 397
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTskqkeikPVRK--KVGVVFQFPESQLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 398 NRlSALENVLVGAHLVSrptflrrllwlPSARRDERAALEHaarcLRRVGLGDLAGNRAS-SLSYGDQRRLEIARALAAE 476
Cdd:PRK13643 99 EE-TVLKDVAFGPQNFG-----------IPKEKAEKIAAEK----LEMVGLADEFWEKSPfELSGGQMRRVAIAGILAME 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 477 PSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEIAADPAVIEAY- 555
Cdd:PRK13643 163 PEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEVDFLKAHe 242
|
250
....*....|....*
gi 502712709 556 LGTadddPGGSSVAD 570
Cdd:PRK13643 243 LGV----PKATHFAD 253
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
304-553 |
1.04e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 99.15 E-value: 1.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 304 PAAGETVVSLTGLA-----KEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIG-RT 377
Cdd:PRK13631 15 PLSDDIILRVKNLYcvfdeKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGdKK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 378 PVHRVAAAGVSRTFQHSKLFNRLSALENVLVGAHLVsRPTFLRRLLWLPSA--RRDERAAlEHAARCLRRVGLGDLAGNR 455
Cdd:PRK13631 95 NNHELITNPYSKKIKNFKELRRRVSMVFQFPEYQLF-KDTIEKDIMFGPVAlgVKKSEAK-KLAKFYLNKMGLDDSYLER 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 456 AS-SLSYGDQRRLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFG 534
Cdd:PRK13631 173 SPfGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKG 252
|
250
....*....|....*....
gi 502712709 535 EVIASGTPAEIAADPAVIE 553
Cdd:PRK13631 253 KILKTGTPYEIFTDQHIIN 271
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
315-539 |
1.37e-22 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 101.40 E-value: 1.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 315 GLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSS--GSATVLGTTIGRTPVHRVAAAGVSRTFQ 392
Cdd:NF040905 6 GITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEVCRFKDIRDSEALGIVIIHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 393 HSKLFNRLSALENVLVGAhlvsrptflrrllwlPSARR---DERAALEHAARCLRRVGLGDLAGNRASSLSYGDQRRLEI 469
Cdd:NF040905 86 ELALIPYLSIAENIFLGN---------------ERAKRgviDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 470 ARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIAS 539
Cdd:NF040905 151 AKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIET 220
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
326-540 |
1.68e-22 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 95.31 E-value: 1.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 326 VRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLgttIGRTPVHRVAAAGVSR-TFQHSKLFNRLSALE 404
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGVSGEVL---INGRPLDKRSFRKIIGyVPQDDILHPTLTVRE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 405 NVLVGAHLvsrptflrrllwlpsarrderaalehaarclrrvglgdlagnraSSLSYGDQRRLEIARALAAEPSLLILDE 484
Cdd:cd03213 102 TLMFAAKL--------------------------------------------RGLSGGERKRVSIALELVSNPSLLFLDE 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502712709 485 PAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNV-GMVLETCTRVVVLDFGEVIASG 540
Cdd:cd03213 138 PTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPsSEIFELFDKLLLLSQGRVIYFG 194
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
308-550 |
2.07e-22 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 99.72 E-value: 2.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 308 ETVVSLTGLAKeyggvhAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGR---TPVHRVAA 384
Cdd:PRK10070 32 EQILEKTGLSL------GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKisdAELREVRR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 385 AGVSRTFQHSKLFNRLSALENVLVGAHLVSrptflrrllwLPSARRDERAAlehaaRCLRRVGLGDLAGNRASSLSYGDQ 464
Cdd:PRK10070 106 KKIAMVFQSFALMPHMTVLDNTAFGMELAG----------INAEERREKAL-----DALRQVGLENYAHSYPDELSGGMR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 465 RRLEIARALAAEPSLLILDEPAAGMNHVEAAQLS-ELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPA 543
Cdd:PRK10070 171 QRVGLARALAINPDILLMDEAFSALDPLIRTEMQdELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPD 250
|
....*..
gi 502712709 544 EIAADPA 550
Cdd:PRK10070 251 EILNNPA 257
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
309-549 |
2.29e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 96.52 E-value: 2.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 309 TVVSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLV-----PPSSGSATVLGTTIGRTPVHRVA 383
Cdd:PRK14247 2 NKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIFKMDVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 384 AAgVSRTFQHSKLFNRLSALENVLVGAHLvsrptflRRLLwlpsarrDERAALEHAAR-CLRRVGLGDLAGNR----ASS 458
Cdd:PRK14247 82 RR-VQMVFQIPNPIPNLSIFENVALGLKL-------NRLV-------KSKKELQERVRwALEKAQLWDEVKDRldapAGK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 459 LSYGDQRRLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQgGLTILFIEHNVGMVLETCTRVVVLDFGEVIA 538
Cdd:PRK14247 147 LSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKK-DMTIVLVTHFPQQAARISDYVAFLYKGQIVE 225
|
250
....*....|.
gi 502712709 539 SGTPAEIAADP 549
Cdd:PRK14247 226 WGPTREVFTNP 236
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
330-557 |
3.20e-22 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 95.80 E-value: 3.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 330 DLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPvhrVAAAGVSRTFQHSKLFNRLSALENVLVG 409
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTP---PSRRPVSMLFQENNLFSHLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 410 AHlvsrptflrrllwlPSAR--RDERAALEHAArclRRVGLGDLAGNRASSLSYGDQRRLEIARALAAEPSLLILDEPAA 487
Cdd:PRK10771 96 LN--------------PGLKlnAAQREKLHAIA---RQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502712709 488 GMNHVEAAQLSELIRSL-AQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEIAADPAVIEAYLG 557
Cdd:PRK10771 159 ALDPALRQEMLTLVSQVcQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKASASALLG 229
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
325-547 |
5.06e-22 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 100.42 E-value: 5.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 325 AVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGT---TIGRTPVHRvaAAGVsrTFQHSKLFNRlS 401
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTdirTVTRASLRR--NIAV--VFQDAGLFNR-S 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 402 ALENVLVGAhlvsrptflrrllwlPSARRDE-RAALEHAAR---CLRRV-GLGDLAGNRASSLSYGDQRRLEIARALAAE 476
Cdd:PRK13657 425 IEDNIRVGR---------------PDATDEEmRAAAERAQAhdfIERKPdGYDTVVGERGRQLSGGERQRLAIARALLKD 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502712709 477 PSLLILDEPAAGMNHVEAAQLSELIRSLAQgGLTILFIEHNVGMVLETcTRVVVLDFGEVIASGTPAEIAA 547
Cdd:PRK13657 490 PPILILDEATSALDVETEAKVKAALDELMK-GRTTFIIAHRLSTVRNA-DRILVFDNGRVVESGSFDELVA 558
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
312-521 |
5.41e-22 |
|
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: 93.96 E-value: 5.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 312 SLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHR---VAAAGvs 388
Cdd:TIGR01189 2 AARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPhenILYLG-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 389 rtfQHSKLFNRLSALENVlvgahlvsrpTFLRRLLwlpsarRDERAALEHAarcLRRVGLGDLAGNRASSLSYGDQRRLE 468
Cdd:TIGR01189 80 ---HLPGLKPELSALENL----------HFWAAIH------GGAQRTIEDA---LAAVGLTGFEDLPAAQLSAGQQRRLA 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502712709 469 IARALAAEPSLLILDEPAAGMNHVEAAQLSELIRS-LAQGGLTILFIEHNVGMV 521
Cdd:TIGR01189 138 LARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAhLARGGIVLLTTHQDLGLV 191
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
308-578 |
6.74e-22 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 95.82 E-value: 6.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 308 ETVVSLTG--LAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIgrtpvHRVAAA 385
Cdd:PRK10253 3 ESVARLRGeqLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHI-----QHYASK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 386 GVSRTFqhsKLFNRLSALENVLVGAHLVSRPTFLRRLLWLPSARRDERAAlehaARCLRRVGLGDLAGNRASSLSYGDQR 465
Cdd:PRK10253 78 EVARRI---GLLAQNATTPGDITVQELVARGRYPHQPLFTRWRKEDEEAV----TKAMQATGITHLADQSVDTLSGGQRQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 466 RLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSL-AQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAE 544
Cdd:PRK10253 151 RAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKE 230
|
250 260 270
....*....|....*....|....*....|....*..
gi 502712709 545 IAAdPAVIEAYLG---TADDDPggssVADGTLADPTG 578
Cdd:PRK10253 231 IVT-AELIERIYGlrcMIIDDP----VAGTPLVVPLG 262
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
325-548 |
8.01e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 96.31 E-value: 8.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 325 AVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGS------------------ATVLGTTIGRTPVHRVAAA- 385
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTiewifkdeknkkktkekeKVLEKLVIQKTRFKKIKKIk 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 386 ------GVSRTFQHSKLFNRlSALENVLVGAhlVSRPTflrrllwlpsarrDERAALEHAARCLRRVGLGDLAGNRAS-S 458
Cdd:PRK13651 102 eirrrvGVVFQFAEYQLFEQ-TIEKDIIFGP--VSMGV-------------SKEEAKKRAAKYIELVGLDESYLQRSPfE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 459 LSYGDQRRLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIA 538
Cdd:PRK13651 166 LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIK 245
|
250
....*....|
gi 502712709 539 SGTPAEIAAD 548
Cdd:PRK13651 246 DGDTYDILSD 255
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
311-601 |
1.19e-21 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 96.71 E-value: 1.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 311 VSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRVAAAGVsrt 390
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMV--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 391 FQHSKLFNRLSALENVLVGAhlvsrptflrRLLWLPSARRDERA--ALEhaarclrrvgLGDLAG--NR-ASSLSYGDQR 465
Cdd:PRK11432 84 FQSYALFPHMSLGENVGYGL----------KMLGVPKEERKQRVkeALE----------LVDLAGfeDRyVDQISGGQQQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 466 RLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQG-GLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAE 544
Cdd:PRK11432 144 RVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQE 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502712709 545 IAADPA--VIEAYLGTAdddpggsSVADGTLADPT---GGSGAPTPDAVTNVDPSAAGTLDI 601
Cdd:PRK11432 224 LYRQPAsrFMASFMGDA-------NIFPATLSGDYvdiYGYRLPRPAAFAFNLPDGECTVGV 278
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
325-548 |
1.45e-21 |
|
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: 93.83 E-value: 1.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 325 AVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVH--RVAAAGVSrtfQHSKLFNRlSA 402
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLAslRRQIGLVS---QDVFLFND-TV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 403 LENVLVGAHLVSRptflrrllwlPSARRDERAALEHAARCLRRVGLGDLAGNRASSLSYGDQRRLEIARALAAEPSLLIL 482
Cdd:cd03251 93 AENIAYGRPGATR----------EEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILIL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502712709 483 DEPAAGMNHVEAAQLSELIRSLAQgGLTILFIEHNVGMVlETCTRVVVLDFGEVIASGTPAEIAAD 548
Cdd:cd03251 163 DEATSALDTESERLVQAALERLMK-NRTTFVIAHRLSTI-ENADRIVVLEDGKIVERGTHEELLAQ 226
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
309-536 |
1.78e-21 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 94.36 E-value: 1.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 309 TVVSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGsaTVLGttiGRTPVHRvAAAGVS 388
Cdd:PRK11247 11 TPLLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAG--ELLA---GTAPLAE-AREDTR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 389 RTFQHSKLFNRLSALENVLVGAhlvsrptflrRLLWLPSARRderaALEhaarclrRVGLGDLAGNRASSLSYGDQRRLE 468
Cdd:PRK11247 85 LMFQDARLLPWKKVIDNVGLGL----------KGQWRDAALQ----ALA-------AVGLADRANEWPAALSGGQKQRVA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502712709 469 IARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSL-AQGGLTILFIEHNVGMVLETCTRVVVLDFGEV 536
Cdd:PRK11247 144 LARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
287-531 |
2.23e-21 |
|
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: 97.74 E-value: 2.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 287 GPGSAADPAPRLAARAHPAAGET--------VVSLTGLAKEYGGV-HAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMIS 357
Cdd:TIGR02857 290 GVAAAEALFAVLDAAPRPLAGKApvtaapasSLEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLL 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 358 GLVPPSSGSATVLGTTIGRTPVH--RVAAAGVSrtfQHSKLFNRlSALENVLVGAHLVSrPTFLRRLLwlpsarrdERAA 435
Cdd:TIGR02857 370 GFVDPTEGSIAVNGVPLADADADswRDQIAWVP---QHPFLFAG-TIAENIRLARPDAS-DAEIREAL--------ERAG 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 436 LEHAARCLRRvGLGDLAGNRASSLSYGDQRRLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGlTILFIE 515
Cdd:TIGR02857 437 LDEFVAALPQ-GLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGR-TVLLVT 514
|
250
....*....|....*.
gi 502712709 516 HNVGmVLETCTRVVVL 531
Cdd:TIGR02857 515 HRLA-LAALADRIVVL 529
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
325-545 |
2.87e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 94.34 E-value: 2.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 325 AVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVH-RVAAAGVSRTFQHS--KLFNRls 401
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKlSDIRKKVGLVFQYPeyQLFEE-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 402 alenvlvgahlvsrpTFLRRLLWLPSAR-RDERAALEHAARCLRRVGLG--DLAGNRASSLSYGDQRRLEIARALAAEPS 478
Cdd:PRK13637 100 ---------------TIEKDIAFGPINLgLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502712709 479 LLILDEPAAGMNHVEAAQLSELIRSLAQG-GLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEI 545
Cdd:PRK13637 165 ILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREV 232
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
322-547 |
3.17e-21 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 92.93 E-value: 3.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 322 GVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRT-PVHRVAAAGVsrTFQHSKLFNRl 400
Cdd:cd03252 14 GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALAdPAWLRRQVGV--VLQENVLFNR- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 401 SALENVLVGahlvsRPTflrrllwlPSARRDERAAL---EHAARCLRRVGLGDLAGNRASSLSYGDQRRLEIARALAAEP 477
Cdd:cd03252 91 SIRDNIALA-----DPG--------MSMERVIEAAKlagAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502712709 478 SLLILDEPAAGMNH-VEAAQLSELIRSLAqgGLTILFIEHNVGMVlETCTRVVVLDFGEVIASGTPAEIAA 547
Cdd:cd03252 158 RILIFDEATSALDYeSEHAIMRNMHDICA--GRTVIIIAHRLSTV-KNADRIIVMEKGRIVEQGSHDELLA 225
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
325-554 |
4.05e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 93.93 E-value: 4.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 325 AVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIG-----------RTPVhrvaaaGVSRTFQH 393
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkknkklkplRKKV------GIVFQFPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 394 SKLFNRlsalenvlvgahlvsrpTFLRRLLWLPS---ARRDEraALEHAARCLRRVGLG-DLAGNRASSLSYGDQRRLEI 469
Cdd:PRK13634 96 HQLFEE-----------------TVEKDICFGPMnfgVSEED--AKQKAREMIELVGLPeELLARSPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 470 ARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQ-GGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEIAAD 548
Cdd:PRK13634 157 AGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKeKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFAD 236
|
....*.
gi 502712709 549 PAVIEA 554
Cdd:PRK13634 237 PDELEA 242
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
322-559 |
4.80e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 93.51 E-value: 4.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 322 GVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRVAAAGVSRTFQHSklfnrls 401
Cdd:PRK13644 14 GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVGIVFQNP------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 402 alENVLVGAHLVSRPTFLRRLLWLPSARRDERaalehAARCLRRVGLGDLAGNRASSLSYGDQRRLEIARALAAEPSLLI 481
Cdd:PRK13644 87 --ETQFVGRTVEEDLAFGPENLCLPPIEIRKR-----VDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502712709 482 LDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMvLETCTRVVVLDFGEVIASGTPAEIAADPAVieAYLGTA 559
Cdd:PRK13644 160 FDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVSL--QTLGLT 234
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
305-548 |
6.87e-21 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 96.27 E-value: 6.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 305 AAGETVVSLTGLAKEyggvhAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTI-GRTPVHRVA 383
Cdd:PRK15439 263 AAGAPVLTVEDLTGE-----GFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEInALSTAQRLA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 384 AAGV--SRTFQHSKLFnrlsaLENVL---VGAHLVSRPTFlrrllWLPSARrdERAALEHAARCLRrVGLGDlAGNRASS 458
Cdd:PRK15439 338 RGLVylPEDRQSSGLY-----LDAPLawnVCALTHNRRGF-----WIKPAR--ENAVLERYRRALN-IKFNH-AEQAART 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 459 LSYGDQRRLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIA 538
Cdd:PRK15439 404 LSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEISG 483
|
250
....*....|
gi 502712709 539 SGTPAEIAAD 548
Cdd:PRK15439 484 ALTGAAINVD 493
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
311-591 |
6.89e-21 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 94.42 E-value: 6.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 311 VSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTtlvnmiSGLVPpssgsATVLGTTIGRTPVHRVAAAGVSRT 390
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**------RGALP-----AHV*GPDAGRRPWRF*TWCANRRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 391 FQHSKLFNR---------LSALENVlvgaHLVSRPtflrrllwLPSARRDERAaleHAARCLRRVGLGDLAGNRASSLSY 461
Cdd:NF000106 83 LRRTIG*HRpvr*grresFSGRENL----YMIGR*--------LDLSRKDARA---RADELLERFSLTEAAGRAAAKYSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 462 GDQRRLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGT 541
Cdd:NF000106 148 GMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGK 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 502712709 542 PAEIAADPA-----VIEAYLGTADDDPGgsSVADGTLaDPTGGSGAPTPDAVTNV 591
Cdd:NF000106 228 VDELKTKVGgrtlqIRPAHAAELDRMVG--AIAQAGL-DGIAGATADHEDGVVNV 279
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
325-553 |
2.43e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 91.40 E-value: 2.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 325 AVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPP---SSGSATVLGTTIGRTPVHRVAAAgVSRTFQHSklfnrls 401
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIREK-VGIVFQNP------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 402 alENVLVGAHL------------VSRPTFLRRLlwlpsarrderaalehaARCLRRVGLGDLAGNRASSLSYGDQRRLEI 469
Cdd:PRK13640 94 --DNQFVGATVgddvafglenraVPRPEMIKIV-----------------RDVLADVGMLDYIDSEPANLSGGQKQRVAI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 470 ARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLA-QGGLTILFIEHNVGMVlETCTRVVVLDFGEVIASGTPAEIAAD 548
Cdd:PRK13640 155 AGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKkKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSK 233
|
....*
gi 502712709 549 PAVIE 553
Cdd:PRK13640 234 VEMLK 238
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
310-553 |
2.81e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 91.22 E-value: 2.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 310 VVSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRVA-AAGVS 388
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLAlRQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 389 RTFQHSklfnrlsalENVLVGAHLVSRPTFLRRLLWLPSArrderaalEHAARCLRRVGLGDLAGNRASS---LSYGDQR 465
Cdd:PRK13638 81 TVFQDP---------EQQIFYTDIDSDIAFSLRNLGVPEA--------EITRRVDEALTLVDAQHFRHQPiqcLSHGQKK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 466 RLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEI 545
Cdd:PRK13638 144 RVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEV 223
|
....*...
gi 502712709 546 AADPAVIE 553
Cdd:PRK13638 224 FACTEAME 231
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
332-555 |
2.88e-20 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 90.38 E-value: 2.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 332 EIRSGEVVGLIGPNGAGKTTLVNMISGLVPpSSGSATVLGTTIGRTPVHRVAaagVSRTF---QHSKLFNRlsalenvlv 408
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAAELA---RHRAYlsqQQTPPFAM--------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 409 gahlvsrPTFLRRLLWLPSARR--DERAALEHAARclrRVGLGDLAGNRASSLSYGDQRR-------LEIARALAAEPSL 479
Cdd:PRK03695 85 -------PVFQYLTLHQPDKTRteAVASALNEVAE---ALGLDDKLGRSVNQLSGGEWQRvrlaavvLQVWPDINPAGQL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502712709 480 LILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEIAADPAVIEAY 555
Cdd:PRK03695 155 LLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVF 230
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
329-560 |
4.06e-20 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 90.59 E-value: 4.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 329 VDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRVAAA--GVSRTFQHSKLFNRLSALENV 406
Cdd:PRK11831 26 ISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVrkRMSMLFQSGALFTDMNVFDNV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 407 lvgahlvSRPtfLRRLLWLPsarrderAALEHAARC--LRRVGLGDLAGNRASSLSYGDQRRLEIARALAAEPSLLILDE 484
Cdd:PRK11831 106 -------AYP--LREHTQLP-------APLLHSTVMmkLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDE 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502712709 485 PAAGMNHVEAAQLSELIRSLAQG-GLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEIAA--DPAVIEAYLGTAD 560
Cdd:PRK11831 170 PFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQAnpDPRVRQFLDGIAD 248
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
320-549 |
4.62e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 89.90 E-value: 4.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 320 YGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPS-----SGSATVLGTTIGRTPVHRVAA-AGVSRTFQH 393
Cdd:PRK14267 14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDVDPIEVrREVGMVFQY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 394 SKLFNRLSALENVLVGAHLVSrptflrrlLWLPSARRDERaaLEHAarcLRRVGLGDLAGNR----ASSLSYGDQRRLEI 469
Cdd:PRK14267 94 PNPFPHLTIYDNVAIGVKLNG--------LVKSKKELDER--VEWA---LKKAALWDEVKDRlndyPSNLSGGQRQRLVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 470 ARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQgGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEIAADP 549
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKK-EYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENP 239
|
|
| livM |
PRK11301 |
leucine/isoleucine/valine transporter permease subunit; Provisional |
64-242 |
4.85e-20 |
|
leucine/isoleucine/valine transporter permease subunit; Provisional
Pssm-ID: 236896 [Multi-domain] Cd Length: 419 Bit Score: 92.72 E-value: 4.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 64 TAVVIGMAVGAVASVVLGLPTMHLRGVFLAIATLGFAEAVRVVLLN-QEWTGGAQGLA-VPRILTVGMAWT--------- 132
Cdd:PRK11301 166 ECLPIAGLMAALFGFLLGFPVLRLRGDYLAIVTLGFGEIIRILLLNnTEITGGPNGISqIPKPTLFGLEFSrtareggwd 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 133 ------------------------ALAVVAYWFW-RMGRSRYGRALEAIREDELAARSMGIDVGRHRLAAFVTSGAVAGL 187
Cdd:PRK11301 246 tfheffglkydpsdrviflylvalLLVVLTLFVInRLLRMPLGRAWEALREDEIACRSLGLNPTRIKLSAFTIGAAFAGF 325
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502712709 188 YGVLFAYYVRLIAPSDFDFTAAVDGLVTAVVGGSTMFLGPILGSGFQTMIPEIQR 242
Cdd:PRK11301 326 AGTFFAARQGFVSPESFTFIESAFILAIVVLGGMGSQFGVILAAILLVVLPELMR 380
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
324-546 |
5.43e-20 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 93.96 E-value: 5.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 324 HAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPS---SGSATVLGTTIGRTPVHRVAAAgvsrTFQHSKLFNRL 400
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKEMRAISAY----VQQDDLFIPTL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 401 SALENVLVGAHLvsrptflRRLLWLPSARRDERAAlehaaRCLRRVGLGDLA------GNRASSLSYGDQRRLEIARALA 474
Cdd:TIGR00955 115 TVREHLMFQAHL-------RMPRRVTKKEKRERVD-----EVLQALGLRKCAntrigvPGRVKGLSGGERKRLAFASELL 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502712709 475 AEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLT-ILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEIA 546
Cdd:TIGR00955 183 TDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTiICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQAV 255
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
308-532 |
5.96e-20 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 89.03 E-value: 5.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 308 ETVVSLTGLAKEY-----GGV--HAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVL----GTTIGR 376
Cdd:COG4778 2 TTLLEVENLSKTFtlhlqGGKrlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 377 TPVHRVAAA-----G-VSrtfQHSKLFNRLSALEnvlvgahLVSRPtfLRRLLWlpsarrDERAALEHAARCLRRVGLGD 450
Cdd:COG4778 82 ASPREILALrrrtiGyVS---QFLRVIPRVSALD-------VVAEP--LLERGV------DREEARARARELLARLNLPE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 451 -LAGNRASSLSYGDQRRLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVV 529
Cdd:COG4778 144 rLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVV 223
|
...
gi 502712709 530 VLD 532
Cdd:COG4778 224 DVT 226
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
310-547 |
6.74e-20 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 94.42 E-value: 6.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 310 VVSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIgRTPVHRVAAA---- 385
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDM-ADARHRRAVCpria 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 386 ----GVSRTfqhskLFNRLSALENVlvgahlvsrpTFLRRLLWLPSARRDERaalehAARCLRRVGLGDLAGNRASSLSY 461
Cdd:NF033858 80 ympqGLGKN-----LYPTLSVFENL----------DFFGRLFGQDAAERRRR-----IDELLRATGLAPFADRPAGKLSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 462 GDQRRLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSL--AQGGLTIL----FIEHnvgmvLETCTRVVVLDFGE 535
Cdd:NF033858 140 GMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIraERPGMSVLvataYMEE-----AERFDWLVAMDAGR 214
|
250
....*....|..
gi 502712709 536 VIASGTPAEIAA 547
Cdd:NF033858 215 VLATGTPAELLA 226
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
303-580 |
1.44e-19 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 88.69 E-value: 1.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 303 HPAAGETVVSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRtpvhrv 382
Cdd:PRK10575 4 YTNHSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLES------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 383 aaagvsrtfQHSKLFNR--------LSALENVLVgAHLVSrptfLRRLLWLPSARRDERAALEHAARCLRRVGLGDLAGN 454
Cdd:PRK10575 78 ---------WSSKAFARkvaylpqqLPAAEGMTV-RELVA----IGRYPWHGALGRFGAADREKVEEAISLVGLKPLAHR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 455 RASSLSYGDQRRLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQG-GLTILFIEHNVGMVLETCTRVVVLDF 533
Cdd:PRK10575 144 LVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRG 223
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 502712709 534 GEVIASGTPAEIaADPAVIEAYLGtadddpggssVADGTLADPTGGS 580
Cdd:PRK10575 224 GEMIAQGTPAEL-MRGETLEQIYG----------IPMGILPHPAGAA 259
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
312-549 |
1.76e-19 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 88.44 E-value: 1.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 312 SLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRVAAAG---VS 388
Cdd:PRK11701 8 SVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSEAErrrLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 389 RT---FQHSklfNRLSALE-NVLVGAHLVSRptflrrlLWLPSAR--RDERAAlehAARCLRRVglgDLAGNR----ASS 458
Cdd:PRK11701 88 RTewgFVHQ---HPRDGLRmQVSAGGNIGER-------LMAVGARhyGDIRAT---AGDWLERV---EIDAARiddlPTT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 459 LSYGDQRRLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSL-AQGGLTILFIEHNVGMVLETCTRVVVLDFGEVI 537
Cdd:PRK11701 152 FSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVV 231
|
250
....*....|..
gi 502712709 538 ASGTPAEIAADP 549
Cdd:PRK11701 232 ESGLTDQVLDDP 243
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
312-536 |
1.93e-19 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 86.12 E-value: 1.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 312 SLTGLAKEYGGVHA--VRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRtpvhrvaaagvsr 389
Cdd:cd03246 2 EVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQ------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 390 tfqhsklfnrlsalenvlvgahlvsrptflrrllWLPSARRDERAALehaarcLRRVGL--GDLAGNrasSLSYGDQRRL 467
Cdd:cd03246 69 ----------------------------------WDPNELGDHVGYL------PQDDELfsGSIAEN---ILSGGQRQRL 105
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502712709 468 EIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGmVLETCTRVVVLDFGEV 536
Cdd:cd03246 106 GLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPE-TLASADRILVLEDGRV 173
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
328-545 |
3.37e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 87.20 E-value: 3.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 328 GVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVpPSSGSATVLGTTIGRTPVHRVAaagVSRTF--QHSklfnrlSALEN 405
Cdd:COG4138 14 PISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELA---RHRAYlsQQQ------SPPFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 406 VLVGAHLVsrptflrrlLWLPSARRDERAALEHAARClRRVGLGDLAGNRASSLSYGDQRRLEIARAL-----AAEPS-- 478
Cdd:COG4138 84 MPVFQYLA---------LHQPAGASSEAVEQLLAQLA-EALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwpTINPEgq 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502712709 479 LLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEI 545
Cdd:COG4138 154 LLLLDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEV 220
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
316-536 |
3.45e-19 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 86.85 E-value: 3.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 316 LAKEY-GGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRVA--AAGVSRTFQ 392
Cdd:PRK10908 7 VSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPflRRQIGMIFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 393 HSKLFNRLSALENVLVGAHLVSRPTflrrllwlPSARRDERAALEhaarclrRVGLGDLAGNRASSLSYGDQRRLEIARA 472
Cdd:PRK10908 87 DHHLLMDRTVYDNVAIPLIIAGASG--------DDIRRRVSAALD-------KVGLLDKAKNFPIQLSGGEQQRVGIARA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502712709 473 LAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEV 536
Cdd:PRK10908 152 VVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
326-549 |
3.48e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 87.41 E-value: 3.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 326 VRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVP------PSSGSATVLGTTIGRTPVHRVAAAgVSRTFQHSKLFNR 399
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLRKE-VGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 400 LSALENVL--VGAHLVsrptflrrllwlpsarRDERAALEHAARCLRRVGLGDLAGNR----ASSLSYGDQRRLEIARAL 473
Cdd:PRK14246 105 LSIYDNIAypLKSHGI----------------KEKREIKKIVEECLRKVGLWKEVYDRlnspASQLSGGQQQRLTIARAL 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502712709 474 AAEPSLLILDEPAAGMNHVEAAQLSELIRSLaQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEIAADP 549
Cdd:PRK14246 169 ALKPKVLLMDEPTSMIDIVNSQAIEKLITEL-KNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSP 243
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
321-550 |
5.09e-19 |
|
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: 90.51 E-value: 5.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 321 GGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPS----SGSATVLGTTIGRTPVH---RVAAAGVSRTFQH 393
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPaahpSGSILFDGQDLLGLSERelrRIRGNRIAMIFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 394 SklfnrLSALeNVL--VGAHlVSRPTFLRRLLwlpsarrDERAALEHAARCLRRVGLGDlAGNRASS----LSYGDQRRL 467
Cdd:COG4172 101 P-----MTSL-NPLhtIGKQ-IAEVLRLHRGL-------SGAAARARALELLERVGIPD-PERRLDAyphqLSGGQRQRV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 468 EIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSL-AQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEIA 546
Cdd:COG4172 166 MIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLqRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELF 245
|
....
gi 502712709 547 ADPA 550
Cdd:COG4172 246 AAPQ 249
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
315-521 |
5.54e-19 |
|
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: 85.62 E-value: 5.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 315 GLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRtpVHRVAAAGVSRTFQHS 394
Cdd:cd03231 5 ELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDF--QRDSIARGLLYLGHAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 395 KLFNRLSALENVlvgahlvsrpTFLRRLlwlpsarrDERAALEHAarcLRRVGLGDLAGNRASSLSYGDQRRLEIARALA 474
Cdd:cd03231 83 GIKTTLSVLENL----------RFWHAD--------HSDEQVEEA---LARVGLNGFEDRPVAQLSAGQQRRVALARLLL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 502712709 475 AEPSLLILDEPAAGMNHVEAAQLSELIRS-LAQGGLTILFIEHNVGMV 521
Cdd:cd03231 142 SGRPLWILDEPTTALDKAGVARFAEAMAGhCARGGMVVLTTHQDLGLS 189
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
314-512 |
9.16e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 84.93 E-value: 9.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 314 TGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIgRTPVHRVAAAGVSrtfqH 393
Cdd:PRK13539 6 EDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI-DDPDVAEACHYLG----H 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 394 SKLFNR-LSALENVlvgahlvsrpTFLRRLLwlpsarrdeRAALEHAARCLRRVGLGDLAGNRASSLSYGDQRRLEIARA 472
Cdd:PRK13539 81 RNAMKPaLTVAENL----------EFWAAFL---------GGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 502712709 473 LAAEPSLLILDEPAAGMNHVEAAQLSELIRS-LAQGGLTIL 512
Cdd:PRK13539 142 LVSNRPIWILDEPTAALDAAAVALFAELIRAhLAQGGIVIA 182
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
324-550 |
9.43e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 89.76 E-value: 9.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 324 HAVRGVDLEIRSGEVVGLIGPNGAGKTT----LVNMIsglvpPSSGSATVLGTtigrtPVH---RVAAAGVSRTFQ---- 392
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQ-----PLHnlnRRQLLPVRHRIQvvfq 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 393 --HSKLFNRLSALENVLVGAHlVSRPTflrrllwLPSARRDERAAlehaaRCLRRVGLGDLAGNR-ASSLSYGDQRRLEI 469
Cdd:PRK15134 370 dpNSSLNPRLNVLQIIEEGLR-VHQPT-------LSAAQREQQVI-----AVMEEVGLDPETRHRyPAEFSGGQRQRIAI 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 470 ARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQG-GLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEIAAD 548
Cdd:PRK15134 437 ARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAA 516
|
..
gi 502712709 549 PA 550
Cdd:PRK15134 517 PQ 518
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
308-518 |
1.03e-18 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 85.60 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 308 ETVVSLTGLAKEYG-GVHAV---RGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRVA 383
Cdd:PRK10584 4 ENIVEVHHLKKSVGqGEHELsilTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 384 ---AAGVSRTFQHSKLFNRLSALENVLVgahlvsrPTFLRRllwlpsarRDERAALEHAARCLRRVGLGDLAGNRASSLS 460
Cdd:PRK10584 84 klrAKHVGFVFQSFMLIPTLNALENVEL-------PALLRG--------ESSRQSRNGAKALLEQLGLGKRLDHLPAQLS 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502712709 461 YGDQRRLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQG-GLTILFIEHNV 518
Cdd:PRK10584 149 GGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDL 207
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
312-546 |
1.03e-18 |
|
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: 84.50 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 312 SLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGL--VPPSSGSATVLGTTIGRTPVHRVAAAGVSR 389
Cdd:cd03217 2 EIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERARLGIFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 390 TFQHSklfnrlSALENVLVGahlvsrpTFlrrllwlpsarrderaalehaarcLRRVGLGdlagnrassLSYGDQRRLEI 469
Cdd:cd03217 82 AFQYP------PEIPGVKNA-------DF------------------------LRYVNEG---------FSGGEKKRNEI 115
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502712709 470 ARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNvGMVLETC--TRVVVLDFGEVIASGtPAEIA 546
Cdd:cd03217 116 LQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHY-QRLLDYIkpDRVHVLYDGRIVKSG-DKELA 192
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
327-512 |
2.17e-18 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 83.70 E-value: 2.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 327 RGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTI--GRTPVHRVA-----AAGVSRtfqhsklfnR 399
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIrrQRDEYHQDLlylghQPGIKT---------E 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 400 LSALENVlvgahlvsrpTFLRRLlwlpsARRDERAALEHAarcLRRVGLG---DLAgnrASSLSYGDQRRLEIARALAAE 476
Cdd:PRK13538 89 LTALENL----------RFYQRL-----HGPGDDEALWEA---LAQVGLAgfeDVP---VRQLSAGQQRRVALARLWLTR 147
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 502712709 477 PSLLILDEP-----AAGMnhveaAQLSELIRS-LAQGGLTIL 512
Cdd:PRK13538 148 APLWILDEPftaidKQGV-----ARLEALLAQhAEQGGMVIL 184
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
325-549 |
3.32e-18 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 85.91 E-value: 3.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 325 AVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTI-GRTPVH-RVAAAGVSRTFQhsklfNRLSA 402
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLlGMKDDEwRAVRSDIQMIFQ-----DPLAS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 403 LENVLVGAHLVSRPtfLRrlLWLPSARRDEraALEHAARCLRRVGLGDLAGNR-ASSLSYGDQRRLEIARALAAEPSLLI 481
Cdd:PRK15079 111 LNPRMTIGEIIAEP--LR--TYHPKLSRQE--VKDRVKAMMLKVGLLPNLINRyPHEFSGGQCQRIGIARALILEPKLII 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502712709 482 LDEPAAGMNHVEAAQLSELIRSL-AQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEIAADP 549
Cdd:PRK15079 185 CDEPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 253
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
321-549 |
7.02e-18 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 84.96 E-value: 7.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 321 GGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSsgsATVlgtTIGR-----------TPVHRVAAAG--V 387
Cdd:COG4170 18 GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDN---WHV---TADRfrwngidllklSPRERRKIIGreI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 388 SRTFQHSklfnrLSALE-NVLVGAHLV-SRPT-FLRRLLWlpsARRDERAalEHAARCLRRVGLGDLAGNRAS---SLSY 461
Cdd:COG4170 92 AMIFQEP-----SSCLDpSAKIGDQLIeAIPSwTFKGKWW---QRFKWRK--KRAIELLHRVGIKDHKDIMNSyphELTE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 462 GDQRRLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQ-GGLTILFIEHNVGMVLETCTRVVVLDFGEVIASG 540
Cdd:COG4170 162 GECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDLESISQWADTITVLYCGQTVESG 241
|
....*....
gi 502712709 541 TPAEIAADP 549
Cdd:COG4170 242 PTEQILKSP 250
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
310-541 |
7.56e-18 |
|
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: 88.15 E-value: 7.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 310 VVSLTGLAKEYGGVH--AVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIgrtpvhrvaAAGV 387
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI---------LTNI 2007
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 388 SRTFQHSKLFNRLSALENVLVG-AHLVsrptFLRRLLWLPsARRDERAAlehaARCLRRVGLGDLAGNRASSLSYGDQRR 466
Cdd:TIGR01257 2008 SDVHQNMGYCPQFDAIDDLLTGrEHLY----LYARLRGVP-AEEIEKVA----NWSIQSLGLSLYADRLAGTYSGGNKRK 2078
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502712709 467 LEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGT 541
Cdd:TIGR01257 2079 LSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGT 2153
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
301-542 |
7.62e-18 |
|
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: 88.15 E-value: 7.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 301 RAHPA--AGETVVSLTGLAKEYGGvHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIgRTP 378
Cdd:TIGR01257 920 RELPGlvPGVCVKNLVKIFEPSGR-PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETN 997
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 379 VHRVAAAgVSRTFQHSKLFNRLSALENVLVGAHLvsrptflrrllwlpSARRDERAALEHAARcLRRVGLGDLAGNRASS 458
Cdd:TIGR01257 998 LDAVRQS-LGMCPQHNILFHHLTVAEHILFYAQL--------------KGRSWEEAQLEMEAM-LEDTGLHHKRNEEAQD 1061
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 459 LSYGDQRRLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLaQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIA 538
Cdd:TIGR01257 1062 LSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIISQGRLYC 1140
|
....
gi 502712709 539 SGTP 542
Cdd:TIGR01257 1141 SGTP 1144
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
325-553 |
8.42e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 83.89 E-value: 8.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 325 AVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVhRVAAAGVSRTFQHSklfnrlsalE 404
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENL-KEIRKKIGIIFQNP---------D 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 405 NVLVGAHLVSRPTF-L--RRLlwlpsARRDERAALEHAARclrRVGLGDLAGNRASSLSYGDQRRLEIARALAAEPSLLI 481
Cdd:PRK13632 94 NQFIGATVEDDIAFgLenKKV-----PPKKMKDIIDDLAK---KVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIII 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502712709 482 LDEPAAGMNHVEAAQLSELIRSLA-QGGLTILFIEHNVGMVLEtCTRVVVLDFGEVIASGTPAEIAADPAVIE 553
Cdd:PRK13632 166 FDESTSMLDPKGKREIKKIMVDLRkTRKKTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKPKEILNNKEILE 237
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
325-545 |
8.45e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 83.98 E-value: 8.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 325 AVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLG---TTIGRTPVHRVAAAGVsrtFQHSKlfNRLS 401
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtSDEENLWDIRNKAGMV---FQNPD--NQIV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 402 AL---ENVLVGA-HLVSRPTFLRrllwlpsARRDEraalehaarCLRRVGLGDLAGNRASSLSYGDQRRLEIARALAAEP 477
Cdd:PRK13633 100 ATiveEDVAFGPeNLGIPPEEIR-------ERVDE---------SLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502712709 478 SLLILDEPAAGMNHVEAAQLSELIRSL-AQGGLTILFIEHNVGMVLETcTRVVVLDFGEVIASGTPAEI 545
Cdd:PRK13633 164 ECIIFDEPTAMLDPSGRREVVNTIKELnKKYGITIILITHYMEEAVEA-DRIIVMDSGKVVMEGTPKEI 231
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
291-517 |
1.22e-17 |
|
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: 86.26 E-value: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 291 AADPAPRLAARAHPAAGETVVSLTGL------AKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSS 364
Cdd:TIGR02868 310 VLDAAGPVAEGSAPAAGAVGLGKPTLelrdlsAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQ 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 365 GSATVLGTTIGRTPVHRVAAAgVSRTFQHSKLFNRlSALENVLVGahlvsRPTflrrllwlpsarrderAALEHAARCLR 444
Cdd:TIGR02868 390 GEVTLDGVPVSSLDQDEVRRR-VSVCAQDAHLFDT-TVRENLRLA-----RPD----------------ATDEELWAALE 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 445 RVGLGDLA-----------GNRASSLSYGDQRRLEIARALAAEPSLLILDEPAAgmnHVEAAQLSELIRSLAQG--GLTI 511
Cdd:TIGR02868 447 RVGLADWLralpdgldtvlGEGGARLSGGERQRLALARALLADAPILLLDEPTE---HLDAETADELLEDLLAAlsGRTV 523
|
....*.
gi 502712709 512 LFIEHN 517
Cdd:TIGR02868 524 VLITHH 529
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
293-547 |
1.36e-17 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 86.31 E-value: 1.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 293 DPAPRL-AARAHPAAGETVVSLTGLAKEYGG--VHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATV 369
Cdd:TIGR02203 312 DSPPEKdTGTRAIERARGDVEFRNVTFRYPGrdRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 370 LGTTIGRTPVhRVAAAGVSRTFQHSKLFNRLSAlENVLVGahlvsrptflrRLLWLPSARRDERAALEHAARCLRRV--G 447
Cdd:TIGR02203 392 DGHDLADYTL-ASLRRQVALVSQDVVLFNDTIA-NNIAYG-----------RTEQADRAEIERALAAAYAQDFVDKLplG 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 448 LGDLAGNRASSLSYGDQRRLEIARALAAEPSLLILDEPAAGMN-----HVEAAqLSELIRslaqgGLTILFIEHNVGMVl 522
Cdd:TIGR02203 459 LDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDneserLVQAA-LERLMQ-----GRTTLVIAHRLSTI- 531
|
250 260
....*....|....*....|....*
gi 502712709 523 ETCTRVVVLDFGEVIASGTPAEIAA 547
Cdd:TIGR02203 532 EKADRIVVMDDGRIVERGTHNELLA 556
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
311-547 |
1.50e-17 |
|
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: 86.01 E-value: 1.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 311 VSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGL--VPPSSG----------------------- 365
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGriiyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 366 SATVLGTTIG-------------RTPVHRVAAAGVSRTFqhsKLFNRLSALENVLVGahlvsrptflrrllwLPSARRDE 432
Cdd:TIGR03269 81 PCPVCGGTLEpeevdfwnlsdklRRRIRKRIAIMLQRTF---ALYGDDTVLDNVLEA---------------LEEIGYEG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 433 RAALEHAARCLRRVGLGDLAGNRASSLSYGDQRRLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQG-GLTI 511
Cdd:TIGR03269 143 KEAVGRAVDLIEMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKAsGISM 222
|
250 260 270
....*....|....*....|....*....|....*.
gi 502712709 512 LFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEIAA 547
Cdd:TIGR03269 223 VLTSHWPEVIEDLSDKAIWLENGEIKEEGTPDEVVA 258
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
325-542 |
2.47e-17 |
|
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: 81.39 E-value: 2.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 325 AVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVH--RVAAAGVSR---TFQHSKLFN- 398
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHdlRSRISIIPQdpvLFSGTIRSNl 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 399 ----------RLSALENVLVGAHLVSRPTflrrllwlpsarrderaalehaarclrrvGLGDLAGNRASSLSYGdQRRL- 467
Cdd:cd03244 99 dpfgeysdeeLWQALERVGLKEFVESLPG-----------------------------GLDTVVEEGGENLSVG-QRQLl 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502712709 468 EIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSlAQGGLTILFIEHNVGMVLEtCTRVVVLDFGEVIASGTP 542
Cdd:cd03244 149 CLARALLRKSKILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFDSP 221
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
309-552 |
3.51e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 81.70 E-value: 3.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 309 TVVSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGsatvlgtTIGRTPVHRVAaagvs 388
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEG-------VIKRNGKLRIG----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 389 rtFQHSKLfnrlsalenvlvgaHL-VSRPTFLRRLLWL-PSARRDEraalehAARCLRRVGLGDLAGNRASSLSYGDQRR 466
Cdd:PRK09544 71 --YVPQKL--------------YLdTTLPLTVNRFLRLrPGTKKED------ILPALKRVQAGHLIDAPMQKLSGGETQR 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 467 LEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQG-GLTILFIEHNVGMVLETCTRVVVLDfGEVIASGTPAEI 545
Cdd:PRK09544 129 VLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLN-HHICCSGTPEVV 207
|
....*..
gi 502712709 546 AADPAVI 552
Cdd:PRK09544 208 SLHPEFI 214
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
323-549 |
4.22e-17 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 81.76 E-value: 4.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 323 VHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSatvlgTTIGRTPVH----RVAAAGVSRTFQHSKlfN 398
Cdd:PRK15112 26 VEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGE-----LLIDDHPLHfgdySYRSQRIRMIFQDPS--T 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 399 RLSALENVlvgAHLVSRPtfLRRLLWLPSARRDERAALehaarCLRRVGL-GDLAGNRASSLSYGDQRRLEIARALAAEP 477
Cdd:PRK15112 99 SLNPRQRI---SQILDFP--LRLNTDLEPEQREKQIIE-----TLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRP 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502712709 478 SLLILDEPAAGMNHVEAAQLSELIRSLAQG-GLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEIAADP 549
Cdd:PRK15112 169 KVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASP 241
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
313-554 |
5.20e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 84.78 E-value: 5.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 313 LTGLAKEY----GGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIgrTPVHRVAAAGVS 388
Cdd:PRK10535 7 LKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDV--ATLDADALAQLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 389 R-----TFQHSKLFNRLSALENVLVGAHLVSrptflrrllwLPSARRDERA-ALehaarcLRRVGLGDLAGNRASSLSYG 462
Cdd:PRK10535 85 RehfgfIFQRYHLLSHLTAAQNVEVPAVYAG----------LERKQRLLRAqEL------LQRLGLEDRVEYQPSQLSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 463 DQRRLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNvGMVLETCTRVVVLDFGEVIaSGTP 542
Cdd:PRK10535 149 QQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRDGEIV-RNPP 226
|
250
....*....|..
gi 502712709 543 AEIAADPAVIEA 554
Cdd:PRK10535 227 AQEKVNVAGGTE 238
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
324-540 |
5.63e-17 |
|
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: 78.89 E-value: 5.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 324 HAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSatvlgTTIGRTPVHRVAAAgVSRTF----QHSKLFNR 399
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGE-----ITLDGVPVSDLEKA-LSSLIsvlnQRPYLFDT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 400 lSALENVlvgahlvsrptflrrllwlpsarrderaalehaarclrrvglgdlaGNRassLSYGDQRRLEIARALAAEPSL 479
Cdd:cd03247 90 -TLRNNL----------------------------------------------GRR---FSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502712709 480 LILDEPAAGMNHVEAAQLSELIRSLAQGGlTILFIEHN-VGMvlETCTRVVVLDFGEVIASG 540
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKDK-TLIWITHHlTGI--EHMDKILFLENGKIIMQG 178
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
316-518 |
1.07e-16 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 79.86 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 316 LAKEY--GGVHA--VRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRVAAA-----G 386
Cdd:PRK11629 11 LCKRYqeGSVQTdvLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELrnqklG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 387 VSRTFQHskLFNRLSALENVlvgahlvSRPtflrrlLWLPSARRDEraALEHAARCLRRVGLGDLAGNRASSLSYGDQRR 466
Cdd:PRK11629 91 FIYQFHH--LLPDFTALENV-------AMP------LLIGKKKPAE--INSRALEMLAAVGLEHRANHRPSELSGGERQR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502712709 467 LEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSL-AQGGLTILFIEHNV 518
Cdd:PRK11629 154 VAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDL 206
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
330-583 |
1.48e-16 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 82.76 E-value: 1.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 330 DLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATvlgttigrtpvhrvaaagvsRTFQHSklfNRLSaLENVlvg 409
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQ--------------------SQFSHI---TRLS-FEQL--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 410 AHLVSRpTFLRRLLWLPSARRDE--RAALE-------HAARCLR---RVGLGDLAGNRASSLSYGDQRRLEIARALAAEP 477
Cdd:PRK10938 76 QKLVSD-EWQRNNTDMLSPGEDDtgRTTAEiiqdevkDPARCEQlaqQFGITALLDRRFKYLSTGETRKTLLCQALMSEP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 478 SLLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEIAADPAVIE-AYL 556
Cdd:PRK10938 155 DLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQALVAQlAHS 234
|
250 260
....*....|....*....|....*..
gi 502712709 557 GTADDDPggSSVADGTLADPTGGSGAP 583
Cdd:PRK10938 235 EQLEGVQ--LPEPDEPSARHALPANEP 259
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
326-521 |
1.78e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 79.70 E-value: 1.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 326 VRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSS-----GSATVLGTTI--GRTPVHRVAAAgVSRTFQHSKLFN 398
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyeRRVNLNRLRRQ-VSMVHPKPNLFP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 399 rLSALENVLVGAHLVSrptflrrllWLPSARRDEraALEHAarcLRRVGLGDLAGNR----ASSLSYGDQRRLEIARALA 474
Cdd:PRK14258 102 -MSVYDNVAYGVKIVG---------WRPKLEIDD--IVESA---LKDADLWDEIKHKihksALDLSGGQQQRLCIARALA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 502712709 475 AEPSLLILDEPAAGMNHVEAAQLSELIRSLA-QGGLTILFIEHNVGMV 521
Cdd:PRK14258 167 VKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLHQV 214
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
302-518 |
1.91e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 79.83 E-value: 1.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 302 AHPAAGETVVSLT-GLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLV---NMISGLVPP--SSGSATVLGTTIG 375
Cdd:PRK14243 1 TSTLNGTETVLRTeNLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILrcfNRLNDLIPGfrVEGKVTFHGKNLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 376 RTPVHRVAA-AGVSRTFQHSKLFNRlSALENVLVGAHLVSRPTFLRRLLwlpsarrdERAalehaarcLRRVGLGDLAGN 454
Cdd:PRK14243 81 APDVDPVEVrRRIGMVFQKPNPFPK-SIYDNIAYGARINGYKGDMDELV--------ERS--------LRQAALWDEVKD 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502712709 455 R----ASSLSYGDQRRLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQgGLTILFIEHNV 518
Cdd:PRK14243 144 KlkqsGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKE-QYTIIIVTHNM 210
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
326-559 |
1.93e-16 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 79.87 E-value: 1.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 326 VRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPS--SGSATVLG-TTIGRTPVHRVAAAgvsrtfqhsklfnRLSA 402
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaPRGARVTGdVTLNGEPLAAIDAP-------------RLAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 403 LENVLVGAHLVSRPTFLRRLLWL---PSARR---DERAALEHAARCLRRVGLGDLAGNRASSLSYGDQRRLEIARALA-- 474
Cdd:PRK13547 84 LRAVLPQAAQPAFAFSAREIVLLgryPHARRagaLTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAql 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 475 -------AEPSLLILDEPAAGMNHVEAAQLSELIRSLAQG-GLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEIA 546
Cdd:PRK13547 164 wpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVL 243
|
250
....*....|...
gi 502712709 547 AdPAVIEAYLGTA 559
Cdd:PRK13547 244 T-PAHIARCYGFA 255
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
311-532 |
2.22e-16 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 76.33 E-value: 2.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 311 VSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGsatvlgtTIGRTPVHRVAaagvsrT 390
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEG-------IVTWGSTVKIG------Y 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 391 FQHsklfnrlsalenvlvgahlvsrptflrrllwlpsarrderaalehaarclrrvglgdlagnrassLSYGDQRRLEIA 470
Cdd:cd03221 68 FEQ-----------------------------------------------------------------LSGGEKMRLALA 82
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502712709 471 RALAAEPSLLILDEPAagmNH--VEA-AQLSELIRSLaQGglTILFIEHNVGMVLETCTRVVVLD 532
Cdd:cd03221 83 KLLLENPNLLLLDEPT---NHldLESiEALEEALKEY-PG--TVILVSHDRYFLDQVATKIIELE 141
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
313-539 |
2.75e-16 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 81.70 E-value: 2.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 313 LTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRVAAAGVSRTFQ 392
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 393 HSKLFNRLSALENVLVGAHlvsrPT---FLrrllwlpsarrDERAALEHAARCLRRVGLGDLAGNRASSLSYGDQRRLEI 469
Cdd:PRK10982 81 ELNLVLQRSVMDNMWLGRY----PTkgmFV-----------DQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEI 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 470 ARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIAS 539
Cdd:PRK10982 146 AKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIAT 215
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
326-547 |
2.88e-16 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 82.10 E-value: 2.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 326 VRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSA------------TVLGTTIGRTPvhrvaaagvsrtfQH 393
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVrldgadlsqwdrEELGRHIGYLP-------------QD 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 394 SKLFNRLSAlENVlvgahlvsrptflrrllwlpsARRDE--RAALEHAArclRRVGLGDL-----------AGNRASSLS 460
Cdd:COG4618 415 VELFDGTIA-ENI---------------------ARFGDadPEKVVAAA---KLAGVHEMilrlpdgydtrIGEGGARLS 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 461 YGDQRRLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGmVLETCTRVVVLDFGEVIASG 540
Cdd:COG4618 470 GGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPS-LLAAVDKLLVLRDGRVQAFG 548
|
....*..
gi 502712709 541 TPAEIAA 547
Cdd:COG4618 549 PRDEVLA 555
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
322-540 |
3.22e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 79.16 E-value: 3.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 322 GVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIgRTPVHRVAAAGVSRTFQHSKLFNRLs 401
Cdd:PRK15056 19 GHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPT-RQALQKNLVAYVPQSEEVDWSFPVL- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 402 aLENVLvgahLVSRptfLRRLLWLPSARRDERAALEHAarcLRRVGLGDLAGNRASSLSYGDQRRLEIARALAAEPSLLI 481
Cdd:PRK15056 97 -VEDVV----MMGR---YGHMGWLRRAKKRDRQIVTAA---LARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVIL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502712709 482 LDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDfGEVIASG 540
Cdd:PRK15056 166 LDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVK-GTVLASG 223
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
329-550 |
4.13e-16 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 79.92 E-value: 4.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 329 VDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTT-------IGRTPVHRvaaaGVSRTFQHSKLFNRLS 401
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVlfdaekgICLPPEKR----RIGYVFQDARLFPHYK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 402 ALENVLVGAHLVSRPTFLR--RLLwlpsarrderaalehaarclrrvGLGDLAGNRASSLSYGDQRRLEIARALAAEPSL 479
Cdd:PRK11144 93 VRGNLRYGMAKSMVAQFDKivALL-----------------------GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPEL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 480 LILDEPAAG---------MNHVEaaQLSELIRslaqggLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEIAADPA 550
Cdd:PRK11144 150 LLMDEPLASldlprkrelLPYLE--RLAREIN------IPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSA 221
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
326-536 |
5.43e-16 |
|
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: 77.51 E-value: 5.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 326 VRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPvHRVAAAGVSRTFQHSKLFNRlSALEN 405
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYE-HKYLHSKVSLVGQEPVLFAR-SLQDN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 406 VLVGahlvsrptflrrLLWLPSARRDERAALEHAARCLRRVGLG--DLAGNRASSLSYGDQRRLEIARALAAEPSLLILD 483
Cdd:cd03248 108 IAYG------------LQSCSFECVKEAAQKAHAHSFISELASGydTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502712709 484 EPAAGMNHVEAAQLSELIRSLAQgGLTILFIEHNVGMVlETCTRVVVLDFGEV 536
Cdd:cd03248 176 EATSALDAESEQQVQQALYDWPE-RRTVLVIAHRLSTV-ERADQILVLDGGRI 226
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
321-549 |
7.18e-16 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 79.08 E-value: 7.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 321 GGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSsgsatvLGTTIGR-----------TPVHRVAAAG--V 387
Cdd:PRK15093 18 GWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDN------WRVTADRmrfddidllrlSPRERRKLVGhnV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 388 SRTFQHSKlfNRLSALENVlvGAHLV-SRPTFLRRLLWLPSARRDERAALEhaarCLRRVGLGD---LAGNRASSLSYGD 463
Cdd:PRK15093 92 SMIFQEPQ--SCLDPSERV--GRQLMqNIPGWTYKGRWWQRFGWRKRRAIE----LLHRVGIKDhkdAMRSFPYELTEGE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 464 QRRLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQ-GGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTP 542
Cdd:PRK15093 164 CQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPS 243
|
....*..
gi 502712709 543 AEIAADP 549
Cdd:PRK15093 244 KELVTTP 250
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
311-550 |
8.47e-16 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 79.12 E-value: 8.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 311 VSLTGLAKEY-GGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSatvlgTTIGRTPVHRVAAA--GV 387
Cdd:PRK11650 4 LKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGE-----IWIGGRVVNELEPAdrDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 388 SRTFQHSKLFNRLSALENVLVGahLVSRPTflrrllwlPSARRDERaaLEHAARCLrrvGLGDLAGNRASSLSYGDQRRL 467
Cdd:PRK11650 79 AMVFQNYALYPHMSVRENMAYG--LKIRGM--------PKAEIEER--VAEAARIL---ELEPLLDRKPRELSGGQRQRV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 468 EIARALAAEPSLLILDEPaagMNHVEA-------AQLSELIRSLaqgGLTILFIEHNvgmVLETCT---RVVVLDFGEVI 537
Cdd:PRK11650 144 AMGRAIVREPAVFLFDEP---LSNLDAklrvqmrLEIQRLHRRL---KTTSLYVTHD---QVEAMTladRVVVMNGGVAE 214
|
250
....*....|...
gi 502712709 538 ASGTPAEIAADPA 550
Cdd:PRK11650 215 QIGTPVEVYEKPA 227
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
325-555 |
1.53e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 77.51 E-value: 1.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 325 AVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIG--------RTPVHRVaaaGVSRTFQHSKL 396
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIThktkdkyiRPVRKRI---GMVFQFPESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 397 FnrlsalenvlvgahlvsRPTFLRRLLWLP-SARRDERAALEHAARCLRRVGLG-DLAGNRASSLSYGDQRRLEIARALA 474
Cdd:PRK13646 99 F-----------------EDTVEREIIFGPkNFKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 475 AEPSLLILDEPAAGMNHVEAAQLSELIRSLA-QGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEIAADPAVIE 553
Cdd:PRK13646 162 MNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKKKLA 241
|
..
gi 502712709 554 AY 555
Cdd:PRK13646 242 DW 243
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
329-549 |
3.23e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 78.73 E-value: 3.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 329 VDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPpSSGSATVLGTTIGRTPVH--RVAAAGVSrtfQHSKLFNRlSALENV 406
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP-YQGSLKINGIELRELDPEswRKHLSWVG---QNPQLPHG-TLRDNV 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 407 LVGAHLVSrptflrrllwlpsarrDER--AALEHA--ARCLRRVGLG-DLA-GNRASSLSYGDQRRLEIARALAAEPSLL 480
Cdd:PRK11174 444 LLGNPDAS----------------DEQlqQALENAwvSEFLPLLPQGlDTPiGDQAAGLSVGQAQRLALARALLQPCQLL 507
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 481 ILDEPAAGMN-HVEAAQLSELIRslAQGGLTILFIEHNVGMvLETCTRVVVLDFGEVIASGTPAEIAADP 549
Cdd:PRK11174 508 LLDEPTASLDaHSEQLVMQALNA--ASRRQTTLMVTHQLED-LAQWDQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
327-547 |
4.93e-15 |
|
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: 74.88 E-value: 4.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 327 RGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVH--RVAAAGVSrtfQHSKLFNRlSALE 404
Cdd:cd03249 20 KGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRwlRSQIGLVS---QEPVLFDG-TIAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 405 NVLVGAhlvsrptflrrllwlPSARRDERAALEHAARCLRRV-----GLGDLAGNRASSLSYGDQRRLEIARALAAEPSL 479
Cdd:cd03249 96 NIRYGK---------------PDATDEEVEEAAKKANIHDFImslpdGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502712709 480 LILDEPAAGM-NHVEAAQLSELIRslAQGGLTILFIEHNvgmvLET---CTRVVVLDFGEVIASGTPAEIAA 547
Cdd:cd03249 161 LLLDEATSALdAESEKLVQEALDR--AMKGRTTIVIAHR----LSTirnADLIAVLQNGQVVEQGTHDELMA 226
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
304-542 |
5.16e-15 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 73.99 E-value: 5.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 304 PAAGEtvVSLTGLAKEYGG--VHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHR 381
Cdd:cd03369 2 PEHGE--IEVENLSVRYAPdlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 382 vaaagvsrtfqhskLFNRLSALENvlvgahlvsRPTFLRRLLWLPSARRDE------RAALehaarclrRVGLGdlagnr 455
Cdd:cd03369 80 --------------LRSSLTIIPQ---------DPTLFSGTIRSNLDPFDEysdeeiYGAL--------RVSEG------ 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 456 ASSLSYGDQRRLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGlTILFIEHNVGMVLEtCTRVVVLDFGE 535
Cdd:cd03369 123 GLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNS-TILTIAHRLRTIID-YDKILVMDAGE 200
|
....*..
gi 502712709 536 VIASGTP 542
Cdd:cd03369 201 VKEYDHP 207
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
326-516 |
7.22e-15 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 77.54 E-value: 7.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 326 VRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGsatvlgtTIGRTPVHRVaaagvsrtfqhskLFnrlsalen 405
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSG-------RIARPAGARV-------------LF-------- 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 406 vlvgahLVSRPTF----LRRLLWLPSARRD-ERAALEHAarcLRRVGLGDLAG------NRASSLSYGDQRRLEIARALA 474
Cdd:COG4178 431 ------LPQRPYLplgtLREALLYPATAEAfSDAELREA---LEAVGLGHLAErldeeaDWDQVLSLGEQQRLAFARLLL 501
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 502712709 475 AEPSLLILDEPAAGMNHVEAAQLSELIRSLAQgGLTILFIEH 516
Cdd:COG4178 502 HKPDWLFLDEATSALDEENEAALYQLLREELP-GTTVISVGH 542
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
327-551 |
9.00e-15 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 77.84 E-value: 9.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 327 RGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVH----RVAAAGvsrtfQHSKLFNRlSA 402
Cdd:TIGR00958 498 KGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHylhrQVALVG-----QEPVLFSG-SV 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 403 LENVLVGahlvsrptflrrllwLPSARRDERAALEHAARCLRRV-----GLGDLAGNRASSLSYGDQRRLEIARALAAEP 477
Cdd:TIGR00958 572 RENIAYG---------------LTDTPDEEIMAAAKAANAHDFImefpnGYDTEVGEKGSQLSGGQKQRIAIARALVRKP 636
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502712709 478 SLLILDEPAAGMNhVEAAQLseLIRSLAQGGLTILFIEHNVGMVlETCTRVVVLDFGEVIASGTPAEIAADPAV 551
Cdd:TIGR00958 637 RVLILDEATSALD-AECEQL--LQESRSRASRTVLLIAHRLSTV-ERADQILVLKKGSVVEMGTHKQLMEDQGC 706
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
292-548 |
1.42e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 76.79 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 292 ADPAPRLAARAHPAAGETVVSLTGLAKEY--GGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATV 369
Cdd:PRK11160 320 QKPEVTFPTTSTAAADQVSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 370 LGTTIgrtpvhrvaaagvsRTFQHSKLFNRLSALENVLvgaHLVSrpTFLRR--LLWLPSARrDERaaLEHAarcLRRVG 447
Cdd:PRK11160 400 NGQPI--------------ADYSEAALRQAISVVSQRV---HLFS--ATLRDnlLLAAPNAS-DEA--LIEV---LQQVG 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 448 LGDLA------------GNRAssLSYGDQRRLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGlTILFIE 515
Cdd:PRK11160 455 LEKLLeddkglnawlgeGGRQ--LSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNK-TVLMIT 531
|
250 260 270
....*....|....*....|....*....|...
gi 502712709 516 HNVgMVLETCTRVVVLDFGEVIASGTPAEIAAD 548
Cdd:PRK11160 532 HRL-TGLEQFDRICVMDNGQIIEQGTHQELLAQ 563
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
327-547 |
1.60e-14 |
|
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: 73.42 E-value: 1.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 327 RGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRV-AAAGVsrTFQHSKLFNRlSALEN 405
Cdd:cd03253 18 KDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLrRAIGV--VPQDTVLFND-TIGYN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 406 VLVGAhlvsrptflrrllwlPSARRDERAALEHAARCLRRV-----GLGDLAGNRASSLSYGDQRRLEIARALAAEPSLL 480
Cdd:cd03253 95 IRYGR---------------PDATDEEVIEAAKAAQIHDKImrfpdGYDTIVGERGLKLSGGEKQRVAIARAILKNPPIL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502712709 481 ILDEPAAGMNHVEAAQLSELIRSLAQGGlTILFIEHNVGMVLeTCTRVVVLDFGEVIASGTPAEIAA 547
Cdd:cd03253 160 LLDEATSALDTHTEREIQAALRDVSKGR-TTIVIAHRLSTIV-NADKIIVLKDGRIVERGTHEELLA 224
|
|
| TM_PBP1_transp_AraH_like |
cd06579 |
Transmembrane subunit (TM) of Escherichia coli AraH and related proteins. E. coli AraH is the ... |
6-226 |
2.59e-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: 73.21 E-value: 2.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 6 ATTLTFIALGAIFaysfyaVLIAGQLSLGQAGFASVAAFSAATLAPSGDdVGDVPALLTAVVIGMAVGAV---ASVVLGL 82
Cdd:cd06579 1 AAVLGILALGMTL------VIITGGIDLSVGSVAALSAVVAALLLVNAG-LPIPLAILAALAVGALIGLLnglLVAYLRI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 83 PTMhlrgvflaIATLGFAEAVR---VVLLNQEWTGGAQGLAVPRI-------LTVGMAWTALAVVAYWFWrMGRSRYGRA 152
Cdd:cd06579 74 PPF--------IVTLGTMFILRglaLLITGGRPISGLPPLFSFFLggglilgIPVPVLIALAVALVAWFL-LRRTRFGRY 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502712709 153 LEAIREDELAARSMGIDVGRHRLAAFVTSGAVAGLYGVLFAYYVRLIAPS---DFDFTAavdglVTAVVGGSTMFLG 226
Cdd:cd06579 145 LYAVGGNPEAARLSGINVRRVKILAYVLSGLLAGLAGILLAARLGSAQPTagnGYELDA-----IAAVVLGGTSLTG 216
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
326-547 |
2.77e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 73.61 E-value: 2.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 326 VRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRVAAAgVSRTFQHSklfnrlsalEN 405
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHK-IGMVFQNP---------DN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 406 VLVGAHLVSRPTFLRRLLWLPSARRDERaaLEHAarcLRRVGLGDLAGNRASSLSYGDQRRLEIARALAAEPSLLILDEp 485
Cdd:PRK13650 93 QFVGATVEDDVAFGLENKGIPHEEMKER--VNEA---LELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDE- 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502712709 486 AAGMNHVEAAQlsELIRSLA----QGGLTILFIEHNVGMVLETcTRVVVLDFGEVIASGTPAEIAA 547
Cdd:PRK13650 167 ATSMLDPEGRL--ELIKTIKgirdDYQMTVISITHDLDEVALS-DRVLVMKNGQVESTSTPRELFS 229
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
326-536 |
3.58e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 75.21 E-value: 3.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 326 VRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIG-RTPVHRV--AAAGVSRTFQHSKLFNRLSA 402
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDAVkkGMAYITESRRDNGFFPNFSI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 403 LENVLVGAHLvsRPTFLRRLLWLPSARRDERAAleHAARCLRRVGLGDLAGNrASSLSYGDQRRLEIARALAAEPSLLIL 482
Cdd:PRK09700 359 AQNMAISRSL--KDGGYKGAMGLFHEVDEQRTA--ENQRELLALKCHSVNQN-ITELSGGNQQKVLISKWLCCCPEVIIF 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502712709 483 DEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEV 536
Cdd:PRK09700 434 DEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
286-549 |
6.56e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 72.44 E-value: 6.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 286 GGPGSAAD---PAPRLAArahpaagetvvslTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPP 362
Cdd:PRK14271 7 GGQSGAADvdaAAPAMAA-------------VNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 363 SSG---SATVL--GTTIGRTPVHRVAAAGVSRTFQHSKLFNrLSALENVLVG--AH-LVSRPTFlrrllwlpsarrdeRA 434
Cdd:PRK14271 74 VSGyrySGDVLlgGRSIFNYRDVLEFRRRVGMLFQRPNPFP-MSIMDNVLAGvrAHkLVPRKEF--------------RG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 435 ALEhaARcLRRVGLGDLAGNRASS----LSYGDQRRLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQgGLT 510
Cdd:PRK14271 139 VAQ--AR-LTEVGLWDAVKDRLSDspfrLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLAD-RLT 214
|
250 260 270
....*....|....*....|....*....|....*....
gi 502712709 511 ILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEIAADP 549
Cdd:PRK14271 215 VIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSP 253
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
324-516 |
8.35e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 70.76 E-value: 8.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 324 HAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVP--PSSGSATVLGTTIGRtpvhrvaaagvsrtfqhsklfnRLS 401
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQFGR----------------------EAS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 402 ALENVlvgahlvsrptflrrllwlpsARRDERAAlehAARCLRRVGLGDLAGNRA--SSLSYGDQRRLEIARALAAEPSL 479
Cdd:COG2401 102 LIDAI---------------------GRKGDFKD---AVELLNAVGLSDAVLWLRrfKELSTGQKFRFRLALLLAERPKL 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 502712709 480 LILDEPAAGMNHVEAAQLSELIRSLAQ-GGLTILFIEH 516
Cdd:COG2401 158 LVIDEFCSHLDRQTAKRVARNLQKLARrAGITLVVATH 195
|
|
| LivH |
COG0559 |
Branched-chain amino acid ABC-type transport system, permease component [Amino acid transport ... |
59-231 |
8.45e-14 |
|
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: 72.02 E-value: 8.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 59 VPALLTAVVIGMAVGAVASVVLGLPTMHLRGVFLAIATLGFA----EAVRVV----------LLNQEWTGGAQGLAVPRI 124
Cdd:COG0559 62 WLALLLAVLVAALLGVLLERLVIRPLRGAPPLALLLATIGLSlvlqGLVLLIfgadprsfpaLLSGSVELGGVSIPAYRL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 125 LTVGMAWTALAVVAYWFwrmGRSRYGRALEAIREDELAARSMGIDVGRHRLAAFVTSGAVAGLYGVLFAYYVRLIApsDF 204
Cdd:COG0559 142 FIIVVALVLLAALWLFL---RRTRLGLAMRAVAQNREAARLMGINVDRVIALTFALGAALAGLAGVLLAPIYSVSP--TM 216
|
170 180
....*....|....*....|....*..
gi 502712709 205 DFTAAVDGLVTAVVGGSTMFLGPILGS 231
Cdd:COG0559 217 GFLLGLKAFAAVVLGGLGSIPGAVVGG 243
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
327-535 |
9.66e-14 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 70.19 E-value: 9.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 327 RGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTigrtpvhrvaaAGVSrtfQHSKLFNRlSALENV 406
Cdd:cd03250 22 KDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSI-----------AYVS---QEPWIQNG-TIRENI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 407 LVGAHLvsRPTFLRRLLwlpsarrdERAALEhaaRCLRRVGLGDLA--GNRASSLSYGDQRRLEIARALAAEPSLLILDE 484
Cdd:cd03250 87 LFGKPF--DEERYEKVI--------KACALE---PDLEILPDGDLTeiGEKGINLSGGQKQRISLARAVYSDADIYLLDD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 502712709 485 P-AAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGmVLETCTRVVVLDFGE 535
Cdd:cd03250 154 PlSAVDAHVGRHIFENCILGLLLNNKTRILVTHQLQ-LLPHADQIVVLDNGR 204
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
306-549 |
1.00e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 72.69 E-value: 1.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 306 AGETVVSLTGLAKEY----------GGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIG 375
Cdd:PRK11308 1 SQQPLLQAIDLKKHYpvkrglfkpeRLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 376 RTPVHRVAAA--GVSRTFQ--HSKLFNRLSalenvlVGAHLvSRPtflrrLLWLPSARRDERAalEHAARCLRRVGLGDL 451
Cdd:PRK11308 81 KADPEAQKLLrqKIQIVFQnpYGSLNPRKK------VGQIL-EEP-----LLINTSLSAAERR--EKALAMMAKVGLRPE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 452 AGNRASSLSYGDQR-RLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQG-GLTILFIEHNVGMVLETCTRVV 529
Cdd:PRK11308 147 HYDRYPHMFSGGQRqRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVM 226
|
250 260
....*....|....*....|
gi 502712709 530 VLDFGEVIASGTPAEIAADP 549
Cdd:PRK11308 227 VMYLGRCVEKGTKEQIFNNP 246
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
308-550 |
1.66e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 70.57 E-value: 1.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 308 ETVVSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTL---VNMISGLVP--PSSGSATVLGTTIGRTPVHRV 382
Cdd:PRK14239 3 EPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLlrsINRMNDLNPevTITGSIVYNGHNIYSPRTDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 383 A-AAGVSRTFQHSKLFNrLSALENVLVGAHLvsrptflrrllwlpsARRDERAALEHAA-RCLRRVGLGDLAGNR----A 456
Cdd:PRK14239 83 DlRKEIGMVFQQPNPFP-MSIYENVVYGLRL---------------KGIKDKQVLDEAVeKSLKGASIWDEVKDRlhdsA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 457 SSLSYGDQRRLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQgGLTILFIEHNVGMVLETCTRVVVLDFGEV 536
Cdd:PRK14239 147 LGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKD-DYTMLLVTRSMQQASRISDRTGFFLDGDL 225
|
250
....*....|....
gi 502712709 537 IASGTPAEIAADPA 550
Cdd:PRK14239 226 IEYNDTKQMFMNPK 239
|
|
| AraH |
COG1172 |
Ribose/xylose/arabinose/galactoside ABC-type transport system, permease component ... |
2-226 |
2.27e-13 |
|
Ribose/xylose/arabinose/galactoside ABC-type transport system, permease component [Carbohydrate transport and metabolism];
Pssm-ID: 440785 Cd Length: 322 Bit Score: 71.29 E-value: 2.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 2 LAQYATTLTFIALGAIFaysfyaVLIAGQLSLGQAGFASVAAFSAATLApSGDDVGDVPALLTAVVIGMAVGAV---ASV 78
Cdd:COG1172 48 ILRQAAILGILALGMTL------VIITGGIDLSVGSVVALSGVVAALLL-VALGLPILLAILLALLVGALLGLLnglLVA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 79 VLGLPTMhlrgvflaIATLGFAEAVRVvlLNQEWTGGAQGLAVPRILT-----------VGMAWTALAVVAYWFWrMGRS 147
Cdd:COG1172 121 KLRIPPF--------IVTLGTMFIARG--LALLLTGGRPISGLPDAFRalgqgsllgipVPVLIALVVALVAWFL-LRRT 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 148 RYGRALEAIREDELAARSMGIDVGRHRLAAFVTSGAVAGLYGVLFAYYVRLIAPS---DFDFTAavdglVTAVVGGSTMF 224
Cdd:COG1172 190 RFGRYIYAVGGNEEAARLSGINVRRVKILAYVLSGLLAGLAGILLAARLGSAQPNagsGYELDA-----IAAVVIGGTSL 264
|
..
gi 502712709 225 LG 226
Cdd:COG1172 265 TG 266
|
|
| TM_PBP1_LivH_like |
cd06582 |
Transmembrane subunit (TM) of Escherichia coli LivH and related proteins. LivH is one of two ... |
59-231 |
3.24e-13 |
|
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: 70.15 E-value: 3.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 59 VPALLTAVVIGMAVGAVASVVLGLPTMHlRGVFLAIATLG----FAEAVRVV-----------LLNQEWTGGAQGLAVPR 123
Cdd:cd06582 52 WLALLLALLVAALLGVLLERLVLRPLRG-APLLTLLITFGglliLLQGLLLIfggdprvppppLLSGSVELGGVTIPPYR 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 124 ILTVGMAWTALAVVAYWFwrmGRSRYGRALEAIREDELAARSMGIDVGRHRLAAFVTSGAVAGLYGVLFAYYVRLIApsD 203
Cdd:cd06582 131 LFIIAVALVLLAALYLFL---RRTRLGRAIRAVAQNPEAARLLGINVRRVFALTFALGAALAGLAGVLLAPITGVSP--T 205
|
170 180
....*....|....*....|....*...
gi 502712709 204 FDFTAAVDGLVTAVVGGSTMFLGPILGS 231
Cdd:cd06582 206 MGLLLLLKAFAAVVLGGLGSIPGAVVGG 233
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
323-540 |
5.47e-13 |
|
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: 67.35 E-value: 5.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 323 VHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMIsglvppssgsatvlgttigrtpvhrVAAAGVSRTFQHSKLFNRLSA 402
Cdd:cd03238 8 VHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEG-------------------------LYASGKARLISFLPKFSRNKL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 403 LenvlvgahlvsrptFLRRLlwlpsarrderaalehaaRCLRRVGLGDLAGNR-ASSLSYGDQRRLEIARALAAEP--SL 479
Cdd:cd03238 63 I--------------FIDQL------------------QFLIDVGLGYLTLGQkLSTLSGGELQRVKLASELFSEPpgTL 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502712709 480 LILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVletCTRVVVLDFG--------EVIASG 540
Cdd:cd03238 111 FILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVL---SSADWIIDFGpgsgksggKVVFSG 176
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
296-559 |
6.11e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 71.19 E-value: 6.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 296 PRLAArahpAAGETVVSLTGLAKEygGVHavrGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTI- 374
Cdd:PRK10762 247 PRLDK----APGEVRLKVDNLSGP--GVN---DVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVv 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 375 GRTPVHRVAA--AGVSRTFQHSKLFNRLSALENVLVGA--HLVSRPTFLRRllwlpsarRDERAALEHAARCL------- 443
Cdd:PRK10762 318 TRSPQDGLANgiVYISEDRKRDGLVLGMSVKENMSLTAlrYFSRAGGSLKH--------ADEQQAVSDFIRLFniktpsm 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 444 -RRVGLgdlagnrassLSYGDQRRLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVL 522
Cdd:PRK10762 390 eQAIGL----------LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVL 459
|
250 260 270
....*....|....*....|....*....|....*..
gi 502712709 523 ETCTRVVVLDFGEViaSGtpaEIAADPAVIEAYLGTA 559
Cdd:PRK10762 460 GMSDRILVMHEGRI--SG---EFTREQATQEKLMAAA 491
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
323-547 |
7.51e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 69.35 E-value: 7.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 323 VHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRVAAAgVSRTFQHSklfnrlsa 402
Cdd:PRK13642 20 VNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRK-IGMVFQNP-------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 403 lENVLVGAHLVSRPTFLRRLLWLPsarRDEraALEHAARCLRRVGLGDLAGNRASSLSYGDQRRLEIARALAAEPSLLIL 482
Cdd:PRK13642 91 -DNQFVGATVEDDVAFGMENQGIP---REE--MIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502712709 483 DEPAAGMNHVEAAQLSELIRSLA-QGGLTILFIEHNVGMVLETcTRVVVLDFGEVIASGTPAEIAA 547
Cdd:PRK13642 165 DESTSMLDPTGRQEIMRVIHEIKeKYQLTVLSITHDLDEAASS-DRILVMKAGEIIKEAAPSELFA 229
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
330-537 |
1.08e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 70.75 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 330 DLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSAT-----------------VLGTtigrtpVHRVAAAGVSRTFQ 392
Cdd:PRK11147 23 ELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIyeqdlivarlqqdpprnVEGT------VYDFVAEGIEEQAE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 393 HSKLFNRLSalenvlvgaHLVS---RPTFLRRLlwlpsARRDERaaLEHA---------ARCLRRVGLGdlAGNRASSLS 460
Cdd:PRK11147 97 YLKRYHDIS---------HLVEtdpSEKNLNEL-----AKLQEQ--LDHHnlwqlenriNEVLAQLGLD--PDAALSSLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 461 YGDQRRLEIARALAAEPSLLILDEPAagmNH--VEAAQ-LSELIRSLaQGglTILFIEHNVGMVLETCTRVVVLDFGEVI 537
Cdd:PRK11147 159 GGWLRKAALGRALVSNPDVLLLDEPT---NHldIETIEwLEGFLKTF-QG--SIIFISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
334-535 |
1.28e-12 |
|
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: 70.58 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 334 RSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSatvlgttIGRTPvhrvAAAGVSRTFQHSKLFNRLSALENvlvGAHLV 413
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGD-------YDEEP----SWDEVLKRFRGTELQDYFKKLAN---GEIKV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 414 SR--------PTFL----RRLLwlpsARRDERAALEHAArclRRVGLGDLAGNRASSLSYGDQRRLEIARALAAEPSLLI 481
Cdd:COG1245 163 AHkpqyvdliPKVFkgtvRELL----EKVDERGKLDELA---EKLGLENILDRDISELSGGELQRVAIAAALLRDADFYF 235
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502712709 482 LDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVgMVLETCTRVVVLDFGE 535
Cdd:COG1245 236 FDEPSSYLDIYQRLNVARLIRELAEEGKYVLVVEHDL-AILDYLADYVHILYGE 288
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
321-550 |
1.94e-12 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 68.60 E-value: 1.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 321 GGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPS---SGSATVLGTTIGRTPVH---RVAAAGVSRTFQhs 394
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPEKelnKLRAEQISMIFQ-- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 395 klfNRLSALENVL-VGAHLVsrptflrRLLWLpSARRDERAALEHAARCLRRVGLGDlAGNRAS----SLSYGDQRRLEI 469
Cdd:PRK09473 105 ---DPMTSLNPYMrVGEQLM-------EVLML-HKGMSKAEAFEESVRMLDAVKMPE-ARKRMKmyphEFSGGMRQRVMI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 470 ARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQG-GLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEIAAD 548
Cdd:PRK09473 173 AMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQ 252
|
..
gi 502712709 549 PA 550
Cdd:PRK09473 253 PS 254
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
307-521 |
2.83e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 69.45 E-value: 2.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 307 GETVVSLTGLAKEYGG----VHAvrGvdlEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATvLGTTIGRTPvhrv 382
Cdd:PRK13409 337 RETLVEYPDLTKKLGDfsleVEG--G---EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD-PELKISYKP---- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 383 aaagvsrtfQhsklfnRLSALENVLVGAHLVSRPTFLRRLLWLPSarrderaalehaarCLRRVGLGDLAGNRASSLSYG 462
Cdd:PRK13409 407 ---------Q------YIKPDYDGTVEDLLRSITDDLGSSYYKSE--------------IIKPLQLERLLDKNVKDLSGG 457
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502712709 463 DQRRLEIARALAAEPSLLILDEPAAgmnHVEAAQ---LSELIRSLAQG-GLTILFIEHNVGMV 521
Cdd:PRK13409 458 ELQRVAIAACLSRDADLYLLDEPSA---HLDVEQrlaVAKAIRRIAEErEATALVVDHDIYMI 517
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
294-485 |
3.58e-12 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 69.19 E-value: 3.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 294 PAPRLaarahpaaGETVVSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVlGTT 373
Cdd:TIGR03719 314 PGPRL--------GDKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GET 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 374 IgrtpvhRVAAAGVSR-TFQHSK-LFNRLS-ALENVLVGAHLVsrptflrrllwlPSarrdeRAalehaarclrRVGLGD 450
Cdd:TIGR03719 385 V------KLAYVDQSRdALDPNKtVWEEISgGLDIIKLGKREI------------PS-----RA----------YVGRFN 431
|
170 180 190
....*....|....*....|....*....|....*....
gi 502712709 451 LAGN----RASSLSYGDQRRLEIARALAAEPSLLILDEP 485
Cdd:TIGR03719 432 FKGSdqqkKVGQLSGGERNRVHLAKTLKSGGNVLLLDEP 470
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
307-544 |
4.62e-12 |
|
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: 68.66 E-value: 4.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 307 GETVVSLTGLAKEYGG--VHAVRGvdlEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATvLGTTIGRTPvhrvaa 384
Cdd:COG1245 338 EETLVEYPDLTKSYGGfsLEVEGG---EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD-EDLKISYKP------ 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 385 agvsrtfQhsklfnRLSALENVLVGAhlvsrptFLRrllwlpSARRDERAALEHAARCLRRVGLGDLAGNRASSLSYGDQ 464
Cdd:COG1245 408 -------Q------YISPDYDGTVEE-------FLR------SANTDDFGSSYYKTEIIKPLGLEKLLDKNVKDLSGGEL 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 465 RRLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQG-GLTILFIEHNVGMVLETCTRVVVLDfgeviasGTPA 543
Cdd:COG1245 462 QRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENrGKTAMVVDHDIYLIDYISDRLMVFE-------GEPG 534
|
.
gi 502712709 544 E 544
Cdd:COG1245 535 V 535
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
329-536 |
5.78e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 68.40 E-value: 5.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 329 VDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIG-RTPVHRVAAAGV----SRTFQhsKLFNRLSAL 403
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDiRSPRDAIRAGIMlcpeDRKAE--GIIPVHSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 404 ENVLVGAhlvsRPTFLRRLLWLPSARRDERAALEHAARCLRRVGLGDLAGNrassLSYGDQRRLEIARALAAEPSLLILD 483
Cdd:PRK11288 350 DNINISA----RRHHLRAGCLINNRWEAENADRFIRSLNIKTPSREQLIMN----LSGGNQQKAILGRWLSEDMKVILLD 421
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502712709 484 EPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEV 536
Cdd:PRK11288 422 EPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
328-516 |
6.61e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 68.37 E-value: 6.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 328 GVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLgtTIGRTPVHRVaaagVSRTfqhsklfnRLSALENVL 407
Cdd:PLN03211 86 GVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTIL--ANNRKPTKQI----LKRT--------GFVTQDDIL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 408 VgAHLVSRPTFLR-RLLWLP-SARRDERAALehAARCLRRVGL----GDLAGNR-ASSLSYGDQRRLEIARALAAEPSLL 480
Cdd:PLN03211 152 Y-PHLTVRETLVFcSLLRLPkSLTKQEKILV--AESVISELGLtkceNTIIGNSfIRGISGGERKRVSIAHEMLINPSLL 228
|
170 180 190
....*....|....*....|....*....|....*.
gi 502712709 481 ILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEH 516
Cdd:PLN03211 229 ILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMH 264
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
324-547 |
6.96e-12 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 67.99 E-value: 6.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 324 HAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTigrtpvhrvAAAGVSrtfqhSKLFNRLSAL 403
Cdd:PRK13545 38 YALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSA---------ALIAIS-----SGLNGQLTGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 404 ENVlvgahlvsrptflrRLLWLPSARRDERAAlEHAARCLRRVGLGDLAGNRASSLSYGDQRRLEIARALAAEPSLLILD 483
Cdd:PRK13545 104 ENI--------------ELKGLMMGLTKEKIK-EIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVID 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502712709 484 EPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEIAA 547
Cdd:PRK13545 169 EALSVGDQTFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVD 232
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
318-550 |
8.37e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 67.96 E-value: 8.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 318 KEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGR-------------TPVHRVAA 384
Cdd:PRK10261 24 QEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRrsrqvielseqsaAQMRHVRG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 385 AGVSRTFQHSklfnrLSALENVLVGAHLVSRPTFLRRllwlpSARRDEraALEHAARCLRRVGLGD---LAGNRASSLSY 461
Cdd:PRK10261 104 ADMAMIFQEP-----MTSLNPVFTVGEQIAESIRLHQ-----GASREE--AMVEAKRMLDQVRIPEaqtILSRYPHQLSG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 462 GDQRRLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQG-GLTILFIEHNVGMVLETCTRVVVLDFGEVIASG 540
Cdd:PRK10261 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAVETG 251
|
250
....*....|
gi 502712709 541 TPAEIAADPA 550
Cdd:PRK10261 252 SVEQIFHAPQ 261
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
323-549 |
8.52e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 67.96 E-value: 8.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 323 VHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRVAAAGVSRTFQHSKLFNRLSA 402
Cdd:PRK10261 337 VHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFIFQDPYASLDP 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 403 LENVlvgAHLVSRPTFLRRLLwlpsarrDERAALEHAARCLRRVGL-GDLAGNRASSLSYGDQRRLEIARALAAEPSLLI 481
Cdd:PRK10261 417 RQTV---GDSIMEPLRVHGLL-------PGKAAAARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVII 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502712709 482 LDEPAAGMNHVEAAQLSELIRSLAQG-GLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEIAADP 549
Cdd:PRK10261 487 ADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENP 555
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
332-549 |
9.47e-12 |
|
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: 65.51 E-value: 9.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 332 EIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRVA-AAGVSRTFQHSKLfnrlsalenvlvgA 410
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKAdYEGTVRDLLSSIT-------------K 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 411 HLVSRPTFLRRLlwlpsarrderaalehaarcLRRVGLGDLAGNRASSLSYGDQRRLEIARALAAEPSLLILDEPAAgmn 490
Cdd:cd03237 88 DFYTHPYFKTEI--------------------AKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSA--- 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502712709 491 HVEAAQ---LSELIRSLAQGG-LTILFIEHNVGMVLETCTRVVVLDfgeviasGTPAE--IAADP 549
Cdd:cd03237 145 YLDVEQrlmASKVIRRFAENNeKTAFVVEHDIIMIDYLADRLIVFE-------GEPSVngVANPP 202
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
326-550 |
1.12e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 65.49 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 326 VRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPP----SSGSATVLGTtigrtpvhRVAAAGVSRTFQHSKLFNRLS 401
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGK--------PVAPCALRGRKIATIMQNPRS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 402 ALENVL-VGAHlvSRPTFLRRllwlpsARRDERAALehaARCLRRVGLGD---LAGNRASSLSYGDQRRLEIARALAAEP 477
Cdd:PRK10418 91 AFNPLHtMHTH--ARETCLAL------GKPADDATL---TAALEAVGLENaarVLKLYPFEMSGGMLQRMMIALALLCEA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502712709 478 SLLILDEPAAGMNHVEAAQLSELIRSLAQG-GLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEIAADPA 550
Cdd:PRK10418 160 PFIIADEPTTDLDVVAQARILDLLESIVQKrALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPK 233
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
294-374 |
1.27e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 67.45 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 294 PAPRLaarahpaaGETVVSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVlGTT 373
Cdd:PRK11819 316 PGPRL--------GDKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GET 386
|
.
gi 502712709 374 I 374
Cdd:PRK11819 387 V 387
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
325-545 |
1.29e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 65.80 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 325 AVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTI--GRTPVHRVA----AAGVSRTFQHSKLFN 398
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpaNLKKIKEVKrlrkEIGLVFQFPEYQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 399 RLSALENVLVGAHLVSrptflrrllwlpsarrDERAALEHAARCLRRVGLG-DLAGNRASSLSYGDQRRLEIARALAAEP 477
Cdd:PRK13645 106 ETIEKDIAFGPVNLGE----------------NKQEAYKKVPELLKLVQLPeDYVKRSPFELSGGQKRRVALAGIIAMDG 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502712709 478 SLLILDEPAAGMNHVEAAQLSELIRSLAQG-GLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEI 545
Cdd:PRK13645 170 NTLVLDEPTGGLDPKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEI 238
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
324-536 |
2.83e-11 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 64.45 E-value: 2.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 324 HAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTtigrtpvhrvaaagVSRTFQHSKLFNRLSAL 403
Cdd:PRK13546 38 FALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE--------------VSVIAISAGLSGQLTGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 404 ENVLVgahlvsrptflrRLLWLPSARRDERAALehaARCLRRVGLGDLAGNRASSLSYGDQRRLEIARALAAEPSLLILD 483
Cdd:PRK13546 104 ENIEF------------KMLCMGFKRKEIKAMT---PKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVID 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502712709 484 EPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEV 536
Cdd:PRK13546 169 EALSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKL 221
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
310-537 |
4.71e-11 |
|
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: 65.34 E-value: 4.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 310 VVSLTGLAKEY-GGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATV-LGTTIGRTPvhrvaaagv 387
Cdd:TIGR03719 4 IYTMNRVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPqPGIKVGYLP--------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 388 srtfQHSKLFNRLSALENVLVGA----HLVSRPTFLRRLLWLPSARRDERAA--------------------LEHAARCL 443
Cdd:TIGR03719 75 ----QEPQLDPTKTVRENVEEGVaeikDALDRFNEISAKYAEPDADFDKLAAeqaelqeiidaadawdldsqLEIAMDAL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 444 RrVGLGDLagnRASSLSYGDQRRLEIARALAAEPSLLILDEPAagmNHVEAAQLSELIRSLAQGGLTILFIEH------N 517
Cdd:TIGR03719 151 R-CPPWDA---DVTKLSGGERRRVALCRLLLSKPDMLLLDEPT---NHLDAESVAWLERHLQEYPGTVVAVTHdryfldN 223
|
250 260
....*....|....*....|.
gi 502712709 518 V-GMVLEtctrvvvLDFGEVI 537
Cdd:TIGR03719 224 VaGWILE-------LDRGRGI 237
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
326-550 |
4.76e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 65.50 E-value: 4.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 326 VRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPpsSGSATVLGTTI---GRTPVH-------RVAAAGVSRTFQHSK 395
Cdd:PRK15134 25 VNDVSLQIEAGETLALVGESGSGKSVTALSILRLLP--SPPVVYPSGDIrfhGESLLHaseqtlrGVRGNKIAMIFQEPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 396 L-FNRLSALENVLVgahlvsrptflrRLLWLPSARRDErAALEHAARCLRRVGLGDLAGNRAS---SLSYGDQRRLEIAR 471
Cdd:PRK15134 103 VsLNPLHTLEKQLY------------EVLSLHRGMRRE-AARGEILNCLDRVGIRQAAKRLTDyphQLSGGERQRVMIAM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 472 ALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQG-GLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAEIAADPA 550
Cdd:PRK15134 170 ALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPT 249
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
333-535 |
5.03e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 65.60 E-value: 5.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 333 IRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSatvlgttigrtPVHRVAAAGVSRTFQHSKLFNRLSAL-ENVLVGAH 411
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGD-----------YEEEPSWDEVLKRFRGTELQNYFKKLyNGEIKVVH 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 412 lvsRPTFL-----------RRLLwlpsARRDERAALEHAArclRRVGLGDLAGNRASSLSYGDQRRLEIARALAAEPSLL 480
Cdd:PRK13409 165 ---KPQYVdlipkvfkgkvRELL----KKVDERGKLDEVV---ERLGLENILDRDISELSGGELQRVAIAAALLRDADFY 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502712709 481 ILDEPAAGMNHVEAAQLSELIRSLAQGGlTILFIEHNVgMVLETCTRVVVLDFGE 535
Cdd:PRK13409 235 FFDEPTSYLDIRQRLNVARLIRELAEGK-YVLVVEHDL-AVLDYLADNVHIAYGE 287
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
290-487 |
6.79e-11 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 64.82 E-value: 6.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 290 SAADPAPRLAARAHPAAGETVvSLTGLAKEYGGVHAVRG-----VDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSS 364
Cdd:COG4615 308 AAEPAAADAAAPPAPADFQTL-ELRGVTYRYPGEDGDEGftlgpIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPES 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 365 GSATVLGTTIgrTPVHRVAaagvsrtfqHSKLFnrlSAlenVLVGAHLvsrptFlRRLLWLPSARRDERaalehAARCLR 444
Cdd:COG4615 387 GEILLDGQPV--TADNREA---------YRQLF---SA---VFSDFHL-----F-DRLLGLDGEADPAR-----ARELLE 438
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 502712709 445 RVGLGD---LAGNRASS--LSYGDQRRLEIARALAAEPSLLILDEPAA 487
Cdd:COG4615 439 RLELDHkvsVEDGRFSTtdLSQGQRKRLALLVALLEDRPILVFDEWAA 486
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
435-546 |
6.90e-11 |
|
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: 65.42 E-value: 6.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 435 ALEHAARCLRRVGLGDLA-GNRASSLSYGDQRRLEIARALAAE---PSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLT 510
Cdd:TIGR00630 805 SISRKLQTLCDVGLGYIRlGQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNT 884
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 502712709 511 ILFIEHNVGmVLETCTRVVVL------DFGEVIASGTPAEIA 546
Cdd:TIGR00630 885 VVVIEHNLD-VIKTADYIIDLgpeggdGGGTVVASGTPEEVA 925
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
334-540 |
7.00e-11 |
|
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: 62.77 E-value: 7.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 334 RSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSatvlgttIGRTPVHRvaaaGVSRTFQHSKLFNRLSALENVLVGAhlV 413
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGK-------FDDPPDWD----EILDEFRGSELQNYFTKLLEGDVKV--I 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 414 SRPTFLRRllwLPSA----------RRDERAALEHAarcLRRVGLGDLAGNRASSLSYGDQRRLEIARALAAEPSLLILD 483
Cdd:cd03236 91 VKPQYVDL---IPKAvkgkvgellkKKDERGKLDEL---VDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502712709 484 EPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGmVLETCTRVVVLDFGEVIASG 540
Cdd:cd03236 165 EPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDLA-VLDYLSDYIHCLYGEPGAYG 220
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
329-545 |
1.03e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 62.85 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 329 VDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGsaTVLGTTigrtpvHRVAAAGVSRTFQHSKLFnrLSALENVLV 408
Cdd:PRK13648 28 VSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSG--EIFYNN------QAITDDNFEKLRKHIGIV--FQNPDNQFV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 409 GA------------HLVSRPTFLRRLlwlpsarrderaalehaARCLRRVGLGDLAGNRASSLSYGDQRRLEIARALAAE 476
Cdd:PRK13648 98 GSivkydvafglenHAVPYDEMHRRV-----------------SEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 477 PSLLILDEPAAGMNHVEAAQLSELIRSL-AQGGLTILFIEHNVGMVLETcTRVVVLDFGEVIASGTPAEI 545
Cdd:PRK13648 161 PSVIILDEATSMLDPDARQNLLDLVRKVkSEHNITIISITHDLSEAMEA-DHVIVMNKGTVYKEGTPTEI 229
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
326-539 |
1.10e-10 |
|
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: 64.08 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 326 VRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPS-SGSATVLGTTIG-RTPVHRVAA--AGVSRTFQHSKLFNRLS 401
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDiRNPAQAIRAgiAMVPEDRKRHGIVPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 402 ALENVLVGAhlVSRPTFLRRLlwlpSARRDERAALEHAARCLRRVGLGDLAgnrASSLSYGDQRRLEIARALAAEPSLLI 481
Cdd:TIGR02633 356 VGKNITLSV--LKSFCFKMRI----DAAAELQIIGSAIQRLKVKTASPFLP---IGRLSGGNQQKAVLAKMLLTNPRVLI 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502712709 482 LDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIAS 539
Cdd:TIGR02633 427 LDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKGD 484
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
333-512 |
1.94e-10 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 60.33 E-value: 1.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 333 IRSGEVVGLIGPNGAGKTTLVNMIS-----GLVppsSGSATVLGTTIGRTpvhrvaaagvsrtfqhsklFNRLSAL---E 404
Cdd:cd03232 30 VKPGTLTALMGESGAGKTTLLDVLAgrktaGVI---TGEILINGRPLDKN-------------------FQRSTGYveqQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 405 NVLVGAHLVsrptflrrllwlpsarrdeRAALEHAArCLRrvglgdlagnrasSLSYGDQRRLEIARALAAEPSLLILDE 484
Cdd:cd03232 88 DVHSPNLTV-------------------REALRFSA-LLR-------------GLSVEQRKRLTIGVELAAKPSILFLDE 134
|
170 180
....*....|....*....|....*...
gi 502712709 485 PAAGMNHVEAAQLSELIRSLAQGGLTIL 512
Cdd:cd03232 135 PTSGLDSQAAYNIVRFLKKLADSGQAIL 162
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
325-549 |
1.16e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 60.14 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 325 AVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVP-PSSGSATVLG------TTIGRTPVHRVAAAGVSRTFQ----- 392
Cdd:PRK11022 22 AVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPGRVMAEKLEfngqdlQRISEKERRNLVGAEVAMIFQdpmts 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 393 ----HSKLFNRLSALENVLVGAHlvsrptflrrllwlpSARRderaalEHAARCLRRVGLGDLAG---NRASSLSYGDQR 465
Cdd:PRK11022 102 lnpcYTVGFQIMEAIKVHQGGNK---------------KTRR------QRAIDLLNQVGIPDPASrldVYPHQLSGGMSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 466 RLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQG-GLTILFIEHNVGMVLETCTRVVVLDFGEVIASGTPAE 544
Cdd:PRK11022 161 RVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKeNMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHD 240
|
....*
gi 502712709 545 IAADP 549
Cdd:PRK11022 241 IFRAP 245
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
325-547 |
1.29e-09 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 60.80 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 325 AVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIG--RTPVHRVAAAGVSrtfQHSKLFNRLSA 402
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRdyTLASLRNQVALVS---QNVHLFNDTIA 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 403 lENVlvgAHlvsrptflrrllwlpsARRDE--RAALEHAARCLRRV--------GLGDLAGNRASSLSYGDQRRLEIARA 472
Cdd:PRK11176 435 -NNI---AY----------------ARTEQysREQIEEAARMAYAMdfinkmdnGLDTVIGENGVLLSGGQRQRIAIARA 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 473 LAAEPSLLILDEPAAGMN-----HVEAAqLSELirslaQGGLTILFIEHNVGMVlETCTRVVVLDFGEVIASGTPAEIAA 547
Cdd:PRK11176 495 LLRDSPILILDEATSALDteserAIQAA-LDEL-----QKNRTSLVIAHRLSTI-EKADEILVVEDGEIVERGTHAELLA 567
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
446-544 |
1.46e-09 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 61.38 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 446 VGLGDLAGNRA-SSLSYGDQRRLEIARALAAEPS--LLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVl 522
Cdd:PRK00635 463 LGLPYLTPERAlATLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMI- 541
|
90 100
....*....|....*....|....*...
gi 502712709 523 ETCTRVVVLD-----F-GEVIASGTPAE 544
Cdd:PRK00635 542 SLADRIIDIGpgagiFgGEVLFNGSPRE 569
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
328-517 |
1.70e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 60.64 E-value: 1.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 328 GVDLEIRsgevVGLIGPNGAGKTTLVNMISGLVPPSSGsatvlgtTIGRTPVHRVAAAGvsrtfQHSklfnrlsalenvL 407
Cdd:PLN03073 531 GIDLDSR----IAMVGPNGIGKSTILKLISGELQPSSG-------TVFRSAKVRMAVFS-----QHH------------V 582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 408 VGAHLVSRPtflrrLLWLpsaRRDERAALEHAARC-LRRVGL-GDLAGNRASSLSYGDQRRLEIARALAAEPSLLILDEP 485
Cdd:PLN03073 583 DGLDLSSNP-----LLYM---MRCFPGVPEQKLRAhLGSFGVtGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEP 654
|
170 180 190
....*....|....*....|....*....|....
gi 502712709 486 AagmNHVEAAQLSELIRSLA--QGGltILFIEHN 517
Cdd:PLN03073 655 S---NHLDLDAVEALIQGLVlfQGG--VLMVSHD 683
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
291-516 |
1.98e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 60.03 E-value: 1.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 291 AADPAprlaARAHPAAGETVVSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVL 370
Cdd:PRK10938 245 PDEPS----ARHALPANEPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGYSNDLTL 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 371 -------GTTIGRTPVHrvaAAGVSRTFqHskLFNRLSA-LENVLVGAHLVSrptflrrlLWLPSARRDERAALehAARC 442
Cdd:PRK10938 321 fgrrrgsGETIWDIKKH---IGYVSSSL-H--LDYRVSTsVRNVILSGFFDS--------IGIYQAVSDRQQKL--AQQW 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 443 LRRVGLGD-LAGNRASSLSYGDQRRLEIARALAAEPSLLILDEPAAGMNHVEaaqlSELIRS-----LAQGGLTILFIEH 516
Cdd:PRK10938 385 LDILGIDKrTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLN----RQLVRRfvdvlISEGETQLLFVSH 460
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
325-516 |
2.64e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 59.99 E-value: 2.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 325 AVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIgrTPVHRVA-AAGVSRTFQHSKLFNRLSAL 403
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPV--TAEQPEDyRKLFSAVFTDFHLFDQLLGP 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 404 ENVLVGAHLVSRptflrrllWLpsarrdERAALEHAARclrrvglgdLAGNRAS--SLSYGDQRRLEIARALAAEPSLLI 481
Cdd:PRK10522 416 EGKPANPALVEK--------WL------ERLKMAHKLE---------LEDGRISnlKLSKGQKKRLALLLALAEERDILL 472
|
170 180 190
....*....|....*....|....*....|....*.
gi 502712709 482 LDEPAAGMN-HVEAAQLSELIRSLAQGGLTILFIEH 516
Cdd:PRK10522 473 LDEWAADQDpHFRREFYQVLLPLLQEMGKTIFAISH 508
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
443-550 |
2.92e-09 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 60.04 E-value: 2.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 443 LRRVGLGDLA-GNRASSLSYGDQRRLEIARALA---AEPSLLILDEPAAGMnHVE-AAQLSELIRSLAQGGLTILFIEHN 517
Cdd:COG0178 810 LQDVGLGYIKlGQPATTLSGGEAQRVKLASELSkrsTGKTLYILDEPTTGL-HFHdIRKLLEVLHRLVDKGNTVVVIEHN 888
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 502712709 518 vgmvLEtctrVV-----VLDFG--------EVIASGTPAEIAADPA 550
Cdd:COG0178 889 ----LD----VIktadwIIDLGpeggdgggEIVAEGTPEEVAKVKA 926
|
|
| BCA_ABC_TP_C |
pfam12399 |
Branched-chain amino acid ATP-binding cassette transporter; This domain family is found in ... |
535-559 |
4.61e-09 |
|
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: 51.87 E-value: 4.61e-09
|
| TM_PBP1_transp_TpRbsC_like |
cd06580 |
Transmembrane subunit (TM) of Treponema pallidum (Tp) RbsC-1, RbsC-2 and related proteins. ... |
6-246 |
4.67e-09 |
|
Transmembrane subunit (TM) of Treponema pallidum (Tp) RbsC-1, RbsC-2 and related proteins. This is a functionally uncharacterized subgroup of TMs which belong to a larger group of TMs of Periplasmic Binding Protein (PBP)-dependent ATP-Binding Cassette (ABC) transporters, which are mainly involved in the uptake of branched-chain amino acids (AAs) or in the uptake of monosaccharides including ribose, galactose, and arabinose, and which generally bind type 1 PBPs. PBP-dependent ABC transporters consist of a PBP, two TMs, and two cytoplasmic ABCs, and are mainly involved in importing solutes from the environment. The solute is captured by the PBP, which delivers it to a gated translocation pathway formed by the two TMs. The two ABCs bind and hydrolyze ATP and drive the transport reaction.
Pssm-ID: 119322 [Multi-domain] Cd Length: 234 Bit Score: 57.06 E-value: 4.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 6 ATTLTFIALGAIFAYSfyavliAGQLSLGQAGFASVAAFSAaTLAPSGDDVGDVPALLTAVVIGMAVGAVASVVLGLPTm 85
Cdd:cd06580 1 ATPLILAALGVAISFR------AGVFNIGLEGQMLLGAFAA-ALVALYLGLPATGSLPLGLLAAALAGALWALLPALLK- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 86 hlrgvflaiATLGFAEAVRVVLLNqewtggaqgLAVPRILTVGMAWTALAVVAYWFWrMGRSRYGRALEAIREDELAARS 165
Cdd:cd06580 73 ---------AKLGVNEVISGLMLN---------YIALGLTSYLLLLALLLVILVWLL-LYRTRFGLRLRAVGENPRAARY 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 166 MGIDVGRHRLAAFVTSGAVAGLYGVLFAYYVRLIAPSDFDFTAAVDGLVTAVVGGSTMF---LGPILGSGFQTMIPEIQR 242
Cdd:cd06580 134 AGINVKRVRLLAMLISGALAGLAGAYLVLGVQGRFTEGMSAGYGFIAIAVALLGRWNPLgilLAALLFGALEAGGIALQR 213
|
....
gi 502712709 243 AVGV 246
Cdd:cd06580 214 SGGV 217
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
453-545 |
6.35e-09 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 59.46 E-value: 6.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 453 GNRASSLSYGDQRRLEIARALAA---EPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVlETCTRVV 529
Cdd:PRK00635 804 GRPLSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVV-KVADYVL 882
|
90 100
....*....|....*....|..
gi 502712709 530 VLD------FGEVIASGTPAEI 545
Cdd:PRK00635 883 ELGpeggnlGGYLLASCSPEEL 904
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
323-542 |
8.91e-09 |
|
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: 56.85 E-value: 8.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 323 VHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVN-----------MISGLVPPSSGSATVLG----------TTIGRTPvhR 381
Cdd:cd03271 8 ENNLKNIDVDIPLGVLTCVTGVSGSGKSSLINdtlypalarrlHLKKEQPGNHDRIEGLEhidkvividqSPIGRTP--R 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 382 VAAAGVSRTFQ----------HSKLFNRlSALENVLVGA---------------HLVSRPTFLRRLlwlpsarrderaal 436
Cdd:cd03271 86 SNPATYTGVFDeirelfcevcKGKRYNR-ETLEVRYKGKsiadvldmtveealeFFENIPKIARKL-------------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 437 ehaaRCLRRVGLGDLA-GNRASSLSYGDQRRLEIARAL---AAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLTIL 512
Cdd:cd03271 151 ----QTLCDVGLGYIKlGQPATTLSGGEAQRIKLAKELskrSTGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVV 226
|
250 260 270
....*....|....*....|....*....|....*.
gi 502712709 513 FIEHNVGmVLETCTRVVVL------DFGEVIASGTP 542
Cdd:cd03271 227 VIEHNLD-VIKCADWIIDLgpeggdGGGQVVASGTP 261
|
|
| NupP |
COG4603 |
ABC-type guanosine uptake system NupNOPQ, permease component NupP [Nucleotide transport and ... |
5-191 |
9.70e-09 |
|
ABC-type guanosine uptake system NupNOPQ, permease component NupP [Nucleotide transport and metabolism];
Pssm-ID: 443653 [Multi-domain] Cd Length: 356 Bit Score: 57.44 E-value: 9.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 5 YATTLTFIALGAIFAYSfyavliAGQLSLGQAGFASVAAFSAATLAPSGDDVGDVPALLTAVVIGMAVGAVASVVLGLPt 84
Cdd:COG4603 65 KATPLILTGLAVAVAFR------AGLFNIGAEGQLYLGALAAAAVGLALPGLPGPLHLPLALLAGALAGALWAAIPGLL- 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 85 MHLRGVFLAIATLGF---AEAVRVVLLNQEWTGGAQGLA----------VPRI-----LTVGMAWTALAVVAYWFWrMGR 146
Cdd:COG4603 138 KARFGVNEVITTLMLnyiALYLVNYLVRGPLRDPGSGFPqtppipesarLPRLlpgtrLHLGLLIALLAAVLVWVL-LNR 216
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 502712709 147 SRYGRALEAIREDELAARSMGIDVGRHRLAAFVTSGAVAGLYGVL 191
Cdd:COG4603 217 TTLGYELRAVGLNPRAARYAGINVKRLIVLAMLISGALAGLAGAV 261
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
329-546 |
1.31e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 58.06 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 329 VDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPvhrvaaagvsrtfQHSKLFNRlSALENVLV 408
Cdd:PLN03232 636 INLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVIRGSVAYVP-------------QVSWIFNA-TVRENILF 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 409 GAhlvsrpTFLRRLLWlpsaRRDERAALEHAARCLRRVGLGDLaGNRASSLSYGDQRRLEIARALAAEPSLLILDEPAAG 488
Cdd:PLN03232 702 GS------DFESERYW----RAIDVTALQHDLDLLPGRDLTEI-GERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSA 770
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502712709 489 MN-HVEAAQLSELIRSLAQGGLTILFIehNVGMVLETCTRVVVLDFGEVIASGTPAEIA 546
Cdd:PLN03232 771 LDaHVAHQVFDSCMKDELKGKTRVLVT--NQLHFLPLMDRIILVSEGMIKEEGTFAELS 827
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
326-536 |
1.32e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 57.63 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 326 VRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVP-PSSGSATVLGTTIG-RTPVHRVAA--AGVSRTFQHSKLFNRLS 401
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKiRNPQQAIAQgiAMVPEDRKRDGIVPVMG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 402 ALENVLVGAhlVSRPTFLRRLlwlpsarrDERAALEHAARCLRRVGLgdlagnRASS-------LSYGDQRRLEIARALA 474
Cdd:PRK13549 358 VGKNITLAA--LDRFTGGSRI--------DDAAELKTILESIQRLKV------KTASpelaiarLSGGNQQKAVLAKCLL 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502712709 475 AEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEV 536
Cdd:PRK13549 422 LNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
326-516 |
4.05e-08 |
|
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: 52.93 E-value: 4.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 326 VRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGsatvlgtTIGRTPVHRVaaagvsrtfqhskLFnrlsalen 405
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSG-------RIGMPEGEDL-------------LF-------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 406 vlvgahLVSRPTF----LRRLLWLPSARRderaalehaarclrrvglgdlagnrassLSYGDQRRLEIARALAAEPSLLI 481
Cdd:cd03223 69 ------LPQRPYLplgtLREQLIYPWDDV----------------------------LSGGEQQRLAFARLLLHKPKFVF 114
|
170 180 190
....*....|....*....|....*....|....*
gi 502712709 482 LDEPAAGMNHVEAAQLSELIRSLaqgGLTILFIEH 516
Cdd:cd03223 115 LDEATSALDEESEDRLYQLLKEL---GITVISVGH 146
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
329-547 |
7.05e-08 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 55.49 E-value: 7.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 329 VDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGrTPVHRVAAAGVSRTFQHSKLFNRlSALENVLV 408
Cdd:PRK10790 360 INLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLS-SLSHSVLRQGVAMVQQDPVVLAD-TFLANVTL 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 409 GAHlVSRPTFLRRLlwlpsarrdERAALEHAARCLRRvGLGDLAGNRASSLSYGDQRRLEIARALAAEPSLLILDEPAAG 488
Cdd:PRK10790 438 GRD-ISEEQVWQAL---------ETVQLAELARSLPD-GLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATAN 506
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502712709 489 MNH-VEAA--QLSELIRSLAqgglTILFIEHNVGMVLETCTrVVVLDFGEVIASGTPAEIAA 547
Cdd:PRK10790 507 IDSgTEQAiqQALAAVREHT----TLVVIAHRLSTIVEADT-ILVLHRGQAVEQGTHQQLLA 563
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
325-536 |
7.42e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.12 E-value: 7.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 325 AVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRVAAAGVS-------RTFQHSKL- 396
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINHGFAlvteerrSTGIYAYLd 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 397 --FNRL-SALENVLVGAHLVSRPTFLRRLLWLPSARRDERAAlehaarclRRVGLGdlagnrasSLSYGDQRRLEIARAL 473
Cdd:PRK10982 343 igFNSLiSNIRNYKNKVGLLDNSRMKSDTQWVIDSMRVKTPG--------HRTQIG--------SLSGGNQQKVIIGRWL 406
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502712709 474 AAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEV 536
Cdd:PRK10982 407 LTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| PRK15432 |
PRK15432 |
autoinducer 2 ABC transporter permease LsrC; Provisional |
62-250 |
1.10e-07 |
|
autoinducer 2 ABC transporter permease LsrC; Provisional
Pssm-ID: 185330 [Multi-domain] Cd Length: 344 Bit Score: 53.97 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 62 LLTAVVIGMAVGAVASVVLGLPTMHLR--GVFLAIATLGFAEAVRVVLLNQEWTGGA----QGLAVPRILTV---GMAWT 132
Cdd:PRK15432 88 LPVACLATLLLGLLAGFFNGVLVAWLRipAIVATLGTLGLYRGIMLLWTGGKWIEGLpaelKQLSAPILLGIspiGWLTL 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 133 ALAVVAYWFwrMGRSRYGRALEAIREDELAARSMGIDVGRHRLAAFVTSGAVAGLYGVLFAYYVRLIAPSDFD------F 206
Cdd:PRK15432 168 ILILAMAWL--LAKTAFGRSFYATGDNLQGARQLGVRTEAIRIVAFSLNGCMAALAGIVFASQIGFIPNQTGTglemkaI 245
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 502712709 207 TAAVDGLVTaVVGGSTMFLGPILGSGFQTMIPEIQRAVGVEAGW 250
Cdd:PRK15432 246 AACVLGGIS-LLGGSGTIIGAVLGAYFLTQIDSVLVLLRIPAWW 288
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
443-557 |
1.23e-07 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 55.02 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 443 LRRVGLGDLAGNR-ASSLSYGDQRRLEIARALAAEPS--LLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVG 519
Cdd:TIGR00630 472 LIDVGLDYLSLSRaAGTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDED 551
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 502712709 520 MVLETcTRVVvlDFG--------EVIASGTPAEIAADPAVIE-AYLG 557
Cdd:TIGR00630 552 TIRAA-DYVI--DIGpgagehggEVVASGTPEEILANPDSLTgQYLS 595
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
327-544 |
1.39e-07 |
|
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: 54.44 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 327 RGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRV-AAAGVsrTFQHSKLFNRlSALEN 405
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLrAAIGI--VPQDTVLFND-TIAYN 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 406 VLVGAhlvsrptflrrllwlPSARRDEraaLEHAARcLRRV---------GLGDLAGNRASSLSYGDQRRLEIARALAAE 476
Cdd:COG5265 452 IAYGR---------------PDASEEE---VEAAAR-AAQIhdfieslpdGYDTRVGERGLKLSGGEKQRVAIARTLLKN 512
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502712709 477 PSLLILDEPAAGMN-HVEAAQLSELiRSLAQGGlTILFIEHNvgmvLET---CTRVVVLDFGEVIASGTPAE 544
Cdd:COG5265 513 PPILIFDEATSALDsRTERAIQAAL-REVARGR-TTLVIAHR----LSTivdADEILVLEAGRIVERGTHAE 578
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
328-548 |
1.54e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 54.74 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 328 GVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGR------------TPVHRVAAAGVSRtFQHSK 395
Cdd:PLN03130 1257 GLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKfglmdlrkvlgiIPQAPVLFSGTVR-FNLDP 1335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 396 lFNRLSALEnvlvgahlvsrptflrrlLWlpsaRRDERAALEHAarcLRR--VGLGDLAGNRASSLSYGDQRRLEIARAL 473
Cdd:PLN03130 1336 -FNEHNDAD------------------LW----ESLERAHLKDV---IRRnsLGLDAEVSEAGENFSVGQRQLLSLARAL 1389
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502712709 474 AAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGgLTILFIEHNVGMVLEtCTRVVVLDFGEVIASGTPAEIAAD 548
Cdd:PLN03130 1390 LRRSKILVLDEATAAVDVRTDALIQKTIREEFKS-CTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLLSN 1462
|
|
| TM_PBP1_branched-chain-AA_like |
cd06574 |
Transmembrane subunit (TM) of Periplasmic Binding Protein (PBP)-dependent ATP-Binding Cassette ... |
63-231 |
1.67e-07 |
|
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: 53.05 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 63 LTAVVIGMAVGAVASVVLGLPTMHLRG-----------------VFLAIATLGFAEAVRVVLLNQEWTGGAQGLAVPRIL 125
Cdd:cd06574 47 WLALIAAILAGAAAGLVTGFLHTRLKIngllagilimiglysinLRIMGGPNIPLGTRDTLLGLLLLFGISGTLSIPVVL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 126 TVGMAWTALAVvaYWFWRmgrSRYGRALEAIREDELAARSMGIDVGRHRLAAFVTSGAVAGLYGVLFAYYVRLIAPSdFD 205
Cdd:cd06574 127 LLIVLLVLFLV--IWFLR---TKLGLAMRATGDNPDMARSLGINVDRTRILGLVISNALAALGGALYAQYQGFADVN-MG 200
|
170 180 190
....*....|....*....|....*....|....
gi 502712709 206 FTAAVDGLVTAVVGGSTM--------FLGPILGS 231
Cdd:cd06574 201 IGTGVIGLAAVIIGGAIVgrrtikasILGVIIGA 234
|
|
| NupQ |
COG1079 |
ABC-type guanosine uptake system NupNOPQ, permease subunit NupQ [Nucleotide transport and ... |
62-193 |
1.85e-07 |
|
ABC-type guanosine uptake system NupNOPQ, permease subunit NupQ [Nucleotide transport and metabolism];
Pssm-ID: 440697 [Multi-domain] Cd Length: 309 Bit Score: 53.15 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 62 LLTAVVIGMAVGAVASVVLGLPTMHLR------GVFLAIATLGFAeavrVVLLNQEWTGGAQGLAVPRI----------- 124
Cdd:COG1079 62 PWLGLLAAALAGALLALLHAFLTITLRanqivsGLALNLLALGLT----AFLGRLLFGQGGQTPSIPGLppipipglsdi 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 125 -----------LTVGMAWTALAVVAYWFWRmgrSRYGRALEAIREDELAARSMGIDVGRHRLAAFVTSGAVAGLYGVLFA 193
Cdd:COG1079 138 pvlgpllfgqsPLVYLALLLVPLVWWVLYR---TRFGLRLRAVGENPAAADALGINVYRIRYLAVLIGGALAGLGGAYLS 214
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
326-545 |
1.91e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 54.60 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 326 VRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLG---TTIGRTPVHRVaaagVSRTFQHSKLFNRLSA 402
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDcdvAKFGLTDLRRV----LSIIPQSPVLFSGTVR 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 403 LENVLVGAHLVSRptflrrlLWlpsaRRDERAALEHAARcLRRVGLGDLAGNRASSLSYGDQRRLEIARALAAEPSLLIL 482
Cdd:PLN03232 1328 FNIDPFSEHNDAD-------LW----EALERAHIKDVID-RNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVL 1395
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502712709 483 DEPAAGMNHVEAAQLSELIRSLAQgGLTILFIEHNVGMVLEtCTRVVVLDFGEVIASGTPAEI 545
Cdd:PLN03232 1396 DEATASVDVRTDSLIQRTIREEFK-SCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQEL 1456
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
341-516 |
2.00e-07 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 51.84 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 341 LIGPNGAGKTTLVNMIS----GLVPPSSGSATVLGTTIGRTPVhrvaAAGVSRTFQHS-----KLFNRLSALENVLvgah 411
Cdd:cd03240 27 IVGQNGAGKTTIIEALKyaltGELPPNSKGGAHDPKLIREGEV----RAQVKLAFENAngkkyTITRSLAILENVI---- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 412 lvsrptFLRR--LLWLpsarrderaALEHAARClrrvglgdLAGNRAS-SLSYgdqrRLEIARALAAEPSLLILDEPAAG 488
Cdd:cd03240 99 ------FCHQgeSNWP---------LLDMRGRC--------SGGEKVLaSLII----RLALAETFGSNCGILALDEPTTN 151
|
170 180 190
....*....|....*....|....*....|.
gi 502712709 489 M--NHVEaAQLSELIRS-LAQGGLTILFIEH 516
Cdd:cd03240 152 LdeENIE-ESLAEIIEErKSQKNFQLIVITH 181
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
339-537 |
2.29e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.58 E-value: 2.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 339 VGLIGPNGAGKTTLVNMISGLVPPSSGSATVL-GTTIGRTPvhrvaaagvsrtfQHSKLFNRLSALENVLVG-AHLVSRp 416
Cdd:PRK11819 36 IGVLGLNGAGKSTLLRIMAGVDKEFEGEARPApGIKVGYLP-------------QEPQLDPEKTVRENVEEGvAEVKAA- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 417 tfLRRLLWL------PSARRDERAA--------------------LEHAARCLRrvgL--GDLAgnrASSLSYGDQRRLE 468
Cdd:PRK11819 102 --LDRFNEIyaayaePDADFDALAAeqgelqeiidaadawdldsqLEIAMDALR---CppWDAK---VTKLSGGERRRVA 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502712709 469 IARALAAEPSLLILDEPAagmNHVEAAQLSELIRSLAQGGLTILFIEH------NV-GMVLEtctrvvvLDFGEVI 537
Cdd:PRK11819 174 LCRLLLEKPDMLLLDEPT---NHLDAESVAWLEQFLHDYPGTVVAVTHdryfldNVaGWILE-------LDRGRGI 239
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
328-512 |
2.43e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.96 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 328 GVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVppSSGSATVlGTTIgrtpvhrVAAAGVSRTFQHSKLF---NRLSaLE 404
Cdd:TIGR00956 781 NVDGWVKPGTLTALMGASGAGKTTLLNVLAERV--TTGVITG-GDRL-------VNGRPLDSSFQRSIGYvqqQDLH-LP 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 405 NVLVGAHLVSrPTFLRRLLWLPSARRDEraALEHAARCLRRVGLGD-LAGNRASSLSYGDQRRLEIARALAAEPSLLI-L 482
Cdd:TIGR00956 850 TSTVRESLRF-SAYLRQPKSVSKSEKME--YVEEVIKLLEMESYADaVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfL 926
|
170 180 190
....*....|....*....|....*....|
gi 502712709 483 DEPAAGMNHVEAAQLSELIRSLAQGGLTIL 512
Cdd:TIGR00956 927 DEPTSGLDSQTAWSICKLMRKLADHGQAIL 956
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
326-516 |
2.55e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 52.34 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 326 VRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGlvPPS----SGSATVLGTTIGRTPVHRVAAAGVSRTFQHsklfnrls 401
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGESILDLEPEERAHLGIFLAFQY-------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 402 ALEnvLVGahlVSRPTFLRrlLWLPSARR-------DERAALEHAARCLRRVGLGD--LAGNRASSLSYGDQRRLEIARA 472
Cdd:CHL00131 93 PIE--IPG---VSNADFLR--LAYNSKRKfqglpelDPLEFLEIINEKLKLVGMDPsfLSRNVNEGFSGGEKKRNEILQM 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 502712709 473 LAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEH 516
Cdd:CHL00131 166 ALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH 209
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
329-548 |
3.00e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 53.97 E-value: 3.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 329 VDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPvhrvaaagvsrtfQHSKLFNRlSALENVLV 408
Cdd:PLN03130 636 INLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVVIRGTVAYVP-------------QVSWIFNA-TVRDNILF 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 409 GAHLvsrptflrrllwlpSARRDERA----ALEHAarcLRRVGLGDLA--GNRASSLSYGDQRRLEIARALAAEPSLLIL 482
Cdd:PLN03130 702 GSPF--------------DPERYERAidvtALQHD---LDLLPGGDLTeiGERGVNISGGQKQRVSMARAVYSNSDVYIF 764
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502712709 483 DEPAAGMN-HVEAAQLSELIRSLAQGGLTILFIehNVGMVLETCTRVVVLDFGEVIASGTPAEIAAD 548
Cdd:PLN03130 765 DDPLSALDaHVGRQVFDKCIKDELRGKTRVLVT--NQLHFLSQVDRIILVHEGMIKEEGTYEELSNN 829
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
329-517 |
3.29e-07 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 51.64 E-value: 3.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 329 VDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRVAAAgVSRTFQHSKLFNRlSALENVLv 408
Cdd:PRK10247 26 ISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQ-VSYCAQTPTLFGD-TVYDNLI- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 409 gahlvsrptflrrllwLPSARRDERAALEHAARCLRRVGLGD-LAGNRASSLSYGDQRRLEIARALAAEPSLLILDEPAA 487
Cdd:PRK10247 103 ----------------FPWQIRNQQPDPAIFLDDLERFALPDtILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITS 166
|
170 180 190
....*....|....*....|....*....|.
gi 502712709 488 GMNHVEAAQLSELIRSLA-QGGLTILFIEHN 517
Cdd:PRK10247 167 ALDESNKHNVNEIIHRYVrEQNIAVLWVTHD 197
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
443-550 |
4.81e-07 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 53.15 E-value: 4.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 443 LRRVGLGDLA-GNRASSLSYGDQRRLEIARALAAEP---SLLILDEPAAGMnHVE-AAQLSELIRSLAQGGLTILFIEHN 517
Cdd:PRK00349 814 LVDVGLGYIKlGQPATTLSGGEAQRVKLAKELSKRStgkTLYILDEPTTGL-HFEdIRKLLEVLHRLVDKGNTVVVIEHN 892
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 502712709 518 VGmVLETCTRVVvlDFG--------EVIASGTPAEIAADPA 550
Cdd:PRK00349 893 LD-VIKTADWII--DLGpeggdgggEIVATGTPEEVAKVEA 930
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
316-445 |
4.99e-07 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 50.26 E-value: 4.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 316 LAKEYGGVHAVrgVDL-EIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPvhrvaaagvsrtfQHS 394
Cdd:cd03222 6 CVKRYGVFFLL--VELgVVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKP-------------QYI 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 502712709 395 KLFNrlSALENVLVGAHLVSRPTFLrrLLWLPSARRDERAALeHAARCLRR 445
Cdd:cd03222 71 DLSG--GELQRVAIAAALLRNATFY--LFDEPSAYLDIEQRL-NAARAIRR 116
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
326-547 |
6.63e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 52.64 E-value: 6.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 326 VRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRVAAAgVSRTFQHSKLFN---RLS- 401
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFK-ITIIPQDPVLFSgslRMNl 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 402 ------ALENVLVGAHLVSRPTFLRRLlwlPsarrderAALEHaaRClrrvglgdlaGNRASSLSYGDQRRLEIARALAA 475
Cdd:TIGR00957 1381 dpfsqySDEEVWWALELAHLKTFVSAL---P-------DKLDH--EC----------AEGGENLSVGQRQLVCLARALLR 1438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502712709 476 EPSLLILDEPAAGMNHVEAAQLSELIRSLAQGgLTILFIEHNVGMVLETcTRVVVLDFGEVIASGTPAEIAA 547
Cdd:TIGR00957 1439 KTKILVLDEATAAVDLETDNLIQSTIRTQFED-CTVLTIAHRLNTIMDY-TRVIVLDKGEVAEFGAPSNLLQ 1508
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
447-556 |
6.71e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 52.91 E-value: 6.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 447 GLGDLA-GNRASSLSYGDQRRLEIARAL---AAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVL 522
Cdd:PRK00635 1687 GLGYLPlGQNLSSLSLSEKIAIKIAKFLylpPKHPTLFLLDEIATSLDNQQKSALLVQLRTLVSLGHSVIYIDHDPALLK 1766
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 502712709 523 ETctrvvvlDF------------GEVIASGTPAEIAA-DPAVIEAYL 556
Cdd:PRK00635 1767 QA-------DYliemgpgsgktgGKILFSGPPKDISAsKDSLLKTYM 1806
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
311-366 |
9.90e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 51.82 E-value: 9.90e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 502712709 311 VSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGS 366
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGT 375
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
329-531 |
1.28e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 49.46 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 329 VDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVHRVAAagvsrTFQH-SKLFNRLSALENV- 406
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMA-----YLGHlPGLKADLSTLENLh 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 407 -LVGAHlvsrptflrrllwlpsarrdERAALEHAARCLRRVGLGDLAGNRASSLSYGDQRRLEIARALAAEPSLLILDEP 485
Cdd:PRK13543 105 fLCGLH--------------------GRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEP 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 502712709 486 AAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVL 531
Cdd:PRK13543 165 YANLDLEGITLVNRMISAHLRGGGAALVTTHGAYAAPPVRTRMLTL 210
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
326-516 |
1.46e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 49.79 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 326 VRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGL--VPPSSGSATVLGTTIGRTPVHRVAAAGVSRTFQHSklfnrlsal 403
Cdd:PRK09580 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAGEGIFMAFQYP--------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 404 envlVGAHLVSRPTFLRRLL--------WLPSARRDERAALEHAARCL--------RRVGLGdlagnrassLSYGDQRRL 467
Cdd:PRK09580 88 ----VEIPGVSNQFFLQTALnavrsyrgQEPLDRFDFQDLMEEKIALLkmpedlltRSVNVG---------FSGGEKKRN 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 502712709 468 EIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEH 516
Cdd:PRK09580 155 DILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTH 203
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
421-540 |
2.18e-06 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 49.18 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 421 RLLWlpsarrdERAALEHAARCLRRVGLGDLAGNR-ASSLSYGDQRRLEIARALAAEPS--LLILDEPAAGMNHVEAAQL 497
Cdd:cd03270 106 RLLF-------ARVGIRERLGFLVDVGLGYLTLSRsAPTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRL 178
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 502712709 498 SELIRSLAQGGLTILFIEHNVGMVLETCTrvvVLDF--------GEVIASG 540
Cdd:cd03270 179 IETLKRLRDLGNTVLVVEHDEDTIRAADH---VIDIgpgagvhgGEIVAQG 226
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
326-540 |
1.11e-05 |
|
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: 46.49 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 326 VRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPS---SGSATVLGTTigrtpvhrvaAAGVSRTFQHSKLFNRlsa 402
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIP----------YKEFAEKYPGEIIYVS--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 403 lENVLVGAHLVSRPTflrrllwlpsarrderaaLEHAARCLrrvglgdlaGNRASS-LSYGDQRRLEIARALAAEPSLLI 481
Cdd:cd03233 90 -EEDVHFPTLTVRET------------------LDFALRCK---------GNEFVRgISGGERKRVSIAEALVSRASVLC 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502712709 482 LDEPAAGMNHVEAAQLSELIRSLAQ--GGLTILFIEHNVGMVLETCTRVVVLDFGEVIASG 540
Cdd:cd03233 142 WDNSTRGLDSSTALEILKCIRTMADvlKTTTFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
325-549 |
1.23e-05 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 48.17 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 325 AVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPVH--RVAAAGVSRT-FqhskLFNRLS 401
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDswRSRLAVVSQTpF----LFSDTV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 402 AlENVLVGAhlvsrptflrrllwlPSARRDEraaLEHAARcLRRV---------GLGDLAGNRASSLSYGDQRRLEIARA 472
Cdd:PRK10789 406 A-NNIALGR---------------PDATQQE---IEHVAR-LASVhddilrlpqGYDTEVGERGVMLSGGQKQRISIARA 465
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502712709 473 LAAEPSLLILDEpaaGMNHVEAAQLSELIRSLAQGG--LTILFIEHNVGMVLETcTRVVVLDFGEVIASGTPAEIAADP 549
Cdd:PRK10789 466 LLLNAEILILDD---ALSAVDGRTEHQILHNLRQWGegRTVIISAHRLSALTEA-SEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
326-550 |
4.03e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 46.32 E-value: 4.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 326 VRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGlvpPS-----SGSATVLGTTIGRTPVHRVAAAGVSRTFQHSKLFNrL 400
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFG---RSygrniSGTVFKDGKEVDVSTVSDAIDAGLAYVTEDRKGYG-L 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 401 SALENV---LVGAHL--VSRPTFLrrllwlpsarrDERAALEHAARCLRRVGLgdlagnRASS-------LSYGDQRRLE 468
Cdd:NF040905 352 NLIDDIkrnITLANLgkVSRRGVI-----------DENEEIKVAEEYRKKMNI------KTPSvfqkvgnLSGGNQQKVV 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 469 IARALAAEPSLLILDEPAAGMNhVEAA-QLSELIRSLAQGGLTILFIEHNVGMVLETCTRVVVLDFGEVIasgtpAEIAA 547
Cdd:NF040905 415 LSKWLFTDPDVLILDEPTRGID-VGAKyEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRIT-----GELPR 488
|
...
gi 502712709 548 DPA 550
Cdd:NF040905 489 EEA 491
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
443-550 |
4.05e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 46.94 E-value: 4.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 443 LRRVGLGDLAGNR-ASSLSYGD-QR-RLeiARALAAE--PSLLILDEPAAGM----NHveaaQLSELIRSLAQGGLTILF 513
Cdd:COG0178 469 LVDVGLDYLTLDRsAGTLSGGEaQRiRL--ATQIGSGlvGVLYVLDEPSIGLhqrdND----RLIETLKRLRDLGNTVIV 542
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 502712709 514 IEHNVGMVLEtCTRVVvlDFG--------EVIASGTPAEIAADPA 550
Cdd:COG0178 543 VEHDEDTIRA-ADYII--DIGpgagehggEVVAQGTPEEILKNPD 584
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
435-522 |
4.84e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 43.89 E-value: 4.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 435 ALEHAARCLRRVGLgdlagnrasslSYGDQRRLEIARALA----AEPSLLILDEPAAGMNHVEAAQLSELIRSLAQGGLT 510
Cdd:cd03227 65 AAVSAELIFTRLQL-----------SGGEKELSALALILAlaslKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQ 133
|
90
....*....|..
gi 502712709 511 ILFIEHNVGMVL 522
Cdd:cd03227 134 VIVITHLPELAE 145
|
|
| PRK09699 |
PRK09699 |
D-allose ABC transporter permease; |
22-226 |
6.39e-05 |
|
D-allose ABC transporter permease;
Pssm-ID: 182035 [Multi-domain] Cd Length: 312 Bit Score: 45.15 E-value: 6.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 22 FYAVLIAG-QLSLGQAGFASVAAFSAATLApsGDDvGDVPALLTAVVIGMAVGAVASVVLGLPTMH-----------LRG 89
Cdd:PRK09699 57 FFAILVAGiDLSVGAILALSGMVTAKLMLA--GVD-PFLAALIGGVLVGGALGAINGCLVNWTGLHpfiitlgtnaiFRG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 90 VFLAIATLGFAEAVRVVLLNQeWTGGAQGLAVPRILTVGMAwtalavVAYWFWrMGRSRYGRALEAIREDELAARSMGID 169
Cdd:PRK09699 134 ITLVISDANSVYGFSFDFVNF-FAASVIGIPVPVIFSLIVA------LILWFL-TTRMRLGRNIYALGGNKNSAFYSGID 205
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 170 VGRHRLAAFVTSGAVAGLYGVLFAYYVRLIAP---SDFDFTAavdgLVTAVVGGSTMFLG 226
Cdd:PRK09699 206 VKFHILVVFIISGVCAGLAGVVSTARLGAAEPlagMGFETYA----IASAIIGGTSFFGG 261
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
329-512 |
6.40e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 44.17 E-value: 6.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 329 VDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTpvhrVAAAGVSRTF--QHSKLFNRLSALENV 406
Cdd:PRK13540 20 ISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKD----LCTYQKQLCFvgHRSGINPYLTLRENC 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 407 LVGAHLVSrptflrrllwlpsarrderAALEHAARClRRVGLGDLAGNRASSLSYGDQRRLEIARALAAEPSLLILDEPA 486
Cdd:PRK13540 96 LYDIHFSP-------------------GAVGITELC-RLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPL 155
|
170 180
....*....|....*....|....*..
gi 502712709 487 AGMNHVEAAQ-LSELIRSLAQGGLTIL 512
Cdd:PRK13540 156 VALDELSLLTiITKIQEHRAKGGAVLL 182
|
|
| araH |
PRK11285 |
L-arabinose transporter permease protein; Provisional |
63-193 |
6.53e-05 |
|
L-arabinose transporter permease protein; Provisional
Pssm-ID: 183076 [Multi-domain] Cd Length: 333 Bit Score: 45.44 E-value: 6.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 63 LTAVVIGM----AVGAVASVVLGLPTMHLRGVFLA-------IATLGFAEAVRVVLLNQEwTGGAQGLAVPRILTVGMA- 130
Cdd:PRK11285 96 VTAVVINAteslWLGVAAGLLLGAAVGLVNGFVIArlkinalITTLATMQIVRGLAYIIS-DGKAVGISDERFFALGYAn 174
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502712709 131 --------WTALAVVAYWFWRMGRSRYGRALEAIREDELAARSMGIDVGRHRLAAFVTSGAVAGLYGVLFA 193
Cdd:PRK11285 175 ffgvpapiWLTVACFVVFGFLLNKTTFGRNTLAIGGNEEAARLAGVPVVRTKIIIFVLQGLVSALAGVILA 245
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
335-379 |
1.71e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 42.36 E-value: 1.71e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 502712709 335 SGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTTIGRTPV 379
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEV 45
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
328-581 |
2.03e-04 |
|
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: 44.55 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 328 GVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVLGTtigrtpvhrvaaagVSRTFQHSKLFNRlSALENVL 407
Cdd:TIGR00957 656 GITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS--------------VAYVPQQAWIQND-SLRENIL 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 408 VGAHL--------VSRPTFLRRLLWLPSARRDEraalehaarclrrvglgdlAGNRASSLSYGDQRRLEIARALAAEPSL 479
Cdd:TIGR00957 721 FGKALnekyyqqvLEACALLPDLEILPSGDRTE-------------------IGEKGVNLSGGQKQRVSLARAVYSNADI 781
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 480 LILDEPAAGMN-HVEAAQLSELIRSLAQ-GGLTILFIEHNVGMVLETcTRVVVLDFGEVIASGT-PAEIAADPAVIEAYL 556
Cdd:TIGR00957 782 YLFDDPLSAVDaHVGKHIFEHVIGPEGVlKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSyQELLQRDGAFAEFLR 860
|
250 260
....*....|....*....|....*
gi 502712709 557 GTADDDPGGSSVADGTLAdpTGGSG 581
Cdd:TIGR00957 861 TYAPDEQQGHLEDSWTAL--VSGEG 883
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
307-516 |
3.83e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 43.40 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 307 GETVVSLTGLAKEYGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGSATVlGTT--IGRTPVHRvAA 384
Cdd:PRK11147 316 GKIVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKleVAYFDQHR-AE 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 385 AGVSRTFQHsklfNRLSALENVLVGA---HLVSrptFLRRLLWLPS-ARRDERAalehaarclrrvglgdlagnrassLS 460
Cdd:PRK11147 394 LDPEKTVMD----NLAEGKQEVMVNGrprHVLG---YLQDFLFHPKrAMTPVKA------------------------LS 442
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502712709 461 YGDQRRLEIARALAAEPSLLILDEPAAGMNhVEAAQLSELIRSLAQGglTILFIEH 516
Cdd:PRK11147 443 GGERNRLLLARLFLKPSNLLILDEPTNDLD-VETLELLEELLDSYQG--TVLLVSH 495
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
326-541 |
6.89e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 42.91 E-value: 6.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 326 VRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGlvpPSSGSATVLGTTIGRTPVHRVAAAGVSRTFQHSKLFN-RLSALE 404
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG---RKTGGYIEGDIRISGFPKKQETFARISGYCEQNDIHSpQVTVRE 972
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 405 NVLVGAhlvsrptFLRrllwLPS--ARRDERAALEHAARCLRRVGLGD----LAGnrASSLSYGDQRRLEIARALAAEPS 478
Cdd:PLN03140 973 SLIYSA-------FLR----LPKevSKEEKMMFVDEVMELVELDNLKDaivgLPG--VTGLSTEQRKRLTIAVELVANPS 1039
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502712709 479 LLILDEPAAGMNHVEAAQLSELIRSLAQGGLTILFIEHNVGM-VLETCTRVVVLDF-GEVIASGT 541
Cdd:PLN03140 1040 IIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIdIFEAFDELLLMKRgGQVIYSGP 1104
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
451-521 |
8.53e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 42.71 E-value: 8.53e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502712709 451 LAGNRASSLSYGDQRRLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLA--QGGLTILfIEHNVGMV 521
Cdd:PTZ00265 572 LVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITII-IAHRLSTI 643
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
459-536 |
9.52e-04 |
|
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: 41.38 E-value: 9.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 459 LSYGDQRRLEIARALAAEPSLLILDEPAAgmnHVEAAQLSELIRSLAQ--GGLTILFIEHNVGMVLEtCTRVVVLDFGEV 536
Cdd:cd03289 139 LSHGHKQLMCLARSVLSKAKILLLDEPSA---HLDPITYQVIRKTLKQafADCTVILSEHRIEAMLE-CQRFLVIEENKV 214
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
320-493 |
1.39e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 41.69 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 320 YGGVHAVRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSGsatvlgtTIGrtpvhrvAAAGVSRTF--QHSklf 397
Cdd:PRK10636 322 YGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSG-------EIG-------LAKGIKLGYfaQHQ--- 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 398 nrlsaLEnvlvgahlvsrptFLrrllwlpsaRRDErAALEHAARCLRRV------------GL-GDLAGNRASSLSYGDQ 464
Cdd:PRK10636 385 -----LE-------------FL---------RADE-SPLQHLARLAPQEleqklrdylggfGFqGDKVTEETRRFSGGEK 436
|
170 180
....*....|....*....|....*....
gi 502712709 465 RRLEIARALAAEPSLLILDEPAagmNHVE 493
Cdd:PRK10636 437 ARLVLALIVWQRPNLLLLDEPT---NHLD 462
|
|
| PRK11618 |
PRK11618 |
inner membrane ABC transporter permease protein YjfF; Provisional |
129-237 |
1.60e-03 |
|
inner membrane ABC transporter permease protein YjfF; Provisional
Pssm-ID: 183235 [Multi-domain] Cd Length: 317 Bit Score: 41.09 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 129 MAWTALAVVAYWFWRMGRSRYGRALEAIREDELAARSMGIDVGRHRLAAFVTSGAVAGLYGVLFAYYVR----LIAPS-D 203
Cdd:PRK11618 165 MALIMLAVVAIGIFLAHRTRFGNNVYAIGGNATSANLMGIPVRRTTIRIYMLSGFLATLAGIVFSLYTSagyaLAAVGvE 244
|
90 100 110
....*....|....*....|....*....|....
gi 502712709 204 FDFTAAVDGLVTAVVGGSTMFLGPILGSGFQTMI 237
Cdd:PRK11618 245 LDAIAAVVIGGTLLTGGVGTVLGTLFGVLIQGLI 278
|
|
| PRK10740 |
PRK10740 |
high-affinity branched-chain amino acid ABC transporter permease LivH; |
61-230 |
1.65e-03 |
|
high-affinity branched-chain amino acid ABC transporter permease LivH;
Pssm-ID: 182689 [Multi-domain] Cd Length: 308 Bit Score: 41.06 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 61 ALLTAVVIGMAVGAVASVVLGLPTMHLRGVFLAIATLGFA----------EAVRVV----LLNQEWT-GGAQGLAVPRIL 125
Cdd:PRK10740 76 GFVGAIVIASAYGWSIERVAYRPVRNSKRLIALISAIGMSiflqnyvsltEGSRDValpsLFNGQWVvGHSENFSASITT 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 126 TVGMAW--TALAVVAYWFWrMGRSRYGRALEAIREDELAARSMGIDVGRHRLAAFVTSGAVAGLYGVLFAYYVRLIAPSd 203
Cdd:PRK10740 156 MQAVIWivTFLAMLALTIF-IRYSRMGRACRACAEDLKMASLLGINTDRVIALTFVIGAAMAAVAGVLLGQFYGVINPY- 233
|
170 180
....*....|....*....|....*..
gi 502712709 204 FDFTAAVDGLVTAVVGGSTMFLGPILG 230
Cdd:PRK10740 234 IGFMAGMKAFTAAVLGGIGSIPGAMIG 260
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
453-559 |
4.37e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 40.40 E-value: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 453 GNRASSLSYGDQRRLEIARALAAEPSLLILDEPAAGMNHVEAAQLSELIRSLA-QGGLTILFIEHNVGMVLETcTRVVVL 531
Cdd:PTZ00265 1353 GPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKdKADKTIITIAHRIASIKRS-DKIVVF 1431
|
90 100 110
....*....|....*....|....*....|....
gi 502712709 532 DFGE-----VIASGTPAE-IAADPAVIEAYLGTA 559
Cdd:PTZ00265 1432 NNPDrtgsfVQAHGTHEElLSVQDGVYKKYVKLA 1465
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
331-505 |
7.48e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 38.07 E-value: 7.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 331 LEIRSGeVVGLIGPNGAGKTTLVN---------------MISGLVPPSSGSATV-LGTTIGRTPVHRVAAAGVSRTFQHS 394
Cdd:COG0419 19 IDFDDG-LNLIVGPNGAGKSTILEairyalygkarsrskLRSDLINVGSEEASVeLEFEHGGKRYRIERRQGEFAEFLEA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502712709 395 KLFNRLSALENvLVGAHLVSRptfLRRLLWLPSARRDERAALEHAARCLRRVGLGDLAG-NRASSLSYGDQRRLEIARAL 473
Cdd:COG0419 98 KPSERKEALKR-LLGLEIYEE---LKERLKELEEALESALEELAELQKLKQEILAQLSGlDPIETLSGGERLRLALADLL 173
|
170 180 190
....*....|....*....|....*....|..
gi 502712709 474 AaepslLILDEPAAGMNHVEaaQLSELIRSLA 505
Cdd:COG0419 174 S-----LILDFGSLDEERLE--RLLDALEELA 198
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
326-365 |
8.30e-03 |
|
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: 38.68 E-value: 8.30e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 502712709 326 VRGVDLEIRSGEVVGLIGPNGAGKTTLVNMISGLVPPSSG 365
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEG 92
|
|
| |
