|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
18-521 |
1.59e-92 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 295.15 E-value: 1.59e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 18 LLFLYPYLKNTKSLLAFGLLGMVIASLIIAPIPYIIGYIIDKVILlNKSYDQLLKTTLILLLIYCINYLISIGYEYLFTR 97
Cdd:COG1132 9 LRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLA-GGDLSALLLLLLLLLGLALLRALLSYLQRYLLAR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 98 VQQNVVNEIRLSMISNIIDAPLSYINQKEKGYILSRI-AESGNVSALFSPNLLRVFSGIFDFFFALFIMFNLSVKLTGII 176
Cdd:COG1132 88 LAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLtNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 177 VIIIPIYFVISKYSSEMISKSTTNVYESSAVLNAEMYETLNGIEDIKLLNGKNIQTNKIKAKLNDVIKSALKQSLHFIFF 256
Cdd:COG1132 168 LLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALF 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 257 MQNLIVTNNFVTVIVLLVSGILILQNQLTIGVYTSFSIYMAKLLATTQALGSLDITLKPVCISIKRIKEFFNL--DVENT 334
Cdd:COG1132 248 FPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEppEIPDP 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 335 LGTNIIKEPINSIEFKDVCFKYNENSDlIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNL 414
Cdd:COG1132 328 PGAVPLPPVRGEIEFENVSFSYPGDRP-VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRD 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 415 IHKESIRARIGIVSQNIFLFKGTILDNILYGQTNKTKEDVVKLIKRYHLTSHLNRFENGLDTIIVQDGSSVSGGQAQFIA 494
Cdd:COG1132 407 LTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIA 486
|
490 500
....*....|....*....|....*..
gi 1267372771 495 FLRAILTQRDIIILDEAASNLhiDTRN 521
Cdd:COG1132 487 IARALLKDPPILILDEATSAL--DTET 511
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
18-541 |
1.99e-85 |
|
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: 279.80 E-value: 1.99e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 18 LLFLYPYLKNTKSLLAFGLLGMVIASLIIAPIPYIIGYIIDKVILlNKSYDQLLKTTLILLLIYCINYLISIGYEYLFTR 97
Cdd:COG2274 144 LRWFLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVIDRVLP-NQDLSTLWVLAIGLLLALLFEGLLRLLRSYLLLR 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 98 VQQNVVNEIRLSMISNIIDAPLSYINQKEKGYILSRIAESGNVSALFSPNLLRVFSGIFDFFFALFIMFNLSVKLTGIIV 177
Cdd:COG2274 223 LGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFRDVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVVL 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 178 IIIPIYFVISKYSSEMISKSTTNVYESSAVLNAEMYETLNGIEDIKLLNGKNIQTNKIKAKLNDVIKSALKQSLHFIFFM 257
Cdd:COG2274 303 LLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLS 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 258 QNLIVTNNFVTVIVLLVSGILILQNQLTIGVYTSFSIYMAKLLATTQALGSLDITLKPVCISIKRIKEFFNLDVENTLGT 337
Cdd:COG2274 383 TLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPPEREEGR 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 338 NIIKEPI--NSIEFKDVCFKYNENSDLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLI 415
Cdd:COG2274 463 SKLSLPRlkGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQI 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 416 HKESIRARIGIVSQNIFLFKGTILDNILYGQTNKTKEDVVKLIKRYHLTSHLNRFENGLDTIIVQDGSSVSGGQAQFIAF 495
Cdd:COG2274 543 DPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAI 622
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1267372771 496 LRAILTQRDIIILDEAASNLHIDTRNLMYEILQNYNLCNILIMISH 541
Cdd:COG2274 623 ARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAH 668
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
321-558 |
1.32e-49 |
|
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: 180.34 E-value: 1.32e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 321 KRIKEFFNLDVENTLGTN--IIKEPINSIEFKDVCFKYnENSDLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLY 398
Cdd:COG4988 309 EKIFALLDAPEPAAPAGTapLPAAGPPSIELEDVSFSY-PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFL 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 399 QPKSGKILINNIDYNLIHKESIRARIGIVSQNIFLFKGTILDNILYGQTNKTKEDVVKLIKRYHLTSHLNRFENGLDTII 478
Cdd:COG4988 388 PPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPL 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 479 VQDGSSVSGGQAQFIAFLRAILTQRDIIILDEAASNLHIDTRNLMYEILQNYNLCNILIMISHQQDGLYFLNKTLELTHG 558
Cdd:COG4988 468 GEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDG 547
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
347-541 |
1.74e-49 |
|
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: 170.87 E-value: 1.74e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVCFKYNENSDLIFDhFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKESIRARIGI 426
Cdd:cd03254 3 IEFENVNFSYDEKKPVLKD-INFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 427 VSQNIFLFKGTILDNILYGQTNKTKEDVVKLIKRYHLTSHLNRFENGLDTIIVQDGSSVSGGQAQFIAFLRAILTQRDII 506
Cdd:cd03254 82 VLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKIL 161
|
170 180 190
....*....|....*....|....*....|....*
gi 1267372771 507 ILDEAASNLHIDTRNLMYEILQNYNLCNILIMISH 541
Cdd:cd03254 162 ILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAH 196
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
203-558 |
8.60e-49 |
|
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: 178.04 E-value: 8.60e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 203 ESSAVLNAEMYETLNGIEDIKLLNGKNIQTNKIKAKLNDVIKSALKQSLHFIF--FMQNLIVtnNFVTVIVLLVSGILIL 280
Cdd:COG4987 189 AARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLSALaqALLQLAA--GLAVVAVLWLAAPLVA 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 281 QNQLT-----IGVYTSFSIYMAkLLATTQALGSLDITLKpvciSIKRIKEFFNLDVENTL-GTNIIKEPINSIEFKDVCF 354
Cdd:COG4987 267 AGALSgpllaLLVLAALALFEA-LAPLPAAAQHLGRVRA----AARRLNELLDAPPAVTEpAEPAPAPGGPSLELEDVSF 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 355 KYNENSDLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKESIRARIGIVSQNIFLF 434
Cdd:COG4987 342 RYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLF 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 435 KGTILDNILYGQTNKTKEDVVKLIKRYHLTSHLNRFENGLDTIIVQDGSSVSGGQAQFIAFLRAILTQRDIIILDEAASN 514
Cdd:COG4987 422 DTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEG 501
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1267372771 515 LHIDT-RNLMYEILQnynLCN--ILIMISHQQDGLYFLNKTLELTHG 558
Cdd:COG4987 502 LDAATeQALLADLLE---ALAgrTVLLITHRLAGLERMDRILVLEDG 545
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
347-529 |
9.99e-48 |
|
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: 166.25 E-value: 9.99e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVCFKYNENSDLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKESIRARIGI 426
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 427 VSQNIFLFKGTILDNILYGQTNKTKEDVVKLIKRYHLTSHLNRFENGLDTIIVQDGSSVSGGQAQFIAFLRAILTQRDII 506
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180
....*....|....*....|...
gi 1267372771 507 ILDEAASNLHIDTRNLMYEILQN 529
Cdd:cd03251 161 ILDEATSALDTESERLVQAALER 183
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
93-515 |
1.49e-47 |
|
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: 174.52 E-value: 1.49e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 93 YLFTRVQQNVVNEIRLSMISNIIDAPLSYINQKEKGYILSRIA-ESGNVSALFSPNLLRVFSGIFDFFFALFIMFNLSVK 171
Cdd:TIGR02203 76 YLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITfDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQ 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 172 LTGIIVIIIPIYFVISKYSSEMISKSTTNVYESSAVLNAEMYETLNGIEDIKLLNGKNIQTNKIKAKLNDVIKSALK--- 248
Cdd:TIGR02203 156 LTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKmts 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 249 -QSLH--FIFFMQNLIVTnnfvtvIVLLVSGILILQNQLTIGVYTSFSIYMAKLLATTQALGSLDITLKPVCISIKRIKE 325
Cdd:TIGR02203 236 aGSISspITQLIASLALA------VVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFT 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 326 FFNLDVENTLGTNIIKEPINSIEFKDVCFKYNENSDLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKI 405
Cdd:TIGR02203 310 LLDSPPEKDTGTRAIERARGDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQI 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 406 LINNIDYNLIHKESIRARIGIVSQNIFLFKGTILDNILYGQTNKT-KEDVVKLIKRYHLTSHLNRFENGLDTIIVQDGSS 484
Cdd:TIGR02203 390 LLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEQAdRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVL 469
|
410 420 430
....*....|....*....|....*....|.
gi 1267372771 485 VSGGQAQFIAFLRAILTQRDIIILDEAASNL 515
Cdd:TIGR02203 470 LSGGQRQRLAIARALLKDAPILILDEATSAL 500
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
347-541 |
5.93e-47 |
|
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: 161.78 E-value: 5.93e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVCFKYNENSDLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKESIRARIGI 426
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 427 VSQNIFLFKGTILDNILygqtnktkedvvklikryhltshlnrfengldtiivqdgssvSGGQAQFIAFLRAILTQRDII 506
Cdd:cd03228 81 VPQDPFLFSGTIRENIL------------------------------------------SGGQRQRIAIARALLRDPPIL 118
|
170 180 190
....*....|....*....|....*....|....*
gi 1267372771 507 ILDEAASNLHIDTRNLMYEILQNYNLCNILIMISH 541
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGKTVIVIAH 153
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
346-543 |
4.67e-46 |
|
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: 161.22 E-value: 4.67e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 346 SIEFKDVCFKYNENSDLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKESIRARIG 425
Cdd:cd03245 2 RIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 426 IVSQNIFLFKGTILDNILYGQTNKTKEDVVKLIKRYHLTSHLNRFENGLDTIIVQDGSSVSGGQAQFIAFLRAILTQRDI 505
Cdd:cd03245 82 YVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPI 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 1267372771 506 IILDEAASNLHIDTRNLMYEILQNYNLCNILIMISHQQ 543
Cdd:cd03245 162 LLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRP 199
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
18-558 |
8.88e-45 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 168.76 E-value: 8.88e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 18 LLFLYPYLKNTKSLLafglLGMVIASLIIAPIPYIIGYIIDKVI---LLNKSYDQLLKTTLILLLIYCINYLISIGYEYL 94
Cdd:TIGR01193 144 LLKFIPLITRQKKLI----VNIVIAAIIVTLISIAGSYYLQKIIdtyIPHKMMGTLGIISIGLIIAYIIQQILSYIQIFL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 95 FTRVQQNVVNEIRLSMISNIIDAPLSYINQKEKGYILSRIAESGNVSALFSPNLLRVFSGIFDFFFALFIMFNLSVKLTG 174
Cdd:TIGR01193 220 LNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFTDASSIIDALASTILSLFLDMWILVIVGLFLVRQNMLLFL 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 175 IIVIIIPIYFVISKYSSEMISKSTTNVYESSAVLNAEMYETLNGIEDIKLLNGKNIQTNKIKAKLNDVIKSALKqsLHFI 254
Cdd:TIGR01193 300 LSLLSIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAERYSKIDSEFGDYLNKSFK--YQKA 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 255 FFMQNLI--VTNNFVTVIVLLVSGILILQNQLTIGVYTSFSIYMAKLLATTQALGSLDITLKPVCISIKRIKEFFNLDVE 332
Cdd:TIGR01193 378 DQGQQAIkaVTKLILNVVILWTGAYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEVYLVDSE 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 333 NTLGTNI--IKEPINSIEFKDVCFKYNENSDLIFDhFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNI 410
Cdd:TIGR01193 458 FINKKKRteLNNLNGDIVINDVSYSYGYGSNILSD-ISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGF 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 411 DYNLIHKESIRARIGIVSQNIFLFKGTILDNILYG-QTNKTKEDVVKLIKRYHLTSHLNRFENGLDTIIVQDGSSVSGGQ 489
Cdd:TIGR01193 537 SLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGaKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQ 616
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1267372771 490 AQFIAFLRAILTQRDIIILDEAASNLHIDTRNLMYEILQNYNLCNIlIMISHQQDGLYFLNKTLELTHG 558
Cdd:TIGR01193 617 KQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDKTI-IFVAHRLSVAKQSDKIIVLDHG 684
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
91-537 |
2.85e-44 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 167.59 E-value: 2.85e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 91 YEYLFTRVQQnvvnEIRLSMISNIIDAPLSYINQKEKGYILSRIAE---------SGNVSaLFSPNLLRVFSGifdfffa 161
Cdd:TIGR00958 225 FNYTMARINL----RIREDLFRSLLRQDLGFFDENKTGELTSRLSSdtqtmsrslSLNVN-VLLRNLVMLLGL------- 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 162 LFIMFNLSVKLTGIIVIIIPIYFVISKYSSEMISKSTTNVYESSAVLNAEMYETLNGIEDIKLLNGKNIQTNKIKAKLND 241
Cdd:TIGR00958 293 LGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEE 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 242 VIKSALKQSLHFIFFMQNLIVTNNFVTVIVLLVSGILILQNQLTIGVYTSFSIYMAKLLATTQALGSLDITLKPVCISIK 321
Cdd:TIGR00958 373 TLQLNKRKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASE 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 322 RIKEFfnLDVENTLGTNIIKEPIN---SIEFKDVCFKYNENSDL-IFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGL 397
Cdd:TIGR00958 453 KVFEY--LDRKPNIPLTGTLAPLNlegLIEFQDVSFSYPNRPDVpVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNL 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 398 YQPKSGKILINNIDYNLIHKESIRARIGIVSQNIFLFKGTILDNILYGQTNKTKEDVVKLIKRYHLTSHLNRFENGLDTI 477
Cdd:TIGR00958 531 YQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTE 610
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 478 IVQDGSSVSGGQAQFIAFLRAILTQRDIIILDEAASNLHIDTRNLMYEILQNYNLCNILI 537
Cdd:TIGR00958 611 VGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLI 670
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
347-541 |
4.22e-41 |
|
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: 148.53 E-value: 4.22e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVCFKYNENSDlIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKESIRARIGI 426
Cdd:cd03253 1 IEFENVTFAYDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 427 VSQNIFLFKGTILDNILYGQTNKTKEDVVKLIKRYHLTSHLNRFENGLDTIIVQDGSSVSGGQAQFIAFLRAILTQRDII 506
Cdd:cd03253 80 VPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPIL 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 1267372771 507 ILDEAASNLhiDTRNLMyEILQNYN-LCN--ILIMISH 541
Cdd:cd03253 160 LLDEATSAL--DTHTER-EIQAALRdVSKgrTTIVIAH 194
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
347-541 |
2.58e-40 |
|
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: 146.53 E-value: 2.58e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVCFKYNENSD-LIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKESIRARIG 425
Cdd:cd03249 1 IEFKNVSFRYPSRPDvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 426 IVSQNIFLFKGTILDNILYGQTNKTKEDVVKLIKRYHLTSHLNRFENGLDTIIVQDGSSVSGGQAQFIAFLRAILTQRDI 505
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 1267372771 506 IILDEAASNLHIDTRNLMYEILQNYNLCNILIMISH 541
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAH 196
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
93-519 |
2.85e-37 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 145.93 E-value: 2.85e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 93 YLFTRVQQNVVNEIRLSMISNIIDAPLSYINQKEKGYILSRIA-ESGNVSALFSPNLLRVF---SGIFDFFFalfIMFNL 168
Cdd:PRK11176 87 YCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITyDSEQVASSSSGALITVVregASIIGLFI---MMFYY 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 169 SVKLTGIIVIIIPIYFVISKYSSEMISKSTTNVYESSAVLNAEMYETLNGIEDIKLLNGKNIQTNKIKAKLNDVIKSALK 248
Cdd:PRK11176 164 SWQLSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQGMK 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 249 ----QSLhfiffmQNLIVT--NNFVTVIVLLVSGILILQNQLTIGVYTS-FSIYMAkLLATTQALGSLDITLKPVCISIK 321
Cdd:PRK11176 244 mvsaSSI------SDPIIQliASLALAFVLYAASFPSVMDTLTAGTITVvFSSMIA-LMRPLKSLTNVNAQFQRGMAACQ 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 322 RIKEFFNLDVENTLGTNIIKEPINSIEFKDVCFKYNENSDLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPK 401
Cdd:PRK11176 317 TLFAILDLEQEKDEGKRVIERAKGDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDID 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 402 SGKILINNIDYNLIHKESIRARIGIVSQNIFLFKGTILDNILYGQTNK-TKEDVVKLIKRYHLTSHLNRFENGLDTIIVQ 480
Cdd:PRK11176 397 EGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTVIGE 476
|
410 420 430
....*....|....*....|....*....|....*....
gi 1267372771 481 DGSSVSGGQAQFIAFLRAILTQRDIIILDEAASNLhiDT 519
Cdd:PRK11176 477 NGVLLSGGQRQRIAIARALLRDSPILILDEATSAL--DT 513
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
346-541 |
1.20e-36 |
|
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: 135.70 E-value: 1.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 346 SIEFKDVCFKYNENSDLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKESIRARIG 425
Cdd:cd03244 2 DIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 426 IVSQNIFLFKGTILDNI-LYGQtnKTKEDVVKLIKRYHLTSHLNRFENGLDTIIVQDGSSVSGGQAQFIAFLRAILTQRD 504
Cdd:cd03244 82 IIPQDPVLFSGTIRSNLdPFGE--YSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSK 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 1267372771 505 IIILDEAASNLHIDTRNLMYEILQNYNLCNILIMISH 541
Cdd:cd03244 160 ILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAH 196
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
347-559 |
1.71e-35 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 132.25 E-value: 1.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVCFKYNENSdlIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKESIRARIGI 426
Cdd:COG4619 1 LELEGLSFRVGGKP--ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 427 VSQNIFLFKGTILDNILYGQTNKTKEDVVKLIKRYhltshLNRFenGLDTIIV-QDGSSVSGGQAQFIAFLRAILTQRDI 505
Cdd:COG4619 79 VPQEPALWGGTVRDNLPFPFQLRERKFDRERALEL-----LERL--GLPPDILdKPVERLSGGERQRLALIRALLLQPDV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1267372771 506 IILDEAASNLHIDTRNLMYEILQNYNLCN--ILIMISH--QQDGLYFlNKTLELTHGN 559
Cdd:COG4619 152 LLLDEPTSALDPENTRRVEELLREYLAEEgrAVLWVSHdpEQIERVA-DRVLTLEAGR 208
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
347-558 |
1.60e-34 |
|
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: 130.68 E-value: 1.60e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVCFKYNENSDLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKESIRARIGI 426
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 427 VSQNIFLFKGTILDNILYGQTNKTKEDVVKLIKRYHLTSHLNRFENGLDTIIVQDGSSVSGGQAQFIAFLRAILTQRDII 506
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1267372771 507 ILDEAASNL-----HIDTRNlMYEILQNynlcNILIMISHQQDGLYFLNKTLELTHG 558
Cdd:cd03252 161 IFDEATSALdyeseHAIMRN-MHDICAG----RTVIIIAHRLSTVKNADRIIVMEKG 212
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
267-519 |
1.39e-33 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 135.09 E-value: 1.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 267 VTVIVLLVSGI-LILQNQLTIGVYTSFsIYMAKLLattqaLGSLD-----ITLkpVCISIKRIKEFFnlDVENTLGTniI 340
Cdd:PRK13657 252 ITMLAILVLGAaLVQKGQLRVGEVVAF-VGFATLL-----IGRLDqvvafINQ--VFMAAPKLEEFF--EVEDAVPD--V 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 341 KEPINS---------IEFKDVCFKYNENSDLIFD-HFNVQieKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNI 410
Cdd:PRK13657 320 RDPPGAidlgrvkgaVEFDDVSFSYDNSRQGVEDvSFEAK--PGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGT 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 411 DYNLIHKESIRARIGIVSQNIFLFKGTILDNILYGQTNKTKEDVVKLIKRYHLTSHLNRFENGLDTIIVQDGSSVSGGQA 490
Cdd:PRK13657 398 DIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGER 477
|
250 260
....*....|....*....|....*....
gi 1267372771 491 QFIAFLRAILTQRDIIILDEAASNLHIDT 519
Cdd:PRK13657 478 QRLAIARALLKDPPILILDEATSALDVET 506
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
347-542 |
1.65e-33 |
|
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: 127.45 E-value: 1.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVCFKYNENSDlIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKESIRARIGI 426
Cdd:COG1122 1 IELENLSFSYPGGTP-ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 427 VSQNIF--LFKGTILDNILYGQTN--KTKEDVVKLI----KRYHLTSHLNRFENGLdtiivqdgssvSGGQAQFIAFLRA 498
Cdd:COG1122 80 VFQNPDdqLFAPTVEEDVAFGPENlgLPREEIRERVeealELVGLEHLADRPPHEL-----------SGGQKQRVAIAGV 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1267372771 499 ILTQRDIIILDEAASNLHIDTRNLMYEILQNYNLCNI-LIMISHQ 542
Cdd:COG1122 149 LAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKtVIIVTHD 193
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
343-542 |
2.20e-33 |
|
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: 133.95 E-value: 2.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 343 PINSIEFKDVCFKYnENSDLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKESIRA 422
Cdd:TIGR02857 318 PASSLEFSGVSVAY-PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRD 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 423 RIGIVSQNIFLFKGTILDNILYGQTNKTKEDVVKLIKRYHLTSHLNRFENGLDTIIVQDGSSVSGGQAQFIAFLRAILTQ 502
Cdd:TIGR02857 397 QIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRD 476
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1267372771 503 RDIIILDEAASNLHIDTRNLMYEILQNYNLCNILIMISHQ 542
Cdd:TIGR02857 477 APLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHR 516
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
346-527 |
6.52e-32 |
|
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: 129.40 E-value: 6.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 346 SIEFKDVCFKYnENSDLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKESIRARIG 425
Cdd:TIGR02868 334 TLELRDLSAGY-PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVS 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 426 IVSQNIFLFKGTILDNILYGQTNKTKEDVVKLIKRYHLTSHLNRFENGLDTIIVQDGSSVSGGQAQFIAFLRAILTQRDI 505
Cdd:TIGR02868 413 VCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPI 492
|
170 180
....*....|....*....|..
gi 1267372771 506 IILDEAASNLHIDTRNLMYEIL 527
Cdd:TIGR02868 493 LLLDEPTEHLDAETADELLEDL 514
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
32-323 |
8.24e-32 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 124.59 E-value: 8.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 32 LAFGLLGMVIASLIIAPIPYIIGYIIDKVILlNKSYDQLLKTTLILLLIYCINYLISIGYEYLFTRVQQNVVNEIRLSMI 111
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIP-AGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 112 SNIIDAPLSYINQKEKGYILSRIAE-SGNVSALFSPNLLRVFSGIFDFFFALFIMFNLSVKLTGIIVIIIPIYFVISKYS 190
Cdd:cd07346 80 RHLQRLSLSFFDRNRTGDLMSRLTSdVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 191 SEMISKSTTNVYESSAVLNAEMYETLNGIEDIKLLNGKNIQTNKIKAKLNDVIKSALKQSLHFIFFMQNLIVTNNFVTVI 270
Cdd:cd07346 160 RRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTAL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1267372771 271 VLLVSGILILQNQLTIGVYTSFSIYMAKLLATTQALGSLDITLKPVCISIKRI 323
Cdd:cd07346 240 VLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
348-547 |
1.01e-30 |
|
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: 119.11 E-value: 1.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 348 EFKDVCFKYNENSDLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKESIRARIGIV 427
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 428 SQNIF--LFKGTILDNILYGQTN------KTKEDVVKLIKRYHLTSHLNRFENGLdtiivqdgssvSGGQAQFIAFLRAI 499
Cdd:cd03225 81 FQNPDdqFFGPTVEEEVAFGLENlglpeeEIEERVEEALELVGLEGLRDRSPFTL-----------SGGQKQRVAIAGVL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1267372771 500 LTQRDIIILDEAASNLHIDTRNLMYEILQNYNLCNI-LIMISHQQDGLY 547
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKtIIIVTHDLDLLL 198
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
347-542 |
1.20e-30 |
|
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: 119.50 E-value: 1.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVCFKYNENSD-LIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKESIRARIG 425
Cdd:cd03248 12 VKFQNVTFAYPTRPDtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 426 IVSQNIFLFKGTILDNILYGQTNKTKEDVVKLIKRYHLTSHLNRFENGLDTIIVQDGSSVSGGQAQFIAFLRAILTQRDI 505
Cdd:cd03248 92 LVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQV 171
|
170 180 190
....*....|....*....|....*....|....*..
gi 1267372771 506 IILDEAASNLHIDTRNLMYEILQNYNLCNILIMISHQ 542
Cdd:cd03248 172 LILDEATSALDAESEQQVQQALYDWPERRTVLVIAHR 208
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
364-513 |
4.02e-30 |
|
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: 115.44 E-value: 4.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 364 FDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKESIRARIGIVSQNIFLFKG-TILDNI 442
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1267372771 443 LYGQTNKTKEDVVKLIKRYHLTSHLnRFENGLDTIIVQDGSSVSGGQAQFIAFLRAILTQRDIIILDEAAS 513
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKL-GLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
347-541 |
6.28e-30 |
|
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: 115.78 E-value: 6.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVCFKYNENSDLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKESIRARIGI 426
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 427 VSQNIFLFKGTILDNILygqtnktkedvvklikryhltshlnrfengldtiivqdgssvSGGQAQFIAFLRAILTQRDII 506
Cdd:cd03246 81 LPQDDELFSGSIAENIL------------------------------------------SGGQRQRLGLARALYGNPRIL 118
|
170 180 190
....*....|....*....|....*....|....*.
gi 1267372771 507 ILDEAASNLHIDTRNLMYEILQNYNLCN-ILIMISH 541
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAALKAAGaTRIVIAH 154
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
346-521 |
3.73e-29 |
|
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: 121.85 E-value: 3.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 346 SIEFKDVCFKYNENSDlIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKESIRARIG 425
Cdd:COG5265 357 EVRFENVSFGYDPERP-ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIG 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 426 IVSQNIFLFKGTILDNILYGQTNKTKEDVVKLIKRYHLTSHLNRFENGLDTIIVQDGSSVSGGQAQFIAFLRAILTQRDI 505
Cdd:COG5265 436 IVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPI 515
|
170
....*....|....*.
gi 1267372771 506 IILDEAASNLhiDTRN 521
Cdd:COG5265 516 LIFDEATSAL--DSRT 529
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
151-515 |
8.01e-29 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 121.22 E-value: 8.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 151 VFSGIFDFFFaLFIMFNLSVKLTGIIVIIIPIYFVISKYSSEMISKSTTNVYESSAVLNAEMYETLNGIEDIKLLNGKNI 230
Cdd:TIGR03797 257 LLSGIFALLN-LGLMFYYSWKLALVAVALALVAIAVTLVLGLLQVRKERRLLELSGKISGLTVQLINGISKLRVAGAENR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 231 QTNKIKAKLNDVIKSALKQSlhfifFMQNLIVTnnFVTVIVLLVSGILI-------LQNQLTIGVY----TSFSIYMAKL 299
Cdd:TIGR03797 336 AFARWAKLFSRQRKLELSAQ-----RIENLLTV--FNAVLPVLTSAALFaaaisllGGAGLSLGSFlafnTAFGSFSGAV 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 300 LATTQALgsldITLKPVCISIKRIKEFFNLDVENTLGTNIIKEPINSIEFKDVCFKYNENSDLIFDHFNVQIEKGDKLLI 379
Cdd:TIGR03797 409 TQLSNTL----ISILAVIPLWERAKPILEALPEVDEAKTDPGKLSGAIEVDRVTFRYRPDGPLILDDVSLQIEPGEFVAI 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 380 DGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKESIRARIGIVSQNIFLFKGTILDNILyGQTNKTKEDVVKLIK 459
Cdd:TIGR03797 485 VGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIA-GGAPLTLDEAWEAAR 563
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1267372771 460 RYHLTSHLNRFENGLDTIIVQDGSSVSGGQAQFIAFLRAILTQRDIIILDEAASNL 515
Cdd:TIGR03797 564 MAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSAL 619
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
346-546 |
1.18e-28 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 120.31 E-value: 1.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 346 SIEFKDVCFKYNENSDLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKESIRARIG 425
Cdd:PRK11160 338 SLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAIS 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 426 IVSQNIFLFKGTILDNILYGQTNKTKEDVVKLIKRYHLTSHLNRfENGLDTIIVQDGSSVSGGQAQFIAFLRAILTQRDI 505
Cdd:PRK11160 418 VVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPL 496
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1267372771 506 IILDEAASNLHIDTRNLMYEILQNYNLCNILIMISHQQDGL 546
Cdd:PRK11160 497 LLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGL 537
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
323-558 |
1.98e-28 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 119.56 E-value: 1.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 323 IKEFFNLDVE-NTLGTNII--KEPInSIEFKDVCFKYNENSDLIfDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGL-- 397
Cdd:PRK11174 324 LVTFLETPLAhPQQGEKELasNDPV-TIEAEDLEILSPDGKTLA-GPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFlp 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 398 YQpksGKILINNIDYNLIHKESIRARIGIVSQNIFLFKGTILDNILYGQTNKTKEDVVKLIKRYHLTSHLNRFENGLDTI 477
Cdd:PRK11174 402 YQ---GSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTP 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 478 IVQDGSSVSGGQAQFIAFLRAILTQRDIIILDEAASNLHIDTRNLMYEILQNYNLCNILIMISHQQDGLYFLNKTLELTH 557
Cdd:PRK11174 479 IGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQD 558
|
.
gi 1267372771 558 G 558
Cdd:PRK11174 559 G 559
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
348-558 |
2.57e-27 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 107.72 E-value: 2.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 348 EFKDVCFKYNENSdlIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKESIRARIGIV 427
Cdd:cd00267 1 EIENLSFRYGGRT--ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 428 SQniflfkgtildnilygqtnktkedvvklikryhltshlnrfengldtiivqdgssVSGGQAQFIAFLRAILTQRDIII 507
Cdd:cd00267 79 PQ-------------------------------------------------------LSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1267372771 508 LDEAASNLHIDTRNLMYEILQNYNLCNI-LIMISHQQDGL-YFLNKTLELTHG 558
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELAEEGRtVIIVTHDPELAeLAADRVIVLKDG 156
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
347-544 |
7.90e-27 |
|
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: 108.35 E-value: 7.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVCFKYNENSDLIF--DHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNID-YNLIHKE--SIR 421
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQalKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDiSKLSEKElaAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 422 AR-IGIVSQNIFLFKG-TILDNILYGQT------NKTKEDVVKLIKRYHLTSHLNRFENGLdtiivqdgssvSGGQAQFI 493
Cdd:cd03255 81 RRhIGFVFQSFNLLPDlTALENVELPLLlagvpkKERRERAEELLERVGLGDRLNHYPSEL-----------SGGQQQRV 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1267372771 494 AFLRAILTQRDIIILDEAASNLHIDTR----NLMYEILQNYNLCniLIMISHQQD 544
Cdd:cd03255 150 AIARALANDPKIILADEPTGNLDSETGkevmELLRELNKEAGTT--IVVVTHDPE 202
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
347-558 |
3.92e-26 |
|
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: 105.09 E-value: 3.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVCFKYNENSDLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYnLIHKESIRARIGI 426
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPV-SDLEKALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 427 VSQNIFLFKGTILDNIlygqtnktkedvvklikryhltshlnrfengldtiivqdGSSVSGGQAQFIAFLRAILTQRDII 506
Cdd:cd03247 80 LNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1267372771 507 ILDEAASNLHIDTR----NLMYEILQNynlcNILIMISHQQDGLYFLNKTLELTHG 558
Cdd:cd03247 121 LLDEPTVGLDPITErqllSLIFEVLKD----KTLIWITHHLTGIEHMDKILFLENG 172
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
347-569 |
1.94e-25 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 105.17 E-value: 1.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVCFKYNENsdLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYnlihkESIRARIGI 426
Cdd:COG1121 7 IELENLTVSYGGR--PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP-----RRARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 427 VSQNIFL---FKGTILDNILYGQTNKT----------KEDVVKLIKRYHLTSHLNRfengldTIivqdgSSVSGGQAQ-- 491
Cdd:COG1121 80 VPQRAEVdwdFPITVRDVVLMGRYGRRglfrrpsradREAVDEALERVGLEDLADR------PI-----GELSGGQQQrv 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 492 FIAflRAILTQRDIIILDEAASNLHIDTRNLMYEILQNYNLCNI-LIMISHQQ-------DGLYFLNKTLeLTHGNKRNA 563
Cdd:COG1121 149 LLA--RALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKtILVVTHDLgavreyfDRVLLLNRGL-VAHGPPEEV 225
|
....*.
gi 1267372771 564 VNGSIL 569
Cdd:COG1121 226 LTPENL 231
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
347-540 |
2.85e-25 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 104.38 E-value: 2.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVCFKYNENsdLIFDHFNVQIEKGDK--LLidGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLiHKESIRARI 424
Cdd:COG1131 1 IEVRGLTKRYGDK--TALDGVSLTVEPGEIfgLL--GPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 425 GIVSQNIFLFKG-TILDNI-----LYGQTNKT-KEDVVKLIKRYHLTSHLNRFENGLdtiivqdgssvSGGQAQFIAFLR 497
Cdd:COG1131 76 GYVPQEPALYPDlTVRENLrffarLYGLPRKEaRERIDELLELFGLTDAADRKVGTL-----------SGGMKQRLGLAL 144
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1267372771 498 AILTQRDIIILDEAASNLHIDTRNLMYEILQNYNLCNILIMIS 540
Cdd:COG1131 145 ALLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLS 187
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
348-541 |
6.37e-25 |
|
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: 102.61 E-value: 6.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 348 EFKDVCFKYNENsdLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNidynlIHKESIRARIGIV 427
Cdd:cd03235 1 EVEDLTVSYGGH--PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG-----KPLEKERKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 428 SQNI---FLFKGTILDNILYG----------QTNKTKEDVVKLIKRYHLTSHLNRfengldTIivqdgSSVSGGQAQ--F 492
Cdd:cd03235 74 PQRRsidRDFPISVRDVVLMGlyghkglfrrLSKADKAKVDEALERVGLSELADR------QI-----GELSGGQQQrvL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1267372771 493 IAflRAILTQRDIIILDEAASNLHIDTRNLMYEILQNYNLCNI-LIMISH 541
Cdd:cd03235 143 LA--RALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMtILVVTH 190
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
347-559 |
2.22e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 102.76 E-value: 2.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVCFKYNENSDLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKESIRARIGI 426
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 427 VSQNI-FLFKG-TILDNILYGQTNK--TKEDVVKLIKRYHLtshlnrfENGLDTIIVQDGSSVSGGQAQFIAFLRAILTQ 502
Cdd:PRK13632 88 IFQNPdNQFIGaTVEDDIAFGLENKkvPPKKMKDIIDDLAK-------KVGMEDYLDKEPQNLSGGQKQRVAIASVLALN 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1267372771 503 RDIIILDEAASNL----HIDTRNLMYEILQNYNLCniLIMISHQQDGLYFLNKTLELTHGN 559
Cdd:PRK13632 161 PEIIIFDESTSMLdpkgKREIKKIMVDLRKTRKKT--LISITHDMDEAILADKVIVFSEGK 219
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
347-543 |
3.27e-24 |
|
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: 101.10 E-value: 3.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVCFKYNENSdlIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLY-----QPKSGKIL-----INNIDYNLIh 416
Cdd:cd03260 1 IELRDLNVYYGDKH--ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLldgkdIYDLDVDVL- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 417 keSIRARIGIVSQNIFLFKGTILDNILYGQ-------TNKTKEDVVKLIKRYHLtshlnrFENGLDTiivQDGSSVSGGQ 489
Cdd:cd03260 78 --ELRRRVGMVFQKPNPFPGSIYDNVAYGLrlhgiklKEELDERVEEALRKAAL------WDEVKDR---LHALGLSGGQ 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 490 AQFIAFLRAILTQRDIIILDEAASNLH-IDTRN---LMYEILQNYNlcniLIMISH--QQ 543
Cdd:cd03260 147 QQRLCLARALANEPEVLLLDEPTSALDpISTAKieeLIAELKKEYT----IVIVTHnmQQ 202
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
347-541 |
5.53e-24 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 101.74 E-value: 5.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVCFKYNENSDLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDY----NLIHkesIRA 422
Cdd:TIGR04520 1 IEVENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTldeeNLWE---IRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 423 RIGIVSQNIflfkgtilDNILYGQT----------------NKTKEDVVKLIKRYHLTSHLNRFENGLdtiivqdgssvS 486
Cdd:TIGR04520 78 KVGMVFQNP--------DNQFVGATveddvafglenlgvprEEMRKRVDEALKLVGMEDFRDREPHLL-----------S 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 487 GGQAQFIAfLRAILTQR-DIIILDEAASNLHIDTR----NLMYEILQNYNLCniLIMISH 541
Cdd:TIGR04520 139 GGQKQRVA-IAGVLAMRpDIIILDEATSMLDPKGRkevlETIRKLNKEEGIT--VISITH 195
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
347-542 |
8.28e-24 |
|
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: 100.32 E-value: 8.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVCFKYNENsdLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDynlIHKESIRAR--I 424
Cdd:COG4555 2 IEVENLSKKYGKV--PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGED---VRKEPREARrqI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 425 GIVSQNIFLFKG-TILDNI-----LYGQTNK-TKEDVVKLIKRYHLTSHLNRFENGLdtiivqdgssvSGGQAQFIAFLR 497
Cdd:COG4555 77 GVLPDERGLYDRlTVRENIryfaeLYGLFDEeLKKRIEELIELLGLEEFLDRRVGEL-----------STGMKKKVALAR 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1267372771 498 AILTQRDIIILDEAASNLHIDTRNLMYEILQNYNLCNILIMIS-HQ 542
Cdd:COG4555 146 ALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSsHI 191
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
106-558 |
1.05e-23 |
|
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: 106.18 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 106 IRLSMISNIIDAPLSYINQKEKGYILSRIAESGNVSALFSPNLLRVFSGIFDFFFALFIMFNLSVKLTGII--------V 177
Cdd:TIGR00957 1040 LHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIipplgllyF 1119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 178 IIIPIYFVISKYSSEMISKSTTNVYessavlnAEMYETLNGIEDIKLLNGKN--IQTNKIKAKLNdviksalkQSLHFIF 255
Cdd:TIGR00957 1120 FVQRFYVASSRQLKRLESVSRSPVY-------SHFNETLLGVSVIRAFEEQErfIHQSDLKVDEN--------QKAYYPS 1184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 256 FMQN--LIVTNNFVTVIVLLVSGI--LILQNQLT---IGVYTSFSIYMAKLLATTQALGSldiTLKPVCISIKRIKEFFN 328
Cdd:TIGR00957 1185 IVANrwLAVRLECVGNCIVLFAALfaVISRHSLSaglVGLSVSYSLQVTFYLNWLVRMSS---EMETNIVAVERLKEYSE 1261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 329 LDVENTLgtnIIKE--------PINSIEFKDVCFKYNENSDLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQP 400
Cdd:TIGR00957 1262 TEKEAPW---QIQEtappsgwpPRGRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINES 1338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 401 KSGKILINNIDYNLIHKESIRARIGIVSQNIFLFKGTILDNI-LYGQTnkTKEDVVKLIKRYHLTSHLNRFENGLDTIIV 479
Cdd:TIGR00957 1339 AEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLdPFSQY--SDEEVWWALELAHLKTFVSALPDKLDHECA 1416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 480 QDGSSVSGGQAQFIAFLRAILTQRDIIILDEAASNLHIDTRNLMYE-ILQNYNLCNILiMISHQQDGLYFLNKTLELTHG 558
Cdd:TIGR00957 1417 EGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQStIRTQFEDCTVL-TIAHRLNTIMDYTRVIVLDKG 1495
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
347-542 |
1.24e-23 |
|
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: 98.70 E-value: 1.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVCFKYNENSDLIFDHF---NVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNidynlihkesiraR 423
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFTLkdiNLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 424 IGIVSQNIFLFKGTILDNILYGQT-NKTK-EDVVKLIkryHLTSHLNRFENGLDTIIVQDGSSVSGGQAQFIAFLRAILT 501
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKPfDEERyEKVIKAC---ALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYS 144
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1267372771 502 QRDIIILDEAASNLHIDTRNLMYE--ILQNYNLCNILIMISHQ 542
Cdd:cd03250 145 DADIYLLDDPLSAVDAHVGRHIFEncILGLLLNNKTRILVTHQ 187
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
347-553 |
1.36e-23 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 99.44 E-value: 1.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVCFKYNensDLIFdHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDynlIHKESIRAR-IG 425
Cdd:COG3840 2 LRLDDLTYRYG---DFPL-RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQD---LTALPPAERpVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 426 IVSQ--NIF--LfkgTILDNILYGQ------TNKTKEDVVKLIKRYHLTSHLNRFEngldtiivqdgSSVSGGQAQFIAF 495
Cdd:COG3840 75 MLFQenNLFphL---TVAQNIGLGLrpglklTAEQRAQVEQALERVGLAGLLDRLP-----------GQLSGGQRQRVAL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1267372771 496 LRAILTQRDIIILDEAASNLHIDTRNLMY----EILQNYNLcnILIMISHQ-QDGLYFLNKTL 553
Cdd:COG3840 141 ARCLVRKRPILLLDEPFSALDPALRQEMLdlvdELCRERGL--TVLMVTHDpEDAARIADRVL 201
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
347-544 |
2.19e-23 |
|
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: 98.36 E-value: 2.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVCFKYNenSDLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDynlIHKESIRAR-IG 425
Cdd:cd03259 1 LELKGLSKTYG--SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRD---VTGVPPERRnIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 426 IVSQNIFLFKG-TILDNILYGQTNK------TKEDVVKLIKRYHLTSHLNRFENGLdtiivqdgssvSGGQAQFIAFLRA 498
Cdd:cd03259 76 MVFQDYALFPHlTVAENIAFGLKLRgvpkaeIRARVRELLELVGLEGLLNRYPHEL-----------SGGQQQRVALARA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1267372771 499 ILTQRDIIILDEAASNLHIDTRNLMYEILQNY--NLCNILIMISHQQD 544
Cdd:cd03259 145 LAREPSLLLLDEPLSALDAKLREELREELKELqrELGITTIYVTHDQE 192
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
341-515 |
2.27e-23 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 100.09 E-value: 2.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 341 KEPInsIEFKDVCFKYNENSDLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKESI 420
Cdd:PRK13635 2 KEEI--IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 421 RARIGIVSQNI-FLFKG-TILDNILYGQTNK--TKEDVVK----LIKRYHLTSHLNRfengldtiivqDGSSVSGGQAQF 492
Cdd:PRK13635 80 RRQVGMVFQNPdNQFVGaTVQDDVAFGLENIgvPREEMVErvdqALRQVGMEDFLNR-----------EPHRLSGGQKQR 148
|
170 180
....*....|....*....|....
gi 1267372771 493 IAfLRAILTQR-DIIILDEAASNL 515
Cdd:PRK13635 149 VA-IAGVLALQpDIIILDEATSML 171
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
347-529 |
2.33e-23 |
|
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: 98.31 E-value: 2.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVCFKYNENSD--LIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNidynlihkESIR--- 421
Cdd:cd03293 1 LEVRNVSKTYGGGGGavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG--------EPVTgpg 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 422 ARIGIVSQNIFLF--KgTILDNILYG------QTNKTKEDVVKLIKRYHLTSHLNRFENGLdtiivqdgssvSGGQAQFI 493
Cdd:cd03293 73 PDRGYVFQQDALLpwL-TVLDNVALGlelqgvPKAEARERAEELLELVGLSGFENAYPHQL-----------SGGMRQRV 140
|
170 180 190
....*....|....*....|....*....|....*.
gi 1267372771 494 AFLRAILTQRDIIILDEAASNLHIDTRNLMYEILQN 529
Cdd:cd03293 141 ALARALAVDPDVLLLDEPFSALDALTREQLQEELLD 176
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
347-540 |
6.00e-23 |
|
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: 95.93 E-value: 6.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVCFKYNENsdLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNlIHKESIRARIGI 426
Cdd:cd03230 1 IEVRNLSKRYGKK--TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIK-KEPEEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 427 VSQNIFLFKG-TILDNILYgqtnktkedvvklikryhltshlnrfengldtiivqdgssvSGGQAQFIAFLRAILTQRDI 505
Cdd:cd03230 78 LPEEPSLYENlTVRENLKL-----------------------------------------SGGMKQRLALAQALLHDPEL 116
|
170 180 190
....*....|....*....|....*....|....*
gi 1267372771 506 IILDEAASNLHIDTRNLMYEILQNYNLCNILIMIS 540
Cdd:cd03230 117 LILDEPTSGLDPESRREFWELLRELKKEGKTILLS 151
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
271-515 |
8.42e-23 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 102.04 E-value: 8.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 271 VLLVSGILILQNQLTIGVYTSFSIYMAKLLATTQALGSLDITLKPVCISIKRIKEFFNLDVENTLGTNIiKEPINSIEFK 350
Cdd:TIGR01842 242 VLGLGAYLAIDGEITPGMMIAGSILVGRALAPIDGAIGGWKQFSGARQAYKRLNELLANYPSRDPAMPL-PEPEGHLSVE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 351 DVCFKYNENSDLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKESIRARIGIVSQN 430
Cdd:TIGR01842 321 NVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQD 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 431 IFLFKGTILDNILYGQTNKTKEDVVKLIKRYHLTSHLNRFENGLDTIIVQDGSSVSGGQAQFIAFLRAILTQRDIIILDE 510
Cdd:TIGR01842 401 VELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDE 480
|
....*
gi 1267372771 511 AASNL 515
Cdd:TIGR01842 481 PNSNL 485
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
347-531 |
1.13e-22 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 96.66 E-value: 1.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVCFKYnENSDLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKESI---RAR 423
Cdd:COG2884 2 IRFENVSKRY-PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIpylRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 424 IGIVSQNI-FLFKGTILDNILY-----GQTNKT-KEDVVKLIKRYHLTSHLNRFENGLdtiivqdgssvSGGQAQFIAFL 496
Cdd:COG2884 81 IGVVFQDFrLLPDRTVYENVALplrvtGKSRKEiRRRVREVLDLVGLSDKAKALPHEL-----------SGGEQQRVAIA 149
|
170 180 190
....*....|....*....|....*....|....*.
gi 1267372771 497 RAILTQRDIIILDEAASNLHIDT-RNLMyEILQNYN 531
Cdd:COG2884 150 RALVNRPELLLADEPTGNLDPETsWEIM-ELLEEIN 184
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
220-558 |
1.19e-22 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 101.81 E-value: 1.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 220 EDIKLLNGKNIQTNKIKAKLNDVIKSALK---QSLHFIFFmqnlIVTNNFVTVIV-LLVSGILILQNQLTIGVYT----- 290
Cdd:COG4178 232 ESIALYRGEAAERRRLRRRFDAVIANWRRlirRQRNLTFF----TTGYGQLAVIFpILVAAPRYFAGEITLGGLMqaasa 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 291 ------SFSIYM------AKLLATTQALGSLDITLKpvcisikrikeffNLDVENTLGTNIIKEPINSIEFKDVCFkYNE 358
Cdd:COG4178 308 fgqvqgALSWFVdnyqslAEWRATVDRLAGFEEALE-------------AADALPEAASRIETSEDGALALEDLTL-RTP 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 359 NSDLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNidynlihkesiRARIGIVSQNIFLFKGTI 438
Cdd:COG4178 374 DGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPA-----------GARVLFLPQRPYLPLGTL 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 439 LDNILYGQTNK--TKEDVVKLIKRYHLTSHLNRfengLDTiiVQDGSSV-SGGQAQFIAFLRAILTQRDIIILDEAASNL 515
Cdd:COG4178 443 REALLYPATAEafSDAELREALEAVGLGHLAER----LDE--EADWDQVlSLGEQQRLAFARLLLHKPDWLFLDEATSAL 516
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1267372771 516 HIDTRNLMYEILQNyNLCNI-LIMISHQQDGLYFLNKTLELTHG 558
Cdd:COG4178 517 DEENEAALYQLLRE-ELPGTtVISVGHRSTLAAFHDRVLELTGD 559
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
347-557 |
3.07e-22 |
|
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: 94.85 E-value: 3.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVCFKYNENsdLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNlIHKESIRARIGI 426
Cdd:COG4133 3 LEAENLSCRRGER--LLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIR-DAREDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 427 VSQNIFLFKG-TILDNI-----LYGqTNKTKEDVVKLIKRYHLTSHLNRFengldtiivqdGSSVSGGQAQFIAFLRAIL 500
Cdd:COG4133 80 LGHADGLKPElTVRENLrfwaaLYG-LRADREAIDEALEAVGLAGLADLP-----------VRQLSAGQKRRVALARLLL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 501 TQRDIIILDEAASNLHIDTRNLMYEILQNYnlCN---ILIMISHQQDGLYFLnKTLELTH 557
Cdd:COG4133 148 SPAPLWLLDEPFTALDAAGVALLAELIAAH--LArggAVLLTTHQPLELAAA-RVLDLGD 204
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
347-541 |
5.25e-22 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 94.73 E-value: 5.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVCFKYN--ENSDLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDynlIHKES----- 419
Cdd:COG1136 5 LELRNLTKSYGtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQD---ISSLSerela 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 420 -IRAR-IGIVSQNIFLFKG-TILDNILYGQT------NKTKEDVVKLIKRYHLTSHLNRFENGLdtiivqdgssvSGGQA 490
Cdd:COG1136 82 rLRRRhIGFVFQFFNLLPElTALENVALPLLlagvsrKERRERARELLERVGLGDRLDHRPSQL-----------SGGQQ 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1267372771 491 QFIAFLRAILTQRDIIILDEAASNLHIDTRNLMYEILQNYN--LCNILIMISH 541
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNreLGTTIVMVTH 203
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
346-559 |
6.17e-22 |
|
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: 94.02 E-value: 6.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 346 SIEFKDVCFKYNENSDLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKESIRARIG 425
Cdd:cd03369 6 EIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 426 IVSQNIFLFKGTILDNI-LYGQtnKTKEDVVKLIKryhltshlnrfengldtiIVQDGSSVSGGQAQFIAFLRAILTQRD 504
Cdd:cd03369 86 IIPQDPTLFSGTIRSNLdPFDE--YSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLKRPR 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1267372771 505 IIILDEAASNLHIDTRNLMYEILQNYNLCNILIMISHQQDGLYFLNKTLELTHGN 559
Cdd:cd03369 146 VLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGE 200
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
278-558 |
1.25e-21 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 98.63 E-value: 1.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 278 LILQNQLTIGVYTSFSIYMAKLLATTQALGSLDITLKPVCISIKRIKEFFNLDVENTLGTNIIKEPINSIEFKDVCFKYN 357
Cdd:PRK10789 245 MVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAEAPVVKDGSEPVPEGRGELDVNIRQFTYP 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 358 ENSDLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKESIRARIGIVSQNIFLFKGT 437
Cdd:PRK10789 325 QTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDT 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 438 ILDNILYGQTNKTKEDVVKLIKRYHLTSHLNRFENGLDTIIVQDGSSVSGGQAQFIAFLRAILTQRDIIILDEAASNlhI 517
Cdd:PRK10789 405 VANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSA--V 482
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1267372771 518 DTRNlMYEILQN---YNLCNILIMISHQQDGLYFLNKTLELTHG 558
Cdd:PRK10789 483 DGRT-EHQILHNlrqWGEGRTVIISAHRLSALTEASEILVMQHG 525
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
342-541 |
1.74e-21 |
|
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: 98.05 E-value: 1.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 342 EPInsIEFKDVCFKYNENSDLIF---DHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKE 418
Cdd:COG1123 258 EPL--LEVRNLSKRYPVRGKGGVravDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 419 SIRA---RIGIVSQNIF--LFKG-TILDNI-----LYGQTNKT--KEDVVKLIKRYHL-TSHLNRFENGLdtiivqdgss 484
Cdd:COG1123 336 SLRElrrRVQMVFQDPYssLNPRmTVGDIIaeplrLHGLLSRAerRERVAELLERVGLpPDLADRYPHEL---------- 405
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1267372771 485 vSGGQAQFIAFLRAILTQRDIIILDEAASNLHIDTR----NLMYEILQNYNLCniLIMISH 541
Cdd:COG1123 406 -SGGQRQRVAIARALALEPKLLILDEPTSALDVSVQaqilNLLRDLQRELGLT--YLFISH 463
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
347-544 |
1.80e-21 |
|
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: 91.86 E-value: 1.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVCFKYNENsdLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKES--IRARI 424
Cdd:cd03229 1 LELKNVSKRYGQK--TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 425 GIVSQNIFLFKG-TILDNILYGqtnktkedvvklikryhltshlnrfengldtiivqdgssVSGGQAQFIAFLRAILTQR 503
Cdd:cd03229 79 GMVFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMDP 119
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1267372771 504 DIIILDEAASNLHIDTRNLMYEILQ--NYNLCNILIMISHQQD 544
Cdd:cd03229 120 DVLLLDEPTSALDPITRREVRALLKslQAQLGITVVLVTHDLD 162
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
266-515 |
2.00e-21 |
|
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: 97.90 E-value: 2.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 266 FVTVIVLLVSGILILQNQLTIGVYTSFSIYMAKLLA-----------TTQALGSLditlkpvcisiKRIKEFFNLDVENT 334
Cdd:COG4618 251 LLQSAVLGLGAYLVIQGEITPGAMIAASILMGRALApieqaiggwkqFVSARQAY-----------RRLNELLAAVPAEP 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 335 LGTNIiKEPINSIEFKDVCFKYNENSDLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNL 414
Cdd:COG4618 320 ERMPL-PRPKGRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQ 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 415 IHKESIRARIGIVSQNIFLFKGTILDNI-LYGQTNktKEDVVK---------LIkryhltshlNRFENGLDTIIVQDGSS 484
Cdd:COG4618 399 WDREELGRHIGYLPQDVELFDGTIAENIaRFGDAD--PEKVVAaaklagvheMI---------LRLPDGYDTRIGEGGAR 467
|
250 260 270
....*....|....*....|....*....|.
gi 1267372771 485 VSGGQAQFIAFLRAILTQRDIIILDEAASNL 515
Cdd:COG4618 468 LSGGQRQRIGLARALYGDPRLVVLDEPNSNL 498
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
363-558 |
5.97e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 96.29 E-value: 5.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 363 IFDHFNVQIEKGDKL-LIdGINGSGKSTFIKLLTGLYQPKSGKILINNidynlihkesiRARIGIVSQNIFLFKG-TILD 440
Cdd:COG0488 13 LLDDVSLSINPGDRIgLV-GRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYLPQEPPLDDDlTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 441 NILYGqtnktKEDVVKLIKRYHLTSH--------LNRFENGLDTIIVQDG-------------------------SSVSG 487
Cdd:COG0488 81 TVLDG-----DAELRALEAELEELEAklaepdedLERLAELQEEFEALGGweaearaeeilsglgfpeedldrpvSELSG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1267372771 488 GQAQFIAFLRAILTQRDIIILDEAASNLHIDTRNLMYEILQNYNlcNILIMISHqqDgLYFL----NKTLELTHG 558
Cdd:COG0488 156 GWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYP--GTVLVVSH--D-RYFLdrvaTRILELDRG 225
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
347-548 |
1.44e-20 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 95.42 E-value: 1.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVCFKYNENSdliFD--HFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKESIRARI 424
Cdd:PRK10522 323 LELRNVTFAYQDNG---FSvgPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 425 GIVSQNIFLFkgtilDNILYGQ-TNKTKEDVVKLIKRYHLTSHLNRFENGLDTIivqdgsSVSGGQAQFIAFLRAILTQR 503
Cdd:PRK10522 400 SAVFTDFHLF-----DQLLGPEgKPANPALVEKWLERLKMAHKLELEDGRISNL------KLSKGQKKRLALLLALAEER 468
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1267372771 504 DIIILDEAASNLHIDTRNLMYEILQNY--NLCNILIMISHqqDGLYF 548
Cdd:PRK10522 469 DILLLDEWAADQDPHFRREFYQVLLPLlqEMGKTIFAISH--DDHYF 513
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
347-515 |
1.54e-20 |
|
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: 90.28 E-value: 1.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVCFKYNENSdlIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKE--SIRARI 424
Cdd:cd03262 1 IEIKNLHKSFGDFH--VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 425 GIVSQNIFLFKG-TILDNILYGQT---NKTKEDVVKLIKRYhltshLNRFenGLDTIIVQDGSSVSGGQAQFIAFLRAIL 500
Cdd:cd03262 79 GMVFQQFNLFPHlTVLENITLAPIkvkGMSKAEAEERALEL-----LEKV--GLADKADAYPAQLSGGQQQRVAIARALA 151
|
170
....*....|....*
gi 1267372771 501 TQRDIIILDEAASNL 515
Cdd:cd03262 152 MNPKVMLFDEPTSAL 166
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
109-558 |
2.11e-20 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 95.81 E-value: 2.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 109 SMISNIIDAPLSYINQKEKGYILSRIAES-GNVSALFSpNLLRVFsgiFDFFFALFIMFNLsVKLTGIIVIIIPIYFVIS 187
Cdd:PLN03232 988 AMLNSILRAPMLFFHTNPTGRVINRFSKDiGDIDRNVA-NLMNMF---MNQLWQLLSTFAL-IGTVSTISLWAIMPLLIL 1062
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 188 KYSSEMISKSTT-NVYESSAVLNAEMY----ETLNGIEDIK---------LLNGKNIQTNkikaklndviksalkqslhf 253
Cdd:PLN03232 1063 FYAAYLYYQSTSrEVRRLDSVTRSPIYaqfgEALNGLSSIRaykaydrmaKINGKSMDNN-------------------- 1122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 254 IFFMQNLIVTNNFVTVIVLLVSGILI-------------LQNQL----TIGVYTSFSIYMAKLLA-----TTQALGSLDi 311
Cdd:PLN03232 1123 IRFTLANTSSNRWLTIRLETLGGVMIwltatfavlrngnAENQAgfasTMGLLLSYTLNITTLLSgvlrqASKAENSLN- 1201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 312 tlkpvciSIKRIKEFFNLDVEntlGTNIIK--EPIN------SIEFKDVCFKYNENSDLIFDHFNVQIEKGDKLLIDGIN 383
Cdd:PLN03232 1202 -------SVERVGNYIDLPSE---ATAIIEnnRPVSgwpsrgSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRT 1271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 384 GSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKESIRARIGIVSQNIFLFKGTILDNI-LYGQTNKTkeDVVKLIKRYH 462
Cdd:PLN03232 1272 GAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIdPFSEHNDA--DLWEALERAH 1349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 463 LTSHLNRFENGLDTIIVQDGSSVSGGQAQFIAFLRAILTQRDIIILDEAASNLHIDTRNLMYE-ILQNYNLCNILImISH 541
Cdd:PLN03232 1350 IKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRtIREEFKSCTMLV-IAH 1428
|
490
....*....|....*..
gi 1267372771 542 QQDGLYFLNKTLELTHG 558
Cdd:PLN03232 1429 RLNTIIDCDKILVLSSG 1445
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
345-541 |
2.83e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 90.97 E-value: 2.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 345 NSIEFKDVCFKYNENSDLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKESIRARI 424
Cdd:PRK13648 6 SIIVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 425 GIVSQNI-FLFKGTILD-NILYGQTN------KTKEDVVKLIKRYHLTSHLNrfengldtiivQDGSSVSGGQAQFIAFL 496
Cdd:PRK13648 86 GIVFQNPdNQFVGSIVKyDVAFGLENhavpydEMHRRVSEALKQVDMLERAD-----------YEPNALSGGQKQRVAIA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1267372771 497 RAILTQRDIIILDEAASNLHIDTR----NLMYEILQNYNLcnILIMISH 541
Cdd:PRK13648 155 GVLALNPSVIILDEATSMLDPDARqnllDLVRKVKSEHNI--TIISITH 201
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
365-541 |
3.01e-20 |
|
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: 89.87 E-value: 3.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 365 DHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKE---SIRARIGIVSQNIF-----LFK- 435
Cdd:cd03257 22 DDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRlrkIRRKEIQMVFQDPMsslnpRMTi 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 436 GTILDNILYGQTNKTKEDVVKLIKRYHL------TSHLNRFENGLdtiivqdgssvSGGQAQFIAFLRAILTQRDIIILD 509
Cdd:cd03257 102 GEQIAEPLRIHGKLSKKEARKEAVLLLLvgvglpEEVLNRYPHEL-----------SGGQRQRVAIARALALNPKLLIAD 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 1267372771 510 EAASNLHIDTR----NLMYEILQNYNLCniLIMISH 541
Cdd:cd03257 171 EPTSALDVSVQaqilDLLKKLQEELGLT--LLFITH 204
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
347-558 |
3.18e-20 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 89.39 E-value: 3.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVCFKYnENSDLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKESI---RAR 423
Cdd:cd03292 1 IEFINVTKTY-PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIpylRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 424 IGIVSQ-NIFLFKGTILDN------ILYGQTNKTKEDVVKLIKRYHLTSHLNRFENGLdtiivqdgssvSGGQAQFIAFL 496
Cdd:cd03292 80 IGVVFQdFRLLPDRNVYENvafaleVTGVPPREIRKRVPAALELVGLSHKHRALPAEL-----------SGGEQQRVAIA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1267372771 497 RAILTQRDIIILDEAASNLHIDTRNLMYEILQNYNLCNILIMISHQQDGLY--FLNKTLELTHG 558
Cdd:cd03292 149 RAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVdtTRHRVIALERG 212
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
85-512 |
3.39e-20 |
|
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: 94.09 E-value: 3.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 85 YLISIGYEYLFTRVQQNVVNEIRLSMISNIIDAPLSYINQKEKGYILSRIAESGNVSALFSPNLLRVFSGIFDFFFALFI 164
Cdd:COG4615 62 LLSRLASQLLLTRLGQHAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFVRLPELLQSVALVLGCLAY 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 165 MFNLSVKLTGIIVIIIPIYFVISKYSSEMISKSTTNVYESSAVLNAEMYETLNGIEDIKLlngkniqtNKIKAK--LNDV 242
Cdd:COG4615 142 LAWLSPPLFLLTLVLLGLGVAGYRLLVRRARRHLRRAREAEDRLFKHFRALLEGFKELKL--------NRRRRRafFDED 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 243 IKSALKQSLHFIFFMQNLIVTN-NFVTVIVLLVSG-ILILQNQLTI---GVYTSFS---IYM----AKLLATTQALGSLD 310
Cdd:COG4615 214 LQPTAERYRDLRIRADTIFALAnNWGNLLFFALIGlILFLLPALGWadpAVLSGFVlvlLFLrgplSQLVGALPTLSRAN 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 311 ItlkpvciSIKRIKEFF-----NLDVENTLGTNIIKEPINSIEFKDVCFKYNENSDlifDH------FNVQIEKGDKLLI 379
Cdd:COG4615 294 V-------ALRKIEELElalaaAEPAAADAAAPPAPADFQTLELRGVTYRYPGEDG---DEgftlgpIDLTIRRGELVFI 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 380 DGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKESIRARIGIVSQNIFLFKGtildniLYGQTNKTKEDVV-KLI 458
Cdd:COG4615 364 VGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDR------LLGLDGEADPARArELL 437
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1267372771 459 KRYHLtSHLNRFENG-LDTIivqdgsSVSGGQAQFIAFLRAILTQRDIIILDE-AA 512
Cdd:COG4615 438 ERLEL-DHKVSVEDGrFSTT------DLSQGQRKRLALLVALLEDRPILVFDEwAA 486
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
345-558 |
5.93e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 90.18 E-value: 5.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 345 NSIEFKDVCFKYNENSD-LIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILinnIDYNLIHKES---I 420
Cdd:PRK13650 3 NIIEVKNLTFKYKEDQEkYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQII---IDGDLLTEENvwdI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 421 RARIGIVSQNI-FLFKG-TILDNILYGQTNKTKEdvvklikryhLTSHLNRFENGLDTIIVQD-----GSSVSGGQAQFI 493
Cdd:PRK13650 80 RHKIGMVFQNPdNQFVGaTVEDDVAFGLENKGIP----------HEEMKERVNEALELVGMQDfkerePARLSGGQKQRV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1267372771 494 AFLRAILTQRDIIILDEAASNLHIDTR----NLMYEILQNYNLcnILIMISHQQDGLYFLNKTLELTHG 558
Cdd:PRK13650 150 AIAGAVAMRPKIIILDEATSMLDPEGRleliKTIKGIRDDYQM--TVISITHDLDEVALSDRVLVMKNG 216
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
347-541 |
1.23e-19 |
|
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: 88.56 E-value: 1.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVCFKYNENSdlIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDynlIHKESIRA---R 423
Cdd:COG1120 2 LEAENLSVGYGGRP--VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRD---LASLSRRElarR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 424 IGIVSQ-NIFLFKGTILDNILYGQT-------NKTKED---VVKLIKRYHLTSHLNRFengLDTIivqdgssvSGGQAQ- 491
Cdd:COG1120 77 IAYVPQePPAPFGLTVRELVALGRYphlglfgRPSAEDreaVEEALERTGLEHLADRP---VDEL--------SGGERQr 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1267372771 492 -FIAflRAILTQRDIIILDEAASNL---H-IDTRNLMYEILQNYNLCniLIMISH 541
Cdd:COG1120 146 vLIA--RALAQEPPLLLLDEPTSHLdlaHqLEVLELLRRLARERGRT--VVMVLH 196
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
347-547 |
1.32e-19 |
|
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: 87.94 E-value: 1.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVCFKYNENSdlIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNID-YNLIHKE--SIRAR 423
Cdd:cd03261 1 IELRGLTKSFGGRT--VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDiSGLSEAElyRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 424 IGIVSQNIFLFKG-TILDNI---LYGQTNKTKEDVVKLIKryhltSHLNRFenGLDTIIVQDGSSVSGGQAQFIAFLRAI 499
Cdd:cd03261 79 MGMLFQSGALFDSlTVFENVafpLREHTRLSEEEIREIVL-----EKLEAV--GLRGAEDLYPAELSGGMKKRVALARAL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1267372771 500 LTQRDIIILDEAASNLHIDTRNLMYEILQNYN--LCNILIMISHQQDGLY 547
Cdd:cd03261 152 ALDPELLLYDEPTAGLDPIASGVIDDLIRSLKkeLGLTSIMVTHDLDTAF 201
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
347-541 |
1.42e-19 |
|
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: 88.11 E-value: 1.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVCFKYNENsdLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDY-NLIHKE--SIRAR 423
Cdd:COG1127 6 IEVRNLTKSFGDR--VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDItGLSEKElyELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 424 IGIVSQNIFLFKG-TILDNILYG---QTNKTKEDVVKLIKRYhltshLNRFenGLDTIIVQDGSSVSGGQAQFIAFLRAI 499
Cdd:COG1127 84 IGMLFQGGALFDSlTVFENVAFPlreHTDLSEAEIRELVLEK-----LELV--GLPGAADKMPSELSGGMRKRVALARAL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1267372771 500 LTQRDIIILDEAASNL------HIDtrNLMYEILQNYNLCniLIMISH 541
Cdd:COG1127 157 ALDPEILLYDEPTAGLdpitsaVID--ELIRELRDELGLT--SVVVTH 200
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
350-515 |
1.79e-19 |
|
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: 86.93 E-value: 1.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 350 KDVCFKYNENSDLIfDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDynlIHKESIRARIGIVSQ 429
Cdd:cd03226 3 ENISFSYKKGTEIL-DDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKP---IKAKERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 430 NI--FLFKGTILDNILYG--QTNKTKEDVVKLIKRYHLtshlnrfeNGLDTiivQDGSSVSGGQAQFIAFLRAILTQRDI 505
Cdd:cd03226 79 DVdyQLFTDSVREELLLGlkELDAGNEQAETVLKDLDL--------YALKE---RHPLSLSGGQKQRLAIAAALLSGKDL 147
|
170
....*....|
gi 1267372771 506 IILDEAASNL 515
Cdd:cd03226 148 LIFDEPTSGL 157
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
347-558 |
2.06e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 91.66 E-value: 2.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVCFKYNENsdLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKIlinnidynlihKESIRARIGI 426
Cdd:COG0488 316 LELEGLSKSYGDK--TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV-----------KLGETVKIGY 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 427 VSQNIFLFKG--TILDNILYGQTNKTKEdvvklikryHLTSHLNRF---ENGLDTIIvqdgSSVSGGQAQFIAFLRAILT 501
Cdd:COG0488 383 FDQHQEELDPdkTVLDELRDGAPGGTEQ---------EVRGYLGRFlfsGDDAFKPV----GVLSGGEKARLALAKLLLS 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1267372771 502 QRDIIILDEAASNLHIDTRNLMYEILQNYNLCniLIMISHQQdglYFL----NKTLELTHG 558
Cdd:COG0488 450 PPNVLLLDEPTNHLDIETLEALEEALDDFPGT--VLLVSHDR---YFLdrvaTRILEFEDG 505
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
268-569 |
2.87e-19 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 92.40 E-value: 2.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 268 TVIVLLVsGILILQNQLTIgVYTSFSIYMaKLLATTQALGSLdITLKPVcisikrikeffnldVENTLGTNIIKEpINSI 347
Cdd:PTZ00265 323 SVISILL-GVLISMFMLTI-ILPNITEYM-KSLEATNSLYEI-INRKPL--------------VENNDDGKKLKD-IKKI 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 348 EFKDVCFKYNENSDL-IFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNiDYNL--IHKESIRARI 424
Cdd:PTZ00265 384 QFKNVRFHYDTRKDVeIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIND-SHNLkdINLKWWRSKI 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 425 GIVSQNIFLFKGTILDNILYG---------------------QTNKTKE------------------------------- 452
Cdd:PTZ00265 463 GVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyynedgndsQENKNKRnscrakcagdlndmsnttdsneliemrknyq 542
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 453 -----DVVKLIKRYHLTSHLNRFENGLDTIIVQDGSSVSGGQAQFIAFLRAILTQRDIIILDEAASNLHIDTRNLMYEIL 527
Cdd:PTZ00265 543 tikdsEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1267372771 528 QNY--NLCNILIMISHQQDGLYFLNKTLELTHGNKRNAVNGSIL 569
Cdd:PTZ00265 623 NNLkgNENRITIIIAHRLSTIRYANTIFVLSNRERGSTVDVDII 666
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
347-559 |
3.72e-19 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 87.27 E-value: 3.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVCFKYNENSDLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKESIRARIGI 426
Cdd:cd03288 20 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 427 VSQNIFLFKGTILDNiLYGQTNKTKEDVVKLIKRYHLTSHLNRFENGLDTIIVQDGSSVSGGQAQFIAFLRAILTQRDII 506
Cdd:cd03288 100 ILQDPILFSGSIRFN-LDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSIL 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1267372771 507 ILDEAASNLHIDTRNLMYEILQNYNLCNILIMISHQQDGLYFLNKTLELTHGN 559
Cdd:cd03288 179 IMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGI 231
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
347-510 |
4.68e-19 |
|
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: 86.59 E-value: 4.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVCFKYNENSDLIfDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKESIRARIGI 426
Cdd:cd03295 1 IEFENVTKRYGGGKKAV-NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 427 VSQNIFLFKG-TILDNI-----LYGQTNKTKEDVVK-LIKRYHL--TSHLNRFENGLdtiivqdgssvSGGQAQFIAFLR 497
Cdd:cd03295 80 VIQQIGLFPHmTVEENIalvpkLLKWPKEKIRERADeLLALVGLdpAEFADRYPHEL-----------SGGQQQRVGVAR 148
|
170
....*....|...
gi 1267372771 498 AILTQRDIIILDE 510
Cdd:cd03295 149 ALAADPPLLLMDE 161
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
368-526 |
6.11e-19 |
|
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: 86.24 E-value: 6.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 368 NVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKEsiRARIGIVSQNIFLFKG-TILDNILYGQ 446
Cdd:cd03299 19 SLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFPHmTVYKNIAYGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 447 TNKtKEDVVKLIKRYHLTSHLnrfeNGLDTIIVQDGSSVSGGQAQFIAFLRAILTQRDIIILDEAASNLHIDTR-NLMYE 525
Cdd:cd03299 97 KKR-KVDKKEIERKVLEIAEM----LGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKeKLREE 171
|
.
gi 1267372771 526 I 526
Cdd:cd03299 172 L 172
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
81-323 |
7.74e-19 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 87.12 E-value: 7.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 81 YCINYLISIGYEYLFTRVQQNVVNEIRLSMISNIIDAPLSYINQKEKGYILSRIAESGNVSALFSPNLLRVFSGIFDFFF 160
Cdd:cd18570 52 YLFQSLLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFETRKTGEIISRFNDANKIREAISSTTISLFLDLLMVII 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 161 ALFIMFNLSVKLTGIIVIIIPIYFVISKYSSEMISKSTTNVYESSAVLNAEMYETLNGIEDIKLLNGKNIQTNKIKAKLN 240
Cdd:cd18570 132 SGIILFFYNWKLFLITLLIIPLYILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFS 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 241 DVIKSALKQSLHFIFFMQNLIVTNNFVTVIVLLVSGILILQNQLTIGVYTSFSIYMAKLLATTQALGSLDITLKPVCISI 320
Cdd:cd18570 212 KLLKKSFKLGKLSNLQSSIKGLISLIGSLLILWIGSYLVIKGQLSLGQLIAFNALLGYFLGPIENLINLQPKIQEAKVAA 291
|
...
gi 1267372771 321 KRI 323
Cdd:cd18570 292 DRL 294
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
346-542 |
1.46e-18 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 90.18 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 346 SIEFKDVCFKYNENSDLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKESIRARIG 425
Cdd:PLN03130 1237 SIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLG 1316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 426 IVSQNIFLFKGTILDNI-LYGQTNKTkeDVVKLIKRYHLTSHLNRFENGLDTIIVQDGSSVSGGQAQFIAFLRAILTQRD 504
Cdd:PLN03130 1317 IIPQAPVLFSGTVRFNLdPFNEHNDA--DLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSK 1394
|
170 180 190
....*....|....*....|....*....|....*....
gi 1267372771 505 IIILDEAASNLHIDTRNLMYE-ILQNYNLCNILImISHQ 542
Cdd:PLN03130 1395 ILVLDEATAAVDVRTDALIQKtIREEFKSCTMLI-IAHR 1432
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
346-541 |
1.65e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 85.87 E-value: 1.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 346 SIEFKDVCFKYNENSDL---IFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDY--NLIHKESI 420
Cdd:PRK13637 2 SIKIENLTHIYMEGTPFekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 421 RARIGIVSQ--NIFLFKGTILDNILYGQTNK--TKEDVVKLIKRYHLTShlnrfenGLDTIIVQDGS--SVSGGQAQFIA 494
Cdd:PRK13637 82 RKKVGLVFQypEYQLFEETIEKDIAFGPINLglSEEEIENRVKRAMNIV-------GLDYEDYKDKSpfELSGGQKRRVA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1267372771 495 FLRAILTQRDIIILDEAASNLHIDTR----NLMYEILQNYNlcNILIMISH 541
Cdd:PRK13637 155 IAGVVAMEPKILILDEPTAGLDPKGRdeilNKIKELHKEYN--MTIILVSH 203
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
347-557 |
2.20e-18 |
|
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: 82.59 E-value: 2.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVCFkYNENSDLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKIlinnidynlIHKEsiRARIGI 426
Cdd:cd03223 1 IELENLSL-ATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---------GMPE--GEDLLF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 427 VSQNIFLFKGTILDNILYgqtnkTKEDVVklikryhltshlnrfengldtiivqdgssvSGGQAQFIAFLRAILTQRDII 506
Cdd:cd03223 69 LPQRPYLPLGTLREQLIY-----PWDDVL------------------------------SGGEQQRLAFARLLLHKPKFV 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1267372771 507 ILDEAASNLHIDTRNLMYEILQnyNLCNILIMISHQQDGLYFLNKTLELTH 557
Cdd:cd03223 114 FLDEATSALDEESEDRLYQLLK--ELGITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
346-558 |
4.50e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 84.88 E-value: 4.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 346 SIEFKDVCFKYNENSDLI---FDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILI--NNIDYNLIHK--E 418
Cdd:PRK13641 2 SIKFENVDYIYSPGTPMEkkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIagYHITPETGNKnlK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 419 SIRARIGIVSQ--NIFLFKGTILDNILYGQTN------KTKEDVVKLIKRYHLTshlnrfenglDTIIVQDGSSVSGGQA 490
Cdd:PRK13641 82 KLRKKVSLVFQfpEAQLFENTVLKDVEFGPKNfgfsedEAKEKALKWLKKVGLS----------EDLISKSPFELSGGQM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 491 QFIAFLRAILTQRDIIILDEAASNLHIDTRNLMYEILQNYNLC-NILIMISHQQDGLY-FLNKTLELTHG 558
Cdd:PRK13641 152 RRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAgHTVILVTHNMDDVAeYADDVLVLEHG 221
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
347-529 |
6.29e-18 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 83.60 E-value: 6.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVCFKYNENSD--LIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYnlihkESIRARI 424
Cdd:COG1116 8 LELRGVSKRFPTGGGgvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPV-----TGPGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 425 GIVSQNIFLF--KgTILDNILYG------QTNKTKEDVVKLIKRYHLTSHLNRFENGLdtiivqdgssvSGGQAQFIAFL 496
Cdd:COG1116 83 GVVFQEPALLpwL-TVLDNVALGlelrgvPKAERRERARELLELVGLAGFEDAYPHQL-----------SGGMRQRVAIA 150
|
170 180 190
....*....|....*....|....*....|...
gi 1267372771 497 RAILTQRDIIILDEAASNLHIDTRNLMYEILQN 529
Cdd:COG1116 151 RALANDPEVLLMDEPFGALDALTRERLQDELLR 183
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
347-528 |
1.74e-17 |
|
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: 81.40 E-value: 1.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVCFKYNENSDLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYnLIHKESIRARIGI 426
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI-RTDRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 427 VSQNIFLFKG-TILDNI-----LYGQTNKT-KEDVVKLIKRYHLTSHLNRFENGLdtiivqdgssvSGGQAQFIAFLRAI 499
Cdd:cd03263 80 CPQFDALFDElTVREHLrfyarLKGLPKSEiKEEVELLLRVLGLTDKANKRARTL-----------SGGMKRKLSLAIAL 148
|
170 180
....*....|....*....|....*....
gi 1267372771 500 LTQRDIIILDEAASNLHIDTRNLMYEILQ 528
Cdd:cd03263 149 IGGPSVLLLDEPTSGLDPASRRAIWDLIL 177
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
347-541 |
1.80e-17 |
|
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: 82.16 E-value: 1.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVC--FKYNENSDLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKESIRARI 424
Cdd:COG1124 2 LEVRNLSvsYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 425 GIVSQNIFLF---KGTILDNI-----LYGQTNkTKEDVVKLIKRYHLT-SHLNRFengldtiivqdGSSVSGGQAQFIAF 495
Cdd:COG1124 82 QMVFQDPYASlhpRHTVDRILaeplrIHGLPD-REERIAELLEQVGLPpSFLDRY-----------PHQLSGGQRQRVAI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1267372771 496 LRAILTQRDIIILDEAASNLHIDTR----NLMYEILQNYNLCniLIMISH 541
Cdd:COG1124 150 ARALILEPELLLLDEPTSALDVSVQaeilNLLKDLREERGLT--YLFVSH 197
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
286-542 |
1.90e-17 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 85.54 E-value: 1.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 286 IGVYTSFSIYMAKL------LATTQALgslditLKPVCISIKRIKEFFNlDVENTLGTNIikEPINS--IEFKDVCFKYN 357
Cdd:PRK10790 281 VGVLYAFISYLGRLneplieLTTQQSM------LQQAVVAGERVFELMD-GPRQQYGNDD--RPLQSgrIDIDNVSFAYR 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 358 ENSdLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKESIRARIGIVSQNIFLFKGT 437
Cdd:PRK10790 352 DDN-LVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADT 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 438 ILDNILYGQtNKTKEDVVKLIKRYHLTSHLNRFENGLDTIIVQDGSSVSGGQAQFIAFLRAILTQRDIIILDEAASNLHI 517
Cdd:PRK10790 431 FLANVTLGR-DISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDS 509
|
250 260
....*....|....*....|....*
gi 1267372771 518 DTRNLMYEILQNYNLCNILIMISHQ 542
Cdd:PRK10790 510 GTEQAIQQALAAVREHTTLVVIAHR 534
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
364-553 |
2.49e-17 |
|
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: 80.80 E-value: 2.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 364 FDHFNVQIE---KGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDY----NLIHKESIRARIGIVSQNIFLFKG 436
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsrKKINLPPQQRKIGLVFQQYALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 437 -TILDNILYG----QTNKTKEDVVKLIKRYHLTSHLNRFENGLdtiivqdgssvSGGQAQFIAFLRAILTQRDIIILDEA 511
Cdd:cd03297 90 lNVRENLAFGlkrkRNREDRISVDELLDLLGLDHLLNRYPAQL-----------SGGEKQRVALARALAAQPELLLLDEP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1267372771 512 ASNLHIDTRN----LMYEILQNYNLcnILIMISHQQDGLYFLNKTL 553
Cdd:cd03297 159 FSALDRALRLqllpELKQIKKNLNI--PVIFVTHDLSEAEYLADRI 202
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
83-296 |
3.13e-17 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 82.52 E-value: 3.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 83 INYLISIGYEYLFTRVQQNVVNEIRLSMISNIIDAPLSYINQKEKGYILSR-IAESGNVSALFSPNLLRVFSGIFDFFFA 161
Cdd:cd18545 52 VNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSRPVGKILSRvINDVNSLSDLLSNGLINLIPDLLTLVGI 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 162 LFIMFNLSVKLTGIIVIIIPIYFVISKYSSEMISKSTTNVYESSAVLNAEMYETLNGIEDIKLLNGKNIQTNKIKAKLND 241
Cdd:cd18545 132 VIIMFSLNVRLALVTLAVLPLLVLVVFLLRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRE 211
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1267372771 242 VIKSALKQSLHFIFFMQNLIVTNNFVTVIVLLVSGILILQNQLTIGVYTSFSIYM 296
Cdd:cd18545 212 NRKANMRAVRLNALFWPLVELISALGTALVYWYGGKLVLGGAITVGVLVAFIGYV 266
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
347-544 |
3.26e-17 |
|
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: 80.61 E-value: 3.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVCFKYNENSDlifdHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNliHKESIRARIGI 426
Cdd:cd03298 1 VRLDKIRFSYGEQPM----HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVT--AAPPADRPVSM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 427 VSQNIFLFKG-TILDNILYGQTNKTKedvVKLIKRYHLTSHLNRFenGLDTIIVQDGSSVSGGQAQFIAFLRAILTQRDI 505
Cdd:cd03298 75 LFQENNLFAHlTVEQNVGLGLSPGLK---LTAEDRQAIEVALARV--GLAGLEKRLPGELSGGERQRVALARVLVRDKPV 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1267372771 506 IILDEAASNLHIDTRNLMYEILQnyNLC----NILIMISHQQD 544
Cdd:cd03298 150 LLLDEPFAALDPALRAEMLDLVL--DLHaetkMTVLMVTHQPE 190
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
347-544 |
3.42e-17 |
|
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: 81.09 E-value: 3.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVCFKYNENSDLI--FDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKES---IR 421
Cdd:cd03258 2 IELKNVSKVFGDTGGKVtaLKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrkAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 422 ARIGIVSQNIFLFKG-TILDNILY-----GQT-NKTKEDVVKLIKRYHLTSHLNRFEngldtiivqdgSSVSGGQAQFIA 494
Cdd:cd03258 82 RRIGMIFQHFNLLSSrTVFENVALpleiaGVPkAEIEERVLELLELVGLEDKADAYP-----------AQLSGGQKQRVG 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1267372771 495 FLRAILTQRDIIILDEAASNLHIDTRN----LMYEILQNYNLcnILIMISHQQD 544
Cdd:cd03258 151 IARALANNPKVLLCDEATSALDPETTQsilaLLRDINRELGL--TIVLITHEME 202
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
366-544 |
4.03e-17 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 80.78 E-value: 4.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 366 HFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDynliHKESIRAR--IGIVSQNIFLFKG-TILDNI 442
Cdd:PRK10771 17 RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD----HTTTPPSRrpVSMLFQENNLFSHlTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 443 LYGQ------TNKTKEDVVKLIKRYHLTSHLNRFEngldtiivqdgSSVSGGQAQFIAFLRAILTQRDIIILDEAASNLH 516
Cdd:PRK10771 93 GLGLnpglklNAAQREKLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
170 180 190
....*....|....*....|....*....|..
gi 1267372771 517 IDTRNLMYEILQnyNLCN----ILIMISHQQD 544
Cdd:PRK10771 162 PALRQEMLTLVS--QVCQerqlTLLMVSHSLE 191
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
347-537 |
5.08e-17 |
|
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: 81.44 E-value: 5.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVCFKYNENSDLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKsGKILINNIDYNLIHKESIRARIGI 426
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 427 VSQNIFLFKGTILDNI-LYGQTNktKEDVVKLIKRYHLTSHLNRFENGLDTIIVQDGSSVSGGQAQFIAFLRAILTQRDI 505
Cdd:cd03289 82 IPQKVFIFSGTFRKNLdPYGKWS--DEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190
....*....|....*....|....*....|...
gi 1267372771 506 IILDEAASNLHIDTRNLMYEIL-QNYNLCNILI 537
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLkQAFADCTVIL 192
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
366-515 |
6.38e-17 |
|
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: 81.15 E-value: 6.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 366 HFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKESIRA----RIGIVSQNIFLF-KGTILD 440
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLpHRTVLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 441 NILYG------QTNKTKEDVVKLIKRYHLTSHLNRFENGLdtiivqdgssvSGGQAQFIAFLRAILTQRDIIILDEAASN 514
Cdd:cd03294 122 NVAFGlevqgvPRAEREERAAEALELVGLEGWEHKYPDEL-----------SGGMQQRVGLARALAVDPDILLMDEAFSA 190
|
.
gi 1267372771 515 L 515
Cdd:cd03294 191 L 191
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
81-295 |
9.09e-17 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 80.91 E-value: 9.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 81 YCINYLISIGYEYLFTRVQQNVVNEIRLSMISNIIDAPLSYINQKEKGYILSRI---AEsgNVSALFSPNLLRVFSGIFD 157
Cdd:cd18547 55 YLLSALFSYLQNRLMARVSQRTVYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVtndVD--NISQALSQSLTQLISSILT 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 158 FFFALFIMFNLSVKLTGIIVIIIPIYFVISKYSSEMISKSTTNVYESSAVLNAEMYETLNGIEDIKLLNGKNIQTNKIKA 237
Cdd:cd18547 133 IVGTLIMMLYISPLLTLIVLVTVPLSLLVTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDE 212
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1267372771 238 KLNDVIKSALK-QSLHFIFF--MQNLivtNNFVTVIVLLVSGILILQNQLTIGVYTSFSIY 295
Cdd:cd18547 213 INEELYKASFKaQFYSGLLMpiMNFI---NNLGYVLVAVVGGLLVINGALTVGVIQAFLQY 270
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
346-510 |
1.34e-16 |
|
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: 79.31 E-value: 1.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 346 SIEFKDVCFKYNENSDLifDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDynlIHKESIRAR-I 424
Cdd:cd03296 2 SIEVRNVSKRFGDFVAL--DDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGED---ATDVPVQERnV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 425 GIVSQNIFLFKG-TILDNILYG----------QTNKTKEDVVKLIKRYHLTSHLNRFENGLdtiivqdgssvSGGQAQFI 493
Cdd:cd03296 77 GFVFQHYALFRHmTVFDNVAFGlrvkprserpPEAEIRAKVHELLKLVQLDWLADRYPAQL-----------SGGQRQRV 145
|
170
....*....|....*..
gi 1267372771 494 AFLRAILTQRDIIILDE 510
Cdd:cd03296 146 ALARALAVEPKVLLLDE 162
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
348-541 |
1.48e-16 |
|
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: 77.86 E-value: 1.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 348 EFKDVCFKYNENSdlIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKESIRARIGIV 427
Cdd:cd03214 1 EVENLSVGYGGRT--VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 428 SQNIFLFkgtildnilygqtnktkeDVVKLIKRYhltshlnrfengLDTIivqdgssvSGGQAQFIAFLRAILTQRDIII 507
Cdd:cd03214 79 PQALELL------------------GLAHLADRP------------FNEL--------SGGERQRVLLARALAQEPPILL 120
|
170 180 190
....*....|....*....|....*....|....*.
gi 1267372771 508 LDEAASNLHIDTRNLMYEILQNYNL-CNIL-IMISH 541
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRRLAReRGKTvVMVLH 156
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
347-515 |
1.58e-16 |
|
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: 78.45 E-value: 1.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVCFKYNENSDLifDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYN-LIHKESiraRIG 425
Cdd:cd03301 1 VELENVTKRFGNVTAL--DDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTdLPPKDR---DIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 426 IVSQNIFLFKG-TILDNILYG-QTNKTKEDVVKliKRYHLTSHLNRFENGLDTIIVQdgssVSGGQAQFIAFLRAILTQR 503
Cdd:cd03301 76 MVFQNYALYPHmTVYDNIAFGlKLRKVPKDEID--ERVREVAELLQIEHLLDRKPKQ----LSGGQRQRVALGRAIVREP 149
|
170
....*....|..
gi 1267372771 504 DIIILDEAASNL 515
Cdd:cd03301 150 KVFLMDEPLSNL 161
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
93-309 |
1.93e-16 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 79.91 E-value: 1.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 93 YLFTRVQQNVVNEIRLSMISNIIDAPLSYINQKEKGYILSRIaeSGNVSAL---FSPNLLRVFSGIFDFFFALFIMFNLS 169
Cdd:cd18557 58 YLFNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRL--SSDTSVLqsaVTDNLSQLLRNILQVIGGLIILFILS 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 170 VKLTGIIVIIIPIYFVISKYSSEMISKSTTNVYESSAVLNAEMYETLNGIEDIKLLNGKNIQTNKIKAKLNDVIKSALKQ 249
Cdd:cd18557 136 WKLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKK 215
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 250 SLHFIFFMQNLIVTNNFVTVIVLLVSGILILQNQLTIGVYTSFSIYMAKLLATTQALGSL 309
Cdd:cd18557 216 ALANALFQGITSLLIYLSLLLVLWYGGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSL 275
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
86-302 |
2.98e-16 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 79.22 E-value: 2.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 86 LISIGYEYLFTRVQQNVVNEIRLSMISNIIDAPLSYINQKEKGYILSRIA-ESGNVSALFSPNLLRVFSGIFDFFFALFI 164
Cdd:pfam00664 56 ILSFLQSYLLNHTGERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTnDTSKIRDGLGEKLGLLFQSLATIVGGIIV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 165 MFNLSVKLTGIIVIIIPIYFVISKYSSEMISKSTTNVYESSAVLNAEMYETLNGIEDIKLLNGKNIQTNKIKAKLNDVIK 244
Cdd:pfam00664 136 MFYYGWKLTLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALK 215
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1267372771 245 SALKQSLHFIFFMQNLIVTNNFVTVIVLLVSGILILQNQLTIGVYTSFSIYMAKLLAT 302
Cdd:pfam00664 216 AGIKKAVANGLSFGITQFIGYLSYALALWFGAYLVISGELSVGDLVAFLSLFAQLFGP 273
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
82-313 |
3.12e-16 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 79.45 E-value: 3.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 82 CINYLISIGYEYLFTRVQQNVVNEIRLSMISNIIDAPLSYINQKEKGYILSRIA-ESGNVSALFSPNLLRVFSGIFDFFF 160
Cdd:cd18550 50 VASALLGVVQTYLSARIGQGVMYDLRVQLYAHLQRMSLAFFTRTRTGEIQSRLNnDVGGAQSVVTGTLTSVVSNVVTLVA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 161 ALFIMFNLSVKLTGIIVIIIPIYFVISKYSSEMISKSTTNVYESSAVLNAEMYETLN--GIEDIKLLNGKNIQTNKIKAK 238
Cdd:cd18550 130 TLVAMLALDWRLALLSLVLLPLFVLPTRRVGRRRRKLTREQQEKLAELNSIMQETLSvsGALLVKLFGREDDEAARFARR 209
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1267372771 239 LNDVIKSALKQSLHFIFFMQNLIVTNNFVTVIVLLVSGILILQNQLTIGVYTSFSIYMAKLLATTQALGSLDITL 313
Cdd:cd18550 210 SRELRDLGVRQALAGRWFFAALGLFTAIGPALVYWVGGLLVIGGGLTIGTLVAFTALLGRLYGPLTQLLNIQVDL 284
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
347-543 |
3.31e-16 |
|
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: 78.05 E-value: 3.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVCFKYNenSDLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYN--LIHKEsiraRI 424
Cdd:cd03300 1 IELENVSKFYG--GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITnlPPHKR----PV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 425 GIVSQNIFLFKG-TILDNILYGQTNK------TKEDVVKLIKRYHLTSHLNRFENGLdtiivqdgssvSGGQAQFIAFLR 497
Cdd:cd03300 75 NTVFQNYALFPHlTVFENIAFGLRLKklpkaeIKERVAEALDLVQLEGYANRKPSQL-----------SGGQQQRVAIAR 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1267372771 498 AILTQRDIIILDEAASNLHIDTRNLMYEILQNY--NLCNILIMISHQQ 543
Cdd:cd03300 144 ALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLqkELGITFVFVTHDQ 191
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
328-523 |
6.43e-16 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 81.61 E-value: 6.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 328 NLDVENTLG-----TNIIKepiNSIEFKDVCFKYNENSDL-IFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPK 401
Cdd:PTZ00265 1145 NIDVRDNGGiriknKNDIK---GKIEIMDVNFRYISRPNVpIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLK 1221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 402 ------------------------------------------------------SGKILINNI---DYNLihkESIRARI 424
Cdd:PTZ00265 1222 ndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfknSGKILLDGVdicDYNL---KDLRNLF 1298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 425 GIVSQNIFLFKGTILDNILYGQTNKTKEDVVKLIKRYHLTSHLNRFENGLDTIIVQDGSSVSGGQAQFIAFLRAILTQRD 504
Cdd:PTZ00265 1299 SIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPK 1378
|
250
....*....|....*....
gi 1267372771 505 IIILDEAASNLHIDTRNLM 523
Cdd:PTZ00265 1379 ILLLDEATSSLDSNSEKLI 1397
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
357-559 |
6.63e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 77.82 E-value: 6.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 357 NENsdLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDY-NLihKESIRAR-IGIVSQNIflF 434
Cdd:COG1101 17 NEK--RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVtKL--PEYKRAKyIGRVFQDP--M 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 435 KGT-----ILDNIL------------YGQTNKTKEDVVKLIKRYHLTshlnrFENGLDTIIvqdgSSVSGGQAQFIAFLR 497
Cdd:COG1101 91 MGTapsmtIEENLAlayrrgkrrglrRGLTKKRRELFRELLATLGLG-----LENRLDTKV----GLLSGGQRQALSLLM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1267372771 498 AILTQRDIIILDE--AAsnlhIDTR------NLMYEILQNYNLCNilIMISHQ-QDGLYFLNKTLELTHGN 559
Cdd:COG1101 162 ATLTKPKLLLLDEhtAA----LDPKtaalvlELTEKIVEENNLTT--LMVTHNmEQALDYGNRLIMMHEGR 226
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
347-558 |
9.13e-16 |
|
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: 77.05 E-value: 9.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVCFKYNENsdLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGkilinnidyNLIH-------KES 419
Cdd:COG1119 4 LELRNVTVRRGGK--TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYG---------NDVRlfgerrgGED 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 420 I---RARIGIVS---QNIFLFKGTILDNIL---YGQ-------TNKTKEDVVKLIKRYHLTSHLNR-Fengldtiivqdg 482
Cdd:COG1119 73 VwelRKRIGLVSpalQLRFPRDETVLDVVLsgfFDSiglyrepTDEQRERARELLELLGLAHLADRpF------------ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 483 SSVSGGQAQ--FIAflRAILTQRDIIILDEAASNLHIDTRNLMYEILQnyNLCNI----LIMISHQ-QDGLYFLNKTLEL 555
Cdd:COG1119 141 GTLSQGEQRrvLIA--RALVKDPELLILDEPTAGLDLGARELLLALLD--KLAAEgaptLVLVTHHvEEIPPGITHVLLL 216
|
...
gi 1267372771 556 THG 558
Cdd:COG1119 217 KDG 219
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
346-544 |
1.02e-15 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 78.65 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 346 SIEFKDVCFKYNeNSDLIFDhFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNlIHKeSIRAR-I 424
Cdd:COG1118 2 SIEVRNISKRFG-SFTLLDD-VSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLF-TNL-PPRERrV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 425 GIVSQNIFLFKG-TILDNILYGQTNK------TKEDVVKLIKRYHLTSHLNRFENGLdtiivqdgssvSGGQAQFIAFLR 497
Cdd:COG1118 78 GFVFQHYALFPHmTVAENIAFGLRVRppskaeIRARVEELLELVQLEGLADRYPSQL-----------SGGQRQRVALAR 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1267372771 498 AILTQRDIIILDEAASNLhiDT-------RNLMyEILQNYNLcnILIMISHQQD 544
Cdd:COG1118 147 ALAVEPEVLLLDEPFGAL--DAkvrkelrRWLR-RLHDELGG--TTVFVTHDQE 195
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
381-510 |
1.43e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 79.29 E-value: 1.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 381 GINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIH-KESIRARIGIVSQNIFLFKG-TILDNILYGQ---------TNK 449
Cdd:COG1129 37 GENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSpRDAQAAGIAIIHQELNLVPNlSVAENIFLGReprrgglidWRA 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1267372771 450 TKEDVVKLIKRYHLtsHLNrfengLDTIIvqdgSSVSGGQAQFIAFLRAILTQRDIIILDE 510
Cdd:COG1129 117 MRRRARELLARLGL--DID-----PDTPV----GDLSVAQQQLVEIARALSRDARVLILDE 166
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
345-525 |
2.91e-15 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 77.45 E-value: 2.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 345 NSIEFKDVCFKYNENSdlIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDynlIHKESIRAR- 423
Cdd:PRK11432 5 NFVVLKNITKRFGSNT--VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGED---VTHRSIQQRd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 424 IGIVSQNIFLFKG-TILDNILYG--QTNKTKEDVVKLIKRYHLTSHLNRFEnglDTIIVQdgssVSGGQAQFIAFLRAIL 500
Cdd:PRK11432 80 ICMVFQSYALFPHmSLGENVGYGlkMLGVPKEERKQRVKEALELVDLAGFE---DRYVDQ----ISGGQQQRVALARALI 152
|
170 180
....*....|....*....|....*
gi 1267372771 501 TQRDIIILDEAASNLHIDTRNLMYE 525
Cdd:PRK11432 153 LKPKVLLFDEPLSNLDANLRRSMRE 177
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
340-560 |
3.26e-15 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 75.14 E-value: 3.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 340 IKEPINSIEFKDVCFKYNENSdlIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKES 419
Cdd:PRK10247 1 MQENSPLLQLQNVGYLAGDAK--ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 420 IRARIGIVSQNIFLFKGTILDNILYG-QTNKTKEDVVKLIKryhltsHLNRFenGL-DTIIVQDGSSVSGGQAQFIAFLR 497
Cdd:PRK10247 79 YRQQVSYCAQTPTLFGDTVYDNLIFPwQIRNQQPDPAIFLD------DLERF--ALpDTILTKNIAELSGGEKQRISLIR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1267372771 498 AILTQRDIIILDEAASNLHIDTRNLMYEILQNYNL-CNILIM-ISHQQDGLYFLNKTLELT-HGNK 560
Cdd:PRK10247 151 NLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVReQNIAVLwVTHDKDEINHADKVITLQpHAGE 216
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
368-510 |
4.60e-15 |
|
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: 74.39 E-value: 4.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 368 NVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDynLIHKESI-RARIGI--VSQNIFLFKG-TILDNIL 443
Cdd:cd03224 20 SLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRD--ITGLPPHeRARAGIgyVPEGRRIFPElTVEENLL 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1267372771 444 YGQTNKTKEDVVKLIKRYhltshLNRFENgLDTIIVQDGSSVSGGQAQFIAFLRAILTQRDIIILDE 510
Cdd:cd03224 98 LGAYARRRAKRKARLERV-----YELFPR-LKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDE 158
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
345-544 |
4.83e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 75.61 E-value: 4.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 345 NSIEFKDVCFKYNENSDLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKS---GKILINNIDYNLIHKESIR 421
Cdd:PRK13640 4 NIVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKTVWDIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 422 ARIGIVSQNI-FLFKG-TILDNILYGQTNK--TKEDVVKLIKRYhltshLNrfENGLDTIIVQDGSSVSGGQAQFIAFLR 497
Cdd:PRK13640 84 EKVGIVFQNPdNQFVGaTVGDDVAFGLENRavPRPEMIKIVRDV-----LA--DVGMLDYIDSEPANLSGGQKQRVAIAG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1267372771 498 AILTQRDIIILDEAASNLHIDTRNLMYEILQNYNLCNILIMISHQQD 544
Cdd:PRK13640 157 ILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHD 203
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
347-558 |
7.83e-15 |
|
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: 71.71 E-value: 7.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVCFKYNENsdLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKIlinnidynlihKESIRARIGI 426
Cdd:cd03221 1 IELENLSKTYGGK--LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV-----------TWGSTVKIGY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 427 VSQniflfkgtildnilygqtnktkedvvklikryhltshlnrfengldtiivqdgssVSGGQAQFIAFLRAILTQRDII 506
Cdd:cd03221 68 FEQ-------------------------------------------------------LSGGEKMRLALAKLLLENPNLL 92
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1267372771 507 ILDEAASNLHIDTRNLMYEILQNYNlcNILIMISHQQdglYFL----NKTLELTHG 558
Cdd:cd03221 93 LLDEPTNHLDLESIEALEEALKEYP--GTVILVSHDR---YFLdqvaTKIIELEDG 143
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
347-541 |
8.05e-15 |
|
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: 77.25 E-value: 8.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVCFKYNENSDLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPK---SGKILINNIDYNLIHKESIRAR 423
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 424 IGIVSQNIF--LFKGTILDNILYGQTNKT------KEDVVKLIKRYHLTSHLNRFENGLdtiivqdgssvSGGQAQFIAF 495
Cdd:COG1123 85 IGMVFQDPMtqLNPVTVGDQIAEALENLGlsraeaRARVLELLEAVGLERRLDRYPHQL-----------SGGQRQRVAI 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1267372771 496 LRAILTQRDIIILDEAASNLHIDTRN----LMYEILQNYNLCniLIMISH 541
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAeildLLRELQRERGTT--VLLITH 201
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
365-541 |
8.84e-15 |
|
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: 74.01 E-value: 8.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 365 DHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDynlI--HKESIRARIGIVS--QNIFLFKG-TIL 439
Cdd:cd03219 17 DDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGED---ItgLPPHEIARLGIGRtfQIPRLFPElTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 440 DNILYGQTNKTKEDVVKLIKRYHLTSHLNRFENGLDTIIVQD-----GSSVSGGQAQFIAFLRAILTQRDIIILDEAASN 514
Cdd:cd03219 94 ENVMVAAQARTGSGLLLARARREEREARERAEELLERVGLADladrpAGELSYGQQRRLEIARALATDPKLLLLDEPAAG 173
|
170 180
....*....|....*....|....*...
gi 1267372771 515 LHIDTRNLMYEILQNYNLCNI-LIMISH 541
Cdd:cd03219 174 LNPEETEELAELIRELRERGItVLLVEH 201
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
345-537 |
1.01e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 74.74 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 345 NSIEFKDVCFKYNEN----SDLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDY-NLIHKES 419
Cdd:PRK13633 3 EMIKCKNVSYKYESNeestEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTsDEENLWD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 420 IRARIGIVSQN----IFlfkGTIL-DNILYGQTN---------KTKEDVVKLIKRYHLTSHLNRFengldtiivqdgssV 485
Cdd:PRK13633 83 IRNKAGMVFQNpdnqIV---ATIVeEDVAFGPENlgippeeirERVDESLKKVGMYEYRRHAPHL--------------L 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1267372771 486 SGGQAQFIAFLRAILTQRDIIILDEAASNLHIDTR----NLMYEILQNYNLCNILI 537
Cdd:PRK13633 146 SGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRrevvNTIKELNKKYGITIILI 201
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
350-546 |
1.73e-14 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 76.87 E-value: 1.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 350 KDVCFKYNENSDLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKsGKILINNIDYNLIHKESIRARIGIVSQ 429
Cdd:TIGR01271 1221 QGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWRKAFGVIPQ 1299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 430 NIFLFKGTILDNiLYGQTNKTKEDVVKLIKRYHLTSHLNRFENGLDTIIVQDGSSVSGGQAQFIAFLRAILTQRDIIILD 509
Cdd:TIGR01271 1300 KVFIFSGTFRKN-LDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLD 1378
|
170 180 190
....*....|....*....|....*....|....*...
gi 1267372771 510 EAASNLHIDTRNLMYEIL-QNYNLCNIlIMISHQQDGL 546
Cdd:TIGR01271 1379 EPSAHLDPVTLQIIRKTLkQSFSNCTV-ILSEHRVEAL 1415
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
354-530 |
1.80e-14 |
|
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: 72.79 E-value: 1.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 354 FKYNENSDLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDynlIHKE--SIRARIGIVSQNI 431
Cdd:cd03266 11 FRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFD---VVKEpaEARRRLGFVSDST 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 432 FLFKG-TILDNI-----LYG-QTNKTKEDVVKLIKRYHLTSHLNRfengldtiivqDGSSVSGGQAQFIAFLRAILTQRD 504
Cdd:cd03266 88 GLYDRlTARENLeyfagLYGlKGDELTARLEELADRLGMEELLDR-----------RVGGFSTGMRQKVAIARALVHDPP 156
|
170 180
....*....|....*....|....*.
gi 1267372771 505 IIILDEAASNLHIDTRNLMYEILQNY 530
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALREFIRQL 182
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
347-544 |
2.14e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 73.59 E-value: 2.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVCFKYNENSDL-IFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKESIRARIG 425
Cdd:PRK13642 5 LEVENLVFKYEKESDVnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 426 IVSQNI--FLFKGTILDNILYGQTNK--TKEDVVKLIKRYHLTSHLNRFEngldtiiVQDGSSVSGGQAQFIAFLRAILT 501
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMENQgiPREEMIKRVDEALLAVNMLDFK-------TREPARLSGGQKQRVAVAGIIAL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1267372771 502 QRDIIILDEAASNLHIDTRN----LMYEILQNYNLcnILIMISHQQD 544
Cdd:PRK13642 158 RPEIIILDESTSMLDPTGRQeimrVIHEIKEKYQL--TVLSITHDLD 202
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
347-544 |
2.55e-14 |
|
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: 72.60 E-value: 2.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVcFKYNENSDLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYN-LIHKE--SIRAR 423
Cdd:cd03256 1 IEVENL-SKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINkLKGKAlrQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 424 IGIVSQNIFLFKG-TILDNILYG---QTNK--------TKEDVVKLIkryhltSHLNRFenGLDTIIVQDGSSVSGGQAQ 491
Cdd:cd03256 80 IGMIFQQFNLIERlSVLENVLSGrlgRRSTwrslfglfPKEEKQRAL------AALERV--GLLDKAYQRADQLSGGQQQ 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1267372771 492 FIAFLRAILTQRDIIILDEAASNLH-IDTRNLMYEILQNYNLCNILIMIS-HQQD 544
Cdd:cd03256 152 RVAIARALMQQPKLILADEPVASLDpASSRQVMDLLKRINREEGITVIVSlHQVD 206
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
86-309 |
2.88e-14 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 73.29 E-value: 2.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 86 LISIGYEYLFTRVQQNVVNEIRLSMISNIIDAPLSYINQKEKGYILSRIaeSGNVSAL---FSPNLLRVFSGIFDFFFAL 162
Cdd:cd18576 51 VFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRL--SNDVTQIqdtLTTTLAEFLRQILTLIGGV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 163 FIMFNLSVKLTGIIVIIIPIYFVISKYSSEMISKSTTNVYESSAVLNAEMYETLNGIEDIKLLNGKNIQTNKIKAKLNDV 242
Cdd:cd18576 129 VLLFFISWKLTLLMLATVPVVVLVAVLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERV 208
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1267372771 243 IKSALKQSLH---FIFFMQNLIvtnnFVTVIVLL-VSGILILQNQLTIGVYTSFSIYMAKLlatTQALGSL 309
Cdd:cd18576 209 VKLALKRARIralFSSFIIFLL----FGAIVAVLwYGGRLVLAGELTAGDLVAFLLYTLFI---AGSIGSL 272
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
365-510 |
2.90e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 75.45 E-value: 2.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 365 DHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNlIH--KESIRARIGIVSQNIFLFKG-TILDN 441
Cdd:COG3845 22 DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVR-IRspRDAIALGIGMVHQHFMLVPNlTVAEN 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1267372771 442 ILYGQ---------TNKTKEDVVKLIKRYHLtsHLNrfengLDTIIvqdgSSVSGGQAQFIAFLRAILTQRDIIILDE 510
Cdd:COG3845 101 IVLGLeptkggrldRKAARARIRELSERYGL--DVD-----PDAKV----EDLSVGEQQRVEILKALYRGARILILDE 167
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
347-528 |
3.17e-14 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 72.43 E-value: 3.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVCFKYNENSdlIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYN--LIHKESIRARI 424
Cdd:PRK09493 2 IEFKNVSKHFGPTQ--VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 425 GIVSQNIFLF-KGTILDNILYGQTN---KTKEDVVK----LIKRYHLTSHLNRFEngldtiivqdgSSVSGGQAQFIAFL 496
Cdd:PRK09493 80 GMVFQQFYLFpHLTALENVMFGPLRvrgASKEEAEKqareLLAKVGLAERAHHYP-----------SELSGGQQQRVAIA 148
|
170 180 190
....*....|....*....|....*....|..
gi 1267372771 497 RAILTQRDIIILDEAASNLHIDTRnlmYEILQ 528
Cdd:PRK09493 149 RALAVKPKLMLFDEPTSALDPELR---HEVLK 177
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
104-323 |
4.50e-14 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 72.98 E-value: 4.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 104 NEIRLSMISNIID----APLSYINQKEKGYILSRIAESGNVSALFSPNLLRVFSGIFDFFFALFIMFNLSVKLTGIIVII 179
Cdd:cd18568 71 NRIDLSLLSDFYKhllsLPLSFFASRKVGDIITRFQENQKIRRFLTRSALTTILDLLMVFIYLGLMFYYNLQLTLIVLAF 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 180 IPIYFVISKYSSEMISKSTTNVYESSAVLNAEMYETLNGIEDIKLLNGKNIQTNKIKAKLNDVIKSALK-QSLHFIF-FM 257
Cdd:cd18568 151 IPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERPIRWRWENKFAKALNTRFRgQKLSIVLqLI 230
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1267372771 258 QNLIvtNNFVTVIVLLVSGILILQNQLTIGVYTSFSIYMAKLLATTQALGSLDITLKPVCISIKRI 323
Cdd:cd18568 231 SSLI--NHLGTIAVLWYGAYLVISGQLTIGQLVAFNMLFGSVINPLLALVGLWDELQETRISVERL 294
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
347-544 |
6.47e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 72.36 E-value: 6.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVCFKYNENSDL----IFDhFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINN--IDYNLIHKE-- 418
Cdd:PRK13634 3 ITFQKVEHRYQYKTPFerraLYD-VNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGErvITAGKKNKKlk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 419 SIRARIGIVSQniF----LFKGTILDNILYGQTN------KTKEDVVKLIKRYHLT-SHLNR--FEngldtiivqdgssV 485
Cdd:PRK13634 82 PLRKKVGIVFQ--FpehqLFEETVEKDICFGPMNfgvseeDAKQKAREMIELVGLPeELLARspFE-------------L 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1267372771 486 SGGQAQFIAFLRAILTQRDIIILDEAASNLHIDTRNLM----YEILQNYNLCNILimISHQQD 544
Cdd:PRK13634 147 SGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMmemfYKLHKEKGLTTVL--VTHSME 207
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
347-558 |
9.64e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 71.56 E-value: 9.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVCFKYNENSDLIfDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHK-ESIRARIG 425
Cdd:PRK13644 2 IRLENVSYSYPDGTPAL-ENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 426 IVSQNI-FLFKG-TILDNILYGQTNKT--KEDVVKLIKRyhltshlNRFENGLDTIIVQDGSSVSGGQAQFIAFLRAILT 501
Cdd:PRK13644 81 IVFQNPeTQFVGrTVEEDLAFGPENLClpPIEIRKRVDR-------ALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTM 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1267372771 502 QRDIIILDEAASNLHIDT-RNLMYEILQNYNLCNILIMISHQQDGLYFLNKTLELTHG 558
Cdd:PRK13644 154 EPECLIFDEVTSMLDPDSgIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRG 211
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
347-540 |
1.08e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 71.65 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVCFKYNENSDLIfDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILI--NNIDYNLIHKESIRARI 424
Cdd:PRK13639 2 LETRDLKYSYPDGTEAL-KGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIkgEPIKYDKKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 425 GIVSQNI--FLFKGTILDNILYGQTNK--TKEDVVKLIKRYHLTSHLNRFENgldtiivQDGSSVSGGQAQFIAFLRAIL 500
Cdd:PRK13639 81 GIVFQNPddQLFAPTVEEDVAFGPLNLglSKEEVEKRVKEALKAVGMEGFEN-------KPPHHLSGGQKKRVAIAGILA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1267372771 501 TQRDIIILDEAASNLHIDTRNLMYEILQNYNLCNILIMIS 540
Cdd:PRK13639 154 MKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIIS 193
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
83-296 |
1.19e-13 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 71.70 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 83 INYLISIGYEYLFTRVQQNVVNEIRLSMISNIIDAPLSYINQKEKGYILSRI-AESGNVSALFSPNLLRVFSGIFDFFFA 161
Cdd:cd18551 48 LQAVLSALSSYLLGRTGERVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVtNDTTLLRELITSGLPQLVTGVLTVVGA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 162 LFIMFNLSVKLTGIIVIIIPIYFVISKYSSEMISKSTTNVYESSAVLNAEMYETLNGIEDIKLLNGKNIQTNKIKAKLND 241
Cdd:cd18551 128 VVLMFLLDWVLTLVTLAVVPLAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAER 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1267372771 242 VIKSALKQSLHFIFFM--QNLIVTnnFVTVIVLLVSGILILQNQLTIGVYTSFSIYM 296
Cdd:cd18551 208 LYRAGLKAAKIEALIGplMGLAVQ--LALLVVLGVGGARVASGALTVGTLVAFLLYL 262
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
346-510 |
1.38e-13 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 70.43 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 346 SIEFKDVCFKYNENSDLiFDhFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKES------ 419
Cdd:PRK11124 2 SIQLNGINCFYGAHQAL-FD-ITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTPSdkaire 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 420 IRARIGIVSQNIFLFKG-TILDN-------ILYGQTNKTKEDVVKLIKRYHLTSHLNRFENGLdtiivqdgssvSGGQAQ 491
Cdd:PRK11124 80 LRRNVGMVFQQYNLWPHlTVQQNlieapcrVLGLSKDQALARAEKLLERLRLKPYADRFPLHL-----------SGGQQQ 148
|
170
....*....|....*....
gi 1267372771 492 FIAFLRAILTQRDIIILDE 510
Cdd:PRK11124 149 RVAIARALMMEPQVLLFDE 167
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
346-515 |
1.94e-13 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 71.64 E-value: 1.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 346 SIEFKDVCFKYNEnsDLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNlihKESIRAR-I 424
Cdd:COG3839 3 SLELENVSKSYGG--VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVT---DLPPKDRnI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 425 GIVSQNIFLFKG-TILDNILYG--QTNKTKEDVVKLIKR----YHLTSHLNRFENGLdtiivqdgssvSGGQAQFIAFLR 497
Cdd:COG3839 78 AMVFQSYALYPHmTVYENIAFPlkLRKVPKAEIDRRVREaaelLGLEDLLDRKPKQL-----------SGGQRQRVALGR 146
|
170
....*....|....*...
gi 1267372771 498 AILTQRDIIILDEAASNL 515
Cdd:COG3839 147 ALVREPKVFLLDEPLSNL 164
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
346-544 |
2.18e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 70.96 E-value: 2.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 346 SIEFKDVCFKYNENSDLIF---DHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIdyNLIHK----- 417
Cdd:PRK13646 2 TIRFDNVSYTYQKGTPYEHqaiHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDI--TITHKtkdky 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 418 -ESIRARIGIVSQ--NIFLFKGTILDNILYGQTN-KTKEDVVKlIKRYHLTSHLNRFENgldtIIVQDGSSVSGGQAQFI 493
Cdd:PRK13646 80 iRPVRKRIGMVFQfpESQLFEDTVEREIIFGPKNfKMNLDEVK-NYAHRLLMDLGFSRD----VMSQSPFQMSGGQMRKI 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1267372771 494 AFLRAILTQRDIIILDEAASNLHIDTRNLMYEILQNYNL--CNILIMISHQQD 544
Cdd:PRK13646 155 AIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTdeNKTIILVSHDMN 207
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
345-544 |
2.51e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 70.53 E-value: 2.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 345 NSIEFKDVCFKYNENSDLIfDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKESIRARI 424
Cdd:PRK13647 3 NIIEVEDLHFRYKDGTKAL-KGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 425 GIVSQNI--FLFKGTILDNILYGQTNK--TKEDVvklikryhltshLNRFENGLDTIIVQDGSS-----VSGGQAQFIAF 495
Cdd:PRK13647 82 GLVFQDPddQVFSSTVWDDVAFGPVNMglDKDEV------------ERRVEEALKAVRMWDFRDkppyhLSYGQKKRVAI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1267372771 496 LRAILTQRDIIILDEAASNLHIDTRNLMYEILQNYNLCNILIMIS-HQQD 544
Cdd:PRK13647 150 AGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVD 199
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
346-515 |
2.69e-13 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 71.28 E-value: 2.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 346 SIEFKDVCFKYNENsdLIFDHFNVQIEKGD--KLLidGINGSGKSTFIKLLTGLYQPKSGKILINNIDynlIHKESIRAR 423
Cdd:COG3842 5 ALELENVSKRYGDV--TALDDVSLSIEPGEfvALL--GPSGCGKTTLLRMIAGFETPDSGRILLDGRD---VTGLPPEKR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 424 -IGIVSQNIFLFk-gTILDNILYG--QTNKTKED----VVKLIKRYHLTSHLNRFENGLdtiivqdgssvSGGQAQFIAF 495
Cdd:COG3842 78 nVGMVFQDYALFphlTVAENVAFGlrMRGVPKAEirarVAELLELVGLEGLADRYPHQL-----------SGGQQQRVAL 146
|
170 180
....*....|....*....|
gi 1267372771 496 LRAILTQRDIIILDEAASNL 515
Cdd:COG3842 147 ARALAPEPRVLLLDEPLSAL 166
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
347-528 |
3.23e-13 |
|
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: 68.94 E-value: 3.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVCFKYNENSDLifDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDynlIHKES--IRARI 424
Cdd:cd03265 1 IEVENLVKKYGDFEAV--RGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHD---VVREPreVRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 425 GIVSQNIflfkgtILDNILYGQTN-------------KTKEDVVKLIKRYHLTSHLNRfengldtiIVqdgSSVSGGQAQ 491
Cdd:cd03265 76 GIVFQDL------SVDDELTGWENlyiharlygvpgaERRERIDELLDFVGLLEAADR--------LV---KTYSGGMRR 138
|
170 180 190
....*....|....*....|....*....|....*..
gi 1267372771 492 FIAFLRAILTQRDIIILDEAASNLHIDTRNLMYEILQ 528
Cdd:cd03265 139 RLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIE 175
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
347-544 |
3.86e-13 |
|
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: 68.46 E-value: 3.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVCFKYNENSDLifDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNidynliHKESI--RARI 424
Cdd:cd03269 1 LEVENVTKRFGRVTAL--DDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG------KPLDIaaRNRI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 425 GIVSQNIFLF-KGTILDNILY-----GQTNK-TKEDVVKLIKRYHLTSHLNRfenGLDTIivqdgssvSGGQAQFIAFLR 497
Cdd:cd03269 73 GYLPEERGLYpKMKVIDQLVYlaqlkGLKKEeARRRIDEWLERLELSEYANK---RVEEL--------SKGNQQKVQFIA 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1267372771 498 AILTQRDIIILDEAASNLH-IDTRNLMYEILQNYNLCNILIMISHQQD 544
Cdd:cd03269 142 AVIHDPELLILDEPFSGLDpVNVELLKDVIRELARAGKTVILSTHQME 189
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
368-541 |
5.27e-13 |
|
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: 67.07 E-value: 5.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 368 NVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIH-KESIRARIGIVSQniflfkgtildnilygq 446
Cdd:cd03216 20 SLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASpRDARRAGIAMVYQ----------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 447 tnktkedvvklikryhltshlnrfengldtiivqdgssVSGGQAQFIAFLRAILTQRDIIILDEAASNLHIDTRNLMYEI 526
Cdd:cd03216 83 --------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKV 124
|
170
....*....|....*...
gi 1267372771 527 LQnyNLCN---ILIMISH 541
Cdd:cd03216 125 IR--RLRAqgvAVIFISH 140
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
357-525 |
5.65e-13 |
|
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: 69.50 E-value: 5.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 357 NENSDLIFDHF-----------NVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKIlinnidynlihKESirARIG 425
Cdd:cd03291 35 SDDNNLFFSNLclvgapvlkniNLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI-----------KHS--GRIS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 426 IVSQNIFLFKGTILDNILYGQTNKtKEDVVKLIKRYHLTSHLNRFENGLDTIIVQDGSSVSGGQAQFIAFLRAILTQRDI 505
Cdd:cd03291 102 FSSQFSWIMPGTIKENIIFGVSYD-EYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADL 180
|
170 180
....*....|....*....|
gi 1267372771 506 IILDEAASNLHIDTRNLMYE 525
Cdd:cd03291 181 YLLDSPFGYLDVFTEKEIFE 200
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
347-529 |
7.53e-13 |
|
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: 67.60 E-value: 7.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVCFKYNenSDLIFDHFNVQIEKGDKLLIdGINGSGKSTFIKLLTGLYQPKSGKILINNIDyNLIHKESIRARIGI 426
Cdd:cd03264 1 LQLENLTKRYG--KKRALDGVSLTLGPGMYGLL-GPNGAGKTTLMRILATLTPPSSGTIRIDGQD-VLKQPQKLRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 427 VSQNIFLFKG-TILD-----NILYGQTNKT-KEDVVKLIKRYHLTSHLNRFENGLdtiivqdgssvSGGQAQFIAFLRAI 499
Cdd:cd03264 77 LPQEFGVYPNfTVREfldyiAWLKGIPSKEvKARVDEVLELVNLGDRAKKKIGSL-----------SGGMRRRVGIAQAL 145
|
170 180 190
....*....|....*....|....*....|....
gi 1267372771 500 LTQRDIIILDEAASNL----HIDTRNLMYEILQN 529
Cdd:cd03264 146 VGDPSILIVDEPTAGLdpeeRIRFRNLLSELGED 179
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
212-515 |
8.09e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 71.55 E-value: 8.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 212 MYETLNGIEDIKLLNGKNIQTNKIKAKLNDVIKSALKQSLHFIFfmqNLIVTNNFVTVIVLLVSGILIL-QNQLTIG-VY 289
Cdd:PLN03232 482 INEILASMDTVKCYAWEKSFESRIQGIRNEELSWFRKAQLLSAF---NSFILNSIPVVVTLVSFGVFVLlGGDLTPArAF 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 290 TSFSIYmAKLLATTQALGSLDITLKPVCISIKRIKEFFnLDVENTLGTNIIKEP-INSIEFKDVCFKYN-ENSDLIFDHF 367
Cdd:PLN03232 559 TSLSLF-AVLRSPLNMLPNLLSQVVNANVSLQRIEELL-LSEERILAQNPPLQPgAPAISIKNGYFSWDsKTSKPTLSDI 636
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 368 NVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILInnidynlihkesIRARIGIVSQNIFLFKGTILDNILYGqT 447
Cdd:PLN03232 637 NLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV------------IRGSVAYVPQVSWIFNATVRENILFG-S 703
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1267372771 448 NKTKEDVVKLIKRYHLTSHLNRFENGLDTIIVQDGSSVSGGQAQFIAFLRAILTQRDIIILDEAASNL 515
Cdd:PLN03232 704 DFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSAL 771
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
86-300 |
1.20e-12 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 68.61 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 86 LISIGYEYLFTRVQQNVVNEIRLSMISNIIDAPLSYINQKEKGYILSRIaeSGNVSAL---FSPNLLRVFSGIFDFFFAL 162
Cdd:cd18542 54 VFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSFSFHDKARTGDLMSRC--TSDVDTIrrfLAFGLVELVRAVLLFIGAL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 163 FIMFNLSVKLTGIIVIIIPIYFVISKYSSEMISKSTTNVYESSAVLNAEMYETLNGIEDIKLLNGKNIQTNKIKAKLNDV 242
Cdd:cd18542 132 IIMFSINWKLTLISLAIIPFIALFSYVFFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEY 211
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1267372771 243 IKSALKQSLHFIFFMQNLIVTNNFVTVIVLLVSGILILQNQLTIGVYTSFSIYMAKLL 300
Cdd:cd18542 212 RDLNIKLAKLLAKYWPLMDFLSGLQIVLVLWVGGYLVINGEITLGELVAFISYLWMLI 269
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
363-558 |
1.66e-12 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 70.71 E-value: 1.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 363 IFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKIlinnidynlihKESirARIGIVSQNIFLFKGTILDNI 442
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI-----------KHS--GRISFSPQTSWIMPGTIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 443 LYGQTNKTKEdVVKLIKRYHLTSHLNRFENGLDTIIVQDGSSVSGGQAQFIAFLRAILTQRDIIILDEAASNLHIDTRNL 522
Cdd:TIGR01271 508 IFGLSYDEYR-YTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKE 586
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1267372771 523 MYEILqnynLCNIL-----IMISHQQDGLYFLNKTLELTHG 558
Cdd:TIGR01271 587 IFESC----LCKLMsnktrILVTSKLEHLKKADKILLLHEG 623
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
347-544 |
2.38e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 67.84 E-value: 2.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVCFKYNENSDL----IFDhFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKES--- 419
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFasraLFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeik 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 420 -IRARIGIVSQ--NIFLFKGTILDNILYGQTN--KTKEDVVKL-IKRYHLTSHLNRFENgldtiivQDGSSVSGGQAQFI 493
Cdd:PRK13643 81 pVRKKVGVVFQfpESQLFEETVLKDVAFGPQNfgIPKEKAEKIaAEKLEMVGLADEFWE-------KSPFELSGGQMRRV 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1267372771 494 AFLRAILTQRDIIILDEAASNLHIDTRNLMYEILQN-YNLCNILIMISHQQD 544
Cdd:PRK13643 154 AIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESiHQSGQTVVLVTHLMD 205
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
83-299 |
2.47e-12 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 67.80 E-value: 2.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 83 INYLISIGYEYLFTRVQQNVVNEIRLSMISNIIDAPLSYINQKEKGYILSRIA---EsgNVSALFSPNLLRVFSGIFDFF 159
Cdd:cd18544 53 LSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTndtE--ALNELFTSGLVTLIGDLLLLI 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 160 FALFIMFNLSVKLTGIIVIIIPIYFVISKYSSEMISKSTTNVYESSAVLNAEMYETLNGIEDIKLLNGKNIQTNKIKAKL 239
Cdd:cd18544 131 GILIAMFLLNWRLALISLLVLPLLLLATYLFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEIN 210
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 240 NDVIKSALKQSLHFIFFMQNLIVTNNFVTVIVLLVSGILILQNQLTIGVYTSFSIYMAKL 299
Cdd:cd18544 211 QEYRKANLKSIKLFALFRPLVELLSSLALALVLWYGGGQVLSGAVTLGVLYAFIQYIQRF 270
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
90-300 |
3.17e-12 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 67.45 E-value: 3.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 90 GYEYLFTRVQQNVVNEIRLSMISNIIDAPLSYINQKEKGYILSRI-AESGNVSALFSPNLLRVFSGIFDFFFALFIMFNL 168
Cdd:cd18552 58 LQTYLMAYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRItNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 169 SVKLTGIIVIIIPIYFVISKYSSEMISKSTTNVYESSAVLNAEMYETLNGIEDIKLLNGKNIQTNKIKAKLNDVIKSALK 248
Cdd:cd18552 138 DWKLTLIALVVLPLAALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMK 217
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1267372771 249 qslhfIFFMQNLI-----VTNNFVTVIVLLVSGILILQNQLTIGVYTSFSIYMAKLL 300
Cdd:cd18552 218 -----IARARALSsplmeLLGAIAIALVLWYGGYQVISGELTPGEFISFITALLLLY 269
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
368-544 |
7.06e-12 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 67.37 E-value: 7.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 368 NVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIH----KESIRARIGIVSQNIFLFKG-TILDNI 442
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdaelREVRRKKIAMVFQSFALMPHmTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 443 LYGQ------TNKTKEDVVKLIKRYHLTSHLNRFENGLdtiivqdgssvSGGQAQFIAFLRAILTQRDIIILDEAASNLH 516
Cdd:PRK10070 128 AFGMelaginAEERREKALDALRQVGLENYAHSYPDEL-----------SGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190
....*....|....*....|....*....|
gi 1267372771 517 IDTRNLMYEILQNYNLCN--ILIMISHQQD 544
Cdd:PRK10070 197 PLIRTEMQDELVKLQAKHqrTIVFISHDLD 226
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
344-515 |
1.22e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 65.16 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 344 INSIEFKDVCFKYNENSdlIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYN---------- 413
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQT--VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDtarslsqqkg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 414 LIHKesIRARIGIVSQNIFLF-KGTILDNILYGQT---NKTKEDVV----KLIKRYHLTSHLNRFENGLdtiivqdgssv 485
Cdd:PRK11264 79 LIRQ--LRQHVGFVFQNFNLFpHRTVLENIIEGPVivkGEPKEEATararELLAKVGLAGKETSYPRRL----------- 145
|
170 180 190
....*....|....*....|....*....|
gi 1267372771 486 SGGQAQFIAFLRAILTQRDIIILDEAASNL 515
Cdd:PRK11264 146 SGGQQQRVAIARALAMRPEVILFDEPTSAL 175
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
379-515 |
1.29e-11 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 66.05 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 379 IDGINGSGKSTFIKLLTGLYQPKSGKILINniDYNLIHKES-I-----RARIGIVSQNIFLF-----KGtildNILYGQT 447
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLN--GRVLFDAEKgIclppeKRRIGYVFQDARLFphykvRG----NLRYGMA 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1267372771 448 NKTKE---DVVKLIKRYHLtshLNRFEngldtiivqdgSSVSGGQAQFIAFLRAILTQRDIIILDEAASNL 515
Cdd:PRK11144 103 KSMVAqfdKIVALLGIEPL---LDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASL 159
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
359-541 |
1.40e-11 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 64.04 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 359 NSDLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPK---SGKILINNIDYNLIHKEsiRARIGIVSQNIFLFK 435
Cdd:COG4136 12 GGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAE--QRRIGILFQDDLLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 436 G-TILDNILYGQTNKTKedvvKLIKRYHLTSHLNrfENGLDTIIVQDGSSVSGGQAQFIAFLRAILTQRDIIILDEAAS- 513
Cdd:COG4136 90 HlSVGENLAFALPPTIG----RAQRRARVEQALE--EAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSk 163
|
170 180 190
....*....|....*....|....*....|.
gi 1267372771 514 ---NLHIDTRNLMYEILQNYNLcnILIMISH 541
Cdd:COG4136 164 ldaALRAQFREFVFEQIRQRGI--PALLVTH 192
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
363-510 |
1.52e-11 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 65.88 E-value: 1.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 363 IFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKESirARIGIVSQNIFLFKG-TILDN 441
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGFVFQHYALFRHmTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 442 ILYGQT----------NKTKEDVVKLIKRYHLtSHL-NRFEngldtiivqdgSSVSGGQAQFIAFLRAILTQRDIIILDE 510
Cdd:PRK10851 95 IAFGLTvlprrerpnaAAIKAKVTQLLEMVQL-AHLaDRYP-----------AQLSGGQKQRVALARALAVEPQILLLDE 162
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
359-542 |
1.79e-11 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 66.70 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 359 NSDLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNidynlihkesiRARIGIVSQNIFLFKGTI 438
Cdd:TIGR00954 463 NGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPA-----------KGKLFYVPQRPYMTLGTL 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 439 LDNILYGQTNK-------TKEDVVKLIKRYHLTSHLNRfENGLDtiIVQDGSSV-SGGQAQFIAFLRAILTQRDIIILDE 510
Cdd:TIGR00954 532 RDQIIYPDSSEdmkrrglSDKDLEQILDNVQLTHILER-EGGWS--AVQDWMDVlSGGEKQRIAMARLFYHKPQFAILDE 608
|
170 180 190
....*....|....*....|....*....|..
gi 1267372771 511 AASNLHIDTRNLMYEILQNYNLCniLIMISHQ 542
Cdd:TIGR00954 609 CTSAVSVDVEGYMYRLCREFGIT--LFSVSHR 638
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
343-515 |
1.94e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 64.87 E-value: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 343 PINSIEFKDVCFKYNENSDLIFDhFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINN--IDYNLIHKESI 420
Cdd:PRK13636 2 EDYILKVEELNYNYSDGTHALKG-ININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 421 RARIGIVSQNI--FLFKGTILDNILYGQTN-KTKEDVVKLIKRYHLTshlnrfENGLDTIIVQDGSSVSGGQAQFIAFLR 497
Cdd:PRK13636 81 RESVGMVFQDPdnQLFSASVYQDVSFGAVNlKLPEDEVRKRVDNALK------RTGIEHLKDKPTHCLSFGQKKRVAIAG 154
|
170
....*....|....*...
gi 1267372771 498 AILTQRDIIILDEAASNL 515
Cdd:PRK13636 155 VLVMEPKVLVLDEPTAGL 172
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
81-323 |
2.37e-11 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 64.84 E-value: 2.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 81 YCINYLISIGYEYLFTRVQQNVVNEIRLSMISNIIDAPLSYINQKEKGYILSRIA-ESGNVSALFSPNLLRVFSGIFDFF 159
Cdd:cd18563 53 YVLSALLGILRGRLLARLGERITADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTsDTDRLQDFLSDGLPDFLTNILMII 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 160 FALFIMFNLSVKLTGIIVIIIPIYFVISKYSSEMISKSTTNVYESSAVLNAEMYETLNGIEDIKLLNGKNIQTNKIKAKL 239
Cdd:cd18563 133 GIGVVLFSLNWKLALLVLIPVPLVVWGSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEAN 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 240 NDVIKSALK--QSLHFIFFMQNLIVTnnFVTVIVLLVSGILILQNQLTIGVYTSFSIYMAKLLATTQALGSLDITLKPVC 317
Cdd:cd18563 213 QELLDANIRaeKLWATFFPLLTFLTS--LGTLIVWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRAL 290
|
....*.
gi 1267372771 318 ISIKRI 323
Cdd:cd18563 291 TSAERI 296
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
346-544 |
4.10e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 64.00 E-value: 4.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 346 SIEFKDVCFKYNENSDL----IFDhFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHK---- 417
Cdd:PRK13649 2 GINLQNVSYTYQAGTPFegraLFD-VNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnkdi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 418 ESIRARIGIVSQniF----LFKGTILDNILYGQTN--KTKEDVVKLIK-RYHLTshlnrfenGLD-TIIVQDGSSVSGGQ 489
Cdd:PRK13649 81 KQIRKKVGLVFQ--FpesqLFEETVLKDVAFGPQNfgVSQEEAEALAReKLALV--------GISeSLFEKNPFELSGGQ 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1267372771 490 AQFIAFLRAILTQRDIIILDEAASNLHIDTRNLMYEILQNYNLCNILI-MISHQQD 544
Cdd:PRK13649 151 MRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIvLVTHLMD 206
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
365-515 |
4.79e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 65.19 E-value: 4.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 365 DHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYN-LIHKESIRARIGIVSQNIFLFKG-TILDNI 442
Cdd:PRK09700 22 KSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNkLDHKLAAQLGIGIIYQELSVIDElTVLENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 443 LYGQT-------------NKTKEDVVKLIKRYHLTSHLNRFENGLdtiivqdgsSVSggQAQFIAFLRAILTQRDIIILD 509
Cdd:PRK09700 102 YIGRHltkkvcgvniidwREMRVRAAMMLLRVGLKVDLDEKVANL---------SIS--HKQMLEIAKTLMLDAKVIIMD 170
|
....*.
gi 1267372771 510 EAASNL 515
Cdd:PRK09700 171 EPTSSL 176
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
341-523 |
5.41e-11 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 64.58 E-value: 5.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 341 KEPInsIEFKDVCFKYNENSdlIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKEsi 420
Cdd:PRK09452 11 LSPL--VELRGISKSFDGKE--VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 421 RARIGIVSQNIFLFKG-TILDNILYG-QTNKT-----KEDVVKLIKRYHLTSHLNRFENGLdtiivqdgssvSGGQAQFI 493
Cdd:PRK09452 85 NRHVNTVFQSYALFPHmTVFENVAFGlRMQKTpaaeiTPRVMEALRMVQLEEFAQRKPHQL-----------SGGQQQRV 153
|
170 180 190
....*....|....*....|....*....|
gi 1267372771 494 AFLRAILTQRDIIILDEAASNLHIDTRNLM 523
Cdd:PRK09452 154 AIARAVVNKPKVLLLDESLSALDYKLRKQM 183
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
365-542 |
9.65e-11 |
|
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: 61.46 E-value: 9.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 365 DHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNliHKESIRARIgivsqniflfkGTILDN-IL 443
Cdd:cd03268 17 DDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ--KNIEALRRI-----------GALIEApGF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 444 YGqtNKTKEDVVKLIKRYHLTSHlNRFENGLDTIIVQDG-----SSVSGGQAQFIAFLRAILTQRDIIILDEAASNLHID 518
Cdd:cd03268 84 YP--NLTARENLRLLARLLGIRK-KRIDEVLDVVGLKDSakkkvKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPD 160
|
170 180
....*....|....*....|....*
gi 1267372771 519 TRNLMYEILQNYNLCNILIMI-SHQ 542
Cdd:cd03268 161 GIKELRELILSLRDQGITVLIsSHL 185
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
337-543 |
1.22e-10 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 61.98 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 337 TNIIKEPINSIEFKDVCFKYNENsdLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLY--QPK---SGKILIN--N 409
Cdd:COG1117 2 TAPASTLEPKIEVRNLNVYYGDK--QALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNdlIPGarvEGEILLDgeD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 410 I---DYNLIHkesIRARIGIVSQNIFLFKGTILDNILYG---QTNKTKED----VVKLIKRYHLTSHL-NRfengLDtii 478
Cdd:COG1117 80 IydpDVDVVE---LRRRVGMVFQKPNPFPKSIYDNVAYGlrlHGIKSKSEldeiVEESLRKAALWDEVkDR----LK--- 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1267372771 479 vQDGSSVSGGQAQ--FIAflRAILTQRDIIILDEAASNL-HIDTR---NLMYEILQNYNlcniLIMISH--QQ 543
Cdd:COG1117 150 -KSALGLSGGQQQrlCIA--RALAVEPEVLLMDEPTSALdPISTAkieELILELKKDYT----IVIVTHnmQQ 215
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
371-544 |
1.64e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 61.73 E-value: 1.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 371 IEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINN--IDYNLIHKESIRARI----GIVSQNIFLFKGTILDNILY 444
Cdd:PRK15112 36 LREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhpLHFGDYSYRSQRIRMifqdPSTSLNPRQRISQILDFPLR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 445 GQTNKTKEDVVKLIKRY-----HLTSHLNRFENGLdtiivqdgssvSGGQAQFIAFLRAILTQRDIIILDEAASNLHIDT 519
Cdd:PRK15112 116 LNTDLEPEQREKQIIETlrqvgLLPDHASYYPHML-----------APGQKQRLGLARALILRPKVIIADEALASLDMSM 184
|
170 180 190
....*....|....*....|....*....|....
gi 1267372771 520 R----NLMYEILQNYNLCNILI-----MISHQQD 544
Cdd:PRK15112 185 RsqliNLMLELQEKQGISYIYVtqhlgMMKHISD 218
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
365-544 |
1.74e-10 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 64.26 E-value: 1.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 365 DHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILI--NNIDYNLihkESIRARIGIVSQ-NIFLFKGTILDN 441
Cdd:TIGR01257 947 DRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVggKDIETNL---DAVRQSLGMCPQhNILFHHLTVAEH 1023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 442 IL-YGQTNKTKEDVVKLIKRYHLTshlnrfENGLDTIIVQDGSSVSGGQAQFIAFLRAILTQRDIIILDEAASNLHIDTR 520
Cdd:TIGR01257 1024 ILfYAQLKGRSWEEAQLEMEAMLE------DTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSR 1097
|
170 180
....*....|....*....|....
gi 1267372771 521 NLMYEILQNYNLCNILIMISHQQD 544
Cdd:TIGR01257 1098 RSIWDLLLKYRSGRTIIMSTHHMD 1121
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
368-525 |
2.72e-10 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 60.42 E-value: 2.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 368 NVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKESIRAR----IGIVSQNIFLFKGTILDNIL 443
Cdd:cd03290 21 NIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLLNATVEENIT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 444 YGQT-NKTKEDVVklIKRYHLTSHLNRFENGLDTIIVQDGSSVSGGQAQFIAFLRAILTQRDIIILDEAASNLHID-TRN 521
Cdd:cd03290 101 FGSPfNKQRYKAV--TDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlSDH 178
|
....
gi 1267372771 522 LMYE 525
Cdd:cd03290 179 LMQE 182
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
348-541 |
2.99e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 63.05 E-value: 2.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 348 EFKDVCfkYNENSDLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILIN---NIDYNLIHKESIRAri 424
Cdd:PRK11147 321 EMENVN--YQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGtklEVAYFDQHRAELDP-- 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 425 givsqniflfKGTILDNILYGqtnktKEDV-VKLIKRyHLTSHLnrfengldtiivQDG-----------SSVSGGQAQF 492
Cdd:PRK11147 397 ----------EKTVMDNLAEG-----KQEVmVNGRPR-HVLGYL------------QDFlfhpkramtpvKALSGGERNR 448
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1267372771 493 IAFLRAILTQRDIIILDEAASNLHIDTRNLMYEILQNYNlcNILIMISH 541
Cdd:PRK11147 449 LLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQ--GTVLLVSH 495
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
365-541 |
3.19e-10 |
|
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: 61.61 E-value: 3.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 365 DHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPK---SGKILINNIDYNLIHKESIRA----RIGIVSQNIF----- 432
Cdd:COG0444 22 DGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSEKELRKirgrEIQMIFQDPMtslnp 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 433 LFK-GTILDNILYGQTNKTKED----VVKLIKRYHLT---SHLNRFENGLdtiivqdgssvSGGQAQFIAFLRAILTQRD 504
Cdd:COG0444 102 VMTvGDQIAEPLRIHGGLSKAEarerAIELLERVGLPdpeRRLDRYPHEL-----------SGGMRQRVMIARALALEPK 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1267372771 505 IIILDEAASNLHIDTR----NLMYEILQNYNLCniLIMISH 541
Cdd:COG0444 171 LLIADEPTTALDVTIQaqilNLLKDLQRELGLA--ILFITH 209
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
347-519 |
3.75e-10 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 61.63 E-value: 3.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVCFKYNENSDLI--FDHFNVQIEKGDkllIDGI---NGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKESIR 421
Cdd:COG1135 2 IELENLSKTFPTKGGPVtaLDDVSLTIEKGE---IFGIigySGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 422 A---RIGIVSQNIFLFKG-TILDNILY-----GQT-NKTKEDVVKLIKRYHLTSHLNRFENGLdtiivqdgssvSGGQAQ 491
Cdd:COG1135 79 AarrKIGMIFQHFNLLSSrTVAENVALpleiaGVPkAEIRKRVAELLELVGLSDKADAYPSQL-----------SGGQKQ 147
|
170 180
....*....|....*....|....*...
gi 1267372771 492 FIAFLRAILTQRDIIILDEAASNLHIDT 519
Cdd:COG1135 148 RVGIARALANNPKVLLCDEATSALDPET 175
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
93-295 |
4.44e-10 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 60.99 E-value: 4.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 93 YLFTRVQQNVVNEIRLSMISNIIDAPLSYINQKEKGYILSRI-AESGNVSALFSPNLLRVFSGIFDFFFALFIMFNLSVK 171
Cdd:cd18573 63 YLLRIAGERIVARLRKRLFKSILRQDAAFFDKNKTGELVSRLsSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPK 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 172 LTGIIVIIIPIYFVISKYSSEMISKSTTNVYESSAVLNAEMYETLNGIEDIKLLNGKNIQTNKIKAKLNDVIKSALKQSL 251
Cdd:cd18573 143 LTLVMLLVVPPIAVGAVFYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEAL 222
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1267372771 252 HFIFFMQNLIVTNNFVTVIVLLVSGILILQNQLTIGVYTSFSIY 295
Cdd:cd18573 223 ASGLFFGSTGFSGNLSLLSVLYYGGSLVASGELTVGDLTSFLMY 266
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
118-307 |
4.64e-10 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 60.89 E-value: 4.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 118 PLSYINQKEKGYILSRIAES-GNVSALFSPNLLRVFSGIFDFFFALFIMFNLSVKLTGIIVIIIPIYFVISKYSSEMISK 196
Cdd:cd18541 87 SPSFYQKNRTGDLMARATNDlNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRLGKKIHK 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 197 STTNVYESSAVLNAEMYETLNGIEDIKLLNGKNIQTNKIKAKLNDVIKSALKQSLHFIFFMQNLIVTNNFVTVIVLLVSG 276
Cdd:cd18541 167 RFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLIVLWYGG 246
|
170 180 190
....*....|....*....|....*....|.
gi 1267372771 277 ILILQNQLTIGVYTSFSIYMAKLLATTQALG 307
Cdd:cd18541 247 RLVIRGTITLGDLVAFNSYLGMLIWPMMALG 277
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
347-558 |
5.57e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 60.87 E-value: 5.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVCFKYNENSDLIF---DHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHK------ 417
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTELkalDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKtkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 418 ------------------ESIRARIGIVSQniF----LFKGTILDNILYGQTN--KTKEDVVKLIKRY-HLTshlnrfen 472
Cdd:PRK13651 83 vleklviqktrfkkikkiKEIRRRVGVVFQ--FaeyqLFEQTIEKDIIFGPVSmgVSKEEAKKRAAKYiELV-------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 473 GLDTIIVQDGS-SVSGGQAQFIAfLRAILT-QRDIIILDEAASNLHIDTRNLMYEILQNYNLCN-ILIMISHQQDG-LYF 548
Cdd:PRK13651 153 GLDESYLQRSPfELSGGQKRRVA-LAGILAmEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGkTIILVTHDLDNvLEW 231
|
250
....*....|
gi 1267372771 549 LNKTLELTHG 558
Cdd:PRK13651 232 TKRTIFFKDG 241
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
370-541 |
5.76e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 60.75 E-value: 5.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 370 QIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKESIRAR---IGIVSQNIF--LFK----GTILD 440
Cdd:PRK11308 37 TLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLrqkIQIVFQNPYgsLNPrkkvGQILE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 441 NILYGQTNKT----KEDVVKLIKRYHL-TSHLNRFENGLdtiivqdgssvSGGQAQFIAFLRAILTQRDIIILDEAASNL 515
Cdd:PRK11308 117 EPLLINTSLSaaerREKALAMMAKVGLrPEHYDRYPHMF-----------SGGQRQRIAIARALMLDPDVVVADEPVSAL 185
|
170 180 190
....*....|....*....|....*....|
gi 1267372771 516 HIDTR----NLMYEILQNYNLCniLIMISH 541
Cdd:PRK11308 186 DVSVQaqvlNLMMDLQQELGLS--YVFISH 213
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
381-562 |
6.26e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 60.18 E-value: 6.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 381 GINGSGKSTFIK-------LLTGLYqpKSGKILINniDYNLIHKE----SIRARIGIVSQNIFLFKGTILDNILYG-QTN 448
Cdd:PRK14243 43 GPSGCGKSTILRcfnrlndLIPGFR--VEGKVTFH--GKNLYAPDvdpvEVRRRIGMVFQKPNPFPKSIYDNIAYGaRIN 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 449 KTKEDVVKLIKRYHLTSHL-NRFENGLDtiivQDGSSVSGGQAQFIAFLRAILTQRDIIILDEAASNLH-IDTR---NLM 523
Cdd:PRK14243 119 GYKGDMDELVERSLRQAALwDEVKDKLK----QSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDpISTLrieELM 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1267372771 524 YEILQNYNlcniLIMISH--QQ-----DGLYFLNktLELTHGNKRN 562
Cdd:PRK14243 195 HELKEQYT----IIIVTHnmQQaarvsDMTAFFN--VELTEGGGRY 234
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
363-510 |
7.56e-10 |
|
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: 59.48 E-value: 7.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 363 IFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNL--IHKesiRARIGI--VSQNIFLFKG-T 437
Cdd:cd03218 15 VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKlpMHK---RARLGIgyLPQEASIFRKlT 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1267372771 438 ILDNIL--YGQTNKTKEDVVKLIKryHLTSHLNrfengLDTIIVQDGSSVSGGQAQFIAFLRAILTQRDIIILDE 510
Cdd:cd03218 92 VEENILavLEIRGLSKKEREEKLE--ELLEEFH-----ITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDE 159
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
318-515 |
7.69e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 62.06 E-value: 7.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 318 ISIKRIKEFFnLDVENTLGTNIIKEP-INSIEFKDVCFKYNENSDL-IFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLT 395
Cdd:PLN03130 586 VSLKRLEELL-LAEERVLLPNPPLEPgLPAISIKNGYFSWDSKAERpTLSNINLDVPVGSLVAIVGSTGEGKTSLISAML 664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 396 GLYQPKSGKILInnidynlihkesIRARIGIVSQNIFLFKGTILDNILYGQTNKtKEDVVKLIKRYHLTSHLNRFENGLD 475
Cdd:PLN03130 665 GELPPRSDASVV------------IRGTVAYVPQVSWIFNATVRDNILFGSPFD-PERYERAIDVTALQHDLDLLPGGDL 731
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1267372771 476 TIIVQDGSSVSGGQAQFIAFLRAILTQRDIIILDEAASNL 515
Cdd:PLN03130 732 TEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSAL 771
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
93-294 |
7.75e-10 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 60.30 E-value: 7.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 93 YLFTRVQQNVVNEIRLSMISNIIDAPLSYINQKEKGYILSRIAESGNVSALFSPNLLRVFSGIFDFFFALFIMFNLSVKL 172
Cdd:cd18782 64 YLFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTRISELDTIRGFLTGTALTTLLDVLFSVIYIAVLFSYSPLL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 173 TGIIVIIIPIYFVISKYSSEMISKSTTNVYESSAVLNAEMYETLNGIEDIKLLNGKNIQTNKIKAKLNDVIKSALKQSLH 252
Cdd:cd18782 144 TLVVLATVPLQLLLTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELKARWRWQNRYARSLGEGFKLTVL 223
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1267372771 253 FIFFMQNLIVTNNFVTVIVLLVSGILILQNQLTIGVYTSFSI 294
Cdd:cd18782 224 GTTSGSLSQFLNKLSSLLVLWVGAYLVLRGELTLGQLIAFRI 265
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
346-544 |
9.99e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 60.25 E-value: 9.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 346 SIEFKDVCFKYNENSD---LIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNI------------ 410
Cdd:PRK13631 21 ILRVKNLYCVFDEKQEnelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIyigdkknnheli 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 411 DYNLIHK----ESIRARIGIVSQ--NIFLFKGTILDNILYGQTN--KTKEDVVKLIKRYhltshLNRFenGLD-TIIVQD 481
Cdd:PRK13631 101 TNPYSKKiknfKELRRRVSMVFQfpEYQLFKDTIEKDIMFGPVAlgVKKSEAKKLAKFY-----LNKM--GLDdSYLERS 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1267372771 482 GSSVSGGQAQFIAFLRAILTQRDIIILDEAASNLHIDTRNLMYEILQNYNLCN-ILIMISHQQD 544
Cdd:PRK13631 174 PFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNkTVFVITHTME 237
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
346-557 |
1.00e-09 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 60.43 E-value: 1.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 346 SIEFKDVCFKYNENsdLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIhkESIRARIG 425
Cdd:PRK11000 3 SVTLRNVTKAYGDV--VISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDV--PPAERGVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 426 IVSQNIFLFKG-TILDNILYG---------QTNKTKEDVVKLIKRYHLtshLNRFENGLdtiivqdgssvSGGQAQFIAF 495
Cdd:PRK11000 79 MVFQSYALYPHlSVAENMSFGlklagakkeEINQRVNQVAEVLQLAHL---LDRKPKAL-----------SGGQRQRVAI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 496 LRAILTQRDIIILDEAASNLHIDTRNLM-YEI--LQNyNLCNILIMISHQQ-------DGLYFLN--------KTLELTH 557
Cdd:PRK11000 145 GRTLVAEPSVFLLDEPLSNLDAALRVQMrIEIsrLHK-RLGRTMIYVTHDQveamtlaDKIVVLDagrvaqvgKPLELYH 223
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
383-510 |
1.32e-09 |
|
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: 58.84 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 383 NGSGKSTFIKLLTGLYQPKSGKILINNIDynlIHKESI--RARIGI--VSQNIFLFKG-TILDNILYG-QTNKTKEDVVK 456
Cdd:COG0410 38 NGAGKTTLLKAISGLLPPRSGSIRFDGED---ITGLPPhrIARLGIgyVPEGRRIFPSlTVEENLLLGaYARRDRAEVRA 114
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1267372771 457 LIKR-YHLTSHLNRFENgldtiivQDGSSVSGGQAQFIAFLRAILTQRDIIILDE 510
Cdd:COG0410 115 DLERvYELFPRLKERRR-------QRAGTLSGGEQQMLAIGRALMSRPKLLLLDE 162
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
368-542 |
1.68e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 60.95 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 368 NVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNidynlihkesiraRIGIVSQNIFLFKGTILDNILYGQT 447
Cdd:PTZ00243 680 SVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAER-------------SIAYVPQQAWIMNATVRGNILFFDE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 448 NKTkEDVVKLIKRYHLTSHLNRFENGLDTIIVQDGSSVSGGQAQFIAFLRAILTQRDIIILDEAASNL--HIDTRnLMYE 525
Cdd:PTZ00243 747 EDA-ARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALdaHVGER-VVEE 824
|
170
....*....|....*..
gi 1267372771 526 ILQNYNLCNILIMISHQ 542
Cdd:PTZ00243 825 CFLGALAGKTRVLATHQ 841
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
365-544 |
1.75e-09 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 59.85 E-value: 1.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 365 DHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDynLIHKESIRARIGIVSQNIFLFKG-TILDNIL 443
Cdd:PRK11607 36 DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVD--LSHVPPYQRPINMMFQSYALFPHmTVEQNIA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 444 YG--QTNKTKEDVVKLIKRYHLTSHLNRFENgldtiivQDGSSVSGGQAQFIAFLRAILTQRDIIILDEAASNLHIDTRN 521
Cdd:PRK11607 114 FGlkQDKLPKAEIASRVNEMLGLVHMQEFAK-------RKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRD 186
|
170 180
....*....|....*....|....*...
gi 1267372771 522 LM----YEILQNYNL-CnilIMISHQQD 544
Cdd:PRK11607 187 RMqlevVDILERVGVtC---VMVTHDQE 211
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
345-408 |
1.88e-09 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 58.55 E-value: 1.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 345 NSIEFKDV--CFK-YNENSDLIFDHF-----------------NVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGK 404
Cdd:COG1134 3 SMIEVENVskSYRlYHEPSRSLKELLlrrrrtrreefwalkdvSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGR 82
|
....
gi 1267372771 405 ILIN 408
Cdd:COG1134 83 VEVN 86
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
381-542 |
2.07e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 60.06 E-value: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 381 GINGSGKSTFIKLLTGLYQPKSGKILINniDYNLIHKESIRA-RIGI--VSQNIFLFKG-TILDNILYG--QTNKTKEDV 454
Cdd:PRK15439 44 GGNGAGKSTLMKIIAGIVPPDSGTLEIG--GNPCARLTPAKAhQLGIylVPQEPLLFPNlSVKENILFGlpKRQASMQKM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 455 VKLIKRyhLTSHLNrfengLDtiiVQDGSSVSGGQaQFIAFLRAILTQRDIIILDEAASNLH-IDTRNLMYEILQNYNLC 533
Cdd:PRK15439 122 KQLLAA--LGCQLD-----LD---SSAGSLEVADR-QIVEILRGLMRDSRILILDEPTASLTpAETERLFSRIRELLAQG 190
|
....*....
gi 1267372771 534 NILIMISHQ 542
Cdd:PRK15439 191 VGIVFISHK 199
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
381-549 |
2.17e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 59.92 E-value: 2.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 381 GINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIH-KESIRARIGIVSQNIFLF-KGTILDNILYGQTnKTKEDVVKLI 458
Cdd:PRK11288 37 GENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFAStTAALAAGVAIIYQELHLVpEMTVAENLYLGQL-PHKGGIVNRR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 459 K-RYHLTSHLNRFenGLDTIIVQDGSSVSGGQAQFIAFLRAILTQRDIIILDEAASNL-HIDTRNLMYEILQNYNLCNIL 536
Cdd:PRK11288 116 LlNYEAREQLEHL--GVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLsAREIEQLFRVIRELRAEGRVI 193
|
170
....*....|...
gi 1267372771 537 IMISHQQDGLYFL 549
Cdd:PRK11288 194 LYVSHRMEEIFAL 206
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
347-529 |
2.29e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 59.05 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVCFKYNENsdLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNidynlihkESI------ 420
Cdd:PRK13537 8 IDFRNVEKRYGDK--LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCG--------EPVpsrarh 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 421 -RARIGIVSQniflFKG-----TILDNIL-----YGQTNKTKEDVVKLIKRYhltshlNRFENGLDTIIvqdgSSVSGGQ 489
Cdd:PRK13537 78 aRQRVGVVPQ----FDNldpdfTVRENLLvfgryFGLSAAAARALVPPLLEF------AKLENKADAKV----GELSGGM 143
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1267372771 490 AQFIAFLRAILTQRDIIILDEAASNLHIDTRNLMYEILQN 529
Cdd:PRK13537 144 KRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRS 183
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
347-544 |
2.59e-09 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 59.04 E-value: 2.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVCFKYNENSDLI--FDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDY-NLIHKESIRAR 423
Cdd:PRK11153 2 IELKNISKVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtALSEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 424 --IGIVSQNIFLFKG-TILDNI-----LYGQT-NKTKEDVVKLIKRYHLTSHLNRFEngldtiivqdgSSVSGGQAQFIA 494
Cdd:PRK11153 82 rqIGMIFQHFNLLSSrTVFDNValpleLAGTPkAEIKARVTELLELVGLSDKADRYP-----------AQLSGGQKQRVA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1267372771 495 FLRAILTQRDIIILDEAASNLhiD---TR---NLMYEILQNYNLcNILiMISHQQD 544
Cdd:PRK11153 151 IARALASNPKVLLCDEATSAL--DpatTRsilELLKDINRELGL-TIV-LITHEMD 202
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
346-528 |
3.16e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 58.69 E-value: 3.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 346 SIEFKDVCFKYNENsdLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNlIHKESIRARIG 425
Cdd:PRK13536 41 AIDLAGVSKSYGDK--AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVP-ARARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 426 IVSQ--NIFLfKGTILDNIL-----YGQTNKTKEDVVKLIKRYhltshlNRFENGLDTIIvqdgSSVSGGQAQFIAFLRA 498
Cdd:PRK13536 118 VVPQfdNLDL-EFTVRENLLvfgryFGMSTREIEAVIPSLLEF------ARLESKADARV----SDLSGGMKRRLTLARA 186
|
170 180 190
....*....|....*....|....*....|
gi 1267372771 499 ILTQRDIIILDEAASNLHIDTRNLMYEILQ 528
Cdd:PRK13536 187 LINDPQLLILDEPTTGLDPHARHLIWERLR 216
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
362-537 |
3.51e-09 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 57.69 E-value: 3.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 362 LIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNidynlihkESIR-------ARIGIVS--QNIF 432
Cdd:PRK11300 19 LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRG--------QHIEglpghqiARMGVVRtfQHVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 433 LFKG-TILDNILYGQTNKTKEDVVK-LIK--------------------RYHLTSHLNRfengldtiivqDGSSVSGGQA 490
Cdd:PRK11300 91 LFREmTVIENLLVAQHQQLKTGLFSgLLKtpafrraesealdraatwleRVGLLEHANR-----------QAGNLAYGQQ 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1267372771 491 QFIAFLRAILTQRDIIILDEAASNLH----IDTRNLMYEILQNYNLCNILI 537
Cdd:PRK11300 160 RRLEIARCMVTQPEILMLDEPAAGLNpketKELDELIAELRNEHNVTVLLI 210
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
363-517 |
3.74e-09 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 57.89 E-value: 3.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 363 IFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKESIRA---RIGIVSQNIflfkgtil 439
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAfrrDVQLVFQDS-------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 440 dnilYGQTN--KTKEDVVKLIKRyHLTS-----------HLNRfENGLDTIIVQD-GSSVSGGQAQFIAFLRAILTQRDI 505
Cdd:TIGR02769 98 ----PSAVNprMTVRQIIGEPLR-HLTSldeseqkariaELLD-MVGLRSEDADKlPRQLSGGQLQRINIARALAVKPKL 171
|
170
....*....|..
gi 1267372771 506 IILDEAASNLHI 517
Cdd:TIGR02769 172 IVLDEAVSNLDM 183
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
368-559 |
4.85e-09 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 57.33 E-value: 4.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 368 NVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQ----PKSGKILINNIdynlIHKE--------SIRARIGIVSQNIFLF- 434
Cdd:PRK09984 24 DLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdksAGSHIELLGRT----VQREgrlardirKSRANTGYIFQQFNLVn 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 435 KGTILDNILYGQTN-----KTKEDVVKLIKRYHLTSHLNRFenGLDTIIVQDGSSVSGGQAQFIAFLRAILTQRDIIILD 509
Cdd:PRK09984 100 RLSVLENVLIGALGstpfwRTCFSWFTREQKQRALQALTRV--GMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILAD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1267372771 510 EAASNLHIDTRNLMYEILQNYNLCN-ILIMIS-HQQD-GLYFLNKTLELTHGN 559
Cdd:PRK09984 178 EPIASLDPESARIVMDTLRDINQNDgITVVVTlHQVDyALRYCERIVALRQGH 230
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
347-515 |
5.57e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 57.51 E-value: 5.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVCFKYNENSDLIfDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKESIRARIGI 426
Cdd:PRK13652 4 IETRDLCYSYSGSKEAL-NNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 427 VSQNI--FLFKGTILDNILYGQTN-KTKEDVVKlikrYHLTSHLNRFenGLDTIIVQDGSSVSGGQAQFIAFLRAILTQR 503
Cdd:PRK13652 83 VFQNPddQIFSPTVEQDIAFGPINlGLDEETVA----HRVSSALHML--GLEELRDRVPHHLSGGEKKRVAIAGVIAMEP 156
|
170
....*....|..
gi 1267372771 504 DIIILDEAASNL 515
Cdd:PRK13652 157 QVLVLDEPTAGL 168
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
359-557 |
9.41e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 55.65 E-value: 9.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 359 NSDLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDynlIHKESIRARIGIVSQNIFLfKG-- 436
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD---IDDPDVAEACHYLGHRNAM-KPal 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 437 TILDNI-----LYGQTNKTKEDVVKLIKRYHLTsHLnRFENgldtiivqdgssVSGGQAQFIAFLRAILTQRDIIILDEA 511
Cdd:PRK13539 89 TVAENLefwaaFLGGEELDIAAALEAVGLAPLA-HL-PFGY------------LSAGQKRRVALARLLVSNRPIWILDEP 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1267372771 512 ASNLHIDTRNLMYEILQNY-NLCNILIMISHQQDGLYfLNKTLELTH 557
Cdd:PRK13539 155 TAALDAAAVALFAELIRAHlAQGGIVIAATHIPLGLP-GARELDLGP 200
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
354-543 |
1.20e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 55.34 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 354 FKYNENsdLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILI--NNIDYNLIHKES----IRARIGIv 427
Cdd:PRK13540 9 FDYHDQ--PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFerQSIKKDLCTYQKqlcfVGHRSGI- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 428 sqNIFLfkgTILDNILYG-QTNKTKEDVVKLIKRYHLtSHLNRFENGLdtiivqdgssVSGGQAQFIAFLRAILTQRDII 506
Cdd:PRK13540 86 --NPYL---TLRENCLYDiHFSPGAVGITELCRLFSL-EHLIDYPCGL----------LSSGQKRQVALLRLWMSKAKLW 149
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1267372771 507 ILDE---AASNLHIDTrnLMYEILQNYNLCNILIMISHQQ 543
Cdd:PRK13540 150 LLDEplvALDELSLLT--IITKIQEHRAKGGAVLLTSHQD 187
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
363-510 |
1.71e-08 |
|
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: 54.81 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 363 IFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKESIRARIGIVSQNIFLFKGTILDNI 442
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENL 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1267372771 443 LYGQTNKTKEDVVKLIKRYHLtshlnrfeNGLDTIIVqdgSSVSGGQAQFIAFLRAILTQRDIIILDE 510
Cdd:cd03231 95 RFWHADHSDEQVEEALARVGL--------NGFEDRPV---AQLSAGQQRRVALARLLLSGRPLWILDE 151
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
363-544 |
1.77e-08 |
|
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: 55.23 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 363 IFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNidynlihkeSIRARIGI---------VSQNIFl 433
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG---------RVSSLLGLgggfnpeltGRENIY- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 434 FKGTIldnilYGQTNKTKEDVVKLIKRYhltSHLNRFengLDTIIvqdgSSVSGGQAQFIAFLRAILTQRDIIILDEAAS 513
Cdd:cd03220 107 LNGRL-----LGLSRKEIDEKIDEIIEF---SELGDF---IDLPV----KTYSSGMKARLAFAIATALEPDILLIDEVLA 171
|
170 180 190
....*....|....*....|....*....|..
gi 1267372771 514 NLHIDTRNLMYEILQNYNL-CNILIMISHQQD 544
Cdd:cd03220 172 VGDAAFQEKCQRRLRELLKqGKTVILVSHDPS 203
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
32-296 |
2.77e-08 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 55.62 E-value: 2.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 32 LAFGLLGMVIASLIIAPIPYIIGYIIDKVILLNKSYDQLLKTTLILLLIYCINYLISIGYEYLFTRVQQNVVNEIRLSMI 111
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDLVTIGSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 112 SNIIDAPLSYINQKEKGYILSRIAE-SGNVSALFSPNLLRVFSGIFDFFFALFIMFNLSVKLTGIIVI----IIPIYFVI 186
Cdd:cd18778 81 DKLQRLSLRYFDDRQTGDLMSRVINdVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIpipfLALGAWLY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 187 SKYSSEMISKsttnVYESSAVLNAEMYETLNGIEDIKLLNGKNIQTNKIKAKLNDVIKSalkqSLHFIFFMQNLIVTNNF 266
Cdd:cd18778 161 SKKVRPRYRK----VREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKA----QLRAMKLWAIFHPLMEF 232
|
250 260 270
....*....|....*....|....*....|....
gi 1267372771 267 V----TVIVLLVSGILILQNQLTIGVYTSFSIYM 296
Cdd:cd18778 233 LtslgTVLVLGFGGRLVLAGELTIGDLVAFLLYL 266
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
224-515 |
2.86e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 57.10 E-value: 2.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 224 LLNGKNIQTNKIKAKLndVIKSALKQ--SLHFIFFMQNL----------IVTNNFVTVIVLL-VSGILILQNQLTIGVyT 290
Cdd:PTZ00243 1143 ALQGSATITAYGKAHL--VMQEALRRldVVYSCSYLENVanrwlgvrveFLSNIVVTVIALIgVIGTMLRATSQEIGL-V 1219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 291 SFSIYMAklLATTQALGSL---DITLKPVCISIKRIKEFFN---------LDVE------------NTLGTNIIkEPIN- 345
Cdd:PTZ00243 1220 SLSLTMA--MQTTATLNWLvrqVATVEADMNSVERLLYYTDevphedmpeLDEEvdalerrtgmaaDVTGTVVI-EPASp 1296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 346 -----------SIEFKDVCFKYNENSDLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNID--- 411
Cdd:PTZ00243 1297 tsaaphpvqagSLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREiga 1376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 412 YNLihkESIRARIGIVSQNIFLFKGTI---LDNILygqtNKTKEDVVKLIKRYHLTSHLNRFENGLDTIIVQDGSSVSGG 488
Cdd:PTZ00243 1377 YGL---RELRRQFSMIPQDPVLFDGTVrqnVDPFL----EASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVG 1449
|
330 340
....*....|....*....|....*....
gi 1267372771 489 QAQFIAFLRAILtQRD--IIILDEAASNL 515
Cdd:PTZ00243 1450 QRQLMCMARALL-KKGsgFILMDEATANI 1477
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
368-515 |
2.99e-08 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 54.98 E-value: 2.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 368 NVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHK-------------ESIRARIGIVSQNIFLF 434
Cdd:PRK10619 25 SLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDkdgqlkvadknqlRLLRTRLTMVFQHFNLW 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 435 KG-TILDNILygqtnKTKEDVVKLIK---RYHLTSHLNRFenGLDTIIVQD-GSSVSGGQAQFIAFLRAILTQRDIIILD 509
Cdd:PRK10619 105 SHmTVLENVM-----EAPIQVLGLSKqeaRERAVKYLAKV--GIDERAQGKyPVHLSGGQQQRVSIARALAMEPEVLLFD 177
|
....*.
gi 1267372771 510 EAASNL 515
Cdd:PRK10619 178 EPTSAL 183
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
344-542 |
3.31e-08 |
|
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: 54.20 E-value: 3.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 344 INSIEFKDVCFKYNE--NSDLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQP---KSGKILINNIDynlIHKE 418
Cdd:cd03234 1 QRVLPWWDVGLKAKNwnKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQP---RKPD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 419 SIRARIGIVSQNIFLFKG-TILDNILY----------GQTNKTKEDVVKLIKRYHLTSHLNRFENGLdtiivqdgssvSG 487
Cdd:cd03234 78 QFQKCVAYVRQDDILLPGlTVRETLTYtailrlprksSDAIRKKRVEDVLLRDLALTRIGGNLVKGI-----------SG 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1267372771 488 GQAQFIAFLRAILTQRDIIILDEAASNLHIDTRNLMYEILQNYNLCNILIMIS-HQ 542
Cdd:cd03234 147 GERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTiHQ 202
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
93-308 |
5.05e-08 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 54.47 E-value: 5.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 93 YLFTRVQQNVVNEIRLSMISNIIDAPLSYINQKEKGYILSRI-AESGNVSALFSPNLLRVFSGIFDFFFALFIMFNLSVK 171
Cdd:cd18572 58 GCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLtSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWR 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 172 LTGIIVIIIPIYFVISKYSSEMISKSTTNVYESSAVLNAEMYETLNGIEDIKLLNGKNIQTNKIKAKLNDVIKSALKQSL 251
Cdd:cd18572 138 LTLLAFITVPVIALITKVYGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQAL 217
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1267372771 252 HFIFFMQNLIVTNNFVTVIVLLVSGILILQNQLTIGVYTSFSIYMAKLLATTQALGS 308
Cdd:cd18572 218 AYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGD 274
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
365-544 |
5.06e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 55.71 E-value: 5.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 365 DHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYqPK---SGKILIN-------NIdynlihKESIRARIGIVSQNIFLF 434
Cdd:PRK13549 22 DNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEgeelqasNI------RDTERAGIAIIHQELALV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 435 KG-TILDNILYGQtNKTKEDVVKLIKRYHLTSHLNRfENGLDTIIVQDGSSVSGGQAQFIAFLRAILTQRDIIILDEAAS 513
Cdd:PRK13549 95 KElSVLENIFLGN-EITPGGIMDYDAMYLRAQKLLA-QLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTA 172
|
170 180 190
....*....|....*....|....*....|...
gi 1267372771 514 NL-HIDTRNLMyEILQNYNLCNI-LIMISHQQD 544
Cdd:PRK13549 173 SLtESETAVLL-DIIRDLKAHGIaCIYISHKLN 204
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
371-541 |
5.42e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 53.96 E-value: 5.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 371 IEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKIlinnidynlihKESIRARIGIVSQNIFLFKGTIL--DNILYGQTN 448
Cdd:PRK09544 27 LKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-----------KRNGKLRIGYVPQKLYLDTTLPLtvNRFLRLRPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 449 KTKEDVVKLIKRYHlTSHLnrfengldtiIVQDGSSVSGGQAQFIAFLRAILTQRDIIILDEAASNLHIDTRNLMYEI-- 526
Cdd:PRK09544 96 TKKEDILPALKRVQ-AGHL----------IDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLid 164
|
170
....*....|....*.
gi 1267372771 527 -LQNYNLCNILiMISH 541
Cdd:PRK09544 165 qLRRELDCAVL-MVSH 179
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
379-543 |
5.47e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 53.34 E-value: 5.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 379 IDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKesirARIGIVSQNIFL-FKGTILDNI-LYGQTNKTKEDVVK 456
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAK----PYCTYIGHNLGLkLEMTVFENLkFWSEIYNSAETLYA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 457 LIKRYHLTSHLNrfengldtiivQDGSSVSGGQAQFIAFLRAILTQRDIIILDEAASNLHIDTRNLMYE-ILQNYNLCNI 535
Cdd:PRK13541 107 AIHYFKLHDLLD-----------EKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNlIVMKANSGGI 175
|
....*...
gi 1267372771 536 LIMISHQQ 543
Cdd:PRK13541 176 VLLSSHLE 183
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
384-510 |
6.04e-08 |
|
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: 54.72 E-value: 6.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 384 GSGKSTFIKLLTGLYQPKSGKILIN-------NIDYNL-IHKesiRaRIGIVSQNIFLFKG-TILDNILYGQTNKTK--- 451
Cdd:COG4148 35 GSGKTTLLRAIAGLERPDSGRIRLGgevlqdsARGIFLpPHR---R-RIGYVFQEARLFPHlSVRGNLLYGRKRAPRaer 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1267372771 452 ----EDVVKLIkryHLTSHLNRFENGLdtiivqdgssvSGGQAQFIAFLRAILTQRDIIILDE 510
Cdd:COG4148 111 risfDEVVELL---GIGHLLDRRPATL-----------SGGERQRVAIGRALLSSPRLLLMDE 159
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
368-541 |
7.62e-08 |
|
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: 53.49 E-value: 7.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 368 NVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILIN-NIDYNliHKESIRARIGIV----SQNI--------FLF 434
Cdd:cd03267 41 SFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAgLVPWK--RRKKFLRRIGVVfgqkTQLWwdlpvidsFYL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 435 KGTILDnILYGQTNKTKEDVVKLIKRYHLtshlnrfengLDTIIVQdgssVSGGQ---AQFIAflrAILTQRDIIILDEA 511
Cdd:cd03267 119 LAAIYD-LPPARFKKRLDELSELLDLEEL----------LDTPVRQ----LSLGQrmrAEIAA---ALLHEPEILFLDEP 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1267372771 512 ASNLHIDTRNLMYEILQNYN-------------------LCNILIMISH 541
Cdd:cd03267 181 TIGLDVVAQENIRNFLKEYNrergttvlltshymkdieaLARRVLVIDK 229
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
318-513 |
7.84e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 55.72 E-value: 7.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 318 ISIKRIKEFFN---LDVENTLGTNIIKEPINSIEFKDVCFKYNENSDLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLL 394
Cdd:TIGR00957 605 VSLKRLRIFLSheeLEPDSIERRTIKPGEGNSITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 395 TGLYQPKSGKIlinnidynlihkeSIRARIGIVSQNIFLFKGTILDNILYGQTNKTKEdVVKLIKRYHLTSHLNRFENGL 474
Cdd:TIGR00957 685 LAEMDKVEGHV-------------HMKGSVAYVPQQAWIQNDSLRENILFGKALNEKY-YQQVLEACALLPDLEILPSGD 750
|
170 180 190
....*....|....*....|....*....|....*....
gi 1267372771 475 DTIIVQDGSSVSGGQAQFIAFLRAILTQRDIIILDEAAS 513
Cdd:TIGR00957 751 RTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLS 789
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
363-531 |
8.22e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 53.84 E-value: 8.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 363 IFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKESIRARIGIVSQNI----------F 432
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNAttpgditvqeL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 433 LFKGTILDNILYGQTNKTKEDVVKLIKRYHLTSHLNRfengldtiivQDGSSVSGGQAQFiAFLRAILTQR-DIIILDEA 511
Cdd:PRK10253 102 VARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLAD----------QSVDTLSGGQRQR-AWIAMVLAQEtAIMLLDEP 170
|
170 180
....*....|....*....|
gi 1267372771 512 ASNLHIDTRNLMYEILQNYN 531
Cdd:PRK10253 171 TTWLDISHQIDLLELLSELN 190
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
343-518 |
8.30e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 55.25 E-value: 8.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 343 PInsIEFKDVCFKYnENSDLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILinnidynlihkESIRA 422
Cdd:PLN03073 507 PI--ISFSDASFGY-PGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF-----------RSAKV 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 423 RIGIVSQNiflfkgtILDNIlygqtNKTKEDVVKLIKRY------HLTSHLNRFenGLD-TIIVQDGSSVSGGQAQFIAF 495
Cdd:PLN03073 573 RMAVFSQH-------HVDGL-----DLSSNPLLYMMRCFpgvpeqKLRAHLGSF--GVTgNLALQPMYTLSGGQKSRVAF 638
|
170 180
....*....|....*....|...
gi 1267372771 496 LRAILTQRDIIILDEAASNLHID 518
Cdd:PLN03073 639 AKITFKKPHILLLDEPSNHLDLD 661
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
368-546 |
8.53e-08 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 52.95 E-value: 8.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 368 NVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKESI---RARIGIVSQN-IFLFKGTILDN-- 441
Cdd:PRK10908 22 TFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVpflRRQIGMIFQDhHLLMDRTVYDNva 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 442 ---ILYGQTNktkEDvvklIKRyhltshlnRFENGLDTIIVQDGS-----SVSGGQAQFIAFLRAILTQRDIIILDEAAS 513
Cdd:PRK10908 102 iplIIAGASG---DD----IRR--------RVSAALDKVGLLDKAknfpiQLSGGEQQRVGIARAVVNKPAVLLADEPTG 166
|
170 180 190
....*....|....*....|....*....|...
gi 1267372771 514 NLHIDTRNLMYEILQNYNLCNILIMISHQQDGL 546
Cdd:PRK10908 167 NLDDALSEGILRLFEEFNRVGVTVLMATHDIGL 199
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
365-541 |
1.14e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.57 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 365 DHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINnidynlihKESIRARIgivSQ----NIflfKGTILD 440
Cdd:PRK11147 20 DNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE--------QDLIVARL---QQdpprNV---EGTVYD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 441 NILYGQtnktkEDVVKLIKRYHLTSH----------LNR---------------FENGLDTIIVQDG-------SSVSGG 488
Cdd:PRK11147 86 FVAEGI-----EEQAEYLKRYHDISHlvetdpseknLNElaklqeqldhhnlwqLENRINEVLAQLGldpdaalSSLSGG 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1267372771 489 QAQFIAFLRAILTQRDIIILDEAASNLHIDTRNLMYEILQNYNLCniLIMISH 541
Cdd:PRK11147 161 WLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGS--IIFISH 211
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
364-527 |
1.42e-07 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 51.85 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 364 FDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILInnidynlihkeSIRARIGIVSQNIFL---FKGTILD 440
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRR-----------AGGARVAYVPQRSEVpdsLPLTVRD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 441 NILYGQTNK-------TKEDvvklikRYHLTSHLNRFenGLDTIIVQDGSSVSGGQAQFIAFLRAILTQRDIIILDEAAS 513
Cdd:NF040873 77 LVAMGRWARrglwrrlTRDD------RAAVDDALERV--GLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTT 148
|
170
....*....|....
gi 1267372771 514 NLHIDTRNLMYEIL 527
Cdd:NF040873 149 GLDAESRERIIALL 162
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
93-295 |
1.85e-07 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 53.02 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 93 YLFTRVQQNVVNEIRLSMISNIIDAPLSYINQKEKGYILSRIAESGNV--SALFSpNLLRVFSGIFDFFFALFIMFNLSV 170
Cdd:cd18780 64 WLFTLAGERVVARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVlqNAVTV-NLSMLLRYLVQIIGGLVFMFTTSW 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 171 KLTGIIVI----IIPIYFVISKYSSEMISKSTTNVYESSAVlnAEmyETLNGIEDIKLLNGKNIQTNKIKAKLNDVIKSA 246
Cdd:cd18780 143 KLTLVMLSvvppLSIGAVIYGKYVRKLSKKFQDALAAASTV--AE--ESISNIRTVRSFAKETKEVSRYSEKINESYLLG 218
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1267372771 247 LKQSLHFIFFMQNLIVTNNFVTVIVLLVSGILILQNQLTIGVYTSFSIY 295
Cdd:cd18780 219 KKLARASGGFNGFMGAAAQLAIVLVLWYGGRLVIDGELTTGLLTSFLLY 267
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
359-543 |
1.92e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 52.34 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 359 NSDLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTG--LYQPKSGKILINNIDYNLIHKEsIRARIGI---------- 426
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPE-ERAHLGIflafqypiei 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 427 --VSQNIFL---------FKG-TILDNILYGQTNKTKEDVVKLIKRYhltshLNRFengldtiiVQDGssVSGGQAQFIA 494
Cdd:CHL00131 97 pgVSNADFLrlaynskrkFQGlPELDPLEFLEIINEKLKLVGMDPSF-----LSRN--------VNEG--FSGGEKKRNE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1267372771 495 FLRAILTQRDIIILDEAASNLHIDT-RNLMYEILQNYNLCNILIMISHQQ 543
Cdd:CHL00131 162 ILQMALLDSELAILDETDSGLDIDAlKIIAEGINKLMTSENSIILITHYQ 211
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
347-521 |
2.08e-07 |
|
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: 52.05 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVCFKYNENSDL--IFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDynlIHK--ESIRA 422
Cdd:COG4181 9 IELRGLTKTVGTGAGEltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQD---LFAldEDARA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 423 R-----IGIVSQNIFLFKG-TILDNI-----LYGQTNkTKEDVVKLIKRYHLTSHLNRFENGLdtiivqdgssvSGGQAQ 491
Cdd:COG4181 86 RlrarhVGFVFQSFQLLPTlTALENVmlpleLAGRRD-ARARARALLERVGLGHRLDHYPAQL-----------SGGEQQ 153
|
170 180 190
....*....|....*....|....*....|
gi 1267372771 492 FIAFLRAILTQRDIIILDEAASNLhiDTRN 521
Cdd:COG4181 154 RVALARAFATEPAILFADEPTGNL--DAAT 181
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
351-531 |
2.34e-07 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 52.13 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 351 DVCFKYNENSDLIFDHFNV--QIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIH---KESIRAR-I 424
Cdd:PRK11629 10 NLCKRYQEGSVQTDVLHNVsfSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSsaaKAELRNQkL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 425 GIVSQNIFLFKG-TILDNI----LYG-----QTNKTKEDVVKLIkryhltshlnrfenGLDTIIVQDGSSVSGGQAQFIA 494
Cdd:PRK11629 90 GFIYQFHHLLPDfTALENVamplLIGkkkpaEINSRALEMLAAV--------------GLEHRANHRPSELSGGERQRVA 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 1267372771 495 FLRAILTQRDIIILDEAASNLHIDTRNLMYEILQNYN 531
Cdd:PRK11629 156 IARALVNNPRLVLADEPTGNLDARNADSIFQLLGELN 192
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
93-293 |
2.37e-07 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 52.51 E-value: 2.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 93 YLFTRVQQNVVNEIRLSMISNIIDAPLSYINQKEKGYILSRIAESGNVSALFSPNLLRVFSGIFDFFFALFIMFNLSVKL 172
Cdd:cd18555 64 YIIIKLQTKLDKSLMSDFFEHLLKLPYSFFENRSSGDLLFRANSNVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 173 TGIIVIIIPIYFVISKYSSEMISKSTTNVYESSAVLNAEMYETLNGIEDIKLLNGKNIQTNKIKAKLNDVIKSALKQSLH 252
Cdd:cd18555 144 TLIVLLLGLLIVLLLLLTRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERL 223
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1267372771 253 FIFFMQNLIVTNNFVTVIVLLVSGILILQNQLTIGVYTSFS 293
Cdd:cd18555 224 SNILNSISSSIQFIAPLLILWIGAYLVINGELTLGELIAFS 264
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
347-407 |
2.40e-07 |
|
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: 53.40 E-value: 2.40e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1267372771 347 IEFKDVCFKYNENsdLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILI 407
Cdd:TIGR03719 323 IEAENLTKAFGDK--LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI 381
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
365-544 |
2.61e-07 |
|
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: 53.29 E-value: 2.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 365 DHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYqPK---SGKILINNIDYNLIH-KESIRARIGIVSQNIFLFKG-TIL 439
Cdd:TIGR02633 18 DGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHgtwDGEIYWSGSPLKASNiRDTERAGIVIIHQELTLVPElSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 440 DNILYGQT---NKTKEDVVKLIKRYHLTSHLNRFENGLDTIIVQDgssVSGGQAQFIAFLRAILTQRDIIILDEAASNLH 516
Cdd:TIGR02633 97 ENIFLGNEitlPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVGD---YGGGQQQLVEIAKALNKQARLLILDEPSSSLT 173
|
170 180
....*....|....*....|....*....
gi 1267372771 517 IDTRNLMYEILQNYNLCNI-LIMISHQQD 544
Cdd:TIGR02633 174 EKETEILLDIIRDLKAHGVaCVYISHKLN 202
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
365-527 |
3.31e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 52.03 E-value: 3.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 365 DHFNVQIEKGDkllIDGI---NGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHkesiRARIGivsqniFL-------F 434
Cdd:COG4152 18 DDVSFTVPKGE---IFGLlgpNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRRIG------YLpeerglyP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 435 KGTILDNILY-----GQTNKT-KEDVVKLIKRYHLTSHLNrfenglDTIivqdgSSVSGGQAQFIAFLRAILTQRDIIIL 508
Cdd:COG4152 85 KMKVGEQLVYlarlkGLSKAEaKRRADEWLERLGLGDRAN------KKV-----EELSKGNQQKVQLIAALLHDPELLIL 153
|
170
....*....|....*....
gi 1267372771 509 DEAASNLHIDTRNLMYEIL 527
Cdd:COG4152 154 DEPFSGLDPVNVELLKDVI 172
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
347-518 |
3.42e-07 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 52.54 E-value: 3.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVCFKYNENSdlIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDynlIHKESIRA---R 423
Cdd:PRK09536 4 IDVSDLSVEFGDTT--VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDD---VEALSARAasrR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 424 IGIVSQniflfkgtildnilygQTNKTKEDVVKLIKRYHLTSHLNRFEN----------------GLDTIIVQDGSSVSG 487
Cdd:PRK09536 79 VASVPQ----------------DTSLSFEFDVRQVVEMGRTPHRSRFDTwtetdraaveramertGVAQFADRPVTSLSG 142
|
170 180 190
....*....|....*....|....*....|.
gi 1267372771 488 GQAQFIAFLRAILTQRDIIILDEAASNLHID 518
Cdd:PRK09536 143 GERQRVLLARALAQATPVLLLDEPTASLDIN 173
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
106-308 |
3.63e-07 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 51.93 E-value: 3.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 106 IRLSMISNIIDAPLSYINQKEKGYILSR-IAESGNVSALFSPNLLRVFSGIFDFFFALFIMFNLSVKLTGIIVIIIPIYF 184
Cdd:cd18784 71 IRNLLFRSIVSQEIGFFDTVKTGDITSRlTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIA 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 185 VISKYSSEMISKSTTNVYESSAVLNAEMYETLNGIEDIKLLNGKNIQTNKIKAKLNDVIKSALKQSLHFIFFMQNLIVTN 264
Cdd:cd18784 151 IVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTE 230
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1267372771 265 NFVTVIVLLVSGILILQNQLTIGVYTSFSIYMAKLLATTQALGS 308
Cdd:cd18784 231 LALTVSTLYYGGHLVITGQISGGNLISFILYQLELGSCLESVGS 274
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
367-530 |
3.66e-07 |
|
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: 51.64 E-value: 3.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 367 FNVQIEKGD-----KLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDynLIHK-ESIRARigivsqniflFKGTIlD 440
Cdd:cd03237 13 FTLEVEGGSiseseVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT--VSYKpQYIKAD----------YEGTV-R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 441 NILYGQTNKtkedvvKLIKRYHLTSHLNRFenGLDTIIVQDGSSVSGGQAQFIAFLRAILTQRDIIILDEAASNLHIDTR 520
Cdd:cd03237 80 DLLSSITKD------FYTHPYFKTEIAKPL--QIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQR 151
|
170
....*....|
gi 1267372771 521 NLMYEILQNY 530
Cdd:cd03237 152 LMASKVIRRF 161
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
345-429 |
4.58e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.59 E-value: 4.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 345 NSIEFKDVCFKYNENSdlIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKIlinnidynlihKESIRARI 424
Cdd:PRK15064 318 NALEVENLTKGFDNGP--LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV-----------KWSENANI 384
|
....*
gi 1267372771 425 GIVSQ 429
Cdd:PRK15064 385 GYYAQ 389
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
345-510 |
4.61e-07 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 51.69 E-value: 4.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 345 NSIEFKDVCFKYNENsdLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKE---SIR 421
Cdd:PRK11831 6 NLVDMRGVSFTRGNR--CIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSrlyTVR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 422 ARIGIVSQNIFLFKG-TILDNILYGQTNKTK--EDVVKlikryhlTSHLNRFEN-GLDTIIVQDGSSVSGGQAQFIAFLR 497
Cdd:PRK11831 84 KRMSMLFQSGALFTDmNVFDNVAYPLREHTQlpAPLLH-------STVMMKLEAvGLRGAAKLMPSELSGGMARRAALAR 156
|
170
....*....|...
gi 1267372771 498 AILTQRDIIILDE 510
Cdd:PRK11831 157 AIALEPDLIMFDE 169
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
365-544 |
5.86e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.04 E-value: 5.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 365 DHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNL-IHKESIRARIGIVSQNIFLFKG-TILDNI 442
Cdd:PRK10982 15 DNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFkSSKEALENGISMVHQELNLVLQrSVMDNM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 443 LYGQTnKTKEDVVKLIKRYHLTSHLNRfENGLDTIIVQDGSSVSGGQAQFIAFLRAILTQRDIIILDEAASNLHIDTRNL 522
Cdd:PRK10982 95 WLGRY-PTKGMFVDQDKMYRDTKAIFD-ELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNH 172
|
170 180
....*....|....*....|....
gi 1267372771 523 MYEILQNYNL--CNIlIMISHQQD 544
Cdd:PRK10982 173 LFTIIRKLKErgCGI-VYISHKME 195
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
371-541 |
6.83e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 50.55 E-value: 6.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 371 IEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKE---SIRAR-IGIVSQNIFLFKG-TILDNI--- 442
Cdd:PRK10584 33 VKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraKLRAKhVGFVFQSFMLIPTlNALENVelp 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 443 --LYGQT-NKTKEDVVKLIKRYHLTSHLNRFEngldtiivqdgSSVSGGQAQFIAFLRAILTQRDIIILDEAASNLHIDT 519
Cdd:PRK10584 113 alLRGESsRQSRNGAKALLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQT 181
|
170 180
....*....|....*....|....
gi 1267372771 520 RNLMYEIL--QNYNLCNILIMISH 541
Cdd:PRK10584 182 GDKIADLLfsLNREHGTTLILVTH 205
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
371-542 |
8.67e-07 |
|
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: 49.47 E-value: 8.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 371 IEKGDKLLIDGINGSGKSTFIKLLTGL--YQPKSGKILINNIDynlIHKESIRARIGIVSQniflfkgtilDNILYGqtn 448
Cdd:cd03213 32 AKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRP---LDKRSFRKIIGYVPQ----------DDILHP--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 449 ktkedvvklikryHLTSHLN-RFENGLdtiivqdgSSVSGGQAQFIAFLRAILTQRDIIILDEAASNLHIDTRNLMYEIL 527
Cdd:cd03213 96 -------------TLTVRETlMFAAKL--------RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLL 154
|
170
....*....|....*.
gi 1267372771 528 QNYNLCNILIMIS-HQ 542
Cdd:cd03213 155 RRLADTGRTIICSiHQ 170
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
362-411 |
9.02e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 49.80 E-value: 9.02e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1267372771 362 LIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNID 411
Cdd:PRK13538 15 ILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEP 64
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
118-301 |
9.10e-07 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349993 [Multi-domain] Cd Length: 295 Bit Score: 50.91 E-value: 9.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 118 PLSYINQKEKGYILSRIaesgnVSALFS--------PNLLrvFSGIFDFFFALFIMFNLSVKLTGIIVIIIPIYFVISKY 189
Cdd:cd18549 89 SFSFFDNNKTGQLMSRI-----TNDLFDiselahhgPEDL--FISIITIIGSFIILLTINVPLTLIVFALLPLMIIFTIY 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 190 SSEMISKSTTNVYESSAVLNAEMYETLNGIEDIKLLNGKNIQTNKIKAKLNDVIKSALKQSLHFIFFMQNLIVTNNFVTV 269
Cdd:cd18549 162 FNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDRFLESKKKAYKAMAYFFSGMNFFTNLLNL 241
|
170 180 190
....*....|....*....|....*....|..
gi 1267372771 270 IVLLVSGILILQNQLTIGVYTSFSIYMAKLLA 301
Cdd:cd18549 242 VVLVAGGYFIIKGEITLGDLVAFLLYVNVFIK 273
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
356-527 |
9.20e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 49.85 E-value: 9.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 356 YNENSDLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINN-----------IDYnLIHKESIRARI 424
Cdd:PRK13543 19 FSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGktatrgdrsrfMAY-LGHLPGLKADL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 425 GIVSQNIFLfkgtildNILYG-QTNKTKEDVVKLIKryhLTSHlnrfengLDTIIVQdgssVSGGQAQFIAFLRAILTQR 503
Cdd:PRK13543 98 STLENLHFL-------CGLHGrRAKQMPGSALAIVG---LAGY-------EDTLVRQ----LSAGQKKRLALARLWLSPA 156
|
170 180
....*....|....*....|....
gi 1267372771 504 DIIILDEAASNLHIDTRNLMYEIL 527
Cdd:PRK13543 157 PLWLLDEPYANLDLEGITLVNRMI 180
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
347-544 |
9.70e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 50.78 E-value: 9.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVCFKYNENSDLIF---DHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINniDYNL---IHK--- 417
Cdd:PRK13645 7 IILDNVSYTYAKKTPFEFkalNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVG--DYAIpanLKKike 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 418 -ESIRARIGIVSQ--NIFLFKGTILDNILYGQTN--KTKEDVVKLIKRYHLTSHLNRfengldTIIVQDGSSVSGGQAQF 492
Cdd:PRK13645 85 vKRLRKEIGLVFQfpEYQLFQETIEKDIAFGPVNlgENKQEAYKKVPELLKLVQLPE------DYVKRSPFELSGGQKRR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1267372771 493 IAFLRAILTQRDIIILDEAASNL----HIDTRNLMYEILQNYNlcNILIMISHQQD 544
Cdd:PRK13645 159 VALAGIIAMDGNTLVLDEPTGGLdpkgEEDFINLFERLNKEYK--KRIIMVTHNMD 212
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
347-515 |
1.01e-06 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 50.26 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 347 IEFKDVCFKYNENSDLifDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKESI-RARIG 425
Cdd:PRK11614 6 LSFDKVSAHYGKIQAL--HEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKImREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 426 IVSQNIFLF-KGTILDNILYGQTNKTKEDVVKLIKR-YHLTSHLnrFENGldtiiVQDGSSVSGGQAQFIAFLRAILTQR 503
Cdd:PRK11614 84 IVPEGRRVFsRMTVEENLAMGGFFAERDQFQERIKWvYELFPRL--HERR-----IQRAGTMSGGEQQMLAIGRALMSQP 156
|
170
....*....|..
gi 1267372771 504 DIIILDEAASNL 515
Cdd:PRK11614 157 RLLLLDEPSLGL 168
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
365-427 |
1.02e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 50.86 E-value: 1.02e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1267372771 365 DHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDynlIHKESIR--ARIGIV 427
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYV---PFKRRKEfaRRIGVV 100
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
346-411 |
1.08e-06 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 50.16 E-value: 1.08e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1267372771 346 SIEFKDVCFKYNENsdLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNID 411
Cdd:PRK13548 2 MLEARNLSVRLGGR--TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRP 65
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
86-309 |
1.54e-06 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 50.20 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 86 LISIGYEYLFTRVQQNVVNEIRLSMISNIIDAPLSYINQKEKGYILSRIAesGNVSAL---FSPNLLRVFSGIFDFFFAL 162
Cdd:cd18564 69 LASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLT--GDVGAIqdlLVSGVLPLLTNLLTLVGML 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 163 FIMFNLSVKLTGIIVIIIPIYFVISKYSSEMISKSTTNVYESSAVLNAEMYETLNGIEDIKLL-------------NGKN 229
Cdd:cd18564 147 GVMFWLDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFgreeheerrfareNRKS 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 230 IQTN----KIKAKLNDVIksalkqslhfiffmqNLIVTnnFVTVIVLLVSGILILQNQLTIGVYTSFSIYMAKLLATTQA 305
Cdd:cd18564 227 LRAGlraaRLQALLSPVV---------------DVLVA--VGTALVLWFGAWLVLAGRLTPGDLLVFLAYLKNLYKPVRD 289
|
....
gi 1267372771 306 LGSL 309
Cdd:cd18564 290 LAKL 293
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
364-510 |
1.88e-06 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 50.40 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 364 FDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIH-KESIRARIGIVSQN-----IFLfKGT 437
Cdd:COG1129 268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSpRDAIRAGIAYVPEDrkgegLVL-DLS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 438 ILDNIL---------YGQTNKTKED--VVKLIKRYHL-TShlnrfenGLDTIIvqdgSSVSGGQAQFIAFLRAILTQRDI 505
Cdd:COG1129 347 IRENITlasldrlsrGGLLDRRRERalAEEYIKRLRIkTP-------SPEQPV----GNLSGGNQQKVVLAKWLATDPKV 415
|
....*
gi 1267372771 506 IILDE 510
Cdd:COG1129 416 LILDE 420
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
344-560 |
2.14e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 49.26 E-value: 2.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 344 INSIEFKDVCFKYNENSdlIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKS-----GKILI--NNIDYNLIH 416
Cdd:PRK14258 5 IPAIKVNNLSFYYDTQK--ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFfnQNIYERRVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 417 KESIRARIGIVSQNIFLFKGTILDNILYGqtnktkedvVKLIKrYHLTSHLNRF-ENGL------DTI---IVQDGSSVS 486
Cdd:PRK14258 83 LNRLRRQVSMVHPKPNLFPMSVYDNVAYG---------VKIVG-WRPKLEIDDIvESALkdadlwDEIkhkIHKSALDLS 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1267372771 487 GGQAQFIAFLRAILTQRDIIILDEAASNLHIDTRNLMYEILQNYNLCNILIM--ISHQQDGLYFLNKTLELTHGNK 560
Cdd:PRK14258 153 GGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMviVSHNLHQVSRLSDFTAFFKGNE 228
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
118-287 |
5.04e-06 |
|
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).
Pssm-ID: 350032 [Multi-domain] Cd Length: 294 Bit Score: 48.65 E-value: 5.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 118 PLSYINQKEKGYILSRIAESGNVSALFSPNLLrvfSGIFDFFFA---LFIMFNLSVKLTGIIVIIIPIYFVISKYSSEMI 194
Cdd:cd18588 89 PLSYFESRQVGDTVARVRELESIRQFLTGSAL---TLVLDLVFSvvfLAVMFYYSPTLTLIVLASLPLYALLSLLVTPIL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 195 SKSTTNVYESSAVLNAEMYETLNGIEDIKLLNGKNIQTNKIKAKLNDVIKSALKQSL------HFIFFMQNLivtnnfVT 268
Cdd:cd18588 166 RRRLEEKFQRGAENQSFLVETVTGIETVKSLAVEPQFQRRWEELLARYVKASFKTANlsnlasQIVQLIQKL------TT 239
|
170
....*....|....*....
gi 1267372771 269 VIVLLVSGILILQNQLTIG 287
Cdd:cd18588 240 LAILWFGAYLVMDGELTIG 258
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
363-510 |
5.11e-06 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 47.97 E-value: 5.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 363 IFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNL--IHKESIRArIGIVSQNIFLFKG-TIL 439
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLlpLHARARRG-IGYLPQEASIFRRlSVY 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1267372771 440 DNILYG-------QTNKTKEDVVKLIKRYHLtSHLnrfENGLdtiivqdGSSVSGGQAQFIAFLRAILTQRDIIILDE 510
Cdd:PRK10895 97 DNLMAVlqirddlSAEQREDRANELMEEFHI-EHL---RDSM-------GQSLSGGERRRVEIARALAANPKFILLDE 163
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
363-543 |
7.09e-06 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 47.75 E-value: 7.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 363 IFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGL--YQPKSGKILINNIDynlIHKESI--RARIGivsqnIFL----- 433
Cdd:COG0396 15 ILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGED---ILELSPdeRARAG-----IFLafqyp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 434 --FKGTILDNILYGQTNKTKED----------VVKLIKRYHL-TSHLNRFEN-GLdtiivqdgssvSGGQAQFIAFLRAI 499
Cdd:COG0396 87 veIPGVSVSNFLRTALNARRGEelsareflklLKEKMKELGLdEDFLDRYVNeGF-----------SGGEKKRNEILQML 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1267372771 500 LTQRDIIILDEAASNLHIDTRNLMYEILQNYNLCNI-LIMISHQQ 543
Cdd:COG0396 156 LLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRgILIITHYQ 200
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
378-550 |
1.14e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 47.96 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 378 LIdGINGSGKSTFIKLLTGLYQPKSGKIlinNIDYNLihkesiraRIGIVSQNIFLF-KGTILDNILYGQTN--KTKEDv 454
Cdd:PRK15064 32 LI-GANGCGKSTFMKILGGDLEPSAGNV---SLDPNE--------RLGKLRQDQFAFeEFTVLDTVIMGHTElwEVKQE- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 455 vklikRYHLTSHLNRFEngldtiivQDGSSVSGGQAQFIAF-----------------------------------LRAI 499
Cdd:PRK15064 99 -----RDRIYALPEMSE--------EDGMKVADLEVKFAEMdgytaearagelllgvgipeeqhyglmsevapgwkLRVL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1267372771 500 LTQR-----DIIILDEAASNLHIDTRNLMYEILQNYNlCNILImISHQQdglYFLN 550
Cdd:PRK15064 166 LAQAlfsnpDILLLDEPTNNLDINTIRWLEDVLNERN-STMII-ISHDR---HFLN 216
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
381-510 |
1.89e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 47.31 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 381 GINGSGKSTFIKLLTGLYQPKSGKI--LINNIDYNLiHKESIRARIGIVSQNIFLFKG-TILDNILYGQ--TN------- 448
Cdd:PRK10762 37 GENGAGKSTMMKVLTGIYTRDAGSIlyLGKEVTFNG-PKSSQEAGIGIIHQELNLIPQlTIAENIFLGRefVNrfgridw 115
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1267372771 449 -KTKEDVVKLIKRYHLTSHLNRFENGLdtiivqdgssvSGGQAQFIAFLRAILTQRDIIILDE 510
Cdd:PRK10762 116 kKMYAEADKLLARLNLRFSSDKLVGEL-----------SIGEQQMVEIAKVLSFESKVIIMDE 167
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
365-527 |
1.92e-05 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 46.23 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 365 DHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYnlihkESIRARIGIVSQNIFLFK-GTILDNI- 442
Cdd:PRK11248 18 EDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV-----EGPGAERGVVFQNEGLLPwRNVQDNVa 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 443 ----LYGQTNKTKEDVV-KLIKRYHLTSHLNRFengldtiIVQdgssVSGGQAQFIAFLRAILTQRDIIILDEAASNLHI 517
Cdd:PRK11248 93 fglqLAGVEKMQRLEIAhQMLKKVGLEGAEKRY-------IWQ----LSGGQRQRVGIARALAANPQLLLLDEPFGALDA 161
|
170
....*....|
gi 1267372771 518 DTRNLMYEIL 527
Cdd:PRK11248 162 FTREQMQTLL 171
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
370-519 |
2.56e-05 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 46.03 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 370 QIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKESIRARIGIVSQNIFLFKGTILDNILYGQ--- 446
Cdd:PRK15056 29 TVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVPQSEEVDWSFPVLVEDVVMMGRygh 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 447 -------TNKTKEDVVKLIKRYHLTSHLNRfengldtiivQDGsSVSGGQAQFIAFLRAILTQRDIIILDEAASNLHIDT 519
Cdd:PRK15056 109 mgwlrraKKRDRQIVTAALARVDMVEFRHR----------QIG-ELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKT 177
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
86-295 |
4.34e-05 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 45.53 E-value: 4.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 86 LISIGYEYLFTRVQQNVVNEIRLSMISNI----IDAPLSYINQKEKGYILSRIAESGNVSALFSPNLLrvfSGIFD---F 158
Cdd:cd18567 53 LLQALLSALRSWLVLYLSTSLNLQWTSNLfrhlLRLPLSYFEKRHLGDIVSRFGSLDEIQQTLTTGFV---EALLDglmA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 159 FFALFIMFNLSVKLTGIIVIIIPIYFVISKYSSEMISKSTTNVYESSAVLNAEMYETLNGIEDIKLLNGKNIQTNKIKAK 238
Cdd:cd18567 130 ILTLVMMFLYSPKLALIVLAAVALYALLRLALYPPLRRATEEQIVASAKEQSHFLETIRGIQTIKLFGREAEREARWLNL 209
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1267372771 239 LNDVIKSALK-QSLHFIF-FMQNLIVtnNFVTVIVLLVSGILILQNQLTIGVYTSFSIY 295
Cdd:cd18567 210 LVDAINADIRlQRLQILFsAANGLLF--GLENILVIYLGALLVLDGEFTVGMLFAFLAY 266
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
374-407 |
4.52e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 46.27 E-value: 4.52e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1267372771 374 GDKLLID---------GI------NGSGKSTFIKLLTGLYQPKSGKILI 407
Cdd:PRK11819 335 GDRLLIDdlsfslppgGIvgiigpNGAGKSTLFKMITGQEQPDSGTIKI 383
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
326-542 |
7.58e-05 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 45.42 E-value: 7.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 326 FFNLDVENTLGTNIIKEPINSIEFKDVCFKYNENSDLIfdhfNV--QIEKGDKLLIDGINGSGKSTFIKLLTGlYQPK-- 401
Cdd:TIGR00955 5 WRNSDVFGRVAQDGSWKQLVSRLRGCFCRERPRKHLLK----NVsgVAKPGELLAVMGSSGAGKTTLMNALAF-RSPKgv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 402 --SGKILINNIDynlIHKESIRARIGIVSQ-NIFLFKGTILDNILYGQTNKTKEDVVKLIKRYHLTSHLNRFenGL---- 474
Cdd:TIGR00955 80 kgSGSVLLNGMP---IDAKEMRAISAYVQQdDLFIPTLTVREHLMFQAHLRMPRRVTKKEKRERVDEVLQAL--GLrkca 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1267372771 475 DTIIVQDGS--SVSGGQAQFIAFLRAILTQRDIIILDEAASNLhiDTrnLM-YEILQN-YNLCN---ILIMISHQ 542
Cdd:TIGR00955 155 NTRIGVPGRvkGLSGGERKRLAFASELLTDPPLLFCDEPTSGL--DS--FMaYSVVQVlKGLAQkgkTIICTIHQ 225
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
363-520 |
9.27e-05 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 44.18 E-value: 9.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 363 IFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINnidynlihkesirarigiVSQNIFLFKGTILDNI 442
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD------------------VPDNQFGREASLIDAI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 443 LygqTNKTKEDVVKLIKRYHLTS---HLNRFENgldtiivqdgssVSGGQAQFIAFLRAILTQRDIIILDEAASnlHIDT 519
Cdd:COG2401 107 G---RKGDFKDAVELLNAVGLSDavlWLRRFKE------------LSTGQKFRFRLALLLAERPKLLVIDEFCS--HLDR 169
|
.
gi 1267372771 520 R 520
Cdd:COG2401 170 Q 170
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
363-543 |
1.10e-04 |
|
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: 43.67 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 363 IFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGL--YQPKSGKILINNIDY-NLIHKESIRARIGIVSQNIFLFKGTIL 439
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDItDLPPEERARLGIFLAFQYPPEIPGVKN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 440 DNILygqtnktkedvvklikRYhltshlnrfengldtiiVQDGssVSGGQAQFIAFLRAILTQRDIIILDEAASNLHIDT 519
Cdd:cd03217 95 ADFL----------------RY-----------------VNEG--FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDA 139
|
170 180
....*....|....*....|....*
gi 1267372771 520 RNLMYEILQNY-NLCNILIMISHQQ 543
Cdd:cd03217 140 LRLVAEVINKLrEEGKSVLIITHYQ 164
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
364-540 |
1.48e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 44.66 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 364 FDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDynlIHKESIRARI--GIV-----SQNIFLFkg 436
Cdd:PRK15439 279 FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKE---INALSTAQRLarGLVylpedRQSSGLY-- 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 437 tiLD--------NILYGQ----TNKTKEDVVklIKRYHltSHLNRFENGLDtiivQDGSSVSGGQAQFIAFLRAILTQRD 504
Cdd:PRK15439 354 --LDaplawnvcALTHNRrgfwIKPARENAV--LERYR--RALNIKFNHAE----QAARTLSGGNQQKVLIAKCLEASPQ 423
|
170 180 190
....*....|....*....|....*....|....*..
gi 1267372771 505 IIILDEAASNLHIDTRNLMYEILQNYNLCNI-LIMIS 540
Cdd:PRK15439 424 LLIVDEPTRGVDVSARNDIYQLIRSIAAQNVaVLFIS 460
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
381-541 |
1.84e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 43.55 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 381 GINGSGKSTFIKLLTGLYQPKSGK------ILINNIDYNLIHKESIRARIGIVSQNIFLFKGTILDNILYGQTNKtkedv 454
Cdd:PRK14271 54 GPTGSGKTTFLRTLNRMNDKVSGYrysgdvLLGGRSIFNYRDVLEFRRRVGMLFQRPNPFPMSIMDNVLAGVRAH----- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 455 vKLIKR--YHLTSHLNRFENGL-DTIIVQDGSS---VSGGQAQFIAFLRAILTQRDIIILDEAASNLHIDTRNLMYEILQ 528
Cdd:PRK14271 129 -KLVPRkeFRGVAQARLTEVGLwDAVKDRLSDSpfrLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIR 207
|
170
....*....|...
gi 1267372771 529 NYNLCNILIMISH 541
Cdd:PRK14271 208 SLADRLTVIIVTH 220
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
365-429 |
2.39e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 43.96 E-value: 2.39e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1267372771 365 DHFNVQIEKGDkllIDGI---NGSGKSTFIKLLTGLYQPKSGKILI-------NNIDynlihkesIRARIGIVSQ 429
Cdd:NF033858 283 DHVSFRIRRGE---IFGFlgsNGCGKSTTMKMLTGLLPASEGEAWLfgqpvdaGDIA--------TRRRVGYMSQ 346
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
92-323 |
2.93e-04 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 349998 [Multi-domain] Cd Length: 299 Bit Score: 43.18 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 92 EYLFTRVQQNVVNEIRLSMISNIIDAPLSYINQKEKGYILSR-IAESGNVSALFSPNLLRVFSGIFDFFFALFIMFNLSV 170
Cdd:cd18554 67 QYFAQWIANKILYDIRKDLFDHLQKLSLRYYANNRSGEIISRvINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNP 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 171 KLTGIIVIIIPIYFVISKYSSEMISKSTTNVYESSAVLNAEMYETLNGIEDIKLLNGKNIQTNKIKAKLNDVIKSALKQS 250
Cdd:cd18554 147 KLTFVSLVIFPFYILAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHT 226
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1267372771 251 LHFIFFMQNLIVTNNFVTVIVLLVSGILILQNQLTIGVYTSFSIYMAKLLATTQALGSLDITLKPVCISIKRI 323
Cdd:cd18554 227 RWNAKTFSAVNTITDLAPLLVIGFAAYLVIEGNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDRV 299
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
359-541 |
2.95e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 42.73 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 359 NSDLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGL---YQPK---SGKILINNIDYNLIHKESIRARIGIVSQNIF 432
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiYDSKikvDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 433 LFKG-TILDNILYGQTN---KTKEDVVKLIKRYHLTSHL-NRFENGLDTiivqDGSSVSGGQAQFIAFLRAILTQRDIII 507
Cdd:PRK14246 101 PFPHlSIYDNIAYPLKShgiKEKREIKKIVEECLRKVGLwKEVYDRLNS----PASQLSGGQQQRLTIARALALKPKVLL 176
|
170 180 190
....*....|....*....|....*....|....
gi 1267372771 508 LDEAASNLHIDTRNLMYEILQNYNLCNILIMISH 541
Cdd:PRK14246 177 MDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSH 210
|
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
93-299 |
3.31e-04 |
|
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents the HMT1 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster. HMT1 is closely related to Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria.
Pssm-ID: 350027 [Multi-domain] Cd Length: 290 Bit Score: 42.90 E-value: 3.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 93 YLFTRVQQNVVNEIRLSMISNIIDAPLSYINQKEKGYILSRIAESGNVSALFSPNLLRVFSGIFDFFFA---LFIMFN-- 167
Cdd:cd18583 59 WLWIPVEQYSYRALSTAAFNHVMNLSMDFHDSKKSGEVLKAIEQGSSINDLLEQILFQIVPMIIDLVIAivyLYYLFDpy 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 168 --------------LSVKLTgiiviiipiyFVISKYSSEMISKSttnvYESSAVlnaeMYETLNGIEDIKLLNGKNIQTN 233
Cdd:cd18583 139 mglivavvmvlyvwSTIKLT----------SWRTKLRRDMIDAD----REERSI----LTESLLNWETVKYFNREPYEKE 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1267372771 234 KIKAKLNDVIKSALK--QSLHFIFFMQNLIVTNNFVTVIVLLVSGilILQNQLTIGVYTSFSIYMAKL 299
Cdd:cd18583 201 RYREAVKNYQKAERKylFSLNLLNAVQSLILTLGLLAGCFLAAYQ--VSQGQATVGDFVTLLTYWAQL 266
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
345-396 |
4.23e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.08 E-value: 4.23e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1267372771 345 NSIEFKDVCFKYNENSdlIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTG 396
Cdd:PRK10938 259 PRIVLNNGVVSYNDRP--ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG 308
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
203-309 |
8.79e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 41.71 E-value: 8.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 203 ESSAVLNAEMYETLNGIEDIKLLNGKNiQTNKIKAKLNDVIKSALKQSLHFI-FFMQNLIVTNNFVTVIVLLVSGILILQ 281
Cdd:cd18546 172 ERIAAVNADLQETLAGIRVVQAFRRER-RNAERFAELSDDYRDARLRAQRLVaIYFPGVELLGNLATAAVLLVGAWRVAA 250
|
90 100
....*....|....*....|....*...
gi 1267372771 282 NQLTIGVYTSFSIYMAKLLATTQALGSL 309
Cdd:cd18546 251 GTLTVGVLVAFLLYLRRFFAPIQQLSQV 278
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
97-292 |
9.52e-04 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 41.31 E-value: 9.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 97 RVQQNVVNEIRLSMISNIIDAPLSYINQKEKGYILSRI-AESGNVSALFSPNLLRVFSGIFDFFFALFIMFNLSVKLTGI 175
Cdd:cd18540 68 KIEMGVSYDLRKKAFEHLQTLSFSYFDKTPVGWIMARVtSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALI 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 176 IVIIIPIYFVISKYSSEMISKSTTNVYESSAVLNAEMYETLNGIEDIKLLN--GKNIQ-----TNKIKAKlndVIKSALK 248
Cdd:cd18540 148 VLAVVPVLAVVSIYFQKKILKAYRKVRKINSRITGAFNEGITGAKTTKTLVreEKNLRefkelTEEMRRA---SVRAARL 224
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1267372771 249 QSLhfifFMQNLIVTNNFVTVIVLLVSGILILQNQLTIGVYTSF 292
Cdd:cd18540 225 SAL----FLPIVLFLGSIATALVLWYGGILVLAGAITIGTLVAF 264
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
374-515 |
1.04e-03 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 41.79 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 374 GDKLLIDGINGSGKSTFIKLLTGLYQPKS--GKILINNidyNLIHKESIRaRIGIVSQNIFLF------KGTILDNILYG 445
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANN---RKPTKQILK-RTGFVTQDDILYphltvrETLVFCSLLRL 169
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1267372771 446 QTNKTKEDVVKLIKRYHLTSHLNRFENgldTIIvqdGSS----VSGGQAQFIAFLRAILTQRDIIILDEAASNL 515
Cdd:PLN03211 170 PKSLTKQEKILVAESVISELGLTKCEN---TII---GNSfirgISGGERKRVSIAHEMLINPSLLILDEPTSGL 237
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
265-309 |
1.36e-03 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 40.93 E-value: 1.36e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1267372771 265 NFVTVIVLLVSGILILQNQLTIGVYTSFSIYMAKLLATTQALGSL 309
Cdd:cd18543 233 ELGLAAVLALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWL 277
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
370-408 |
1.41e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 41.33 E-value: 1.41e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1267372771 370 QIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILIN 408
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE 399
|
|
| ABC_6TM_LapB_like |
cd18587 |
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ... |
194-287 |
1.58e-03 |
|
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), such as LapB. LapB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion, LapA is a RTX (repeats in toxin) protein found in Pseudomonas fluorescens and is required for biofilm formation in this organism. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. In this T1SS system, LapB is a cytoplasmic membrane-localized ATPase, LapC is a membrane fusion protein, and LapE is an outer membrane protein.
Pssm-ID: 350031 Cd Length: 293 Bit Score: 40.88 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 194 ISKSTTNVYESSAVLNAEMYETLNGIEDIKLLNGKNI------QTNKIKAKLNDVIKSALKQSLHFIFFMQNLivtnnfV 267
Cdd:cd18587 164 LRRLVEESMRESAQKNALLVESLSGLETIKALGAEGRmqrrweEAVAALARSSLKSRLLSSSATNFAQFVQQL------V 237
|
90 100
....*....|....*....|
gi 1267372771 268 TVIVLLVSGILILQNQLTIG 287
Cdd:cd18587 238 TVAIVIVGVYLISDGELTMG 257
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
483-541 |
1.95e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 40.84 E-value: 1.95e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1267372771 483 SSVSGGQAQFIAFLRAILTQRDIIILDEAASNLhidTRNLMYEIL-------QNYNLCniLIMISH 541
Cdd:PRK15134 424 AEFSGGQRQRIAIARALILKPSLIILDEPTSSL---DKTVQAQILallkslqQKHQLA--YLFISH 484
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
345-515 |
1.96e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 40.28 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 345 NSIEFKDVCFKYNENSdlIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQ--PK---SGKILINNIDYNLIHKES 419
Cdd:PRK14247 2 NKIEIRDLKVSFGQVE--VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvSGEVYLDGQDIFKMDVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 420 IRARIGIVSQ------NIFLFKGTILD---NILYGQTNKTKEDVVKLIKRYHLTSHLnrfENGLDTiivqDGSSVSGGQA 490
Cdd:PRK14247 80 LRRRVQMVFQipnpipNLSIFENVALGlklNRLVKSKKELQERVRWALEKAQLWDEV---KDRLDA----PAGKLSGGQQ 152
|
170 180
....*....|....*....|....*
gi 1267372771 491 QFIAFLRAILTQRDIIILDEAASNL 515
Cdd:PRK14247 153 QRLCIARALAFQPEVLLADEPTANL 177
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
373-443 |
2.05e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 38.89 E-value: 2.05e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1267372771 373 KGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKILINNIDYNLIHKESIRARIGIVSQNIFLFKGTILDNIL 443
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLAL 71
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
356-405 |
2.18e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 40.92 E-value: 2.18e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1267372771 356 YNENsdLIFDHFNVQIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKI 405
Cdd:PRK10636 322 YGDR--IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI 369
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
86-300 |
2.36e-03 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 40.24 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 86 LISIGYEYLFTRVQQNVVNEIRLSMISNIIDAPLSYINQKEKGYILSRIaeSGNVSAL------FSPNLLRVFSGifdFF 159
Cdd:cd18565 69 LFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVL--NNDVNQLerflddGANSIIRVVVT---VL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 160 FALFIMFNLSVKLTGIIVIIIPIYFVISKYSSEMISKSTTNVYESSAVLNAEMYETLNGIEDIKLLNGKNIQTNKIK--- 236
Cdd:cd18565 144 GIGAILFYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERERVAdas 223
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 237 AKLNDVIKSALKQSLHFIFFMQNLIvtnNFVTVIVLLVSGILILQN------QLTIGVYTSFSIYMAKLL 300
Cdd:cd18565 224 EEYRDANWRAIRLRAAFFPVIRLVA---GAGFVATFVVGGYWVLDGpplftgTLTVGTLVTFLFYTQRLL 290
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
208-309 |
2.48e-03 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 40.07 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267372771 208 LNAEMYETLNGIEDIKLLNGKNIQTNKIKAKLNDVIKSALKQSLHFIFFMQNLIVTNNFVTVIVLLVSGILILQNQLTIG 287
Cdd:cd18548 177 LNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAILWFGGHLINAGSLQVG 256
|
90 100
....*....|....*....|..
gi 1267372771 288 VYTSFSIYMakllatTQALGSL 309
Cdd:cd18548 257 DLVAFINYL------MQILMSL 272
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
370-405 |
3.80e-03 |
|
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: 40.15 E-value: 3.80e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1267372771 370 QIEKGDKLLIDGINGSGKSTFIKLLTGLYQPKSGKI 405
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV 397
|
|
| |
