|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
26-601 |
2.52e-122 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 373.35 E-value: 2.52e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 26 RALSVGLIVATLVAGLLPALAAWLGQRIVDAVVSAMQLHAstgeaplwpVLRYVLLEAGVLALLAGAQRGLSVQQALLRV 105
Cdd:COG1132 20 RGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSA---------LLLLLLLLLGLALLRALLSYLQRYLLARLAQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 106 LLGQKVNTLILEKAQTLSLSQFEDSEFYDKLVRVRREASTRPLALVTKSLGLLQNLISLISFAVLLVHFSPWaLLILVLG 185
Cdd:COG1132 91 RVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWR-LALIVLL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 186 ALPVFFAEAHFSGDAFRLFTRRApetrrQNYIETLLSH--EGY--IKEVKLFGFAPLLLKRYRDTFERLYAEDRRLTVRR 261
Cdd:COG1132 170 VLPLLLLVLRLFGRRLRKLFRRV-----QEALAELNGRlqESLsgIRVVKAFGREERELERFREANEELRRANLRAARLS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 262 DGWGFLLGLLGTASFYLAYAWVVVDAVHGRITLGQMTMYLVLFKQGQAAVSSSLSAISGLYEDGLYLADLYIYLGQPVMP 341
Cdd:COG1132 245 ALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEI 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 342 SAGSLTQGALPGDG-MRFENVSFTYPGtSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSD 420
Cdd:COG1132 325 PDPPGAVPLPPVRGeIEFENVSFSYPG-DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVD 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 421 LQDWDEDALRSRIGVIFQDFIRYQFLVGENLGVGDTHAfhDETRWREAAAQGMAAQFIEQLDKGYATQLGRwfaGGQELS 500
Cdd:COG1132 404 IRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDA--TDEEVEEAAKAAQAHEFIEALPDGYDTVVGE---RGVNLS 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 501 GGQWQKIALSRAYMRrDADILILDEPTAALDAGAEAAVFEHFREYAKGRMTLLISHRFSSVRNAEHIVVLEHGRVLERGD 580
Cdd:COG1132 479 GGQRQRIAIARALLK-DPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGT 557
|
570 580
....*....|....*....|.
gi 488616976 581 HDSLIAAAGRYAALFDLQAQG 601
Cdd:COG1132 558 HEELLARGGLYARLYRLQFGE 578
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
32-599 |
1.29e-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: 281.34 E-value: 1.29e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 32 LIVATLVAGLLpALAAWLG-QRIVDAVVSAMQLHastgeaPLWPVlryvlleAGVLALLAGAQRGLSVQQALLRVLLGQK 110
Cdd:COG2274 161 VLLASLLINLL-ALATPLFtQVVIDRVLPNQDLS------TLWVL-------AIGLLLALLFEGLLRLLRSYLLLRLGQR 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 111 VNTLI----LEKAQTLSLSQFED-------SEFYDkLVRVRReastrplALVTKSLGLLQNLISLISFAVLLVHFSPWaL 179
Cdd:COG2274 227 IDLRLssrfFRHLLRLPLSFFESrsvgdlaSRFRD-VESIRE-------FLTGSLLTALLDLLFVLIFLIVLFFYSPP-L 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 180 LILVLGALPVFFAeahfsgdAFRLFTRRAPET---------RRQNYIETLLSHegyIKEVKLFGFAPLLLKRYRDTFERL 250
Cdd:COG2274 298 ALVVLLLIPLYVL-------LGLLFQPRLRRLsreeseasaKRQSLLVETLRG---IETIKALGAESRFRRRWENLLAKY 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 251 YAEDRRLTVRRDGWGFLLGLLGTASFYLAYAWVVVDAVHGRITLGQMTMYLVLFKQGQAAVSSSLSAISGLYEDGLYLAD 330
Cdd:COG2274 368 LNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALER 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 331 LYIYLGQPV--MPSAGSLTQGALPGDgMRFENVSFTYPGTSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQ 408
Cdd:COG2274 448 LDDILDLPPerEEGRSKLSLPRLKGD-IELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYE 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 409 PDQGRILLDGSDLQDWDEDALRSRIGVIFQDfiryQFL----VGENLGVGDTHAfhDETRWREAAAQGMAAQFIEQLDKG 484
Cdd:COG2274 527 PTSGRILIDGIDLRQIDPASLRRQIGVVLQD----VFLfsgtIRENITLGDPDA--TDEEIIEAARLAGLHDFIEALPMG 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 485 YATQLGrwfAGGQELSGGQWQKIALSRAYMrRDADILILDEPTAALDAGAEAAVFEHFREYAKGRMTLLISHRFSSVRNA 564
Cdd:COG2274 601 YDTVVG---EGGSNLSGGQRQRLAIARALL-RNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLA 676
|
570 580 590
....*....|....*....|....*....|....*
gi 488616976 565 EHIVVLEHGRVLERGDHDSLIAAAGRYAALFDLQA 599
Cdd:COG2274 677 DRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQL 711
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
159-598 |
2.10e-70 |
|
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: 237.69 E-value: 2.10e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 159 QNLISLISFAVLLvhFSPWALLILVLGALPVffaeahfSGDAFRLFTRRAPETRR--QNYIETLL-----SHEGYiKEVK 231
Cdd:TIGR02203 138 ETLTVIGLFIVLL--YYSWQLTLIVVVMLPV-------LSILMRRVSKRLRRISKeiQNSMGQVTtvaeeTLQGY-RVVK 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 232 LFGFAPLLLKRyrdtFERLYAEDRRLTVRRDGWGFLLGLLGTASFYLAYAWVVVDAVH----GRITLGQMTMYLVLFKQG 307
Cdd:TIGR02203 208 LFGGQAYETRR----FDAVSNRNRRLAMKMTSAGSISSPITQLIASLALAVVLFIALFqaqaGSLTAGDFTAFITAMIAL 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 308 QAAVSSsLSAISGLYEDGLYLAD-LYIYLGQPVMPSAGSLTQGALPGDgMRFENVSFTYPGTSRAALENIDLHLAPGRSV 386
Cdd:TIGR02203 284 IRPLKS-LTNVNAPMQRGLAAAEsLFTLLDSPPEKDTGTRAIERARGD-VEFRNVTFRYPGRDRPALDSISLVIEPGETV 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 387 ALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDALRSRIGVIFQDFIRYQFLVGENLGVGDTHAFhDETRWR 466
Cdd:TIGR02203 362 ALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEQA-DRAEIE 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 467 EAAAQGMAAQFIEQLDKGYATQLGrwfAGGQELSGGQWQKIALSRAyMRRDADILILDEPTAALDAGAEAAVFEHFREYA 546
Cdd:TIGR02203 441 RALAAAYAQDFVDKLPLGLDTPIG---ENGVLLSGGQRQRLAIARA-LLKDAPILILDEATSALDNESERLVQAALERLM 516
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 488616976 547 KGRMTLLISHRFSSVRNAEHIVVLEHGRVLERGDHDSLIAAAGRYAALFDLQ 598
Cdd:TIGR02203 517 QGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLYAQLHNMQ 568
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
357-595 |
1.33e-69 |
|
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: 224.80 E-value: 1.33e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 357 RFENVSFTYPGTSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDALRSRIGVI 436
Cdd:cd03251 2 EFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 437 FQDFIRYQFLVGENLGVGDTHAFHDETrwREAAAQGMAAQFIEQLDKGYATQLGRwfaGGQELSGGQWQKIALSRAYMrR 516
Cdd:cd03251 82 SQDVFLFNDTVAENIAYGRPGATREEV--EEAARAANAHEFIMELPEGYDTVIGE---RGVKLSGGQRQRIAIARALL-K 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488616976 517 DADILILDEPTAALDAGAEAAVFEHFREYAKGRMTLLISHRFSSVRNAEHIVVLEHGRVLERGDHDSLIAAAGRYAALF 595
Cdd:cd03251 156 DPPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
357-589 |
5.06e-64 |
|
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: 210.16 E-value: 5.06e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 357 RFENVSFTYPGTsRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDALRSRIGVI 436
Cdd:cd03254 4 EFENVNFSYDEK-KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 437 FQDFIRYQFLVGENLGVGDTHAfhDETRWREAAAQGMAAQFIEQLDKGYATQLGRwfaGGQELSGGQWQKIALSRAyMRR 516
Cdd:cd03254 83 LQDTFLFSGTIMENIRLGRPNA--TDEEVIEAAKEAGAHDFIMKLPNGYDTVLGE---NGGNLSQGERQLLAIARA-MLR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488616976 517 DADILILDEPTAALDAGAEAAVFEHFREYAKGRMTLLISHRFSSVRNAEHIVVLEHGRVLERGDHDSLIAAAG 589
Cdd:cd03254 157 DPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
357-598 |
1.08e-63 |
|
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: 209.32 E-value: 1.08e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 357 RFENVSFTYPgtSRA---ALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDALRSRI 433
Cdd:cd03249 2 EFKNVSFRYP--SRPdvpILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 434 GVIFQDFIRYQFLVGENLGVGDTHAfHDETRwREAAAQGMAAQFIEQLDKGYATQLGrwfAGGQELSGGQWQKIALSRAY 513
Cdd:cd03249 80 GLVSQEPVLFDGTIAENIRYGKPDA-TDEEV-EEAAKKANIHDFIMSLPDGYDTLVG---ERGSQLSGGQKQRIAIARAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 514 MRrDADILILDEPTAALDAGAEAAVFEHFREYAKGRMTLLISHRFSSVRNAEHIVVLEHGRVLERGDHDSLIAAAGRYAA 593
Cdd:cd03249 155 LR-NPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAK 233
|
....*
gi 488616976 594 LFDLQ 598
Cdd:cd03249 234 LVKAQ 238
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
356-574 |
4.26e-62 |
|
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: 202.61 E-value: 4.26e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 356 MRFENVSFTYPGTSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDALRSRIGV 435
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 436 IFQDFIRYQFLVGENLgvgdthafhdetrwreaaaqgmaaqfieqldkgyatqlgrwfaggqeLSGGQWQKIALSRAYMr 515
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------------LSGGQRQRIAIARALL- 112
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488616976 516 RDADILILDEPTAALDAGAEAAVFEHFREYAKGRMTLLISHRFSSVRNAEHIVVLEHGR 574
Cdd:cd03228 113 RDPPILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
357-598 |
5.11e-61 |
|
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: 202.46 E-value: 5.11e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 357 RFENVSFTYPgTSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDALRSRIGVI 436
Cdd:cd03253 2 EFENVTFAYD-PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 437 FQDFIRYQFLVGENLGVGDTHAFHDETRwrEAAAQGMAAQFIEQLDKGYATQLG-RwfagGQELSGGQWQKIALSRAYMR 515
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGRPDATDEEVI--EAAKAAQIHDKIMRFPDGYDTIVGeR----GLKLSGGEKQRVAIARAILK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 516 rDADILILDEPTAALDAGAEAAVFEHFREYAKGRMTLLISHRFSSVRNAEHIVVLEHGRVLERGDHDSLIAAAGRYAALF 595
Cdd:cd03253 155 -NPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMW 233
|
...
gi 488616976 596 DLQ 598
Cdd:cd03253 234 KAQ 236
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
161-597 |
6.78e-60 |
|
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: 209.24 E-value: 6.78e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 161 LISLISFAVLLVHFSPWALLILVLGALPVFFAEAHFSGDAFRLFTRRApETRRQNYIETLLSHEGYIKEVKLFGFAPLLL 240
Cdd:COG4987 140 LLVILAAVAFLAFFSPALALVLALGLLLAGLLLPLLAARLGRRAGRRL-AAARAALRARLTDLLQGAAELAAYGALDRAL 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 241 KRYRDTFERLYAEDRRLTvRRDGWGFLLGLLGTASFYLAYAWVVVDAVHGRITLGQMTMYLVLfkqgqaAVSSSLSAISG 320
Cdd:COG4987 219 ARLDAAEARLAAAQRRLA-RLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLVL------AALALFEALAP 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 321 LyedglylADLYIYLGQpVMPSAGSL--------------TQGALPGDG-MRFENVSFTYPGTSRAALENIDLHLAPGRS 385
Cdd:COG4987 292 L-------PAAAQHLGR-VRAAARRLnelldappavtepaEPAPAPGGPsLELEDVSFRYPGAGRPVLDGLSLTLPPGER 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 386 VALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDALRSRIGVIFQDFirYQFL--VGENLGVGDTHAfhDET 463
Cdd:COG4987 364 VAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRP--HLFDttLRENLRLARPDA--TDE 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 464 RWREAAAQGMAAQFIEQLDKGYATQLGrwfAGGQELSGGQWQKIALSRAYMRrDADILILDEPTAALDAGAEAAVFEHFR 543
Cdd:COG4987 440 ELWAALERVGLGDWLAALPDGLDTWLG---EGGRRLSGGERRRLALARALLR-DAPILLLDEPTEGLDAATEQALLADLL 515
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 488616976 544 EYAKGRMTLLISHRFSSVRNAEHIVVLEHGRVLERGDHDSLIAAAGRYAALFDL 597
Cdd:COG4987 516 EALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQLYQR 569
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
25-589 |
1.68e-59 |
|
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: 208.07 E-value: 1.68e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 25 SRALSVGLIVATLVAGLLPALAAWLGQRIVDAVVsamqlhasTGEAPLWPVLRYVLLEAGVLALLAGAQRGLSVQQALLR 104
Cdd:COG4988 15 ARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLI--------IGGAPLSALLPLLGLLLAVLLLRALLAWLRERAAFRAA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 105 VLLGQKVNTLILEKAQTLSLsqfedsefydklVRVRREASTRPLALVTKSLGLLQN----------LISLISFAVLLVHF 174
Cdd:COG4988 87 ARVKRRLRRRLLEKLLALGP------------AWLRGKSTGELATLLTEGVEALDGyfarylpqlfLAALVPLLILVAVF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 175 --SPWALLILVLGA--LPVFFAeahfsgdAFRLFTRRAPETRRQNY-------------IETLlshegyikevKLFGFAp 237
Cdd:COG4988 155 plDWLSGLILLVTAplIPLFMI-------LVGKGAAKASRRQWRALarlsghfldrlrgLTTL----------KLFGRA- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 238 lllKRYRDTFERLyAED-RRLTVR--RdgwgfllgLLGTASF------YLAYAWVVVDA----VHGRITLGQMTMYLVL- 303
Cdd:COG4988 217 ---KAEAERIAEA-SEDfRKRTMKvlR--------VAFLSSAvleffaSLSIALVAVYIgfrlLGGSLTLFAALFVLLLa 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 304 -------------FKQGQAAVSSSlSAISGLYEdglyladlyiylGQPVMPSAGSLTQGALPGDGMRFENVSFTYPGtSR 370
Cdd:COG4988 285 pefflplrdlgsfYHARANGIAAA-EKIFALLD------------APEPAAPAGTAPLPAAGPPSIELEDVSFSYPG-GR 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 371 AALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDALRSRIG------VIFQDFIRyq 444
Cdd:COG4988 351 PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAwvpqnpYLFAGTIR-- 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 445 flvgENLGVGDTHAfhDETRWREAAAQGMAAQFIEQLDKGYATQLGrwfAGGQELSGGQWQKIALSRAYMRrDADILILD 524
Cdd:COG4988 429 ----ENLRLGRPDA--SDEELEAALEAAGLDEFVAALPDGLDTPLG---EGGRGLSGGQAQRLALARALLR-DAPLLLLD 498
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488616976 525 EPTAALDAGAEAAVFEHFREYAKGRMTLLISHRFSSVRNAEHIVVLEHGRVLERGDHDSLIAAAG 589
Cdd:COG4988 499 EPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
358-598 |
3.39e-59 |
|
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: 197.71 E-value: 3.39e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 358 FENVSFTYPGTSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDALRSRIGVIF 437
Cdd:cd03252 3 FEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 438 QDFIRYQFLVGENLGVGDTHAfhDETRWREAAAQGMAAQFIEQLDKGYATQLGRWFAGgqeLSGGQWQKIALSRAYMrRD 517
Cdd:cd03252 83 QENVLFNRSIRDNIALADPGM--SMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAG---LSGGQRQRIAIARALI-HN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 518 ADILILDEPTAALDAGAEAAVFEHFREYAKGRMTLLISHRFSSVRNAEHIVVLEHGRVLERGDHDSLIAAAGRYAALFDL 597
Cdd:cd03252 157 PRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQL 236
|
.
gi 488616976 598 Q 598
Cdd:cd03252 237 Q 237
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
357-601 |
3.95e-58 |
|
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: 205.05 E-value: 3.95e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 357 RFENVSFTYpGTSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDALRSRIG-- 434
Cdd:COG5265 359 RFENVSFGY-DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGiv 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 435 ----VIFQDFIRYqflvgeNLGVGDTHAFHDETrwrEAAAQgmAAQ---FIEQLDKGYATQLG-RwfagGQELSGGQWQK 506
Cdd:COG5265 438 pqdtVLFNDTIAY------NIAYGRPDASEEEV---EAAAR--AAQihdFIESLPDGYDTRVGeR----GLKLSGGEKQR 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 507 IALSRAYMRrDADILILDEPTAALDAGAEAAVFEHFREYAKGRMTLLISHRFSSVRNAEHIVVLEHGRVLERGDHDSLIA 586
Cdd:COG5265 503 VAIARTLLK-NPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLA 581
|
250
....*....|....*
gi 488616976 587 AAGRYAALFDLQAQG 601
Cdd:COG5265 582 QGGLYAQMWARQQEE 596
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
357-601 |
1.92e-55 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 197.49 E-value: 1.92e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 357 RFENVSFTYPGtSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDALRSRIGVI 436
Cdd:PRK13657 336 EFDDVSFSYDN-SRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVV 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 437 FQDFIRYQFLVGENLGVGDTHAFHDETRwrEAAAQGMAAQFIEQLDKGYATQLGRwfaGGQELSGGQWQKIALSRAYMRr 516
Cdd:PRK13657 415 FQDAGLFNRSIEDNIRVGRPDATDEEMR--AAAERAQAHDFIERKPDGYDTVVGE---RGRQLSGGERQRLAIARALLK- 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 517 DADILILDEPTAALDAGAEAAVFEHFREYAKGRMTLLISHRFSSVRNAEHIVVLEHGRVLERGDHDSLIAAAGRYAALfd 596
Cdd:PRK13657 489 DPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAAL-- 566
|
....*
gi 488616976 597 LQAQG 601
Cdd:PRK13657 567 LRAQG 571
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
358-598 |
2.20e-55 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 197.16 E-value: 2.20e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 358 FENVSFTYPGTSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDALRSRIGVIF 437
Cdd:PRK11176 344 FRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVS 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 438 QDFIRYQFLVGENLGVGDTHAFHDEtRWREAAAQGMAAQFIEQLDKGYATQLGRwfaGGQELSGGQWQKIALSRAYMrRD 517
Cdd:PRK11176 424 QNVHLFNDTIANNIAYARTEQYSRE-QIEEAARMAYAMDFINKMDNGLDTVIGE---NGVLLSGGQRQRIAIARALL-RD 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 518 ADILILDEPTAALDAGAEAAVFEHFREYAKGRMTLLISHRFSSVRNAEHIVVLEHGRVLERGDHDSLIAAAGRYAALFDL 597
Cdd:PRK11176 499 SPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQLHKM 578
|
.
gi 488616976 598 Q 598
Cdd:PRK11176 579 Q 579
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
358-575 |
1.20e-49 |
|
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: 171.62 E-value: 1.20e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 358 FENVSFTYPGTSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDALRSRIGVIF 437
Cdd:cd03245 5 FRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 438 QDFIRYQFLVGENLGVGDTHAfhDETRWREAAAQGMAAQFIEQLDKGYATQLGRwfaGGQELSGGQWQKIALSRAYMrRD 517
Cdd:cd03245 85 QDVTLFYGTLRDNITLGAPLA--DDERILRAAELAGVTDFVNKHPNGLDLQIGE---RGRGLSGGQRQAVALARALL-ND 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488616976 518 ADILILDEPTAALDAGAEAAVFEHFREYAKGRMTLLISHRFSSVRNAEHIVVLEHGRV 575
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
356-594 |
1.41e-47 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 175.40 E-value: 1.41e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 356 MRFENVSFTYPGTSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDALRSRIGV 435
Cdd:PRK11160 339 LTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 436 ------IFQDFIRyqflvgENLGVGDTHAfHDEtRWREAAAQGMAAQFIEQlDKGYATQLGRwfaGGQELSGGQWQKIAL 509
Cdd:PRK11160 419 vsqrvhLFSATLR------DNLLLAAPNA-SDE-ALIEVLQQVGLEKLLED-DKGLNAWLGE---GGRQLSGGEQRRLGI 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 510 SRAYMrRDADILILDEPTAALDAGAEAAVFEHFREYAKGRMTLLISHRFSSVRNAEHIVVLEHGRVLERGDHDSLIAAAG 589
Cdd:PRK11160 487 ARALL-HDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQG 565
|
....*
gi 488616976 590 RYAAL 594
Cdd:PRK11160 566 RYYQL 570
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
128-594 |
8.70e-47 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 175.30 E-value: 8.70e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 128 EDSEFYDK------LVRVRREASTRPLALVTKSLGLLQNLISLISFAVLLVHFSpWALLILVLGALPVFFAEAHFSGDAF 201
Cdd:TIGR00958 247 QDLGFFDEnktgelTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLS-PRLTMVTLINLPLVFLAEKVFGKRY 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 202 RLFTRRAPET---RRQNYIETLlsheGYIKEVKLFGFAPLLLKRYRDTFERLyaedRRLTVRRDGWgfllgllgtasfYL 278
Cdd:TIGR00958 326 QLLSEELQEAvakANQVAEEAL----SGMRTVRSFAAEEGEASRFKEALEET----LQLNKRKALA------------YA 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 279 AYAWVvvdavhgRITLGQMTMYLVLFKQGQAAVSSSLSaiSG------LYED--GLYLADL-YIYLG------------- 336
Cdd:TIGR00958 386 GYLWT-------TSVLGMLIQVLVLYYGGQLVLTGKVS--SGnlvsflLYQEqlGEAVRVLsYVYSGmmqavgasekvfe 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 337 ----QPVMPSAGSLTQGALPGDgMRFENVSFTYPG-TSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQ 411
Cdd:TIGR00958 457 yldrKPNIPLTGTLAPLNLEGL-IEFQDVSFSYPNrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTG 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 412 GRILLDGSDLQDWDEDALRSRIGVIFQDFIRYQFLVGENLGVGDTHAFHDETrwREAAAQGMAAQFIEQLDKGYATQLGR 491
Cdd:TIGR00958 536 GQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEI--MAAAKAANAHDFIMEFPNGYDTEVGE 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 492 wfaGGQELSGGQWQKIALSRAYMRRDAdILILDEPTAALDAGAEAAVFEhFREyAKGRMTLLISHRFSSVRNAEHIVVLE 571
Cdd:TIGR00958 614 ---KGSQLSGGQKQRIAIARALVRKPR-VLILDEATSALDAECEQLLQE-SRS-RASRTVLLIAHRLSTVERADQILVLK 687
|
490 500
....*....|....*....|...
gi 488616976 572 HGRVLERGDHDSLIAAAGRYAAL 594
Cdd:TIGR00958 688 KGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
344-575 |
4.50e-45 |
|
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: 159.56 E-value: 4.50e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 344 GSLTQGALPGDgMRFENVSFTYPGTS-RAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQ 422
Cdd:cd03248 1 GSLAPDHLKGI-VKFQNVTFAYPTRPdTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 423 DWDEDALRSRIGVIFQDFIRYQFLVGENLGVGDTHAFHDETrwREAAAQGMAAQFIEQLDKGYATQLGRwfAGGQeLSGG 502
Cdd:cd03248 80 QYEHKYLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECV--KEAAQKAHAHSFISELASGYDTEVGE--KGSQ-LSGG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488616976 503 QWQKIALSRAYMrRDADILILDEPTAALDAGAEAAVFEHFREYAKGRMTLLISHRFSSVRNAEHIVVLEHGRV 575
Cdd:cd03248 155 QKQRVAIARALI-RNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
328-570 |
1.01e-43 |
|
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: 164.00 E-value: 1.01e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 328 LADLYIYLGQPVMPSAGSLTQGALPGDGMRFENVSFTYPGTsRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLY 407
Cdd:TIGR02857 294 AEALFAVLDAAPRPLAGKAPVTAAPASSLEFSGVSVAYPGR-RPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFV 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 408 QPDQGRILLDGSDLQDWDEDALRSRIGVIFQDFIRYQFLVGENLGVGDTHAfhDETRWREAAAQGMAAQFIEQLDKGYAT 487
Cdd:TIGR02857 373 DPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDA--SDAEIREALERAGLDEFVAALPQGLDT 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 488 QLGRwfaGGQELSGGQWQKIALSRAYMrRDADILILDEPTAALDAGAEAAVFEHFREYAKGRMTLLISHRFSSVRNAEHI 567
Cdd:TIGR02857 451 PIGE---GGAGLSGGQAQRLALARAFL-RDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRI 526
|
...
gi 488616976 568 VVL 570
Cdd:TIGR02857 527 VVL 529
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
357-574 |
7.44e-39 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 141.84 E-value: 7.44e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 357 RFENVSFTYPGTSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDALRSRIGVI 436
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 437 FQDFiRYQFL---VGE-------NLGVGDTHAfhdETRWREAAAQ-GMAAQFIEQLdkgyatqlgrwfaggQELSGGQWQ 505
Cdd:cd03225 81 FQNP-DDQFFgptVEEevafgleNLGLPEEEI---EERVEEALELvGLEGLRDRSP---------------FTLSGGQKQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488616976 506 KIALSRAYMrRDADILILDEPTAALDAGAEAAVFEHFREYAKGRMTLLI-SHRFSSVRN-AEHIVVLEHGR 574
Cdd:cd03225 142 RVAIAGVLA-MDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIvTHDLDLLLElADRVIVLEDGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
357-586 |
1.70e-38 |
|
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: 141.70 E-value: 1.70e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 357 RFENVSFTYPGtSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDALRSRIGVI 436
Cdd:COG1122 2 ELENLSFSYPG-GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 437 FQDfIRYQFL---VGE-------NLGVGDTHAfhdETRWREAAAQ-GMAaqfiEQLDKgyATqlgrwfaggQELSGGQWQ 505
Cdd:COG1122 81 FQN-PDDQLFaptVEEdvafgpeNLGLPREEI---RERVEEALELvGLE----HLADR--PP---------HELSGGQKQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 506 KIALSRAY-MRrdADILILDEPTAALDAGAEAAVFEHFREYAKGRMT-LLISHRFSSV-RNAEHIVVLEHGRVLERGDHD 582
Cdd:COG1122 142 RVAIAGVLaME--PEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTvIIVTHDLDLVaELADRVIVLDDGRIVADGTPR 219
|
....
gi 488616976 583 SLIA 586
Cdd:COG1122 220 EVFS 223
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
373-527 |
3.47e-38 |
|
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: 138.16 E-value: 3.47e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 373 LENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDALRSRIGVIFQD-FIRYQFLVGENL 451
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDpQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488616976 452 GVGDTHAFHDEtrwREAAAQgmAAQFIEQLD-KGYATQlgRWFAGGQELSGGQWQKIALSRAYMRRdADILILDEPT 527
Cdd:pfam00005 81 RLGLLLKGLSK---REKDAR--AEEALEKLGlGDLADR--PVGERPGTLSGGQRQRVAIARALLTK-PKLLLLDEPT 149
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
281-598 |
2.43e-37 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 146.40 E-value: 2.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 281 AWVVVdavHGRITLGQMT---MYLVLF--------------KQGQAAVS--SSLSAISGLYEDGlyladlyiylGQPVMP 341
Cdd:PRK10789 243 SWMVV---NGSLTLGQLTsfvMYLGLMiwpmlalawmfnivERGSAAYSriRAMLAEAPVVKDG----------SEPVPE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 342 SAGSLTqgalpgdgmrFENVSFTYPGTSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDL 421
Cdd:PRK10789 310 GRGELD----------VNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPL 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 422 QDWDEDALRSRIGVIFQDFIRYQFLVGENLGVGDTHAFHDETrwREAAAQGMAAQFIEQLDKGYATQLGRwfaGGQELSG 501
Cdd:PRK10789 380 TKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEI--EHVARLASVHDDILRLPQGYDTEVGE---RGVMLSG 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 502 GQWQKIALSRAYMrRDADILILDEPTAALDAGAEAAVFEHFREYAKGRmTLLIS-HRFSSVRNAEHIVVLEHGRVLERGD 580
Cdd:PRK10789 455 GQKQRISIARALL-LNAEILILDDALSAVDGRTEHQILHNLRQWGEGR-TVIISaHRLSALTEASEILVMQHGHIAQRGN 532
|
330
....*....|....*...
gi 488616976 581 HDSLIAAAGRYAALFDLQ 598
Cdd:PRK10789 533 HDQLAQQSGWYRDMYRYQ 550
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
357-588 |
7.52e-37 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 137.12 E-value: 7.52e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 357 RFENVSFTYPGTsrAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDwDEDALRSRIGVI 436
Cdd:COG1131 2 EVRGLTKRYGDK--TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 437 FQDFIRYQFL-VGENLG-VGDTHAFhdetrwREAAAQGMAAQFIEQLD-KGYATQLGRwfaggqELSGGQWQKIALSRAY 513
Cdd:COG1131 79 PQEPALYPDLtVRENLRfFARLYGL------PRKEARERIDELLELFGlTDAADRKVG------TLSGGMKQRLGLALAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488616976 514 MrRDADILILDEPTAALDAGAEAAVFEHFREYAKGRMTLLIS-HRFSSV-RNAEHIVVLEHGRVLERGDHDSLIAAA 588
Cdd:COG1131 147 L-HDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAeRLCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
357-587 |
6.47e-36 |
|
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: 141.19 E-value: 6.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 357 RFENVSFTYPGTSR---AALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDED---ALR 430
Cdd:COG1123 262 EVRNLSKRYPVRGKggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRslrELR 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 431 SRIGVIFQDfiRYQFL-----VGENLGVG-DTHAFHDETRWREAAAQgMAAQFieQLDKGYATQLGRwfaggqELSGGQW 504
Cdd:COG1123 342 RRVQMVFQD--PYSSLnprmtVGDIIAEPlRLHGLLSRAERRERVAE-LLERV--GLPPDLADRYPH------ELSGGQR 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 505 QKIALSRAYMrRDADILILDEPTAALDAGAEAAVFEHFREYAK--GRMTLLISHRFSSVRN-AEHIVVLEHGRVLERGDH 581
Cdd:COG1123 411 QRVAIARALA-LEPKLLILDEPTSALDVSVQAQILNLLRDLQRelGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPT 489
|
....*.
gi 488616976 582 DSLIAA 587
Cdd:COG1123 490 EEVFAN 495
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
356-579 |
1.73e-35 |
|
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: 131.67 E-value: 1.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 356 MRFENVSFTYPGTSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWdEDALRSRIGV 435
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL-EKALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 436 IFQDFIRYQFLVGENLgvgdthafhdetrwreaaaqgmaaqfieqldkgyatqlgrwfagGQELSGGQWQKIALSRAYMr 515
Cdd:cd03247 80 LNQRPYLFDTTLRNNL--------------------------------------------GRRFSGGERQRLALARILL- 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488616976 516 RDADILILDEPTAALDAGAEAAVFEHFREYAKGRMTLLISHRFSSVRNAEHIVVLEHGRVLERG 579
Cdd:cd03247 115 QDAPIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
357-603 |
9.05e-35 |
|
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: 138.11 E-value: 9.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 357 RFENVSFTYPGTSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPD---QGRILLDGSDLQDWDEDALRSRI 433
Cdd:COG1123 6 EVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRRI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 434 GVIFQDFirYQFLVGenLGVGDTHAFHDETRWREAAAqgMAAQFIEQLDKGYATQLGRWFAggQELSGGQWQKIALSRAy 513
Cdd:COG1123 86 GMVFQDP--MTQLNP--VTVGDQIAEALENLGLSRAE--ARARVLELLEAVGLERRLDRYP--HQLSGGQRQRVAIAMA- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 514 MRRDADILILDEPTAALDAGAEAAVFEHFREYAK--GRMTLLISHRFSSV-RNAEHIVVLEHGRVLERGDHDSLIAAAGR 590
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILAAPQA 236
|
250
....*....|...
gi 488616976 591 YAALFDLQAQGYR 603
Cdd:COG1123 237 LAAVPRLGAARGR 249
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
356-579 |
2.41e-34 |
|
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: 129.92 E-value: 2.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 356 MRFENVSFTYPGTSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDALRSRIGV 435
Cdd:cd03244 3 IEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 436 IFQDFIRYQFLVGENLGVGDTHAfhDETRWrEAAAQGMAAQFIEQLDKGYATQLGrwfAGGQELSGGQWQKIALSRAYMR 515
Cdd:cd03244 83 IPQDPVLFSGTIRSNLDPFGEYS--DEELW-QALERVGLKEFVESLPGGLDTVVE---EGGENLSVGQRQLLCLARALLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488616976 516 RdADILILDEPTAALDAGAEAAVFEHFREYAKGRMTLLISHRFSSVRNAEHIVVLEHGRVLERG 579
Cdd:cd03244 157 K-SKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFD 219
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
359-575 |
4.13e-34 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 127.51 E-value: 4.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 359 ENVSFTYPgtSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDwDEDALRSRIGVIFQ 438
Cdd:cd03230 4 RNLSKRYG--KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 439 DFIRYQFL-VGENLgvgdthafhdetrwreaaaqgmaaqfieqldkgyatqlgrwfaggqELSGGQWQKIALSRAYMrRD 517
Cdd:cd03230 81 EPSLYENLtVRENL----------------------------------------------KLSGGMKQRLALAQALL-HD 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 518 ADILILDEPTAALDAGAEAAVFEHFREYAKGRMT-LLISHRFSSVRN-AEHIVVLEHGRV 575
Cdd:cd03230 114 PELLILDEPTSGLDPESRREFWELLRELKKEGKTiLLSSHILEEAERlCDRVAILNNGRI 173
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
344-595 |
1.37e-33 |
|
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: 136.41 E-value: 1.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 344 GSLTQGALPGDGMRFENVSFTYpGTSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQD 423
Cdd:TIGR01193 462 KKRTELNNLNGDIVINDVSYSY-GYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKD 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 424 WDEDALRSRIGVIFQDFIRYQFLVGENLGVGDTHAFHDETRWREAAAQGMAAQfIEQLDKGYATQLGrwfAGGQELSGGQ 503
Cdd:TIGR01193 541 IDRHTLRQFINYLPQEPYIFSGSILENLLLGAKENVSQDEIWAACEIAEIKDD-IENMPLGYQTELS---EEGSSISGGQ 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 504 WQKIALSRAYMrRDADILILDEPTAALDAGAEAAVFEHFReYAKGRMTLLISHRFSSVRNAEHIVVLEHGRVLERGDHDS 583
Cdd:TIGR01193 617 KQRIALARALL-TDSKVLILDESTSNLDTITEKKIVNNLL-NLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDE 694
|
250
....*....|..
gi 488616976 584 LIAAAGRYAALF 595
Cdd:TIGR01193 695 LLDRNGFYASLI 706
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
359-597 |
5.31e-33 |
|
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: 126.90 E-value: 5.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 359 ENVSFTYPgtSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDwDEDALRSRIGVIFQ 438
Cdd:COG4555 5 ENLSKKYG--KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRK-EPREARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 439 DFIRYQFL-VGENLgvgdthafhdetrWREAAAQGM----AAQFIEQLDKgyATQLG-----RWfaggQELSGGQWQKIA 508
Cdd:COG4555 82 ERGLYDRLtVRENI-------------RYFAELYGLfdeeLKKRIEELIE--LLGLEefldrRV----GELSTGMKKKVA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 509 LSRAYMrRDADILILDEPTAALDAGAEAAVFEHFREYAK-GRMTLLISHRFSSVRN-AEHIVVLEHGRVLERGDHDSLIA 586
Cdd:COG4555 143 LARALV-HDPKVLLLDEPTNGLDVMARRLLREILRALKKeGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELRE 221
|
250
....*....|....
gi 488616976 587 AAGR---YAALFDL 597
Cdd:COG4555 222 EIGEenlEDAFVAL 235
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
357-577 |
6.03e-33 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 125.94 E-value: 6.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 357 RFENVSFTYPGtSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDG---SDLQDWDEDALRSRI 433
Cdd:COG2884 3 RFENVSKRYPG-GREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGqdlSRLKRREIPYLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 434 GVIFQDFiryQFL----VGENLgvgdthAF------HDETRWREAAAQ-----GMAaqfieqlDKGYAtqlgrwFAggQE 498
Cdd:COG2884 82 GVVFQDF---RLLpdrtVYENV------ALplrvtgKSRKEIRRRVREvldlvGLS-------DKAKA------LP--HE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 499 LSGGQWQKIALSRAYMRRdADILILDEPTAALDAGAEAAVFEHFREYAKGRMTLLI-SHRFSSVRNAEH-IVVLEHGRVL 576
Cdd:COG2884 138 LSGGEQQRVAIARALVNR-PELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIaTHDLELVDRMPKrVLELEDGRLV 216
|
.
gi 488616976 577 E 577
Cdd:COG2884 217 R 217
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
357-579 |
7.28e-33 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 125.70 E-value: 7.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 357 RFENVSFTYP--GTSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDED---ALRS 431
Cdd:cd03257 3 EVKNLSVSFPtgGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRlrkIRRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 432 RIGVIFQDFIRY---QFLVGENLGVGDTHAFHDETRWREAAAQGMAAQFIEqLDKGYATQLGRwfaggqELSGGQWQKIA 508
Cdd:cd03257 83 EIQMVFQDPMSSlnpRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVG-LPEEVLNRYPH------ELSGGQRQRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488616976 509 LSRAyMRRDADILILDEPTAALDAGAEAAVFEHFREYAKGR-MTLL-ISHRFSSVRN-AEHIVVLEHGRVLERG 579
Cdd:cd03257 156 IARA-LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELgLTLLfITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
357-575 |
7.76e-33 |
|
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: 123.69 E-value: 7.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 357 RFENVSFTYPGTsrAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWD-EDALRSRIGV 435
Cdd:cd03216 2 ELRGITKRFGGV--KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASpRDARRAGIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 436 IFQdfiryqflvgenlgvgdthafhdetrwreaaaqgmaaqfieqldkgyatqlgrwfaggqeLSGGQWQKIALSRAyMR 515
Cdd:cd03216 80 VYQ------------------------------------------------------------LSVGERQMVEIARA-LA 98
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488616976 516 RDADILILDEPTAALDAGAEAAVFEHFRE-YAKGRMTLLISHRFSSVRN-AEHIVVLEHGRV 575
Cdd:cd03216 99 RNARLLILDEPTAALTPAEVERLFKVIRRlRAQGVAVIFISHRLDEVFEiADRVTVLRDGRV 160
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
356-580 |
1.73e-32 |
|
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: 125.54 E-value: 1.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 356 MRFENVSFTYPGtsRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDALRSRIGV 435
Cdd:COG1120 2 LEAENLSVGYGG--RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 436 IFQDFIryqflVGENLGVGDT-----HAFHDETRWREAAAQGMAAQFIEQLDkgyATQL-GRWFaggQELSGGQWQKIAL 509
Cdd:COG1120 80 VPQEPP-----APFGLTVRELvalgrYPHLGLFGRPSAEDREAVEEALERTG---LEHLaDRPV---DELSGGERQRVLI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488616976 510 SRAYMrRDADILILDEPTAALDAGAEAAVFEHFREYAK--GRMTLLISH------RFssvrnAEHIVVLEHGRVLERGD 580
Cdd:COG1120 149 ARALA-QEPPLLLLDEPTSHLDLAHQLEVLELLRRLARerGRTVVMVLHdlnlaaRY-----ADRLVLLKDGRIVAQGP 221
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
357-574 |
1.83e-32 |
|
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: 122.35 E-value: 1.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 357 RFENVSFTYPGtsRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDALRSRIGVI 436
Cdd:cd00267 1 EIENLSFRYGG--RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 437 FQdfiryqflvgenlgvgdthafhdetrwreaaaqgmaaqfieqldkgyatqlgrwfaggqeLSGGQWQKIALSRAYMrR 516
Cdd:cd00267 79 PQ------------------------------------------------------------LSGGQRQRVALARALL-L 97
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 517 DADILILDEPTAALDAGAEAAVFEHFREYA-KGRMTLLISHRFSSVRNA-EHIVVLEHGR 574
Cdd:cd00267 98 NPDLLLLDEPTSGLDPASRERLLELLRELAeEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
164-557 |
1.91e-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: 131.33 E-value: 1.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 164 LISFAVLLVH-FSPWALLILVLGALPVFFAEAHFSGDAFRLFTRRAPETRRQNYIETLLSHEGyIKEVKLFGFAPLLLKR 242
Cdd:TIGR02868 140 VGAAAVAAIAvLSVPAALILAAGLLLAGFVAPLVSLRAARAAEQALARLRGELAAQLTDALDG-AAELVASGALPAALAQ 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 243 YRDTFERLYAEDRRlTVRRDGWGFLLGLLGTASFYLAYAWVVVDAVHGRITLGQMTMYLVLFK----QGQAAVSSSLSAI 318
Cdd:TIGR02868 219 VEEADRELTRAERR-AAAATALGAALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPlaafEAFAALPAAAQQL 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 319 SGLYEDGLYLADLyiyLGQPVMPSAGSL-TQGALPGD--GMRFENVSFTYPGTSRAaLENIDLHLAPGRSVALVGENGSG 395
Cdd:TIGR02868 298 TRVRAAAERIVEV---LDAAGPVAEGSApAAGAVGLGkpTLELRDLSAGYPGAPPV-LDGVSLDLPPGERVAILGPSGSG 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 396 KTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDALRSRIGVIFQDFIRYQFLVGENLGVGDTHAFHDETRWreAAAQGMAA 475
Cdd:TIGR02868 374 KSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWA--ALERVGLA 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 476 QFIEQLDKGYATQLGrwfAGGQELSGGQWQKIALSRAYMrRDADILILDEPTAALDAGAEAAVFEHFREYAKGRMTLLIS 555
Cdd:TIGR02868 452 DWLRALPDGLDTVLG---EGGARLSGGERQRLALARALL-ADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLIT 527
|
..
gi 488616976 556 HR 557
Cdd:TIGR02868 528 HH 529
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
357-586 |
2.33e-32 |
|
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: 125.11 E-value: 2.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 357 RFENVSFTYPGtSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDALRSRIGVI 436
Cdd:cd03295 2 EFENVTKRYGG-GKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 437 FQDFIRY-QFLVGENLGVGDTHafhdeTRWREAAAQGMAAQFIEQLDKGYATQLGRWfagGQELSGGQWQKIALSRAyMR 515
Cdd:cd03295 81 IQQIGLFpHMTVEENIALVPKL-----LKWPKEKIRERADELLALVGLDPAEFADRY---PHELSGGQQQRVGVARA-LA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488616976 516 RDADILILDEPTAALDAGAEAAVFEHFREYAK--GRMTLLISHR-FSSVRNAEHIVVLEHGRVLERGDHDSLIA 586
Cdd:cd03295 152 ADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDiDEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
359-575 |
9.81e-32 |
|
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: 120.78 E-value: 9.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 359 ENVSFTYPGTSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDALRSRIGVIFQ 438
Cdd:cd03246 4 ENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 439 DFIRYQFLVGENLgvgdthafhdetrwreaaaqgmaaqfieqldkgyatqlgrwfaggqeLSGGQWQKIALSRAyMRRDA 518
Cdd:cd03246 84 DDELFSGSIAENI-----------------------------------------------LSGGQRQRLGLARA-LYGNP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488616976 519 DILILDEPTAALDAGAEAAVFEHFREY-AKGRMTLLISHRFSSVRNAEHIVVLEHGRV 575
Cdd:cd03246 116 RILVLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
357-575 |
1.08e-31 |
|
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: 122.21 E-value: 1.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 357 RFENVSFTYP--GTSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDAL----R 430
Cdd:cd03255 2 ELKNLSKTYGggGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafrR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 431 SRIGVIFQDF--IRYqFLVGENLGVGdthAFHDETRWREAAAQgmAAQFIEQLdkGYATQLGRwFAGgqELSGGQWQKIA 508
Cdd:cd03255 82 RHIGFVFQSFnlLPD-LTALENVELP---LLLAGVPKKERRER--AEELLERV--GLGDRLNH-YPS--ELSGGQQQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488616976 509 LSRAYMrRDADILILDEPTAALDAGAEAAVFEHFREYAK--GRMTLLISHRFSSVRNAEHIVVLEHGRV 575
Cdd:cd03255 151 IARALA-NDPKIILADEPTGNLDSETGKEVMELLRELNKeaGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
357-587 |
7.02e-31 |
|
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: 127.17 E-value: 7.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 357 RFENVSFTYPGTSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDALRSRIGVI 436
Cdd:COG4618 332 SVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYL 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 437 FQDFiryQFL---VGEN---LGVGDTHAFHdetrwreAAAQgMAA--QFIEQLDKGYATQLGrwfAGGQELSGGQWQKIA 508
Cdd:COG4618 412 PQDV---ELFdgtIAENiarFGDADPEKVV-------AAAK-LAGvhEMILRLPDGYDTRIG---EGGARLSGGQRQRIG 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 509 LSRAyMRRDADILILDEPTA---ALDAGAEAAVFEHFReyAKGRMTLLISHRFSSVRNAEHIVVLEHGRVLERGDHDSLI 585
Cdd:COG4618 478 LARA-LYGDPRLVVLDEPNSnldDEGEAALAAAIRALK--ARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVL 554
|
..
gi 488616976 586 AA 587
Cdd:COG4618 555 AR 556
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
371-594 |
2.27e-30 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 125.73 E-value: 2.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 371 AALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRlYQPDQGRILLDGSDLQDWDEDALRSRIGVIFQDFIRYQFLVGEN 450
Cdd:PRK11174 364 TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLG-FLPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDN 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 451 LGVGDTHAfhDETRWREAAAQGMAAQFIEQLDKGYATQLGRWFAGgqeLSGGQWQKIALSRAYMRrDADILILDEPTAAL 530
Cdd:PRK11174 443 VLLGNPDA--SDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAG---LSVGQAQRLALARALLQ-PCQLLLLDEPTASL 516
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488616976 531 DAGAEAAVFEHFREYAKGRMTLLISHRFSSVRNAEHIVVLEHGRVLERGDHDSLIAAAGRYAAL 594
Cdd:PRK11174 517 DAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
357-590 |
4.31e-30 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 123.98 E-value: 4.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 357 RFENVSFTYPGTsrAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWD-EDALRSRIGV 435
Cdd:COG1129 6 EMRGISKSFGGV--KALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSpRDAQAAGIAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 436 IFQDFIRYQFL-VGENLGVGDTHAFHDETRWREAAAQgmAAQFIEQLDKGY--ATQLGrwfaggqELSGGQWQKIALSRA 512
Cdd:COG1129 84 IHQELNLVPNLsVAENIFLGREPRRGGLIDWRAMRRR--ARELLARLGLDIdpDTPVG-------DLSVAQQQLVEIARA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 513 yMRRDADILILDEPTAALDAGAEAAVFEHFREY-AKGRMTLLISHRFSSVRN-AEHIVVLEHGRVLERG-----DHDSLI 585
Cdd:COG1129 155 -LSRDARVLILDEPTASLTEREVERLFRIIRRLkAQGVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGpvaelTEDELV 233
|
....*.
gi 488616976 586 AA-AGR 590
Cdd:COG1129 234 RLmVGR 239
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
359-579 |
4.82e-30 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 116.38 E-value: 4.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 359 ENVSFTYPGtsRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDALRSRIGVIFQ 438
Cdd:cd03214 3 ENLSVGYGG--RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 439 dfiryqflVGENLGVGDthafhdetrwreaaaqgMAAQFIEqldkgyatqlgrwfaggqELSGGQWQKIALSRAYMrRDA 518
Cdd:cd03214 81 --------ALELLGLAH-----------------LADRPFN------------------ELSGGERQRVLLARALA-QEP 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488616976 519 DILILDEPTAALDAGAEAAVFEHFREYAK--GRMTLLISH------RFssvrnAEHIVVLEHGRVLERG 579
Cdd:cd03214 117 PILLLDEPTSHLDIAHQIELLELLRRLARerGKTVVMVLHdlnlaaRY-----ADRVILLKDGRIVAQG 180
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
358-601 |
7.36e-30 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 124.45 E-value: 7.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 358 FENVSFTYpGTSRAALENIDLHLaPGRS-VALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDALRSRIGVI 436
Cdd:PRK10790 343 IDNVSFAY-RDDNLVLQNINLSV-PSRGfVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 437 FQD--FIRYQFLVGENLGvgdtHAFHDETRWrEAAAQGMAAQFIEQLDKGYATQLGRwfaGGQELSGGQWQKIALSRAYM 514
Cdd:PRK10790 421 QQDpvVLADTFLANVTLG----RDISEEQVW-QALETVQLAELARSLPDGLYTPLGE---QGNNLSVGQKQLLALARVLV 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 515 RRDAdILILDEPTAALDAGAEAAVFEHFREYAKGRMTLLISHRFSSVRNAEHIVVLEHGRVLERGDHDSLIAAAGRYAAL 594
Cdd:PRK10790 493 QTPQ-ILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQM 571
|
....*..
gi 488616976 595 FDLQAQG 601
Cdd:PRK10790 572 YQLQLAG 578
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
357-575 |
1.39e-29 |
|
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: 116.90 E-value: 1.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 357 RFENVSFTYPGtSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDAL---RSRI 433
Cdd:cd03256 2 EVENLSKTYPN-GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqlRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 434 GVIFQDF-IRYQFLVGENLGVG---DTHAFHDETRWREAAAQGMAAQFIEQLD-KGYATQlgRwfagGQELSGGQWQKIA 508
Cdd:cd03256 81 GMIFQQFnLIERLSVLENVLSGrlgRRSTWRSLFGLFPKEEKQRALAALERVGlLDKAYQ--R----ADQLSGGQQQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 509 LSRAYMrRDADILILDEPTAALDAGAEAAVFEHFREYAKGR-MTLLIS-HRFSSVR-NAEHIVVLEHGRV 575
Cdd:cd03256 155 IARALM-QQPKLILADEPVASLDPASSRQVMDLLKRINREEgITVIVSlHQVDLAReYADRIVGLKDGRI 223
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
356-579 |
1.65e-29 |
|
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: 116.08 E-value: 1.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 356 MRFENVSFTYPGTsrAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWdeDALRSRIGV 435
Cdd:cd03259 1 LELKGLSKTYGSV--RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGV--PPERRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 436 IFQDFIRYQFL-VGENLGVGDTHAfhdetRWREAAAQGMAAQFIEQLDKgyATQLGRWFAggqELSGGQWQKIALSRAyM 514
Cdd:cd03259 77 VFQDYALFPHLtVAENIAFGLKLR-----GVPKAEIRARVRELLELVGL--EGLLNRYPH---ELSGGQQQRVALARA-L 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488616976 515 RRDADILILDEPTAALDAGAEAAVFEHFREYAK--GRMTLLISH-RFSSVRNAEHIVVLEHGRVLERG 579
Cdd:cd03259 146 AREPSLLLLDEPLSALDAKLREELREELKELQRelGITTIYVTHdQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
372-580 |
6.57e-28 |
|
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: 112.15 E-value: 6.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 372 ALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDAlRSRIGV--------IFQDFIry 443
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHE-IARLGIgrtfqiprLFPELT-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 444 qflVGENLGVG-----DTHAFHDETRWREAAAQGMAAQFIEQLdkGYAtqlGRWFAGGQELSGGQWQKIALSRAYMrRDA 518
Cdd:cd03219 92 ---VLENVMVAaqartGSGLLLARARREEREARERAEELLERV--GLA---DLADRPAGELSYGQQRRLEIARALA-TDP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488616976 519 DILILDEPTAALDAGAEAAVFEHFREYAKGRMT-LLISHRFSSVRN-AEHIVVLEHGRVLERGD 580
Cdd:cd03219 163 KLLLLDEPAAGLNPEETEELAELIRELRERGITvLLVEHDMDVVMSlADRVTVLDQGRVIAEGT 226
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
356-579 |
1.16e-27 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 112.80 E-value: 1.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 356 MRFENVSFTYPGTSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQD---WDedaLRSR 432
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEetvWD---VRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 433 IGVIFQDfIRYQFlVGENlgVGDTHAF--------HDE--TRWREAAAQGMAAQFIEQldkgyatqlgrwfaGGQELSGG 502
Cdd:PRK13635 83 VGMVFQN-PDNQF-VGAT--VQDDVAFglenigvpREEmvERVDQALRQVGMEDFLNR--------------EPHRLSGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488616976 503 QWQKIALSRAYMRRdADILILDEPTAALDAGAEAAVFEHFREY-AKGRMTLL-ISHRFSSVRNAEHIVVLEHGRVLERG 579
Cdd:PRK13635 145 QKQRVAIAGVLALQ-PDIIILDEATSMLDPRGRREVLETVRQLkEQKGITVLsITHDLDEAAQADRVIVMNKGEILEEG 222
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
356-577 |
1.29e-27 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 110.90 E-value: 1.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 356 MRFENVSFTYP--GTSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDAL---- 429
Cdd:COG1136 5 LELRNLTKSYGtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 430 RSRIGVIFQDFiryqFLVG-----ENLGVGDTHAfhdetRWREAAAQGMAAQFIEQLdkGYATQLGRwFAGgqELSGGQW 504
Cdd:COG1136 85 RRHIGFVFQFF----NLLPeltalENVALPLLLA-----GVSRKERRERARELLERV--GLGDRLDH-RPS--QLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488616976 505 QKIALSRAYMRRdADILILDEPTAALDAGAEAAVFEHFREYAK--GRMTLLISHRFSSVRNAEHIVVLEHGRVLE 577
Cdd:COG1136 151 QRVAIARALVNR-PKLILADEPTGNLDSKTGEEVLELLRELNRelGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
358-580 |
2.55e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 111.62 E-value: 2.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 358 FENVSFTYPGTSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDALRSRIGVIF 437
Cdd:PRK13632 10 VENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGIIF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 438 Q--DfirYQFlVGenLGVGDTHAFHDETR-------WR---EAAAQ-GMaaqfIEQLDKgyatqlgrwfaGGQELSGGQW 504
Cdd:PRK13632 90 QnpD---NQF-IG--ATVEDDIAFGLENKkvppkkmKDiidDLAKKvGM----EDYLDK-----------EPQNLSGGQK 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488616976 505 QKIALSRAyMRRDADILILDEPTAALDAGAEAAVFEHFREYAKGRMTLLIS--HRFSSVRNAEHIVVLEHGRVLERGD 580
Cdd:PRK13632 149 QRVAIASV-LALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISitHDMDEAILADKVIVFSEGKLIAQGK 225
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
20-587 |
6.08e-27 |
|
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: 115.28 E-value: 6.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 20 LVWTTSRALSVGLIVATLVAGLLPA-LAAWLGQRIvdavvsamqlhASTGEAPLWPVLRYVLLEAGVLALLAGAQRGLS- 97
Cdd:COG4615 6 LLLRESRWLLLLALLLGLLSGLANAgLIALINQAL-----------NATGAALARLLLLFAGLLVLLLLSRLASQLLLTr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 98 -VQQAL--LRVLLGQKVntlilEKAQTLSLSQFEDSEFYDKLVRvrreaSTRPLALVTKSL-GLLQNLISLISFAVLLVH 173
Cdd:COG4615 75 lGQHAVarLRLRLSRRI-----LAAPLERLERIGAARLLAALTE-----DVRTISQAFVRLpELLQSVALVLGCLAYLAW 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 174 FSPWALLI-LVLGALPVFFAeAHFSGDAFRLFTR-RAPETRRQNYIETLLshEGyIKEVKLFGfaplllKRYRDTFERLY 251
Cdd:COG4615 145 LSPPLFLLtLVLLGLGVAGY-RLLVRRARRHLRRaREAEDRLFKHFRALL--EG-FKELKLNR------RRRRAFFDEDL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 252 AED----RRLTVRRDGWGFLLGLLGTASFYLAYAWVV-VDAVHGRITLGQMTMYL--VLFKQG--QAAVSS--------- 313
Cdd:COG4615 215 QPTaeryRDLRIRADTIFALANNWGNLLFFALIGLILfLLPALGWADPAVLSGFVlvLLFLRGplSQLVGAlptlsranv 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 314 SLSAISGLyedglylaDLYIYLGQPVMPSAGSLTQGALPgDGMRFENVSFTYPGTSRA---ALENIDLHLAPGRSVALVG 390
Cdd:COG4615 295 ALRKIEEL--------ELALAAAEPAAADAAAPPAPADF-QTLELRGVTYRYPGEDGDegfTLGPIDLTIRRGELVFIVG 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 391 ENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDALRSRIGVIFQDFiryqFLVGENLGVGDthafhdetrwreAAA 470
Cdd:COG4615 366 GNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDF----HLFDRLLGLDG------------EAD 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 471 QGMAAQFIEQLDKGYATQlgrwFAGGQ----ELSGGQWQKIALSRAYMrRDADILILDE------Ptaaldagaeaavfe 540
Cdd:COG4615 430 PARARELLERLELDHKVS----VEDGRfsttDLSQGQRKRLALLVALL-EDRPILVFDEwaadqdP-------------- 490
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 488616976 541 HFREY----------AKGRMTLLISH--RFSSVrnAEHIVVLEHGRVLERGDHDSLIAA 587
Cdd:COG4615 491 EFRRVfytellpelkARGKTVIAISHddRYFDL--ADRVLKMDYGKLVELTGPAALAAS 547
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
357-575 |
8.07e-27 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 114.35 E-value: 8.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 357 RFENVSFTYPGTsrAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWD-EDALRSRIGV 435
Cdd:COG3845 7 ELRGITKRFGGV--VANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSpRDAIALGIGM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 436 IFQDF--IRyQFLVGEN--LGVGDTHAFHdeTRWREAAAQgmaaqfIEQLDKGYatqlgrwfagG---------QELSGG 502
Cdd:COG3845 85 VHQHFmlVP-NLTVAENivLGLEPTKGGR--LDRKAARAR------IRELSERY----------GldvdpdakvEDLSVG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488616976 503 QWQKIALSRA-YmrRDADILILDEPTAALDAGAEAAVFEHFREYAKGRMT-LLISHRFSSVR-NAEHIVVLEHGRV 575
Cdd:COG3845 146 EQQRVEILKAlY--RGARILILDEPTAVLTPQEADELFEILRRLAAEGKSiIFITHKLREVMaIADRVTVLRRGKV 219
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
357-587 |
1.12e-26 |
|
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: 108.44 E-value: 1.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 357 RFENVSFTYPGTSRA--ALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDAL---RS 431
Cdd:cd03258 3 ELKNVSKVFGDTGGKvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkaRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 432 RIGVIFQdfiryQFLVGENLGVGDTHAFHDE-TRWREAAAQGMAAQFIEQL---DKG--YATQlgrwfaggqeLSGGQWQ 505
Cdd:cd03258 83 RIGMIFQ-----HFNLLSSRTVFENVALPLEiAGVPKAEIEERVLELLELVgleDKAdaYPAQ----------LSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 506 KIALSRAyMRRDADILILDEPTAALDAGAEAAVFEHFREYAK--GRMTLLISHRFSSVRN-AEHIVVLEHGRVLERGDHD 582
Cdd:cd03258 148 RVGIARA-LANNPKVLLCDEATSALDPETTQSILALLRDINRelGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVE 226
|
....*
gi 488616976 583 SLIAA 587
Cdd:cd03258 227 EVFAN 231
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
356-580 |
1.42e-26 |
|
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: 108.04 E-value: 1.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 356 MRFENVSFTYpgTSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLY-----QPDQGRILLDGSDLQDWDED--A 428
Cdd:cd03260 1 IELRDLNVYY--GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLDVDvlE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 429 LRSRIGVIFQDFIRYQFLVGENLGVGDTH---AFHDETRWREAAAQGMAAQFIEQLDKgyatqlgrwfAGGQELSGGQWQ 505
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVAYGLRLhgiKLKEELDERVEEALRKAALWDEVKDR----------LHALGLSGGQQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488616976 506 KIALSRAYMRRdADILILDEPTAALDAGAEAAVFEHFREYAKGRMTLLISHRFSSV-RNAEHIVVLEHGRVLERGD 580
Cdd:cd03260 149 RLCLARALANE-PEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAaRVADRTAFLLNGRLVEFGP 223
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
356-526 |
1.48e-26 |
|
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: 107.94 E-value: 1.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 356 MRFENVSFTYPGTSRA--ALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDwdedaLRSRI 433
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-----PGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 434 GVIFQDFIRYQFL-VGENLGVGDTHAFHDETRWREAaaqgmAAQFIEQLD-KGYATQLGRwfaggqELSGGQWQKIALSR 511
Cdd:cd03293 76 GYVFQQDALLPWLtVLDNVALGLELQGVPKAEARER-----AEELLELVGlSGFENAYPH------QLSGGMRQRVALAR 144
|
170
....*....|....*
gi 488616976 512 AYMrRDADILILDEP 526
Cdd:cd03293 145 ALA-VDPDVLLLDEP 158
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
357-575 |
1.91e-26 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 108.25 E-value: 1.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 357 RFENVSFTYPGtsRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQdwdedALRSRIGVI 436
Cdd:COG1121 8 ELENLTVSYGG--RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR-----RARRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 437 FQDF-IRYQF------LVGenLG-VGDTHAFhdetRWREAAAQGMAAQFIEQLD-KGYA-TQLGrwfaggqELSGGQWQK 506
Cdd:COG1121 81 PQRAeVDWDFpitvrdVVL--MGrYGRRGLF----RRPSRADREAVDEALERVGlEDLAdRPIG-------ELSGGQQQR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488616976 507 IALSRAYMrRDADILILDEPTAALDAGAEAAVFEHFREYAKGRMT-LLISHRFSSVR-NAEHIVVLEHGRV 575
Cdd:COG1121 148 VLLARALA-QDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTiLVVTHDLGAVReYFDRVLLLNRGLV 217
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
357-587 |
3.08e-26 |
|
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: 107.37 E-value: 3.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 357 RFENVSFTYpGtSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDED---ALRSRI 433
Cdd:COG1127 7 EVRNLTKSF-G-DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKelyELRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 434 GVIFQ-----DFIRyqflVGENLgvgdthAF----HdeTRWREAAAQGMAAQFIEQLD-KGYATQLGRwfaggqELSGGQ 503
Cdd:COG1127 85 GMLFQggalfDSLT----VFENV------AFplreH--TDLSEAEIRELVLEKLELVGlPGAADKMPS------ELSGGM 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 504 wQK-IALSRAyMRRDADILILDEPTAALDAGAEAAVFEHFREYAK--GRMTLLISHRFSSVRN-AEHIVVLEHGRVLERG 579
Cdd:COG1127 147 -RKrVALARA-LALDPEILLYDEPTAGLDPITSAVIDELIRELRDelGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEG 224
|
....*...
gi 488616976 580 DHDSLIAA 587
Cdd:COG1127 225 TPEELLAS 232
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
372-590 |
7.22e-25 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 108.62 E-value: 7.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 372 ALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLyQPDQGRILLDGSDLQDWDEDA---LRSRIGVIFQDfiryQF--- 445
Cdd:COG4172 301 AVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSRRAlrpLRRRMQVVFQD----PFgsl 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 446 --------LVGENLGVgdtHafhdETRWREAAAQGMAAQFIEQ--LDKGYatqLGRWfagGQELSGGQWQKIALSRAyMR 515
Cdd:COG4172 376 sprmtvgqIIAEGLRV---H----GPGLSAAERRARVAEALEEvgLDPAA---RHRY---PHEFSGGQRQRIAIARA-LI 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 516 RDADILILDEPTAALDAGAEAAVFEHFREY-AKGRMT-LLISHRFSSVRN-AEHIVVLEHGRVLERGD---------HD- 582
Cdd:COG4172 442 LEPKLLVLDEPTSALDVSVQAQILDLLRDLqREHGLAyLFISHDLAVVRAlAHRVMVMKDGKVVEQGPteqvfdapqHPy 521
|
250
....*....|
gi 488616976 583 --SLIAAAGR 590
Cdd:COG4172 522 trALLAAAPL 531
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
356-586 |
1.12e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 103.91 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 356 MRFENVSFTYP-GTSraALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDE-DALRSRI 433
Cdd:PRK13644 2 IRLENVSYSYPdGTP--ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 434 GVIFQDfIRYQFL---VGENLGVGDTHAFHDETRWREAAAQGMAaqfieqldkgyATQLGRW-FAGGQELSGGQWQKIAL 509
Cdd:PRK13644 80 GIVFQN-PETQFVgrtVEEDLAFGPENLCLPPIEIRKRVDRALA-----------EIGLEKYrHRSPKTLSGGQGQCVAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488616976 510 SrAYMRRDADILILDEPTAALDAGAEAAVFEHFRE-YAKGRMTLLISHRFSSVRNAEHIVVLEHGRVLERGDHDSLIA 586
Cdd:PRK13644 148 A-GILTMEPECLIFDEVTSMLDPDSGIAVLERIKKlHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
356-574 |
1.25e-24 |
|
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: 101.11 E-value: 1.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 356 MRFENVSFTYPGtsRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDED--ALRSRI 433
Cdd:cd03229 1 LELKNVSKRYGQ--KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDElpPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 434 GVIFQDFIRYQFL-VGENLGVGdthafhdetrwreaaaqgmaaqfieqldkgyatqlgrwfaggqeLSGGQWQKIALSRA 512
Cdd:cd03229 79 GMVFQDFALFPHLtVLENIALG--------------------------------------------LSGGQQQRVALARA 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488616976 513 YMrRDADILILDEPTAALDAGAEAAVFEHFREYAK--GRMTLLISHRFSSVRN-AEHIVVLEHGR 574
Cdd:cd03229 115 LA-MDPDVLLLDEPTSALDPITRREVRALLKSLQAqlGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
352-579 |
1.65e-24 |
|
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: 101.72 E-value: 1.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 352 PGDG-MRFENVSFTYPGTSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDALR 430
Cdd:cd03369 2 PEHGeIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 431 SRIGVIFQDFIRYQFLVGENLGVGDThaFHDEtrwreaaaQGMAAQFIEQldkgyatqlgrwfaGGQELSGGQWQKIALS 510
Cdd:cd03369 82 SSLTIIPQDPTLFSGTIRSNLDPFDE--YSDE--------EIYGALRVSE--------------GGLNLSQGQRQLLCLA 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488616976 511 RAYMRRdADILILDEPTAALDAGAEAAVFEHFREYAKGRMTLLISHRFSSVRNAEHIVVLEHGRVLERG 579
Cdd:cd03369 138 RALLKR-PRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYD 205
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
357-586 |
2.99e-24 |
|
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: 101.42 E-value: 2.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 357 RFENVSFTYPGtsRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDED---ALRSRI 433
Cdd:cd03261 2 ELRGLTKSFGG--RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAelyRLRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 434 GVIFQDFIRYQFL-VGENLGVG-DTHAFHDETRWREAAAQGMAAQFIEQLDKGYATqlgrwfaggqELSGGQWQKIALSR 511
Cdd:cd03261 80 GMLFQSGALFDSLtVFENVAFPlREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPA----------ELSGGMKKRVALAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488616976 512 AYMrRDADILILDEPTAALDAGAEAAVFEHFREY--AKGRMTLLISHRFSSVRN-AEHIVVLEHGRVLERGDHDSLIA 586
Cdd:cd03261 150 ALA-LDPELLLYDEPTAGLDPIASGVIDDLIRSLkkELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
372-586 |
3.45e-24 |
|
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: 100.97 E-value: 3.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 372 ALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDAlRSRIGV--------IFQDFIry 443
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHE-RARAGIgyvpegrrIFPELT-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 444 qflVGENLGVGDTHAFHDETRWReaaaqgmaaqfieqLDKGYAT--QLG-RWFAGGQELSGGQWQKIALSRAYMRRdADI 520
Cdd:cd03224 92 ---VEENLLLGAYARRRAKRKAR--------------LERVYELfpRLKeRRKQLAGTLSGGEQQMLAIARALMSR-PKL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488616976 521 LILDEPTAALDAGAEAAVFEHFREYAKGRMT-LLISHRFSSVRN-AEHIVVLEHGRVLERGDHDSLIA 586
Cdd:cd03224 154 LLLDEPSEGLAPKIVEEIFEAIRELRDEGVTiLLVEQNARFALEiADRAYVLERGRVVLEGTAAELLA 221
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
357-526 |
3.64e-24 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 102.09 E-value: 3.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 357 RFENVSFTYP--GTSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLqdwdeDALRSRIG 434
Cdd:COG1116 9 ELRGVSKRFPtgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPV-----TGPGPDRG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 435 VIFQDFIRYQFL-VGENLGVGdthafHDETRWREAAAQGMAAQFIEQLD-KGYATQLGRwfaggqELSGGQWQKIALSRA 512
Cdd:COG1116 84 VVFQEPALLPWLtVLDNVALG-----LELRGVPKAERRERARELLELVGlAGFEDAYPH------QLSGGMRQRVAIARA 152
|
170
....*....|....
gi 488616976 513 YMRrDADILILDEP 526
Cdd:COG1116 153 LAN-DPEVLLMDEP 165
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
357-556 |
5.76e-24 |
|
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: 100.02 E-value: 5.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 357 RFENVSFTYPGTSRAaLENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDedaLRSRIGVI 436
Cdd:cd03226 1 RIENISFSYKKGTEI-LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE---RRKSIGYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 437 FQDfIRYQFL---VGENLGVGDTHAfhdetrwreAAAQGMAAQFIEQLD-KGYATQLGRwfaggqELSGGQWQKIALSRA 512
Cdd:cd03226 77 MQD-VDYQLFtdsVREELLLGLKEL---------DAGNEQAETVLKDLDlYALKERHPL------SLSGGQKQRLAIAAA 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488616976 513 YMrRDADILILDEPTAALDAGAEAAVFEHFREYAK-GRMTLLISH 556
Cdd:cd03226 141 LL-SGKDLLIFDEPTSGLDYKNMERVGELIRELAAqGKAVIVITH 184
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
356-556 |
1.25e-23 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 99.09 E-value: 1.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 356 MRFENVSFTYPGtsRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDwDEDALRSRIGV 435
Cdd:COG4133 3 LEAENLSCRRGE--RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 436 IFQDFIRYQFL-VGENLgvgdthAFHDETrWREAAAQGMAAQFIEQLD-KGYATQLGRwfaggqELSGGQWQKIALSRAY 513
Cdd:COG4133 80 LGHADGLKPELtVRENL------RFWAAL-YGLRADREAIDEALEAVGlAGLADLPVR------QLSAGQKRRVALARLL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488616976 514 MrRDADILILDEPTAALDAGAEAAVFEHFREY-AKGRMTLLISH 556
Cdd:COG4133 147 L-SPAPLWLLDEPFTALDAAGVALLAELIAAHlARGGAVLLTTH 189
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
358-575 |
1.77e-23 |
|
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: 98.63 E-value: 1.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 358 FENVSFTYPGTSrAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDA---LRSRIG 434
Cdd:cd03292 3 FINVTKTYPNGT-AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipyLRRKIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 435 VIFQDfiryqFLVGENLGVGDTHAFHDETRW---REAAAQGMAAqfIEQLDKGyatqlGRWFAGGQELSGGQWQKIALSR 511
Cdd:cd03292 82 VVFQD-----FRLLPDRNVYENVAFALEVTGvppREIRKRVPAA--LELVGLS-----HKHRALPAELSGGEQQRVAIAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488616976 512 AYMRRDAdILILDEPTAALDAGAEAAVFEHFREYAKGRMTLLIS-HRFSSVRNAEH-IVVLEHGRV 575
Cdd:cd03292 150 AIVNSPT-ILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVAtHAKELVDTTRHrVIALERGKL 214
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
357-573 |
2.37e-23 |
|
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: 98.37 E-value: 2.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 357 RFENVSFTYPGtsRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDwdedaLRSRIGVI 436
Cdd:cd03235 1 EVEDLTVSYGG--HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK-----ERKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 437 FQ------DF-IRYQFLVGENLgVGDTHAFHDETR-WREAAAQ-----GMAAqFIEQldkgyatQLGrwfaggqELSGGQ 503
Cdd:cd03235 74 PQrrsidrDFpISVRDVVLMGL-YGHKGLFRRLSKaDKAKVDEalervGLSE-LADR-------QIG-------ELSGGQ 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488616976 504 WQKIALSRAYMrRDADILILDEPTAALDAGAEAAVFEHFREYAKGRMT-LLISHRFSSV-RNAEHIVVLEHG 573
Cdd:cd03235 138 QQRVLLARALV-QDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTiLVVTHDLGLVlEYFDRVLLLNRT 208
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
356-590 |
1.89e-22 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 101.14 E-value: 1.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 356 MRFENVSFTYPGTSraALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWD-EDALRSRIG 434
Cdd:PRK11288 5 LSFDGIGKTFPGVK--ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFAStTAALAAGVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 435 VIFQDF-IRYQFLVGENLGVG---DTHAFHDETRWREAAAQGMAAQFIEqLDKgyATQLGRwfaggqeLSGGQWQKIALS 510
Cdd:PRK11288 83 IIYQELhLVPEMTVAENLYLGqlpHKGGIVNRRLLNYEAREQLEHLGVD-IDP--DTPLKY-------LSIGQRQMVEIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 511 RAYMrRDADILILDEPTAALDAGAEAAVFEHFREY-AKGRMTLLISHRFSSV-RNAEHIVVLEHGRV------LERGDHD 582
Cdd:PRK11288 153 KALA-RNARVIAFDEPTSSLSAREIEQLFRVIRELrAEGRVILYVSHRMEEIfALCDAITVFKDGRYvatfddMAQVDRD 231
|
....*....
gi 488616976 583 SLIAA-AGR 590
Cdd:PRK11288 232 QLVQAmVGR 240
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
372-575 |
2.11e-22 |
|
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: 95.67 E-value: 2.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 372 ALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDA--LRSRIGVIFQDFIRYQFL-VG 448
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNIneLRQKVGMVFQQFNLFPHLtVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 449 ENLGVGDTHAFHdetrWREAAAQGMAAQFIEQLdkGYATQLGRWFAggqELSGGQWQKIALSRAYMRRdADILILDEPTA 528
Cdd:cd03262 95 ENITLAPIKVKG----MSKAEAEERALELLEKV--GLADKADAYPA---QLSGGQQQRVAIARALAMN-PKVMLFDEPTS 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488616976 529 ALDAGAEAAVFEHFREYAKGRMTLLI-SHRFSSVRN-AEHIVVLEHGRV 575
Cdd:cd03262 165 ALDPELVGEVLDVMKDLAEEGMTMVVvTHEMGFAREvADRVIFMDDGRI 213
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
359-527 |
2.71e-22 |
|
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: 95.96 E-value: 2.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 359 ENVSFTYPGTSRA--ALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDA---LRSR- 432
Cdd:COG4181 12 RGLTKTVGTGAGEltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDArarLRARh 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 433 IGVIFQDFiryQFLVG----ENLGV-----GDTHAfhdetrwREAAAQGMAAQFIEQLDKGYATQlgrwfaggqeLSGGQ 503
Cdd:COG4181 92 VGFVFQSF---QLLPTltalENVMLplelaGRRDA-------RARARALLERVGLGHRLDHYPAQ----------LSGGE 151
|
170 180
....*....|....*....|....
gi 488616976 504 WQKIALSRAYMRRdADILILDEPT 527
Cdd:COG4181 152 QQRVALARAFATE-PAILFADEPT 174
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
360-587 |
4.53e-22 |
|
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: 97.43 E-value: 4.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 360 NVSF-TYPGTSRAaLENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQP---DQGRILLDGSDLQDWDEDALR----S 431
Cdd:COG0444 8 KVYFpTRRGVVKA-VDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELRkirgR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 432 RIGVIFQD--------F-IRYQflVGENLgvgDTHAFHDETRWREAAAQGMAAQFI----EQLDKgYAtqlgrwfaggQE 498
Cdd:COG0444 87 EIQMIFQDpmtslnpvMtVGDQ--IAEPL---RIHGGLSKAEARERAIELLERVGLpdpeRRLDR-YP----------HE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 499 LSGGQWQKIALSRAYMrRDADILILDEPTAALDAGAEAAVFEHFREYAKGR-MT-LLISHRFSSVRN-AEHIVVLEHGRV 575
Cdd:COG0444 151 LSGGMRQRVMIARALA-LEPKLLIADEPTTALDVTIQAQILNLLKDLQRELgLAiLFITHDLGVVAEiADRVAVMYAGRI 229
|
250
....*....|..
gi 488616976 576 LERGDHDSLIAA 587
Cdd:COG0444 230 VEEGPVEELFEN 241
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
357-579 |
4.64e-22 |
|
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: 94.74 E-value: 4.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 357 RFENVSFTYpgtsrAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDwDEDALRSRIGVI 436
Cdd:cd03266 10 RFRDVKKTV-----QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 437 FQDFIRYQFL-VGENLG-VGDTHAFhdetrwREAAAQGMAAQFIEQLDkgYATQLGRWFAGgqeLSGGQWQKIALSRAYM 514
Cdd:cd03266 84 SDSTGLYDRLtARENLEyFAGLYGL------KGDELTARLEELADRLG--MEELLDRRVGG---FSTGMRQKVAIARALV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488616976 515 rRDADILILDEPTAALDAGAEAAVFEHFREY-AKGRMTLLISHRFSSV-RNAEHIVVLEHGRVLERG 579
Cdd:cd03266 153 -HDPPVLLLDEPTTGLDVMATRALREFIRQLrALGKCILFSTHIMQEVeRLCDRVVVLHRGRVVYEG 218
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
359-579 |
5.61e-22 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 97.52 E-value: 5.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 359 ENVSFTYPgtSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLqDWDEDALRSRIGVIFQ 438
Cdd:COG1118 6 RNISKRFG--SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL-FTNLPPRERRVGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 439 DFIRYQFL-VGENLGVGDTHAFHDETRWREAAAQGMAAQFIEQLDKGYATQlgrwfaggqeLSGGQWQKIALSRAyMRRD 517
Cdd:COG1118 83 HYALFPHMtVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQ----------LSGGQRQRVALARA-LAVE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488616976 518 ADILILDEPtaaldagaeaavF----------------EHFREYakGRMTLLISH-RFSSVRNAEHIVVLEHGRVLERG 579
Cdd:COG1118 152 PEVLLLDEP------------FgaldakvrkelrrwlrRLHDEL--GGTTVFVTHdQEEALELADRVVVMNQGRIEQVG 216
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
356-583 |
3.05e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 94.13 E-value: 3.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 356 MRFENVSFTY-PGTS--RAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDG----SDLQDWDEDA 428
Cdd:PRK13641 3 IKFENVDYIYsPGTPmeKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitPETGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 429 LRSRIGVIFQdFIRYQFLvgENLGVGDTHAFHDETRWREAAAQGMAAQFIEQLdkGYATQLGRwfAGGQELSGGQWQKIA 508
Cdd:PRK13641 83 LRKKVSLVFQ-FPEAQLF--ENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKV--GLSEDLIS--KSPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488616976 509 LSrAYMRRDADILILDEPTAALDAGAEAAVFEHFREYAK-GRMTLLISHRFSSVRN-AEHIVVLEHGRVLErgdHDS 583
Cdd:PRK13641 156 IA-GVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKaGHTVILVTHNMDDVAEyADDVLVLEHGKLIK---HAS 228
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
358-579 |
4.66e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 93.71 E-value: 4.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 358 FENVSFTYPGTSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPD---QGRILLDGSDLQD---WDedaLRS 431
Cdd:PRK13640 8 FKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDdnpNSKITVDGITLTAktvWD---IRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 432 RIGVIFQDfIRYQFlVGENlgVGDTHAFHDETRW--REaAAQGMAAQFIEQLDkgyatQLGRWFAGGQELSGGQWQKIAL 509
Cdd:PRK13640 85 KVGIVFQN-PDNQF-VGAT--VGDDVAFGLENRAvpRP-EMIKIVRDVLADVG-----MLDYIDSEPANLSGGQKQRVAI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488616976 510 SrAYMRRDADILILDEPTAALDAGAEAAVFEHFREYAKGR-MTLL-ISHRFSSVRNAEHIVVLEHGRVLERG 579
Cdd:PRK13640 155 A-GILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnLTVIsITHDIDEANMADQVLVLDDGKLLAQG 225
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
372-527 |
4.95e-21 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 94.41 E-value: 4.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 372 ALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDAL---RSRIGVIFQDfiRYQFL-- 446
Cdd:COG4608 33 AVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELrplRRRMQMVFQD--PYASLnp 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 447 ---VGENLGVG-DTHafhdeTRWREAAAQGMAAQFIEQ--LDKGYAtqlGRWfagGQELSGGQWQKIALSRAYMRRdADI 520
Cdd:COG4608 111 rmtVGDIIAEPlRIH-----GLASKAERRERVAELLELvgLRPEHA---DRY---PHEFSGGQRQRIGIARALALN-PKL 178
|
....*..
gi 488616976 521 LILDEPT 527
Cdd:COG4608 179 IVCDEPV 185
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
359-579 |
7.66e-21 |
|
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: 91.10 E-value: 7.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 359 ENVSFTYPGtsRAALENIDLHLAPGRSvALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDwDEDALRSRIGVIFQ 438
Cdd:cd03264 4 ENLTKRYGK--KRALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 439 DFIRY-QFLVGENL-------GVGDTHAfhdetrwREAAAQGMAAQFIEQLDKGYAtqlgrwfaggQELSGGQWQKIALS 510
Cdd:cd03264 80 EFGVYpNFTVREFLdyiawlkGIPSKEV-------KARVDEVLELVNLGDRAKKKI----------GSLSGGMRRRVGIA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 511 RAyMRRDADILILDEPTAALDAGAEAAVFEHFREYAKGRMTLLISHRFSSVRN-AEHIVVLEHGRVLERG 579
Cdd:cd03264 143 QA-LVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
359-575 |
7.79e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 93.19 E-value: 7.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 359 ENVSFTY-PGT--SRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLqdWDEDA----LRS 431
Cdd:PRK13637 6 ENLTHIYmEGTpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDI--TDKKVklsdIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 432 RIGVIFQdFIRYQfLVGE-----------NLGVGDthafhDETRWREAAAQGMAAQFIEQL-DKGYatqlgrwFaggqEL 499
Cdd:PRK13637 84 KVGLVFQ-YPEYQ-LFEEtiekdiafgpiNLGLSE-----EEIENRVKRAMNIVGLDYEDYkDKSP-------F----EL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488616976 500 SGGQWQKIALSrAYMRRDADILILDEPTAALDAGAEAAVFEHFRE-YAKGRMT-LLISHRFSSV-RNAEHIVVLEHGRV 575
Cdd:PRK13637 146 SGGQKRRVAIA-GVVAMEPKILILDEPTAGLDPKGRDEILNKIKElHKEYNMTiILVSHSMEDVaKLADRIIVMNKGKC 223
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
359-579 |
9.04e-21 |
|
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: 90.74 E-value: 9.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 359 ENVSFTYPGtsRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDwDEDALRsRIGVIFQ 438
Cdd:cd03268 4 NDLTKTYGK--KRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK-NIEALR-RIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 439 DFIRYQFLVG-ENLGVGDThafhdETRWREAAAQgmaaqfiEQLDKGYATQLGRWFAGGqeLSGGQWQKIALSRAYMrRD 517
Cdd:cd03268 80 APGFYPNLTArENLRLLAR-----LLGIRKKRID-------EVLDVVGLKDSAKKKVKG--FSLGMKQRLGIALALL-GN 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488616976 518 ADILILDEPTAALDAGAEAAVFEHFREYAKGRMTLLI-SHRFSSVRN-AEHIVVLEHGRVLERG 579
Cdd:cd03268 145 PDLLILDEPTNGLDPDGIKELRELILSLRDQGITVLIsSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
341-583 |
9.80e-21 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 97.35 E-value: 9.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 341 PSAGSLtqgalpgdgmRFENVSFTYPGTSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSD 420
Cdd:PLN03232 1230 PSRGSI----------KFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCD 1299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 421 LQDWDEDALRSRIGVIFQDFIRYQFLVGENLgvgDTHAFHDETRWREAAAQGMAAQFIEQLDKGYATQLgrwFAGGQELS 500
Cdd:PLN03232 1300 VAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI---DPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEV---SEGGENFS 1373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 501 GGQWQKIALSRAYMRRdADILILDEPTAALDAGAEAAVFEHFREYAKGRMTLLISHRFSSVRNAEHIVVLEHGRVLErgd 580
Cdd:PLN03232 1374 VGQRQLLSLARALLRR-SKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLE--- 1449
|
...
gi 488616976 581 HDS 583
Cdd:PLN03232 1450 YDS 1452
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
358-585 |
1.22e-20 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 91.31 E-value: 1.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 358 FENVSFTYPGTsrAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQD--WDEDALRSRIGV 435
Cdd:PRK09493 4 FKNVSKHFGPT--QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkVDERLIRQEAGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 436 IFQDFIRY-QFLVGENLGVGDTHAfhdetrwREAAAQGMAAQFIEQLDK-GYATQLGRWFAggqELSGGQWQKIALSRAY 513
Cdd:PRK09493 82 VFQQFYLFpHLTALENVMFGPLRV-------RGASKEEAEKQARELLAKvGLAERAHHYPS---ELSGGQQQRVAIARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488616976 514 MRRdADILILDEPTAALDAGAEAAVFEHFREYAKGRMTLLI-SHRFSSVRN-AEHIVVLEHGRVLERGDHDSLI 585
Cdd:PRK09493 152 AVK-PKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIvTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLI 224
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
356-585 |
2.76e-20 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 95.87 E-value: 2.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 356 MRFENVSFTYpgTSRAALE---NIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILL-DGSDLQDWDEDALRS 431
Cdd:PTZ00265 383 IQFKNVRFHY--DTRKDVEiykDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRS 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 432 RIGVIFQDFIRYQFLVGENLGVG----------------DTHAFHDETRWREAAAQGMAAQ------------------- 476
Cdd:PTZ00265 461 KIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyyneDGNDSQENKNKRNSCRAKCAGDlndmsnttdsneliemrkn 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 477 --------------------FIEQLDKGYATQLGrwfAGGQELSGGQWQKIALSRAYMrRDADILILDEPTAALDAGAEA 536
Cdd:PTZ00265 541 yqtikdsevvdvskkvlihdFVSALPDKYETLVG---SNASKLSGGQKQRISIARAII-RNPKILILDEATSSLDNKSEY 616
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 488616976 537 AVFEHFREYA--KGRMTLLISHRFSSVRNAEHIVVLEHGRVLERGDHDSLI 585
Cdd:PTZ00265 617 LVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLSNRERGSTVDVDIIG 667
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
356-576 |
2.83e-20 |
|
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: 89.87 E-value: 2.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 356 MRFENVSFTYPGTSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDwDEDALRSRIGV 435
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 436 IFQDFIRYQFLVG-ENL-------GVGDTHAFHDetrwreaaaqgmAAQFIEQLD-KGYATQLGRwfaggqELSGGQWQK 506
Cdd:cd03263 80 CPQFDALFDELTVrEHLrfyarlkGLPKSEIKEE------------VELLLRVLGlTDKANKRAR------TLSGGMKRK 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488616976 507 IALSRAYMrRDADILILDEPTAALDAGAEAAVFEHFREYAKGRMTLLISHrfsSVRNAE----HIVVLEHGRVL 576
Cdd:cd03263 142 LSLAIALI-GGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTH---SMDEAEalcdRIAIMSDGKLR 211
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
358-579 |
1.00e-19 |
|
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: 87.72 E-value: 1.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 358 FENVSFTYpGTSRAaLENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQdwdeDALRSRIGVIF 437
Cdd:cd03269 3 VENVTKRF-GRVTA-LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD----IAARNRIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 438 QDFIRYQFL-VGENL-------GVGDTHAFHDETRWreaaaqgmaaqfIEQLDKGyatqlGRWFAGGQELSGGQWQKIAL 509
Cdd:cd03269 77 EERGLYPKMkVIDQLvylaqlkGLKKEEARRRIDEW------------LERLELS-----EYANKRVEELSKGNQQKVQF 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488616976 510 SRAYMrRDADILILDEPTAALDAGAEAAVFEHFREYA-KGRMTLLISHRFSSV-RNAEHIVVLEHGRVLERG 579
Cdd:cd03269 140 IAAVI-HDPELLILDEPFSGLDPVNVELLKDVIRELArAGKTVILSTHQMELVeELCDRVLLLNKGRAVLYG 210
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
338-586 |
1.70e-19 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 93.26 E-value: 1.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 338 PVMPSAGSLtqgalpgdgmRFENVSFTYPGTSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLD 417
Cdd:PLN03130 1230 PGWPSSGSI----------KFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILID 1299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 418 GSDLQDWDEDALRSRIGVIFQDFIRYQFLVGENLGVGDTHafHDETRWrEAAAQGMAAQFIEQLDKGYATQLgrwFAGGQ 497
Cdd:PLN03130 1300 GCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEH--NDADLW-ESLERAHLKDVIRRNSLGLDAEV---SEAGE 1373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 498 ELSGGQWQKIALSRAYMRRdADILILDEPTAALDAGAEAAVFEHFREYAKGRMTLLISHRFSSVRNAEHIVVLEHGRVLE 577
Cdd:PLN03130 1374 NFSVGQRQLLSLARALLRR-SKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVE 1452
|
....*....
gi 488616976 578 RGDHDSLIA 586
Cdd:PLN03130 1453 FDTPENLLS 1461
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
356-574 |
2.08e-19 |
|
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: 86.75 E-value: 2.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 356 MRFENVSFTYPG---TSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDlqdwdedALRSR 432
Cdd:cd03250 1 ISVEDASFTWDSgeqETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSI-------AYVSQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 433 IGVIFQDFIRyqflvgENLGVGdthAFHDETRWREAAAqgmAAQF---IEQLDKGYATQLGrwfAGGQELSGGQWQKIAL 509
Cdd:cd03250 74 EPWIQNGTIR------ENILFG---KPFDEERYEKVIK---ACALepdLEILPDGDLTEIG---EKGINLSGGQKQRISL 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488616976 510 SRA-YmrRDADILILDEPTAALDAGAEAAVFEH--FREYAKGRMTLLISHRFSSVRNAEHIVVLEHGR 574
Cdd:cd03250 139 ARAvY--SDADIYLLDDPLSAVDAHVGRHIFENciLGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
355-579 |
2.22e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 88.65 E-value: 2.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 355 GMRFENVSFTY-PGT--SRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDG----SDLQDWDED 427
Cdd:PRK13649 2 GINLQNVSYTYqAGTpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDtlitSTSKNKDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 428 ALRSRIGVIFQdFIRYQFLVG----------ENLGVGDTHAfhdETRWREAAAQ-GMAAQFIEQldkgyatqlgrwfaGG 496
Cdd:PRK13649 82 QIRKKVGLVFQ-FPESQLFEEtvlkdvafgpQNFGVSQEEA---EALAREKLALvGISESLFEK--------------NP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 497 QELSGGQWQKIALSrAYMRRDADILILDEPTAALDAGAEAAVFEHFREYAKGRMTL-LISHRFSSVRN-AEHIVVLEHGR 574
Cdd:PRK13649 144 FELSGGQMRRVAIA-GILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIvLVTHLMDDVANyADFVYVLEKGK 222
|
....*
gi 488616976 575 VLERG 579
Cdd:PRK13649 223 LVLSG 227
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
355-579 |
2.23e-19 |
|
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: 87.78 E-value: 2.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 355 GMRFENVSFTYPGTSraALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQdwDEDALRSRIG 434
Cdd:cd03296 2 SIEVRNVSKRFGDFV--ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDAT--DVPVQERNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 435 VIFQDFIRYQFL-VGENLGVGdTHAFHDETRWREAAAQGMAAQFIE--QLDkgyatqlgrWFAGG--QELSGGQWQKIAL 509
Cdd:cd03296 78 FVFQHYALFRHMtVFDNVAFG-LRVKPRSERPPEAEIRAKVHELLKlvQLD---------WLADRypAQLSGGQRQRVAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488616976 510 SRAyMRRDADILILDEPtaalDAGAEAAVFEHFREYAK------GRMTLLISHRFS-SVRNAEHIVVLEHGRVLERG 579
Cdd:cd03296 148 ARA-LAVEPKVLLLDEP----FGALDAKVRKELRRWLRrlhdelHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVG 219
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
353-586 |
2.26e-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: 88.04 E-value: 2.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 353 GDGMRFENVSFTYPGTSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDALRSR 432
Cdd:cd03288 17 GGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 433 IGVIFQDFIRYQFLVGENLGVGDTHAfhDETRWrEAAAQGMAAQFIEQLDKGYATQLGRwfaGGQELSGGQWQKIALSRA 512
Cdd:cd03288 97 LSIILQDPILFSGSIRFNLDPECKCT--DDRLW-EALEIAQLKNMVKSLPGGLDAVVTE---GGENFSVGQRQLFCLARA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488616976 513 YMRRDAdILILDEPTAALDAGAEAAVFEHFREYAKGRMTLLISHRFSSVRNAEHIVVLEHGRVLERGDHDSLIA 586
Cdd:cd03288 171 FVRKSS-ILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLA 243
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
358-579 |
2.34e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 88.27 E-value: 2.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 358 FENVSFTYPGTSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDALRSRIGVIF 437
Cdd:PRK13648 10 FKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIVF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 438 QDfiryqflvGENLGVGDTHAF------------HDETrwreaaaQGMAAQFIEQLDkgyatQLGRWFAGGQELSGGQWQ 505
Cdd:PRK13648 90 QN--------PDNQFVGSIVKYdvafglenhavpYDEM-------HRRVSEALKQVD-----MLERADYEPNALSGGQKQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488616976 506 KIALSrAYMRRDADILILDEPTAALDAGAEAAVFEHFREYAKGRMTLLIS--HRFSSVRNAEHIVVLEHGRVLERG 579
Cdd:PRK13648 150 RVAIA-GVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISitHDLSEAMEADHVIVMNKGTVYKEG 224
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
357-587 |
2.72e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 87.44 E-value: 2.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 357 RFENVSFTYPGTSRA--------------------ALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILL 416
Cdd:COG1134 6 EVENVSKSYRLYHEPsrslkelllrrrrtrreefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 417 DGsdlqdwdedalrsRIGvifqdfiryqFLVGenLGVGdthaFHDETRWRE-----AAAQGMAAQFIEQLdkgyatqLG- 490
Cdd:COG1134 86 NG-------------RVS----------ALLE--LGAG----FHPELTGREniylnGRLLGLSRKEIDEK-------FDe 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 491 -RWFAGGQE--------LSGGQWQKIALSRAyMRRDADILILDEptaaldagaeaaVF----EHFREYAKGRM------- 550
Cdd:COG1134 130 iVEFAELGDfidqpvktYSSGMRARLAFAVA-TAVDPDILLVDE------------VLavgdAAFQKKCLARIrelresg 196
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 488616976 551 -TLLI-SHRFSSVRN-AEHIVVLEHGRVLERGDHDSLIAA 587
Cdd:COG1134 197 rTVIFvSHSMGAVRRlCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
357-526 |
5.31e-19 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 88.59 E-value: 5.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 357 RFENVSFTYPGTsrAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWdeDALRSRIGVI 436
Cdd:COG3839 5 ELENVSKSYGGV--EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDL--PPKDRNIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 437 FQDFIRYQFL-VGENLGVGDTHAFHDETRWREAAAQgMAAQF-IEQLdkgyatqLGRwFAGgqELSGGQWQKIALSRAyM 514
Cdd:COG3839 81 FQSYALYPHMtVYENIAFPLKLRKVPKAEIDRRVRE-AAELLgLEDL-------LDR-KPK--QLSGGQRQRVALGRA-L 148
|
170
....*....|..
gi 488616976 515 RRDADILILDEP 526
Cdd:COG3839 149 VREPKVFLLDEP 160
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
358-527 |
5.59e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 90.51 E-value: 5.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 358 FENVSFTYPGtsRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGsDL------QDWDEDALRS 431
Cdd:COG0488 1 LENLSKSFGG--RPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-GLrigylpQEPPLDDDLT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 432 RIGVIFQDFIRYQFLVGENLGVGDTHAFHDETRWREAAAQGMaaqfIEQLDkGYA---------TQLGrwFAGGQ----- 497
Cdd:COG0488 78 VLDTVLDGDAELRALEAELEELEAKLAEPDEDLERLAELQEE----FEALG-GWEaearaeeilSGLG--FPEEDldrpv 150
|
170 180 190
....*....|....*....|....*....|.
gi 488616976 498 -ELSGGQWQKIALSRAYMrRDADILILDEPT 527
Cdd:COG0488 151 sELSGGWRRRVALARALL-SEPDLLLLDEPT 180
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
356-579 |
5.99e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 87.48 E-value: 5.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 356 MRFENVSFTY----PGTSRAaLENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRI----LLDGSDLQDWDED 427
Cdd:PRK13643 2 IKFEKVNYTYqpnsPFASRA-LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdIVVSSTSKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 428 ALRSRIGVIFQdFIRYQFLvgENLGVGDTHAFHDETRWREAAAQGMAAQFIEQLdkGYATQLgrWFAGGQELSGGQWQKI 507
Cdd:PRK13643 81 PVRKKVGVVFQ-FPESQLF--EETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMV--GLADEF--WEKSPFELSGGQMRRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488616976 508 ALSrAYMRRDADILILDEPTAALDAGAEAAVFEHFRE-YAKGRMTLLISHRFSSVRN-AEHIVVLEHGRVLERG 579
Cdd:PRK13643 154 AIA-GILAMEPEVLVLDEPTAGLDPKARIEMMQLFESiHQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCG 226
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
360-587 |
6.35e-19 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 90.13 E-value: 6.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 360 NVSFTYPGTSRAALENIDLHLAPGRSVALVGENGSGKT----TLIKLLTRLYQPDQGRILLDGSDLQDWDEDALR----S 431
Cdd:COG4172 13 SVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRrirgN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 432 RIGVIFQD---------FIRYQflVGENLgvgdthAFHdeTRWREAAAQGMAaqfIEQLDK-GY---ATQLGRWfagGQE 498
Cdd:COG4172 93 RIAMIFQEpmtslnplhTIGKQ--IAEVL------RLH--RGLSGAAARARA---LELLERvGIpdpERRLDAY---PHQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 499 LSGGQWQK--IALSRAymrRDADILILDEPTAALDAGAEAAVFEHFREY-AKGRMT-LLISHRFSSVRN-AEHIVVLEHG 573
Cdd:COG4172 157 LSGGQRQRvmIAMALA---NEPDLLIADEPTTALDVTVQAQILDLLKDLqRELGMAlLLITHDLGVVRRfADRVAVMRQG 233
|
250
....*....|....
gi 488616976 574 RVLERGDHDSLIAA 587
Cdd:COG4172 234 EIVEQGPTAELFAA 247
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
359-579 |
8.13e-19 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 86.36 E-value: 8.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 359 ENVSFTYPGtsRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDALRSRIGVIFQ 438
Cdd:PRK13548 6 RNLSVRLGG--RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 439 DF-IRYQFLVGENLGVGDTHAFHDETRWREAAAQGMAAQFIEQLdkgyatqLGRWFaggQELSGGQWQKIALSRAYMRRD 517
Cdd:PRK13548 84 HSsLSFPFTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHL-------AGRDY---PQLSGGEQQRVQLARVLAQLW 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488616976 518 AD-----ILILDEPTAALDAGAEAAVFEHFREYAK--GRMTLLISH------RFssvrnAEHIVVLEHGRVLERG 579
Cdd:PRK13548 154 EPdgpprWLLLDEPTSALDLAHQHHVLRLARQLAHerGLAVIVVLHdlnlaaRY-----ADRIVLLHQGRLVADG 223
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
357-579 |
1.56e-18 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 87.16 E-value: 1.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 357 RFENVSFTYPGTSRA--ALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDALRS--- 431
Cdd:PRK11153 3 ELKNISKVFPQGGRTihALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKarr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 432 RIGVIFQDFiryqflvgeNL----GVGDTHAFHDEtrwreaaAQGMAAQFIEQ-----LDK-GYATQLGRWFAggqELSG 501
Cdd:PRK11153 83 QIGMIFQHF---------NLlssrTVFDNVALPLE-------LAGTPKAEIKArvtelLELvGLSDKADRYPA---QLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 502 GQWQKIALSRAyMRRDADILILDEPTAALDAGAEAAVFEHFREYAK--GRMTLLISHRFSSVRN-AEHIVVLEHGRVLER 578
Cdd:PRK11153 144 GQKQRVAIARA-LASNPKVLLCDEATSALDPATTRSILELLKDINRelGLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQ 222
|
.
gi 488616976 579 G 579
Cdd:PRK11153 223 G 223
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
372-588 |
1.65e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 88.99 E-value: 1.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 372 ALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYqPDQGRILLDGSDLQDWDEDAL---RSRIGVIFQD-------FI 441
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDpnsslnpRL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 442 RYQFLVGENLGVgdtHAFHDETRWREaaAQGMAAQFIEQLDkgyATQLGRWFAggqELSGGQWQKIALSRAYMRRdADIL 521
Cdd:PRK15134 380 NVLQIIEEGLRV---HQPTLSAAQRE--QQVIAVMEEVGLD---PETRHRYPA---EFSGGQRQRIAIARALILK-PSLI 447
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 522 ILDEPTAALDAGAEAAVFEHFREY-AKGRMT-LLISHRFSSVRNAEH-IVVLEHGRVLERGDHDSLIAAA 588
Cdd:PRK15134 448 ILDEPTSSLDKTVQAQILALLKSLqQKHQLAyLFISHDLHVVRALCHqVIVLRQGEVVEQGDCERVFAAP 517
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
357-580 |
1.81e-18 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 87.06 E-value: 1.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 357 RFENVSFTYPGTSRA--ALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDAL---RS 431
Cdd:COG1135 3 ELENLSKTFPTKGGPvtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELraaRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 432 RIGVIFQDFiryqflvgeNLgvgdthafhdetRWREAAAQ---------GMAAQFIEQ-----------LDKG--YATQl 489
Cdd:COG1135 83 KIGMIFQHF---------NL------------LSSRTVAEnvalpleiaGVPKAEIRKrvaellelvglSDKAdaYPSQ- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 490 grwfaggqeLSGGQWQKIALSRAyMRRDADILILDEPTaaldagae----aavfehfREYakGRMTLLISHRFSSVRN-A 564
Cdd:COG1135 141 ---------LSGGQKQRVGIARA-LANNPKVLLCDEATsaldpettrsildllkdinREL--GLTIVLITHEMDVVRRiC 208
|
250
....*....|....*.
gi 488616976 565 EHIVVLEHGRVLERGD 580
Cdd:COG1135 209 DRVAVLENGRIVEQGP 224
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
356-575 |
1.82e-18 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 84.54 E-value: 1.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 356 MRFENVSFTYPGtSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSD---LQDWDEDALRSR 432
Cdd:PRK10908 2 IRFEHVSKAYLG-GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDitrLKNREVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 433 IGVIFQD-FIRYQFLVGENLGVG--DTHAFHDETRWREAAAqgmaaqfieqLDKGYATQLGRWFAggQELSGGQWQKIAL 509
Cdd:PRK10908 81 IGMIFQDhHLLMDRTVYDNVAIPliIAGASGDDIRRRVSAA----------LDKVGLLDKAKNFP--IQLSGGEQQRVGI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488616976 510 SRAYMRRDAdILILDEPTAALDAGAEAAVFEHFREYAK-GRMTLLISHRFSSV-RNAEHIVVLEHGRV 575
Cdd:PRK10908 149 ARAVVNKPA-VLLADEPTGNLDDALSEGILRLFEEFNRvGVTVLMATHDIGLIsRRSYRMLTLSDGHL 215
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
357-526 |
2.31e-18 |
|
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: 84.60 E-value: 2.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 357 RFENVSFTYPGTsrAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWdeDALRSRIGVI 436
Cdd:cd03300 2 ELENVSKFYGGF--VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNL--PPHKRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 437 FQDFIRYQFL-VGENLGVGDTHAFHDETRWREAAAQGMAAQFIEQLDKGYAtqlgrwfaggQELSGGQWQKIALSRAYMR 515
Cdd:cd03300 78 FQNYALFPHLtVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKP----------SQLSGGQQQRVAIARALVN 147
|
170
....*....|.
gi 488616976 516 RDAdILILDEP 526
Cdd:cd03300 148 EPK-VLLLDEP 157
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
357-526 |
2.61e-18 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 86.69 E-value: 2.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 357 RFENVSFTYPGTsrAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLqdwdeDAL---RSRI 433
Cdd:COG3842 7 ELENVSKRYGDV--TALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV-----TGLppeKRNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 434 GVIFQDFIryqfL-----VGENLGVGDTHAfhdetRWREAAAQGMAAQFIEQLD-KGYATQLGRwfaggqELSGGQWQKI 507
Cdd:COG3842 80 GMVFQDYA----LfphltVAENVAFGLRMR-----GVPKAEIRARVAELLELVGlEGLADRYPH------QLSGGQQQRV 144
|
170
....*....|....*....
gi 488616976 508 ALSRAyMRRDADILILDEP 526
Cdd:COG3842 145 ALARA-LAPEPRVLLLDEP 162
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
373-587 |
4.10e-18 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 84.03 E-value: 4.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 373 LENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRI-----LLDGS---DLQDWDEDALRSRIGVIFQDFIRY- 443
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTArslSQQKGLIRQLRQHVGFVFQNFNLFp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 444 QFLVGENLGVGDThAFHDETRwREAAAQGMaaqfiEQLDK-GYAtqlGRWFAGGQELSGGQWQKIALSRAYMRRdADILI 522
Cdd:PRK11264 99 HRTVLENIIEGPV-IVKGEPK-EEATARAR-----ELLAKvGLA---GKETSYPRRLSGGQQQRVAIARALAMR-PEVIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488616976 523 LDEPTAALDAGAEAAVFEHFREYAKGRMTLLI-SHRFSSVRN-AEHIVVLEHGRVLERGDHDSLIAA 587
Cdd:PRK11264 168 FDEPTSALDPELVGEVLNTIRQLAQEKRTMVIvTHEMSFARDvADRAIFMDQGRIVEQGPAKALFAD 234
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
365-555 |
4.51e-18 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 82.47 E-value: 4.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 365 YPGTSRAaLENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLqDWDEDAL---RSRIGVIFQDFI 441
Cdd:TIGR01166 1 YPGGPEV-LKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPL-DYSRKGLlerRQRVGLVFQDPD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 442 RYQFL--VGE-------NLGVGDTHAfhdETRWREA-AAQGMAaqfieqldkGYATQLGrwfaggQELSGGQWQKIALSR 511
Cdd:TIGR01166 79 DQLFAadVDQdvafgplNLGLSEAEV---ERRVREAlTAVGAS---------GLRERPT------HCLSGGEKKRVAIAG 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488616976 512 AYMRRdADILILDEPTAALDAGAEAAVFEHFREYAKGRMTLLIS 555
Cdd:TIGR01166 141 AVAMR-PDVLLLDEPTAGLDPAGREQMLAILRRLRAEGMTVVIS 183
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
356-579 |
4.62e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 84.83 E-value: 4.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 356 MRFENVSFTY-PGT--SRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDA---- 428
Cdd:PRK13646 3 IRFDNVSYTYqKGTpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKyirp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 429 LRSRIGVIFQ--------DFIRYQFLVG-ENLGVGdthafhdetrwreaaaqgmaaqfIEQLdKGYATQLGRWFAGGQ-- 497
Cdd:PRK13646 83 VRKRIGMVFQfpesqlfeDTVEREIIFGpKNFKMN-----------------------LDEV-KNYAHRLLMDLGFSRdv 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 498 ------ELSGGQWQKIALSrAYMRRDADILILDEPTAALDAGAEAAVFEHFREYA--KGRMTLLISHRFSSV-RNAEHIV 568
Cdd:PRK13646 139 msqspfQMSGGQMRKIAIV-SILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVI 217
|
250
....*....|.
gi 488616976 569 VLEHGRVLERG 579
Cdd:PRK13646 218 VMKEGSIVSQT 228
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
356-587 |
5.99e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 84.86 E-value: 5.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 356 MRFENVSFTYpgTSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDAlRSRIGV 435
Cdd:PRK13537 8 IDFRNVEKRY--GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-RQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 436 IFQ-DFIRYQFLVGENLGVgdthaFHDETRWREAAAQGMAAQFIEqldkgYATQLGRWFAGGQELSGGQWQKIALSRAYM 514
Cdd:PRK13537 85 VPQfDNLDPDFTVRENLLV-----FGRYFGLSAAAARALVPPLLE-----FAKLENKADAKVGELSGGMKRRLTLARALV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488616976 515 rRDADILILDEPTAALDAGAEAAVFEHFRE-YAKGRMTLLISHRFSSV-RNAEHIVVLEHGRVLERGDHDSLIAA 587
Cdd:PRK13537 155 -NDPDVLVLDEPTTGLDPQARHLMWERLRSlLARGKTILLTTHFMEEAeRLCDRLCVIEEGRKIAEGAPHALIES 228
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
359-590 |
7.24e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 84.39 E-value: 7.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 359 ENVSFTYpgTSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDedalRSRIGvifq 438
Cdd:COG4152 5 KGLTKRF--GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRRIG---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 439 dfiryqFLVGE-----NLGVGDTHAF----HDETRwREAAAQgmAAQFIEQLDKGyatqlGRWFAGGQELSGGQWQKIAL 509
Cdd:COG4152 75 ------YLPEErglypKMKVGEQLVYlarlKGLSK-AEAKRR--ADEWLERLGLG-----DRANKKVEELSKGNQQKVQL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 510 SRAYMrRDADILILDEPtaaldagaeaavFEHF------------REYA-KGRMTLLISHRFSSV-RNAEHIVVLEHGRV 575
Cdd:COG4152 141 IAALL-HDPELLILDEP------------FSGLdpvnvellkdviRELAaKGTTVIFSSHQMELVeELCDRIVIINKGRK 207
|
250
....*....|....*
gi 488616976 576 LERGDHDSLIAAAGR 590
Cdd:COG4152 208 VLSGSVDEIRRQFGR 222
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
349-585 |
9.30e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 84.88 E-value: 9.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 349 GALPGDGMRFENVSFTYPGtsRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDA 428
Cdd:PRK13536 35 GSMSTVAIDLAGVSKSYGD--KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 429 lRSRIGVIFQ-DFIRYQFLVGENLGVGDTHaFHDETRWREAAAQGMaAQFiEQLDKGYATQLGrwfaggqELSGGQWQKI 507
Cdd:PRK13536 113 -RARIGVVPQfDNLDLEFTVRENLLVFGRY-FGMSTREIEAVIPSL-LEF-ARLESKADARVS-------DLSGGMKRRL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 508 ALSRAYMrRDADILILDEPTAALDAGAEAAVFEHFRE-YAKGRMTLLISHRFSSV-RNAEHIVVLEHGRVLERGDHDSLI 585
Cdd:PRK13536 182 TLARALI-NDPQLLILDEPTTGLDPHARHLIWERLRSlLARGKTILLTTHFMEEAeRLCDRLCVLEAGRKIAEGRPHALI 260
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
340-526 |
1.28e-17 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 82.80 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 340 MPSAGSLTQGaLPgdgMRFENVSFTYPGtsRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGS 419
Cdd:PRK11247 1 MMNTARLNQG-TP---LLLNAVSKRYGE--RTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 420 DLQDWDEDalrsrIGVIFQDfirYQFL----VGENLGVGDThafhdeTRWREAAAQGMAAQfieqldkGYATQLGRWFAG 495
Cdd:PRK11247 75 PLAEARED-----TRLMFQD---ARLLpwkkVIDNVGLGLK------GQWRDAALQALAAV-------GLADRANEWPAA 133
|
170 180 190
....*....|....*....|....*....|.
gi 488616976 496 gqeLSGGQWQKIALSRAYMRRDAdILILDEP 526
Cdd:PRK11247 134 ---LSGGQKQRVALARALIHRPG-LLLLDEP 160
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
356-526 |
1.42e-17 |
|
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: 81.53 E-value: 1.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 356 MRFENVSFTYPGTSraALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDW---DEDalrsr 432
Cdd:cd03301 1 VELENVTKRFGNVT--ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLppkDRD----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 433 IGVIFQDFIRYQFL-VGENLGVGDT--HAFHDE--TRWREAAA--QgmaaqfIEQLDKGYATQlgrwfaggqeLSGGQWQ 505
Cdd:cd03301 74 IAMVFQNYALYPHMtVYDNIAFGLKlrKVPKDEidERVREVAEllQ------IEHLLDRKPKQ----------LSGGQRQ 137
|
170 180
....*....|....*....|.
gi 488616976 506 KIALSRAyMRRDADILILDEP 526
Cdd:cd03301 138 RVALGRA-IVREPKVFLMDEP 157
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
358-589 |
2.03e-17 |
|
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: 86.54 E-value: 2.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 358 FENVSFTYPGTSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDALRSRIGVIF 437
Cdd:TIGR00957 1287 FRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIP 1366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 438 QDFIRYQFLVGENLgvGDTHAFHDETRWReAAAQGMAAQFIEQLDKGYATQLGRwfaGGQELSGGQWQKIALSRAYMRRd 517
Cdd:TIGR00957 1367 QDPVLFSGSLRMNL--DPFSQYSDEEVWW-ALELAHLKTFVSALPDKLDHECAE---GGENLSVGQRQLVCLARALLRK- 1439
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488616976 518 ADILILDEPTAALDAGAEAAVFEHFREYAKGRMTLLISHRFSSVRNAEHIVVLEHGRVLERGDHDSLIAAAG 589
Cdd:TIGR00957 1440 TKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRG 1511
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
357-579 |
2.38e-17 |
|
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: 82.05 E-value: 2.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 357 RFENVSFTYPGtsRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQG---RILldGSDLQDWDEDALRSRI 433
Cdd:COG1119 5 ELRNVTVRRGG--KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvRLF--GERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 434 GVIFQDFIRYqFLVGENlgVGDT--HAFHDET-RWRE--AAAQGMAAQFIEQLD-KGYATQlgRWfaggQELSGGQWQKI 507
Cdd:COG1119 81 GLVSPALQLR-FPRDET--VLDVvlSGFFDSIgLYREptDEQRERARELLELLGlAHLADR--PF----GTLSQGEQRRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 508 ALSRAYMrRDADILILDEPTAALDAGAEAAVFEHFREYAKGRMT--LLISHR-------FSsvrnaeHIVVLEHGRVLER 578
Cdd:COG1119 152 LIARALV-KDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPtlVLVTHHveeippgIT------HVLLLKDGRVVAA 224
|
.
gi 488616976 579 G 579
Cdd:COG1119 225 G 225
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
357-590 |
3.00e-17 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 82.04 E-value: 3.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 357 RFENVSFTYPGTSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDED---ALRSRI 433
Cdd:PRK10419 12 HYAHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAqrkAFRRDI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 434 GVIFQDFI---RYQFLVGENLGVGDTHAfhdeTRWREAAAQGMAAQFIEQ--LDKGYATQLgrwfagGQELSGGQWQKIA 508
Cdd:PRK10419 92 QMVFQDSIsavNPRKTVREIIREPLRHL----LSLDKAERLARASEMLRAvdLDDSVLDKR------PPQLSGGQLQRVC 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 509 LSRAyMRRDADILILDEPTAALDAGAEAAVFEHFREYAKGRMT--LLISHRFSSV-RNAEHIVVLEHGRVLER---GDHD 582
Cdd:PRK10419 162 LARA-LAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTacLFITHDLRLVeRFCQRVMVMDNGQIVETqpvGDKL 240
|
....*...
gi 488616976 583 SLIAAAGR 590
Cdd:PRK10419 241 TFSSPAGR 248
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
360-587 |
3.02e-17 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 86.24 E-value: 3.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 360 NVSFTYPGTSRAAL-ENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLY------------------------QPDQ--- 411
Cdd:PTZ00265 1170 DVNFRYISRPNVPIyKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYdlkndhhivfknehtndmtneqdyQGDEeqn 1249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 412 ---------------------------GRILLDGSDLQDWDEDALRSRIGVIFQDFIRYQFLVGENLGVGDthafHDETR 464
Cdd:PTZ00265 1250 vgmknvnefsltkeggsgedstvfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGK----EDATR 1325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 465 WREAAAQGMAA--QFIEQLDKGYATQLGRWfagGQELSGGQWQKIALSRAYMrRDADILILDEPTAALDAGAEAAVFEHF 542
Cdd:PTZ00265 1326 EDVKRACKFAAidEFIESLPNKYDTNVGPY---GKSLSGGQKQRIAIARALL-REPKILLLDEATSSLDSNSEKLIEKTI 1401
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 488616976 543 REYAK--GRMTLLISHRFSSVRNAEHIVVLEH-----GRVLERGDHDSLIAA 587
Cdd:PTZ00265 1402 VDIKDkaDKTIITIAHRIASIKRSDKIVVFNNpdrtgSFVQAHGTHEELLSV 1453
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
369-595 |
3.07e-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: 81.92 E-value: 3.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 369 SRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDALRS----RIGVIFQDFIRYq 444
Cdd:cd03294 36 QTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALL- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 445 flvgENLGVGDTHAFHDETRWR-EAAAQGMAAQFIEQLD-KGYATQLGRwfaggqELSGGQWQKIALSRAyMRRDADILI 522
Cdd:cd03294 115 ----PHRTVLENVAFGLEVQGVpRAEREERAAEALELVGlEGWEHKYPD------ELSGGMQQRVGLARA-LAVDPDILL 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488616976 523 LDEPTAALDAGAEAAVFEHFREYAK--GRMTLLISHRFS-SVRNAEHIVVLEHGRVLERGDHDSLIAA-AGRYAALF 595
Cdd:cd03294 184 MDEAFSALDPLIRREMQDELLRLQAelQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTNpANDYVREF 260
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
373-580 |
5.79e-17 |
|
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: 80.46 E-value: 5.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 373 LENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDalRSRIGVIFQDFIRYQFL-VGENL 451
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFPHMtVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 452 GVGDTHAFHD----ETRWREAAAQ-GMAaqfiEQLDKGYATqlgrwfaggqeLSGGQWQKIALSRAYMrRDADILILDEP 526
Cdd:cd03299 93 AYGLKKRKVDkkeiERKVLEIAEMlGID----HLLNRKPET-----------LSGGEQQRVAIARALV-VNPKILLLDEP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488616976 527 TAALDAGAEAAVFEHFREYAKGRMT--LLISHRFSSVRN-AEHIVVLEHGRVLERGD 580
Cdd:cd03299 157 FSALDVRTKEKLREELKKIRKEFGVtvLHVTHDFEEAWAlADKVAIMLNGKLIQVGK 213
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
357-574 |
6.35e-17 |
|
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: 77.87 E-value: 6.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 357 RFENVSFTYPGtsRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRIlldgsdlqdwdedalrsrigvi 436
Cdd:cd03221 2 ELENLSKTYGG--KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV---------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 437 fqdfiryqfLVGENLGVGdthafhdetrwreaaaqgmaaqFIEQldkgyatqlgrwfaggqeLSGGQWQKIALSRAyMRR 516
Cdd:cd03221 58 ---------TWGSTVKIG----------------------YFEQ------------------LSGGEKMRLALAKL-LLE 87
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488616976 517 DADILILDEPTAALDAGAEAAVFEHFREYaKGRMtLLISHRFSSVRN-AEHIVVLEHGR 574
Cdd:cd03221 88 NPNLLLLDEPTNHLDLESIEALEEALKEY-PGTV-ILVSHDRYFLDQvATKIIELEDGK 144
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
372-584 |
7.70e-17 |
|
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: 79.72 E-value: 7.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 372 ALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDwDEDALRSRIGVIFQDFIRYQFLVG-EN 450
Cdd:cd03265 15 AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSVDDELTGwEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 451 LGVGDTHAFHDETRWREAAAQGMAaqFIEQLDKgyATQLGRWFaggqelSGGQWQKIALSRAYMRRdADILILDEPTAAL 530
Cdd:cd03265 94 LYIHARLYGVPGAERRERIDELLD--FVGLLEA--ADRLVKTY------SGGMRRRLEIARSLVHR-PEVLFLDEPTIGL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488616976 531 DAGAEAAVFEHFREY-AKGRMT-LLISHRFSSVRN-AEHIVVLEHGRVLERGDHDSL 584
Cdd:cd03265 163 DPQTRAHVWEYIEKLkEEFGMTiLLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
356-574 |
8.49e-17 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 83.44 E-value: 8.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 356 MRfeNVSFTYPGTSraALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYqPD---QGRILLDGSDLQDWD-EDALRS 431
Cdd:PRK13549 8 MK--NITKTFGGVK--ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNiRDTERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 432 RIGVIFQDFIRYQFL-VGENLGVGDTHAFHDETRWRE--AAAQGMAAQFieQLDKGYATQLGrwfaggqELSGGQWQKIA 508
Cdd:PRK13549 83 GIAIIHQELALVKELsVLENIFLGNEITPGGIMDYDAmyLRAQKLLAQL--KLDINPATPVG-------NLGLGQQQLVE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488616976 509 LSRAyMRRDADILILDEPTAALDAGAEAAVFEHFREY-AKGRMTLLISHRFSSVRN-AEHIVVLEHGR 574
Cdd:PRK13549 154 IAKA-LNKQARLLILDEPTASLTESETAVLLDIIRDLkAHGIACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
359-579 |
9.59e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 80.90 E-value: 9.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 359 ENVSFTY----PGTSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQD----WDedaLR 430
Cdd:PRK13633 8 KNVSYKYesneESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDeenlWD---IR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 431 SRIGVIFQD--------FIRYQFLVG-ENLGVGDthafhDETRWR--EA-AAQGMAAQfieqldKGYATQLgrwfaggqe 498
Cdd:PRK13633 85 NKAGMVFQNpdnqivatIVEEDVAFGpENLGIPP-----EEIRERvdESlKKVGMYEY------RRHAPHL--------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 499 LSGGQWQKIALSRAYMRRdADILILDEPTAALDAGAEAAVFEHFREYAK--GRMTLLISHRFSSVRNAEHIVVLEHGRVL 576
Cdd:PRK13633 145 LSGGQKQRVAIAGILAMR-PECIIFDEPTAMLDPSGRREVVNTIKELNKkyGITIILITHYMEEAVEADRIIVMDSGKVV 223
|
...
gi 488616976 577 ERG 579
Cdd:PRK13633 224 MEG 226
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
356-600 |
1.34e-16 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 79.67 E-value: 1.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 356 MRFENVSFTYpGTSRAaLENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDALRSRIGV 435
Cdd:PRK11231 3 LRTENLTVGY-GTKRI-LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 436 IFQdfiryQFLVGENLGVGDTHAF--------------HDETRwreaAAQGMAAQFIEQLDKGYATqlgrwfaggqELSG 501
Cdd:PRK11231 81 LPQ-----HHLTPEGITVRELVAYgrspwlslwgrlsaEDNAR----VNQAMEQTRINHLADRRLT----------DLSG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 502 GQWQKIALSRAyMRRDADILILDEPTAALDAGAEAAVFEHFREY-AKGRMTLLISHRFS-SVRNAEHIVVLEHGRVLERG 579
Cdd:PRK11231 142 GQRQRAFLAMV-LAQDTPVVLLDEPTTYLDINHQVELMRLMRELnTQGKTVVTVLHDLNqASRYCDHLVVLANGHVMAQG 220
|
250 260
....*....|....*....|.
gi 488616976 580 DHDSLIaAAGRYAALFDLQAQ 600
Cdd:PRK11231 221 TPEEVM-TPGLLRTVFDVEAE 240
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
363-586 |
2.00e-16 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 80.78 E-value: 2.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 363 FTYPGTSRAaLENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDA---LRSRIGVIFQD 439
Cdd:PRK11308 22 FKPERLVKA-LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAqklLRQKIQIVFQN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 440 fiRYQFL-----VGENLG---VGDTHAFHDEtrwREAAAQGMAAQFieQLDKGYATQLGRWFaggqelSGGQWQKIALSR 511
Cdd:PRK11308 101 --PYGSLnprkkVGQILEeplLINTSLSAAE---RREKALAMMAKV--GLRPEHYDRYPHMF------SGGQRQRIAIAR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 512 AYMrRDADILILDEPTAALDAGAEAAVFEHF----REYakGRMTLLISHRFSSVRN-AEHIVVLEHGRVLERGDHDSLIA 586
Cdd:PRK11308 168 ALM-LDPDVVVADEPVSALDVSVQAQVLNLMmdlqQEL--GLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFN 244
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
359-527 |
2.03e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 79.36 E-value: 2.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 359 ENVSFT-YPGTS--RAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDAlRSR-IG 434
Cdd:COG1101 5 KNLSKTfNPGTVneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYK-RAKyIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 435 VIFQDFiryqfLVG--------ENLGV----GDTHAFhdetRWREAAAQgmAAQFIEQLdkgyaTQLGRwfagGQE---- 498
Cdd:COG1101 84 RVFQDP-----MMGtapsmtieENLALayrrGKRRGL----RRGLTKKR--RELFRELL-----ATLGL----GLEnrld 143
|
170 180 190
....*....|....*....|....*....|....
gi 488616976 499 -----LSGGQWQKIALSRAYMRRdADILILDEPT 527
Cdd:COG1101 144 tkvglLSGGQRQALSLLMATLTK-PKLLLLDEHT 176
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
356-583 |
2.41e-16 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 78.90 E-value: 2.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 356 MRFENVSFTYpGTSRAaLENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGS--DL-QDWDEDA---L 429
Cdd:PRK11124 3 IQLNGINCFY-GAHQA-LFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFsKTPSDKAireL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 430 RSRIGVIFQDFIRYQFL-VGENL--------GVGdthafhdetrwrEAAAQGMAAQFIEQLD-KGYAtqlGRWfagGQEL 499
Cdd:PRK11124 81 RRNVGMVFQQYNLWPHLtVQQNLieapcrvlGLS------------KDQALARAEKLLERLRlKPYA---DRF---PLHL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 500 SGGQWQKIALSRAYMRRdADILILDEPTAALDAGAEAAVFEHFREYAKGRMTLLI-SHRFSSVRN-AEHIVVLEHGRVLE 577
Cdd:PRK11124 143 SGGQQQRVAIARALMME-PQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIvTHEVEVARKtASRVVYMENGHIVE 221
|
....*.
gi 488616976 578 RGDHDS 583
Cdd:PRK11124 222 QGDASC 227
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
356-525 |
2.42e-16 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 82.33 E-value: 2.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 356 MRFENVSFTYPGTSrAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDALRSRIGV 435
Cdd:PRK10522 323 LELRNVTFAYQDNG-FSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 436 IFQDFIRYQFLVGENlgvgdthafhdetrwREAAAQGMAAQFIEQLDKGYATQLGRWFAGGQELSGGQWQKIALSRAyMR 515
Cdd:PRK10522 402 VFTDFHLFDQLLGPE---------------GKPANPALVEKWLERLKMAHKLELEDGRISNLKLSKGQKKRLALLLA-LA 465
|
170
....*....|
gi 488616976 516 RDADILILDE 525
Cdd:PRK10522 466 EERDILLLDE 475
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
360-596 |
2.54e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 81.43 E-value: 2.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 360 NVSFTYPGTSraALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDALRSRIGVIFQD 439
Cdd:PRK09536 8 DLSVEFGDTT--VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 440 F-IRYQFLVGENLGVG--------DTHAFHDETRWREAAAQGMAAQFIEQldkgyatqlgrwfaGGQELSGGQWQKIALS 510
Cdd:PRK09536 86 TsLSFEFDVRQVVEMGrtphrsrfDTWTETDRAAVERAMERTGVAQFADR--------------PVTSLSGGERQRVLLA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 511 RAyMRRDADILILDEPTAALDAGAEAAVFEHFREYAK-GRMTLLISHRFS-SVRNAEHIVVLEHGRVLERGDHDSLIaAA 588
Cdd:PRK09536 152 RA-LAQATPVLLLDEPTASLDINHQVRTLELVRRLVDdGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVL-TA 229
|
....*...
gi 488616976 589 GRYAALFD 596
Cdd:PRK09536 230 DTLRAAFD 237
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
356-527 |
3.46e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 81.65 E-value: 3.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 356 MRFENVSFTYPGtsRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLdgsdlqdwdedalrsrigv 435
Cdd:COG0488 316 LELEGLSKSYGD--KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL------------------- 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 436 ifqdfiryqflvGENLGVG----DTHAFHDETRWREAAAQGMaaqfiEQLDKGYATQ-LGRW-FAGGQ------ELSGGQ 503
Cdd:COG0488 375 ------------GETVKIGyfdqHQEELDPDKTVLDELRDGA-----PGGTEQEVRGyLGRFlFSGDDafkpvgVLSGGE 437
|
170 180
....*....|....*....|....
gi 488616976 504 WQKIALSRAyMRRDADILILDEPT 527
Cdd:COG0488 438 KARLALAKL-LLSPPNVLLLDEPT 460
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
359-589 |
3.90e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 79.01 E-value: 3.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 359 ENVSFTYPGTSRAaLENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDALRSRIGVIFQ 438
Cdd:PRK13647 8 EDLHFRYKDGTKA-LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 439 DfiryqflvgenlgvGDTHAFhDETRWREAA----AQGMAAQFIEQLDKGYATQLGRW-FA--GGQELSGGQWQKIALSr 511
Cdd:PRK13647 87 D--------------PDDQVF-SSTVWDDVAfgpvNMGLDKDEVERRVEEALKAVRMWdFRdkPPYHLSYGQKKRVAIA- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 512 AYMRRDADILILDEPTAALDAGAEAAVFEHF-REYAKGRMTLLISHRFS-SVRNAEHIVVLEHGRVLERGD-----HDSL 584
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLDPRGQETLMEILdRLHNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGDkslltDEDI 230
|
....*
gi 488616976 585 IAAAG 589
Cdd:PRK13647 231 VEQAG 235
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
372-579 |
4.75e-16 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 77.76 E-value: 4.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 372 ALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGsdLQDWDE-DALRSRIGVIFQDfiRYQflVGEN 450
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG--LVPWKRrKKFLRRIGVVFGQ--KTQ--LWWD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 451 LGVGDTHAFHDET-RWREAAAQGMAAQFIEQLDKG--YATQLgrwfaggQELSGGQWQKIALSRAYMrRDADILILDEPT 527
Cdd:cd03267 110 LPVIDSFYLLAAIyDLPPARFKKRLDELSELLDLEelLDTPV-------RQLSLGQRMRAEIAAALL-HEPEILFLDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488616976 528 AALDAGAEAAVFEHFREYAKGRMT--LLISHRFSSV-RNAEHIVVLEHGRVLERG 579
Cdd:cd03267 182 IGLDVVAQENIRNFLKEYNRERGTtvLLTSHYMKDIeALARRVLVIDKGRLLYDG 236
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
356-579 |
4.86e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 78.91 E-value: 4.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 356 MRFENVSFTY-PGT--SRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLdGSDL-----QDWDED 427
Cdd:PRK13634 3 ITFQKVEHRYqYKTpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVitagkKNKKLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 428 ALRSRIGVIFQdFIRYQfLVGE-----------NLGVgdthafhdetrwREAAAQGMAAQFIEQ--LDKGYATQlgrwfa 494
Cdd:PRK13634 82 PLRKKVGIVFQ-FPEHQ-LFEEtvekdicfgpmNFGV------------SEEDAKQKAREMIELvgLPEELLAR------ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 495 GGQELSGGQWQKIALSrAYMRRDADILILDEPTAALDAGAEAAVFEHF----REyaKGRMTLLISHRFSSVRN-AEHIVV 569
Cdd:PRK13634 142 SPFELSGGQMRRVAIA-GVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFyklhKE--KGLTTVLVTHSMEDAARyADQIVV 218
|
250
....*....|
gi 488616976 570 LEHGRVLERG 579
Cdd:PRK13634 219 MHKGTVFLQG 228
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
356-588 |
5.10e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 78.49 E-value: 5.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 356 MRFENVSFTYPGTSRAalENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDALRSRIGV 435
Cdd:PRK10253 8 LRGEQLTLGYGKYTVA--ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 436 IFQDF-----IRYQFLVGENlgvgdtHAFHDE--TRWR----EAAAQGMAAQFIEQLdkgyATQlgrwfaGGQELSGGQW 504
Cdd:PRK10253 86 LAQNAttpgdITVQELVARG------RYPHQPlfTRWRkedeEAVTKAMQATGITHL----ADQ------SVDTLSGGQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 505 QK--IALSRAymrRDADILILDEPTAALDAGAEAAVFEHFREY--AKGRMTLLISHRFS-SVRNAEHIVVLEHGRVLERG 579
Cdd:PRK10253 150 QRawIAMVLA---QETAIMLLDEPTTWLDISHQIDLLELLSELnrEKGYTLAAVLHDLNqACRYASHLIALREGKIVAQG 226
|
....*....
gi 488616976 580 DHDSLIAAA 588
Cdd:PRK10253 227 APKEIVTAE 235
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
318-592 |
5.21e-16 |
|
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: 82.30 E-value: 5.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 318 ISGLYEDGLYLADLYIYLGQPVMPSAGSLTQGALPGDG--MRFENVSFTYPGTSRAALENIDLHLAPGRSVALVGENGSG 395
Cdd:TIGR00957 597 ISSIVQASVSLKRLRIFLSHEELEPDSIERRTIKPGEGnsITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCG 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 396 KTTLIKLLTRLYQPDQGRILLDGS----DLQDWdedalrsrigvIFQDFIRYQFLVGENLgvgdthafhDETRWREAAAQ 471
Cdd:TIGR00957 677 KSSLLSALLAEMDKVEGHVHMKGSvayvPQQAW-----------IQNDSLRENILFGKAL---------NEKYYQQVLEA 736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 472 GMAAQFIEQLDKGYATQLGRwfaGGQELSGGQWQKIALSRAyMRRDADILILDEPTAALDAGAEAAVFEHF---REYAKG 548
Cdd:TIGR00957 737 CALLPDLEILPSGDRTEIGE---KGVNLSGGQKQRVSLARA-VYSNADIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKN 812
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 488616976 549 RMTLLISHRFSSVRNAEHIVVLEHGRVLERGDHDSLIAAAGRYA 592
Cdd:TIGR00957 813 KTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFA 856
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
356-573 |
6.08e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 80.98 E-value: 6.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 356 MRFENVSFTYPGTSraALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWD-EDALRSRIG 434
Cdd:PRK09700 6 ISMAGIGKSFGPVH--ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDhKLAAQLGIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 435 VIFQDF-IRYQFLVGENLGVGD--THAFH--DETRWREaaaqgMAAQFIEQLDK-GYATQLGRWFAggqELSGGQWQKIA 508
Cdd:PRK09700 84 IIYQELsVIDELTVLENLYIGRhlTKKVCgvNIIDWRE-----MRVRAAMMLLRvGLKVDLDEKVA---NLSISHKQMLE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488616976 509 LSRAYMrRDADILILDEPTAALDAGAEAAVFEHFREYAK-GRMTLLISHRFSSVRN-AEHIVVLEHG 573
Cdd:PRK09700 156 IAKTLM-LDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKeGTAIVYISHKLAEIRRiCDRYTVMKDG 221
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
377-579 |
1.11e-15 |
|
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: 75.99 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 377 DLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDwdEDALRSRIGVIFQDFIRYQFL-VGENLGVGD 455
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTA--APPADRPVSMLFQENNLFAHLtVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 456 THAFHDETRWREAAAQGMAAQFIEQLDKGYAtqlgrwfaggQELSGGQWQKIALSRAYMrRDADILILDEPTAALDAGAE 535
Cdd:cd03298 96 SPGLKLTAEDRQAIEVALARVGLAGLEKRLP----------GELSGGERQRVALARVLV-RDKPVLLLDEPFAALDPALR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488616976 536 AAVFEHFRE-YAKGRMTLLI-SHRFS-SVRNAEHIVVLEHGRVLERG 579
Cdd:cd03298 165 AEMLDLVLDlHAETKMTVLMvTHQPEdAKRLAQRVVFLDNGRIAAQG 211
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
370-556 |
1.60e-15 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 75.47 E-value: 1.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 370 RAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDALRSRIGVIFQDFIRYQFLVGE 449
Cdd:TIGR01189 13 RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSALE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 450 NLGV-GDTHAFHDETRWREAAAQGMAAqfIEQLDKGYatqlgrwfaggqeLSGGQWQKIALSRAYMRRdADILILDEPTA 528
Cdd:TIGR01189 93 NLHFwAAIHGGAQRTIEDALAAVGLTG--FEDLPAAQ-------------LSAGQQRRLALARLWLSR-RPLWILDEPTT 156
|
170 180
....*....|....*....|....*....
gi 488616976 529 ALDAGAEAAVFEHFREY-AKGRMTLLISH 556
Cdd:TIGR01189 157 ALDKAGVALLAGLLRAHlARGGIVLLTTH 185
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
375-579 |
1.64e-15 |
|
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: 75.79 E-value: 1.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 375 NIDLHLaPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQD----WDEDALRSRIGVIFQDFIRYQFL-VGE 449
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrkkINLPPQQRKIGLVFQQYALFPHLnVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 450 NLGVGDTHAFHDETRWREAaaqgmaaqfiEQLDKGYATQLGrwFAGGQELSGGQWQKIALSRAyMRRDADILILDEPTAA 529
Cdd:cd03297 95 NLAFGLKRKRNREDRISVD----------ELLDLLGLDHLL--NRYPAQLSGGEKQRVALARA-LAAQPELLLLDEPFSA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488616976 530 LDAGAEAAVFEHFREYAK--GRMTLLISHRFSSV-RNAEHIVVLEHGRVLERG 579
Cdd:cd03297 162 LDRALRLQLLPELKQIKKnlNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
356-526 |
3.49e-15 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 75.50 E-value: 3.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 356 MRFENVSFTYPGTsrAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDALRSRIGV 435
Cdd:COG4604 2 IEIKNVSKRYGGK--VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 436 IFQdfiryqflvgEN-----LGVGDTHAF------------HDETRWREAAAQ----GMAAQFIEqldkgyatqlgrwfa 494
Cdd:COG4604 80 LRQ----------ENhinsrLTVRELVAFgrfpyskgrltaEDREIIDEAIAYldleDLADRYLD--------------- 134
|
170 180 190
....*....|....*....|....*....|....*.
gi 488616976 495 ggqELSGGQWQkialsRAY----MRRDADILILDEP 526
Cdd:COG4604 135 ---ELSGGQRQ-----RAFiamvLAQDTDYVLLDEP 162
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
360-579 |
5.86e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 75.50 E-value: 5.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 360 NVSFTYP-GTSraALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLqDWDEDAL---RSRIGV 435
Cdd:PRK13639 6 DLKYSYPdGTE--ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLlevRKTVGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 436 IFQDFIRYQF--LVGE-------NLGVGDTHAfhdETRWREA-AAQGMaaqfieqldKGYATQlgrwfaGGQELSGGQWQ 505
Cdd:PRK13639 83 VFQNPDDQLFapTVEEdvafgplNLGLSKEEV---EKRVKEAlKAVGM---------EGFENK------PPHHLSGGQKK 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488616976 506 KIALSrAYMRRDADILILDEPTAALDAGAEAAVFEHFREYAKGRMTLLIS-HRFSSV-RNAEHIVVLEHGRVLERG 579
Cdd:PRK13639 145 RVAIA-GILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIIStHDVDLVpVYADKVYVMSDGKIIKEG 219
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
356-575 |
6.31e-15 |
|
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: 75.28 E-value: 6.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 356 MRFENVSFTYPGTSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDqGRILLDGSD-----LQDWdedalR 430
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSwnsvpLQKW-----R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 431 SRIGVIFQDFIRYQFLVGENLGVGDTHAfhDETRWREAAAQGMAA---QFIEQLDkgyaTQLgrwFAGGQELSGGQWQKI 507
Cdd:cd03289 77 KAFGVIPQKVFIFSGTFRKNLDPYGKWS--DEEIWKVAEEVGLKSvieQFPGQLD----FVL---VDGGCVLSHGHKQLM 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488616976 508 ALSRAYMRRdADILILDEPTAALDAGAEAAVFEHFREYAKGRMTLLISHRFSSVRNAEHIVVLEHGRV 575
Cdd:cd03289 148 CLARSVLSK-AKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKV 214
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
372-579 |
9.27e-15 |
|
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: 73.72 E-value: 9.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 372 ALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSdlqdwdedaLRSRIGvifqdfiryqflvgenL 451
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR---------VSSLLG----------------L 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 452 GVGdthaFHDETRWRE-----AAAQGMAAQFIEQ-LDKGYA-TQLGRWF-AGGQELSGGQWQKIALSRAyMRRDADILIL 523
Cdd:cd03220 92 GGG----FNPELTGREniylnGRLLGLSRKEIDEkIDEIIEfSELGDFIdLPVKTYSSGMKARLAFAIA-TALEPDILLI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488616976 524 DEPTAALDAGAEAAVFEHFREY-AKGRMTLLISHRFSSVRN-AEHIVVLEHGRVLERG 579
Cdd:cd03220 167 DEVLAVGDAAFQEKCQRRLRELlKQGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
353-575 |
1.02e-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: 78.03 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 353 GDGMRFENVSFTYPGTSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDqGRILLDGSD-----LQDWded 427
Cdd:TIGR01271 1215 GGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSwnsvtLQTW--- 1290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 428 alRSRIGVIFQDFIRYQFLVGENLgvgDTHA-FHDETRWREAAAQGMAAqFIEQLDKGYATQLgrwFAGGQELSGGQWQK 506
Cdd:TIGR01271 1291 --RKAFGVIPQKVFIFSGTFRKNL---DPYEqWSDEEIWKVAEEVGLKS-VIEQFPDKLDFVL---VDGGYVLSNGHKQL 1361
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488616976 507 IALSRAYMRRdADILILDEPTAALDAGAEAAVFEHFREYAKGRMTLLISHRFSSVRNAEHIVVLEHGRV 575
Cdd:TIGR01271 1362 MCLARSILSK-AKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSV 1429
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
357-526 |
1.12e-14 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 73.64 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 357 RFENVSFTYPGTsraaLENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDwDEDALRSrIGVI 436
Cdd:COG3840 3 RLDDLTYRYGDF----PLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTA-LPPAERP-VSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 437 FQDfiryQFL-----VGENLGVGdthaFHDETRWREA---AAQGMAAQFieqldkGYATQLGRWFAggqELSGGQWQKIA 508
Cdd:COG3840 77 FQE----NNLfphltVAQNIGLG----LRPGLKLTAEqraQVEQALERV------GLAGLLDRLPG---QLSGGQRQRVA 139
|
170
....*....|....*...
gi 488616976 509 LSRAYMRrDADILILDEP 526
Cdd:COG3840 140 LARCLVR-KRPILLLDEP 156
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
360-575 |
1.53e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 74.38 E-value: 1.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 360 NVSFTY-PGTSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQD---WDedaLRSRIGV 435
Cdd:PRK13650 9 NLTFKYkEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEenvWD---IRHKIGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 436 IFQDfIRYQFlVGENlgVGDTHAFHDETrwreaaaQGMAAQ-FIEQLDKgyATQLgrwfAGGQE--------LSGGQWQK 506
Cdd:PRK13650 86 VFQN-PDNQF-VGAT--VEDDVAFGLEN-------KGIPHEeMKERVNE--ALEL----VGMQDfkereparLSGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488616976 507 IALSRAYMRRdADILILDEPTAALDAGAEAAVFEHFREYAKG-RMTLL-ISHRFSSVRNAEHIVVLEHGRV 575
Cdd:PRK13650 149 VAIAGAVAMR-PKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVIsITHDLDEVALSDRVLVMKNGQV 218
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
356-594 |
1.65e-14 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 73.37 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 356 MRFENVSFTYPGTSraALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWD-EDALRSRIG 434
Cdd:PRK11614 6 LSFDKVSAHYGKIQ--ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQtAKIMREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 435 VIFQD---FIRyqFLVGENLGVGDTHAFHDETRWREAAAQGMAAQFIEQLDKGYATqlgrwfaggqeLSGGQWQKIALSR 511
Cdd:PRK11614 84 IVPEGrrvFSR--MTVEENLAMGGFFAERDQFQERIKWVYELFPRLHERRIQRAGT-----------MSGGEQQMLAIGR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 512 AYMRRdADILILDEPTAALDAGAEAAVFEHFREYAKGRMTLLISHRFS--SVRNAEHIVVLEHGRVLERGDHDSLIA-AA 588
Cdd:PRK11614 151 ALMSQ-PRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNAnqALKLADRGYVLENGHVVLEDTGDALLAnEA 229
|
....*.
gi 488616976 589 GRYAAL 594
Cdd:PRK11614 230 VRSAYL 235
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
364-557 |
1.67e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 76.20 E-value: 1.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 364 TYPGTSraALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQ-DWDEDALRSRIGVIFQDF-I 441
Cdd:PRK10762 13 AFPGVK--ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfNGPKSSQEAGIGIIHQELnL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 442 RYQFLVGEN--LGVGDTHAFhDETRWREAAAQgmAAQFIEQLDKGYATQ--LGrwfaggqELSGGQWQKIALSRAyMRRD 517
Cdd:PRK10762 91 IPQLTIAENifLGREFVNRF-GRIDWKKMYAE--ADKLLARLNLRFSSDklVG-------ELSIGEQQMVEIAKV-LSFE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488616976 518 ADILILDEPTAALDAGAEAAVFEHFREY-AKGRMTLLISHR 557
Cdd:PRK10762 160 SKVIIMDEPTDALTDTETESLFRVIRELkSQGRGIVYISHR 200
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
375-580 |
1.70e-14 |
|
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: 75.14 E-value: 1.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 375 NIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDED----ALRSRIGVIFQD---FIRYQflV 447
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGiflpPHRRRIGYVFQEarlFPHLS--V 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 448 GENLGVGdthafhdetRWReAAAQGMAAQF---IEQLdkGYATQLGRWFAGgqeLSGGQWQKIALSRAYMRRdADILILD 524
Cdd:COG4148 95 RGNLLYG---------RKR-APRAERRISFdevVELL--GIGHLLDRRPAT---LSGGERQRVAIGRALLSS-PRLLLMD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 525 EPTAALDAGAEAAV---FEHFREYAKGRMtLLISHRFSSV-RNAEHIVVLEHGRVLERGD 580
Cdd:COG4148 159 EPLAALDLARKAEIlpyLERLRDELDIPI-LYVSHSLDEVaRLADHVVLLEQGRVVASGP 217
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
372-579 |
2.43e-14 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 73.10 E-value: 2.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 372 ALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDALrSRIGVI--FQDfIRY--QFLV 447
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQI-ARMGVVrtFQH-VRLfrEMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 448 GENL--------------GVGDTHAFhdetRWREAAAQGMAAQFIEQLDkgyATQLGRWFAGgqELSGGQWQKIALSRAY 513
Cdd:PRK11300 98 IENLlvaqhqqlktglfsGLLKTPAF----RRAESEALDRAATWLERVG---LLEHANRQAG--NLAYGQQRRLEIARCM 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488616976 514 MRRdADILILDEPTA----ALDAGAEAAVFEHFREYakGRMTLLISHRFSSVRN-AEHIVVLEHGRVLERG 579
Cdd:PRK11300 169 VTQ-PEILMLDEPAAglnpKETKELDELIAELRNEH--NVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANG 236
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
357-527 |
3.76e-14 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 72.59 E-value: 3.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 357 RFENVSFTYPG--TSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDwdEDALRsriG 434
Cdd:COG4525 5 TVRHVSVRYPGggQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG--PGADR---G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 435 VIFQDFIRYQFL-VGENLGVGDTHAFHDETRWREAAA--------QGMAAQFIeqldkgyatqlgrWfaggqELSGGQWQ 505
Cdd:COG4525 80 VVFQKDALLPWLnVLDNVAFGLRLRGVPKAERRARAEellalvglADFARRRI-------------W-----QLSGGMRQ 141
|
170 180
....*....|....*....|..
gi 488616976 506 KIALSRAyMRRDADILILDEPT 527
Cdd:COG4525 142 RVGIARA-LAADPRFLLMDEPF 162
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
370-556 |
4.24e-14 |
|
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: 71.37 E-value: 4.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 370 RAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDALRSRIGVIFQDFIRYQFLVGE 449
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 450 NLGVgdTHAFHDETRWREAAAQ-GMAAqfIEQLDKGYatqlgrwfaggqeLSGGQWQKIALSRAYMRRdADILILDEPTA 528
Cdd:cd03231 93 NLRF--WHADHSDEQVEEALARvGLNG--FEDRPVAQ-------------LSAGQQRRVALARLLLSG-RPLWILDEPTT 154
|
170 180
....*....|....*....|....*....
gi 488616976 529 ALDAGAEAAVFEHFREY-AKGRMTLLISH 556
Cdd:cd03231 155 ALDKAGVARFAEAMAGHcARGGMVVLTTH 183
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
356-586 |
4.78e-14 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 74.84 E-value: 4.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 356 MRFENVSFTYPGtsRAALENIDLHLAPGRSVALVGENGSGKTTLIKLL--TRLYQPDQGRIL------------------ 415
Cdd:TIGR03269 1 IEVKNLTKKFDG--KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIIyhvalcekcgyverpskv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 416 ----------LDGSDLQDWDED-----ALRSRIGVIFQdfiRYQFLVGENLGVGDTHAFHDETRWREAAAQGMAAQFIEQ 480
Cdd:TIGR03269 79 gepcpvcggtLEPEEVDFWNLSdklrrRIRKRIAIMLQ---RTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 481 LDKGY-ATQLGRwfaggqELSGGQWQKIALSRAyMRRDADILILDEPTAALDAGAEAAVFEHFREYAKGR-MTLLISHRF 558
Cdd:TIGR03269 156 VQLSHrITHIAR------DLSGGEKQRVVLARQ-LAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgISMVLTSHW 228
|
250 260 270
....*....|....*....|....*....|
gi 488616976 559 SSVRN--AEHIVVLEHGRVLERGDHDSLIA 586
Cdd:TIGR03269 229 PEVIEdlSDKAIWLENGEIKEEGTPDEVVA 258
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
358-579 |
6.25e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 72.73 E-value: 6.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 358 FENVSFTYPGTSR---AALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDG----SDLQDWDE-DAL 429
Cdd:PRK13645 9 LDNVSYTYAKKTPfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipANLKKIKEvKRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 430 RSRIGVIFQdFIRYQFL---VGENLGVGDTHAFHDEtrwREAAAQGMAAQFIEQLDKGYATQlgrwfaGGQELSGGQWQK 506
Cdd:PRK13645 89 RKEIGLVFQ-FPEYQLFqetIEKDIAFGPVNLGENK---QEAYKKVPELLKLVQLPEDYVKR------SPFELSGGQKRR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488616976 507 IALSrAYMRRDADILILDEPTAALDAGAEAAVFEHFREYAK--GRMTLLISHRFSSV-RNAEHIVVLEHGRVLERG 579
Cdd:PRK13645 159 VALA-GIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKeyKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIG 233
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
348-587 |
6.75e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 72.13 E-value: 6.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 348 QGALPGDGMRFENVSFTYPGtsRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDED 427
Cdd:PRK10575 4 YTNHSDTTFALRNVSFRVPG--RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 428 ALRSRIGVIFQdfiryQFLVGENLGVGDTHAFhdeTRWREAAAQG-MAAQFIEQLDKGYATQLGRWFAGG--QELSGGQW 504
Cdd:PRK10575 82 AFARKVAYLPQ-----QLPAAEGMTVRELVAI---GRYPWHGALGrFGAADREKVEEAISLVGLKPLAHRlvDSLSGGER 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 505 QK--IALSRAymrRDADILILDEPTAALDAGAEAAVFE--HFREYAKGRMTLLISHRFS-SVRNAEHIVVLEHGRVLERG 579
Cdd:PRK10575 154 QRawIAMLVA---QDSRCLLLDEPTSALDIAHQVDVLAlvHRLSQERGLTVIAVLHDINmAARYCDYLVALRGGEMIAQG 230
|
....*...
gi 488616976 580 DHDSLIAA 587
Cdd:PRK10575 231 TPAELMRG 238
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
373-586 |
7.28e-14 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 71.92 E-value: 7.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 373 LENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQ-DWDEDA------------LRSRIGVIFQD 439
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlVRDKDGqlkvadknqlrlLRTRLTMVFQH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 440 FIRYQFL-VGEN--------LGVGDTHAfhdetrwREAAAQGMAAQFIEQLDKG-YATqlgrwfaggqELSGGQWQKIAL 509
Cdd:PRK10619 101 FNLWSHMtVLENvmeapiqvLGLSKQEA-------RERAVKYLAKVGIDERAQGkYPV----------HLSGGQQQRVSI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488616976 510 SRAyMRRDADILILDEPTAALDAGAEAAVFEHFREYA-KGRMTLLISHRFSSVRN-AEHIVVLEHGRVLERGDHDSLIA 586
Cdd:PRK10619 164 ARA-LAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAeEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFG 241
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
372-574 |
8.93e-14 |
|
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: 74.09 E-value: 8.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 372 ALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPD--QGRILLDGSDLQDWD-EDALRSRIGVIFQDFIRYQFL-V 447
Cdd:TIGR02633 16 ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPLKASNiRDTERAGIVIIHQELTLVPELsV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 448 GENLGVGDtHAFHDETRWREAAAQGMAAQFIEQLdKGYATQLGRWFAggqELSGGQWQKIALSRAyMRRDADILILDEPT 527
Cdd:TIGR02633 96 AENIFLGN-EITLPGGRMAYNAMYLRAKNLLREL-QLDADNVTRPVG---DYGGGQQQLVEIAKA-LNKQARLLILDEPS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488616976 528 AALDAGAEAAVFEHFREY-AKGRMTLLISHRFSSVRN-AEHIVVLEHGR 574
Cdd:TIGR02633 170 SSLTEKETEILLDIIRDLkAHGVACVYISHKLNEVKAvCDTICVIRDGQ 218
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
373-527 |
1.41e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 70.58 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 373 LENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDED---ALRSR-IGVIFQDFIRYQFLVG 448
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraKLRAKhVGFVFQSFMLIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 449 -ENLGVGDTHAFHDETRWREAaaqgmAAQFIEQLdkGYATQLGRWFAggqELSGGQWQKIALSRAYMRRdADILILDEPT 527
Cdd:PRK10584 106 lENVELPALLRGESSRQSRNG-----AKALLEQL--GLGKRLDHLPA---QLSGGEQQRVALARAFNGR-PDVLFADEPT 174
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
361-588 |
1.45e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 73.59 E-value: 1.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 361 VSFTYPGTSRAALENIDLHLAPGRSVALVGENGSGKT-TLIKLLTRLYQPD----QGRILLDGSDLQDWDEDALR----S 431
Cdd:PRK15134 13 VAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHASEQTLRgvrgN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 432 RIGVIFQD-FIRYQFLVGENLGVGDTHAFHDETRwREAAAqgmaAQFIEQLDK-GYATQLGRWFAGGQELSGGQWQKIAL 509
Cdd:PRK15134 93 KIAMIFQEpMVSLNPLHTLEKQLYEVLSLHRGMR-REAAR----GEILNCLDRvGIRQAAKRLTDYPHQLSGGERQRVMI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 510 SRAYMRRdADILILDEPTAALDAGAEAAVFEHFREYAKG-RMTLL-ISHRFSSVRN-AEHIVVLEHGRVLERGDHDSLIA 586
Cdd:PRK15134 168 AMALLTR-PELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLfITHNLSIVRKlADRVAVMQNGRCVEQNRAATLFS 246
|
..
gi 488616976 587 AA 588
Cdd:PRK15134 247 AP 248
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
356-579 |
1.45e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 71.20 E-value: 1.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 356 MRFENVSFTYpgTSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQ---GRILLDGSDLQ-----DWDED 427
Cdd:PRK09984 5 IRVEKLAKTF--NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagSHIELLGRTVQregrlARDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 428 ALRSRIGVIFQDF-IRYQFLVGENL---GVGDTHAFHDETRWREAAAQGMAAQFIeqldkgyaTQLGRWFAGGQE---LS 500
Cdd:PRK09984 83 KSRANTGYIFQQFnLVNRLSVLENVligALGSTPFWRTCFSWFTREQKQRALQAL--------TRVGMVHFAHQRvstLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 501 GGQWQKIALSRAYMRRdADILILDEPTAALDAGAEAAVFEHFREYAK--GRMTLLISHRFS-SVRNAEHIVVLEHGRVLE 577
Cdd:PRK09984 155 GGQQQRVAIARALMQQ-AKVILADEPIASLDPESARIVMDTLRDINQndGITVVVTLHQVDyALRYCERIVALRQGHVFY 233
|
..
gi 488616976 578 RG 579
Cdd:PRK09984 234 DG 235
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
368-575 |
1.76e-13 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 69.00 E-value: 1.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 368 TSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWD-EDALRSRIGvifqdfiryqfL 446
Cdd:cd03215 11 SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSpRDAIRAGIA-----------Y 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 447 VGENlgvgdthafhdetRWREAAAQGMAaqfieqldkgyatqLGRWFAGGQELSGGQWQKIALSRAyMRRDADILILDEP 526
Cdd:cd03215 80 VPED-------------RKREGLVLDLS--------------VAENIALSSLLSGGNQQKVVLARW-LARDPRVLILDEP 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488616976 527 TAALDAGAEAAVFEHFREYA-KGRMTLLISHRFSSV-RNAEHIVVLEHGRV 575
Cdd:cd03215 132 TRGVDVGAKAEIYRLIRELAdAGKAVLLISSELDELlGLCDRILVMYEGRI 182
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
351-575 |
2.59e-13 |
|
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: 73.51 E-value: 2.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 351 LPG--DGMRFENVSFTYPGTSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDwDEDA 428
Cdd:TIGR01257 922 LPGlvPGVCVKNLVKIFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDA 1000
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 429 LRSRIGVIFQDFIRYQflvgeNLGVGDTHAFHDETR---WREAAAQgMAAQFieqLDKGYATQLGRwfaGGQELSGGQWQ 505
Cdd:TIGR01257 1001 VRQSLGMCPQHNILFH-----HLTVAEHILFYAQLKgrsWEEAQLE-MEAML---EDTGLHHKRNE---EAQDLSGGMQR 1068
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488616976 506 KIALSRAYMrRDADILILDEPTAALDAGAEAAVFEHFREYAKGRMTLLISHRFSSVRN-AEHIVVLEHGRV 575
Cdd:TIGR01257 1069 KLSVAIAFV-GDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLlGDRIAIISQGRL 1138
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
356-438 |
2.76e-13 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 70.07 E-value: 2.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 356 MRFENVSFTYpgTSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLY--QPDQ---GRILLDGSDLQDWDED--A 428
Cdd:COG1117 12 IEVRNLNVYY--GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNdlIPGArveGEILLDGEDIYDPDVDvvE 89
|
90
....*....|
gi 488616976 429 LRSRIGVIFQ 438
Cdd:COG1117 90 LRRRVGMVFQ 99
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
360-580 |
3.11e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 70.89 E-value: 3.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 360 NVSFTY-PGTSRA--ALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRI--------LLDGSDLQDWDED- 427
Cdd:PRK13651 7 NIVKIFnKKLPTElkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdekNKKKTKEKEKVLEk 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 428 ---------------ALRSRIGVIFQdFIRYQF---------LVGE-NLGVgdthafhdetrwREAAAQGMAAQFIEQ-- 480
Cdd:PRK13651 87 lviqktrfkkikkikEIRRRVGVVFQ-FAEYQLfeqtiekdiIFGPvSMGV------------SKEEAKKRAAKYIELvg 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 481 LDKGYatqLGRW-FaggqELSGGQWQKIALSrAYMRRDADILILDEPTAALDAGAEAAVFEHFRE-YAKGRMTLLISHRF 558
Cdd:PRK13651 154 LDESY---LQRSpF----ELSGGQKRRVALA-GILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNlNKQGKTIILVTHDL 225
|
250 260
....*....|....*....|...
gi 488616976 559 SSV-RNAEHIVVLEHGRVLERGD 580
Cdd:PRK13651 226 DNVlEWTKRTIFFKDGKIIKDGD 248
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
373-526 |
3.83e-13 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 70.90 E-value: 3.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 373 LENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDwdeDALRSR-IGVIFQDFIRYQFL-VGEN 450
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH---RSIQQRdICMVFQSYALFPHMsLGEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 451 LGVG----DTHAFHDETRWREAAA----QGMAAQFIEQldkgyatqlgrwfaggqeLSGGQWQKIALSRAYMRRdADILI 522
Cdd:PRK11432 99 VGYGlkmlGVPKEERKQRVKEALElvdlAGFEDRYVDQ------------------ISGGQQQRVALARALILK-PKVLL 159
|
....
gi 488616976 523 LDEP 526
Cdd:PRK11432 160 FDEP 163
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
373-579 |
3.86e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 69.56 E-value: 3.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 373 LENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQ--PD---QGRILLDGSDLQDWDEDALRSRIGVIFQDFIRYQFL- 446
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNPIPNLs 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 447 VGENLGVG--------DTHAFHDETRWREAAAQgMAAQFIEQLDkgyatqlgrwfAGGQELSGGQWQKIALSRAyMRRDA 518
Cdd:PRK14247 99 IFENVALGlklnrlvkSKKELQERVRWALEKAQ-LWDEVKDRLD-----------APAGKLSGGQQQRLCIARA-LAFQP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488616976 519 DILILDEPTAALDAGAEAAVFEHFREYAKGRMTLLISH-RFSSVRNAEHIVVLEHGRVLERG 579
Cdd:PRK14247 166 EVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWG 227
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
372-585 |
5.23e-13 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 71.22 E-value: 5.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 372 ALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDALRS----RIGVIFQDF-IRYQFL 446
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFaLMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 447 VGENLGVGDTHAFHDETRWREAAAQGMAAQFIEQLDKGYAtqlgrwfaggQELSGGQWQKIALSRAyMRRDADILILDEP 526
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYP----------DELSGGMRQRVGLARA-LAINPDILLMDEA 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488616976 527 TAALDAGAEAAVFEHF--REYAKGRMTLLISHRF-SSVRNAEHIVVLEHGRVLERGDHDSLI 585
Cdd:PRK10070 192 FSALDPLIRTEMQDELvkLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
372-591 |
5.68e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 70.12 E-value: 5.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 372 ALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDwDEDALRSRIGVIF-QdfiRYQFLVgeN 450
Cdd:COG4586 37 AVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFK-RRKEFARRIGVVFgQ---RSQLWW--D 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 451 LGVGDTHAFH------DETRWREAAAQgmaaqFIEQLD-KGYATQLGRwfaggqELSGGQWQK--IALSrayMRRDADIL 521
Cdd:COG4586 111 LPAIDSFRLLkaiyriPDAEYKKRLDE-----LVELLDlGELLDTPVR------QLSLGQRMRceLAAA---LLHRPKIL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488616976 522 ILDEPTAALDAGAEAAVFEHFREYAKGRMT--LLISHRFSSVRN-AEHIVVLEHGRVLERGDHDSLIAAAGRY 591
Cdd:COG4586 177 FLDEPTIGLDVVSKEAIREFLKEYNRERGTtiLLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKERFGPY 249
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
359-526 |
6.08e-13 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 68.96 E-value: 6.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 359 ENVSFTYPGtsRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQdwDEDALRsriGVIFQ 438
Cdd:PRK11248 5 SHLYADYGG--KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVE--GPGAER---GVVFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 439 D--FIRYQFlVGENLGVGDTHAFHDETRWREAAAQGMAAQFIEQLDKGYATQlgrwfaggqeLSGGQWQKIALSRAyMRR 516
Cdd:PRK11248 78 NegLLPWRN-VQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQ----------LSGGQRQRVGIARA-LAA 145
|
170
....*....|
gi 488616976 517 DADILILDEP 526
Cdd:PRK11248 146 NPQLLLLDEP 155
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
356-588 |
3.13e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 67.43 E-value: 3.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 356 MRFENVSFTYPGTSRA-ALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDALRSRIG 434
Cdd:PRK13642 5 LEVENLVFKYEKESDVnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 435 VIFQDfIRYQFlVGENlgVGDTHAFHDETrwreaaaQGMA-AQFIEQLDKGY--ATQLGRWFAGGQELSGGQWQKIALSR 511
Cdd:PRK13642 85 MVFQN-PDNQF-VGAT--VEDDVAFGMEN-------QGIPrEEMIKRVDEALlaVNMLDFKTREPARLSGGQKQRVAVAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488616976 512 AYMRRdADILILDEPTAALDAGAEAAVFEHFREYA-KGRMTLL-ISHRFSSVRNAEHIVVLEHGRVLERGDHDSLIAAA 588
Cdd:PRK13642 154 IIALR-PEIIILDESTSMLDPTGRQEIMRVIHEIKeKYQLTVLsITHDLDEAASSDRILVMKAGEIIKEAAPSELFATS 231
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
373-526 |
3.88e-12 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 67.80 E-value: 3.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 373 LENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWdeDALRSRIGVIFQDFIRYQFL-VGENL 451
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRL--HARDRKVGFVFQHYALFRHMtVFDNI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 452 GVGDTHAFHDEtRWREAAAQGMAAQFIE--QLD---KGYATQlgrwfaggqeLSGGQWQKIALSRAyMRRDADILILDEP 526
Cdd:PRK10851 96 AFGLTVLPRRE-RPNAAAIKAKVTQLLEmvQLAhlaDRYPAQ----------LSGGQKQRVALARA-LAVEPQILLLDEP 163
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
370-527 |
4.00e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 65.67 E-value: 4.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 370 RAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGsdlQDWDEDALRSRIGVI-FQDFIRYQFLVG 448
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG---GDIDDPDVAEACHYLgHRNAMKPALTVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 449 ENL-------GVGDTHAfhdetrwrEAAAQGMAAQFIEQLDKGYatqlgrwfaggqeLSGGQWQKIALSR--AYMRRdad 519
Cdd:PRK13539 92 ENLefwaaflGGEELDI--------AAALEAVGLAPLAHLPFGY-------------LSAGQKRRVALARllVSNRP--- 147
|
....*...
gi 488616976 520 ILILDEPT 527
Cdd:PRK13539 148 IWILDEPT 155
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
369-526 |
4.96e-12 |
|
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: 66.03 E-value: 4.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 369 SRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDAlRSRIGVIF--QDFIRYQFL 446
Cdd:cd03218 12 KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK-RARLGIGYlpQEASIFRKL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 447 -VGENLGVGDTHAFHDETRWREAAAQGMAAQFIEQLDKGYATQlgrwfaggqeLSGGQWQKIALSRAYMrRDADILILDE 525
Cdd:cd03218 91 tVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASS----------LSGGERRRVEIARALA-TNPKFLLLDE 159
|
.
gi 488616976 526 P 526
Cdd:cd03218 160 P 160
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
367-527 |
8.40e-12 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 65.15 E-value: 8.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 367 GTSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRIL-------LDGSDLQDWDEDALRSR-IGvifq 438
Cdd:COG4778 21 GKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILvrhdggwVDLAQASPREILALRRRtIG---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 439 dfirY--QFL-----------VGENL---GVGdthafhdetrwrEAAAQGMAAQFIEQLdkgyatQLGR--WFAGGQELS 500
Cdd:COG4778 97 ----YvsQFLrviprvsaldvVAEPLlerGVD------------REEARARARELLARL------NLPErlWDLPPATFS 154
|
170 180
....*....|....*....|....*..
gi 488616976 501 GGQWQKIALSRAYMRrDADILILDEPT 527
Cdd:COG4778 155 GGEQQRVNIARGFIA-DPPLLLLDEPT 180
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
360-526 |
1.13e-11 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 66.78 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 360 NVSFTYPGtsRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQdwDEDALRSRIGVIFQD 439
Cdd:PRK11607 24 NLTKSFDG--QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS--HVPPYQRPINMMFQS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 440 FIRYQFL-VGENLGVGdthafhdeTRWREAAAQGMAAQFIEQLDKGYATQlgrwFAGGQ--ELSGGQWQKIALSRAYMRR 516
Cdd:PRK11607 100 YALFPHMtVEQNIAFG--------LKQDKLPKAEIASRVNEMLGLVHMQE----FAKRKphQLSGGQRQRVALARSLAKR 167
|
170
....*....|
gi 488616976 517 dADILILDEP 526
Cdd:PRK11607 168 -PKLLLLDEP 176
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
357-526 |
1.29e-11 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 66.51 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 357 RFENVSFTYPGTsrAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQdwDEDALRSRIGVI 436
Cdd:PRK09452 16 ELRGISKSFDGK--EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT--HVPAENRHVNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 437 FQDFIRYQFL-VGENLgvgdthAF--------HDETRWREAAAQGMAaqfieQLDKgyatqlgrwFAGG--QELSGGQWQ 505
Cdd:PRK09452 92 FQSYALFPHMtVFENV------AFglrmqktpAAEITPRVMEALRMV-----QLEE---------FAQRkpHQLSGGQQQ 151
|
170 180
....*....|....*....|.
gi 488616976 506 KIALSRAYMRRdADILILDEP 526
Cdd:PRK09452 152 RVAIARAVVNK-PKVLLLDES 171
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
359-527 |
1.44e-11 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 67.44 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 359 ENVSFTYPG--TSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDAL----RSR 432
Cdd:PRK10535 8 KDIRRSYPSgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 433 IGVIFQdfiRYQFL----VGENLGVGDTHAfHDETRWREAAAQGMaaqfieqldkgyATQLG---RWFAGGQELSGGQWQ 505
Cdd:PRK10535 88 FGFIFQ---RYHLLshltAAQNVEVPAVYA-GLERKQRLLRAQEL------------LQRLGledRVEYQPSQLSGGQQQ 151
|
170 180
....*....|....*....|..
gi 488616976 506 KIALSRAYMrRDADILILDEPT 527
Cdd:PRK10535 152 RVSIARALM-NGGQVILADEPT 172
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
370-587 |
1.69e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 64.68 E-value: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 370 RAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQ------PDQGRILLDGSDLQDWDEDALRSRIGVIFQDFIRY 443
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 444 QFL-VGENLGVG-DTHAFHDETRWREAAAQ-----GMAAQFIEQLDkgyatqlgrwfAGGQELSGGQWQKIALSRAYMRR 516
Cdd:PRK14246 103 PHLsIYDNIAYPlKSHGIKEKREIKKIVEEclrkvGLWKEVYDRLN-----------SPASQLSGGQQQRLTIARALALK 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488616976 517 dADILILDEPTAALDAGAEAAVFEHFREYAKGRMTLLISHRFSSV-RNAEHIVVLEHGRVLERGDHDSLIAA 587
Cdd:PRK14246 172 -PKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEIFTS 242
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
359-527 |
1.72e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 66.68 E-value: 1.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 359 ENVSFTYPGTSraALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQ-DWDEDALRSRIGVIF 437
Cdd:PRK10982 2 SNISKSFPGVK--ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 438 QDF-IRYQFLVGENLGVGD---THAFHDETR-WREAAAqgmaaqFIEQLD------KGYATqlgrwfaggqeLSGGQWQK 506
Cdd:PRK10982 80 QELnLVLQRSVMDNMWLGRyptKGMFVDQDKmYRDTKA------IFDELDididprAKVAT-----------LSVSQMQM 142
|
170 180
....*....|....*....|.
gi 488616976 507 IALSRAYmRRDADILILDEPT 527
Cdd:PRK10982 143 IEIAKAF-SYNAKIVIMDEPT 162
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
368-527 |
2.20e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 66.20 E-value: 2.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 368 TSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWD-EDALRSRIGV---------IF 437
Cdd:COG1129 263 SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSpRDAIRAGIAYvpedrkgegLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 438 QDF-IRyqflvgENLGVGDTHAFHDETRWREAAAQGMAAQFIEQLD-KgyatqlgrwfAGGQE-----LSGGQWQKIALS 510
Cdd:COG1129 343 LDLsIR------ENITLASLDRLSRGGLLDRRRERALAEEYIKRLRiK----------TPSPEqpvgnLSGGNQQKVVLA 406
|
170
....*....|....*..
gi 488616976 511 RAyMRRDADILILDEPT 527
Cdd:COG1129 407 KW-LATDPKVLILDEPT 422
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
375-526 |
3.00e-11 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 65.28 E-value: 3.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 375 NIDLHLaPGRSV-ALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDED----ALRSRIGVIFQD---FIRYQfl 446
Cdd:PRK11144 16 TVNLTL-PAQGItAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGiclpPEKRRIGYVFQDarlFPHYK-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 447 VGENLGVGdthafhdetrwreaAAQGMAAQF--------IEQLdkgyatqLGRWFAGgqeLSGGQWQKIALSRAYMrRDA 518
Cdd:PRK11144 93 VRGNLRYG--------------MAKSMVAQFdkivallgIEPL-------LDRYPGS---LSGGEKQRVAIGRALL-TAP 147
|
....*...
gi 488616976 519 DILILDEP 526
Cdd:PRK11144 148 ELLLMDEP 155
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
356-527 |
4.15e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 63.64 E-value: 4.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 356 MRFENVSFTYpgTSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRL--YQPD---QGRILLDGSDLQDWDEDA-- 428
Cdd:PRK14239 6 LQVSDLSVYY--NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNIYSPRTDTvd 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 429 LRSRIGVIFQDFIRYQFLVGENLGVG-DTHAFHDETRWREAAAQGM--AAQFIEQLDKGYATQLGrwfaggqeLSGGQWQ 505
Cdd:PRK14239 84 LRKEIGMVFQQPNPFPMSIYENVVYGlRLKGIKDKQVLDEAVEKSLkgASIWDEVKDRLHDSALG--------LSGGQQQ 155
|
170 180
....*....|....*....|..
gi 488616976 506 KIALSRAyMRRDADILILDEPT 527
Cdd:PRK14239 156 RVCIARV-LATSPKIILLDEPT 176
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
352-584 |
4.33e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 66.15 E-value: 4.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 352 PG-DGMRFENVSFTYPG-TSRAALENIDLHLAPGRSVALVGENGSGKTTLIK-LLTRLYQPDQGRILLDGSdlqdwdeDA 428
Cdd:PLN03232 610 PGaPAISIKNGYFSWDSkTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRGS-------VA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 429 LRSRIGVIFQDFIRYQFLVGENlgvgdthaFHDETRWReaAAQGMAAQFIEQLDKGY-ATQLGRwfaGGQELSGGQWQKI 507
Cdd:PLN03232 683 YVPQVSWIFNATVRENILFGSD--------FESERYWR--AIDVTALQHDLDLLPGRdLTEIGE---RGVNISGGQKQRV 749
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488616976 508 ALSRAYMrRDADILILDEPTAALDAGAEAAVFEH-FREYAKGRMTLLISHRFSSVRNAEHIVVLEHGRVLERGDHDSL 584
Cdd:PLN03232 750 SMARAVY-SNSDIYIFDDPLSALDAHVAHQVFDScMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAEL 826
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
358-579 |
5.08e-11 |
|
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: 62.18 E-value: 5.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 358 FENVSFTYPG----TSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLT--RLYQPDQGRILLDGSDLqdwDEDALRS 431
Cdd:cd03213 6 FRNLTVTVKSspskSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPL---DKRSFRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 432 RIGVIFQDFIRYQFL-VGENLgvgdthafhdetrwreaaaqgmaaqfieqldkGYATQLgrwfaggQELSGGQWQKIALS 510
Cdd:cd03213 83 IIGYVPQDDILHPTLtVRETL--------------------------------MFAAKL-------RGLSGGERKRVSIA 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488616976 511 RAyMRRDADILILDEPTAALDAGAEAAVFEHFREYAKGRMTLLIS-HRFSS--VRNAEHIVVLEHGRVLERG 579
Cdd:cd03213 124 LE-LVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSiHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
377-594 |
7.21e-11 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 62.68 E-value: 7.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 377 DLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDalRSRIGVIFQDFIRYQFL-VGENLGVGD 455
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFSHLtVAQNIGLGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 456 THAF---HDETRWREAAAQGMaaqfieqldkGYATQLGRWFAggqELSGGQWQKIALSRAYMRRDAdILILDEPTAALDA 532
Cdd:PRK10771 97 NPGLklnAAQREKLHAIARQM----------GIEDLLARLPG---QLSGGQRQRVALARCLVREQP-ILLLDEPFSALDP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488616976 533 GAEAAVFEHFREYAKGR-MTLL-ISHrfsSVRNAEHI----VVLEHGRVLERGDHDSLIAAAGRYAAL 594
Cdd:PRK10771 163 ALRQEMLTLVSQVCQERqLTLLmVSH---SLEDAARIaprsLVVADGRIAWDGPTDELLSGKASASAL 227
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
360-573 |
7.66e-11 |
|
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: 63.34 E-value: 7.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 360 NVSFT-YPGTSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGsdlqdwdEDALRSRIGVIFQ 438
Cdd:cd03291 39 NLFFSnLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------RISFSSQFSWIMP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 439 DFIRyqflvgENLGVGDThafHDETRWREAAAQGMAAQFIEQLDKGYATQLGRwfaGGQELSGGQWQKIALSRAyMRRDA 518
Cdd:cd03291 112 GTIK------ENIIFGVS---YDEYRYKSVVKACQLEEDITKFPEKDNTVLGE---GGITLSGGQRARISLARA-VYKDA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488616976 519 DILILDEPTAALDAGAEAAVFEH-FREYAKGRMTLLISHRFSSVRNAEHIVVLEHG 573
Cdd:cd03291 179 DLYLLDSPFGYLDVFTEKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEG 234
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
361-593 |
8.72e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 63.19 E-value: 8.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 361 VSFTYPGTSRAALENIDLHLaPGRSV-ALVGENGSGKTTLIKLLTRLYQP-----DQGRILLDGSDLQDW-DEDALRSRI 433
Cdd:PRK14271 25 VNLTLGFAGKTVLDQVSMGF-PARAVtSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYrDVLEFRRRV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 434 GVIFQDFIRYQFLVGENLGVG-DTHAFHDETRWREAAaqgmaaqfieqldKGYATQLGRWFAGGQELS-------GGQWQ 505
Cdd:PRK14271 104 GMLFQRPNPFPMSIMDNVLAGvRAHKLVPRKEFRGVA-------------QARLTEVGLWDAVKDRLSdspfrlsGGQQQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 506 KIALSRAyMRRDADILILDEPTAALDAGAEAAVFEHFREYAKGRMTLLISHRFS-SVRNAEHIVVLEHGRVLERGDHDSL 584
Cdd:PRK14271 171 LLCLART-LAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQL 249
|
250
....*....|....
gi 488616976 585 I-----AAAGRYAA 593
Cdd:PRK14271 250 FsspkhAETARYVA 263
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
359-527 |
9.37e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 64.53 E-value: 9.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 359 ENVSFTYPGtsRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRIlldgsdlqDWDEDAlrsRIGVIFQ 438
Cdd:PRK15064 323 ENLTKGFDN--GPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV--------KWSENA---NIGYYAQ 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 439 DFiRYQFLVGENLgvgdthaFHDETRWREAAAQgmaaqfiEQLDKGYatqLGRWFAGGQE-------LSGGQ-----WQK 506
Cdd:PRK15064 390 DH-AYDFENDLTL-------FDWMSQWRQEGDD-------EQAVRGT---LGRLLFSQDDikksvkvLSGGEkgrmlFGK 451
|
170 180
....*....|....*....|.
gi 488616976 507 IALSRaymrrdADILILDEPT 527
Cdd:PRK15064 452 LMMQK------PNVLVMDEPT 466
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
356-579 |
1.04e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 62.94 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 356 MRFENVSFTYP-GTSraALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLqDWDEDA---LRS 431
Cdd:PRK13636 6 LKVEELNYNYSdGTH--ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKGlmkLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 432 RIGVIFQDFIRYQF--LVGENLGVGDTHAFHDETRWREAAAQGMAAQFIEQLdKGYATQLgrwfaggqeLSGGQWQKIAL 509
Cdd:PRK13636 83 SVGMVFQDPDNQLFsaSVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHL-KDKPTHC---------LSFGQKKRVAI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488616976 510 SrAYMRRDADILILDEPTAALDAGAEAAVFEHFREYAKGR-MTLLI-SHRFSSVR-NAEHIVVLEHGRVLERG 579
Cdd:PRK13636 153 A-GVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELgLTIIIaTHDIDIVPlYCDNVFVMKEGRVILQG 224
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
373-527 |
1.19e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 64.20 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 373 LENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDG----SDLQdwdEDALRSRIGVIFqDFiryqflVG 448
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQdlivARLQ---QDPPRNVEGTVY-DF------VA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 449 ENLG-VGDT-HAFHD-----ETRWREAAAQGMA------------------AQFIEQLDKGYATQLgrwfaggQELSGGq 503
Cdd:PRK11147 89 EGIEeQAEYlKRYHDishlvETDPSEKNLNELAklqeqldhhnlwqlenriNEVLAQLGLDPDAAL-------SSLSGG- 160
|
170 180
....*....|....*....|....*
gi 488616976 504 WQ-KIALSRAYMrRDADILILDEPT 527
Cdd:PRK11147 161 WLrKAALGRALV-SNPDVLLLDEPT 184
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
373-580 |
1.45e-10 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 61.00 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 373 LENIDLHLAPGRSVALVGENGSGKTTLIKLLTRL--YQPDQGRILLDGSDLQDWDEDaLRSR--IGVIFQDFIRYQflvg 448
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPE-ERARlgIFLAFQYPPEIP---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 449 enlGVgdthafhdetrwreaaaqgMAAQFIEQLDKGyatqlgrwfaggqeLSGGQWQKIALSRAYMRRdADILILDEPTA 528
Cdd:cd03217 91 ---GV-------------------KNADFLRYVNEG--------------FSGGEKKRNEILQLLLLE-PDLAILDEPDS 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488616976 529 ALDAGAEAAVFEHFREYA-KGRMTLLISHRfssVRNAEHIV-----VLEHGRVLERGD 580
Cdd:cd03217 134 GLDIDALRLVAEVINKLReEGKSVLIITHY---QRLLDYIKpdrvhVLYDGRIVKSGD 188
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
373-588 |
1.58e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 62.33 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 373 LENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLqDWDED---ALRSRIGVIFQDFIRYQFLVG- 448
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRgllALRQQVATVFQDPEQQIFYTDi 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 449 --------ENLGVGDTHAfhdETRWREAA----AQGMAAQFIeqldkgyatqlgrwfaggQELSGGQWQKIALSRAYMRR 516
Cdd:PRK13638 96 dsdiafslRNLGVPEAEI---TRRVDEALtlvdAQHFRHQPI------------------QCLSHGQKKRVAIAGALVLQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488616976 517 dADILILDEPTAALDAGAEAAVFEHFRE-YAKGRMTLLISHRFSSVRN-AEHIVVLEHGRVLERGDHDSLIAAA 588
Cdd:PRK13638 155 -ARYLLLDEPTAGLDPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGAPGEVFACT 227
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
373-570 |
1.68e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 61.27 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 373 LENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDALRSRIGVIFQDfiryQFLVGENlg 452
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQT----PTLFGDT-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 453 VGDTHAFHDETRWREAAAQGMA---AQF---IEQLDKGYAtqlgrwfaggqELSGGQWQKIALSR--AYMRRdadILILD 524
Cdd:PRK10247 97 VYDNLIFPWQIRNQQPDPAIFLddlERFalpDTILTKNIA-----------ELSGGEKQRISLIRnlQFMPK---VLLLD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488616976 525 EPTAALDAGAEAAVFEHFREYA--KGRMTLLISHRFSSVRNAEHIVVL 570
Cdd:PRK10247 163 EITSALDESNKHNVNEIIHRYVreQNIAVLWVTHDKDEINHADKVITL 210
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
360-566 |
1.76e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 60.73 E-value: 1.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 360 NVSFTYpgTSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQdwdedalrsrigvifQD 439
Cdd:PRK13540 6 ELDFDY--HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK---------------KD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 440 FIRYQ---FLVGENLGVGDTHAFHDETRWREAAAQGmaAQFIEQLDKGYATQLGRWFAGGQeLSGGQWQKIALSRAYMRR 516
Cdd:PRK13540 69 LCTYQkqlCFVGHRSGINPYLTLRENCLYDIHFSPG--AVGITELCRLFSLEHLIDYPCGL-LSSGQKRQVALLRLWMSK 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488616976 517 dADILILDEPTAALDAGAEAAVFEHFREY-AKGRMTLLISHRFSSVRNAEH 566
Cdd:PRK13540 146 -AKLWLLDEPLVALDELSLLTIITKIQEHrAKGGAVLLTSHQDLPLNKADY 195
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
386-527 |
3.37e-10 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 60.88 E-value: 3.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 386 VALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLqdwdedALRSRIGVIFQDFIRYQFLVGENLGVGdTHAFhdetrW 465
Cdd:cd03237 28 IGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV------SYKPQYIKADYEGTVRDLLSSITKDFY-THPY-----F 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488616976 466 REAAAQGMaaqfieQLDKGYATQLgrwfaggQELSGGQWQKIALSrAYMRRDADILILDEPT 527
Cdd:cd03237 96 KTEIAKPL------QIEQILDREV-------PELSGGELQRVAIA-ACLSKDADIYLLDEPS 143
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
360-587 |
4.79e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 62.38 E-value: 4.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 360 NVSFTYPGTsrAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEdALRSRIGV--IF 437
Cdd:PRK15439 16 SISKQYSGV--EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTP-AKAHQLGIylVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 438 QDFIRYQFL-VGENLGVGDThafhdetrwREAAAQGMAAQFIEQLDkgyaTQLGRWFAGGQeLSGGQWQKIALSRAYMRr 516
Cdd:PRK15439 93 QEPLLFPNLsVKENILFGLP---------KRQASMQKMKQLLAALG----CQLDLDSSAGS-LEVADRQIVEILRGLMR- 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488616976 517 DADILILDEPTAALDAGAEAAVFEHFREY-AKGRMTLLISHRFSSVRN-AEHIVVLEHGRVLERG-----DHDSLIAA 587
Cdd:PRK15439 158 DSRILILDEPTASLTPAETERLFSRIRELlAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGktadlSTDDIIQA 235
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
363-584 |
5.91e-10 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 60.88 E-value: 5.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 363 FTYPGTSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDED---ALRSRIGVIFQD 439
Cdd:PRK15079 27 FWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDewrAVRSDIQMIFQD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 440 firyqFLVGEN--LGVGDTHA-----FHDEtrwreaaaqgMAAQFIEQLDKGYATQLG-------RWfagGQELSGGQWQ 505
Cdd:PRK15079 107 -----PLASLNprMTIGEIIAeplrtYHPK----------LSRQEVKDRVKAMMLKVGllpnlinRY---PHEFSGGQCQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 506 KIALSRAYMRRdADILILDEPTAALDAGAEAAVFEHFREYAK--GRMTLLISHRFSSVRN-AEHIVVLEHGRVLERGDHD 582
Cdd:PRK15079 169 RIGIARALILE-PKLIICDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYD 247
|
..
gi 488616976 583 SL 584
Cdd:PRK15079 248 EV 249
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
354-573 |
1.25e-09 |
|
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: 61.46 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 354 DGMRFENvsFTYPGTSraALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGsdlqdwdEDALRSRI 433
Cdd:TIGR01271 427 DGLFFSN--FSLYVTP--VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------RISFSPQT 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 434 GVIFQDFIRyqflvgENLGVGDThafHDETRWREAAAQGMAAQFIEQLDKGYATQLGRwfaGGQELSGGQWQKIALSRAy 513
Cdd:TIGR01271 496 SWIMPGTIK------DNIIFGLS---YDEYRYTSVIKACQLEEDIALFPEKDKTVLGE---GGITLSGGQRARISLARA- 562
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488616976 514 MRRDADILILDEPTAALDAGAEAAVFEH-FREYAKGRMTLLISHRFSSVRNAEHIVVLEHG 573
Cdd:TIGR01271 563 VYKDADLYLLDSPFTHLDVVTEKEIFEScLCKLMSNKTRILVTSKLEHLKKADKILLLHEG 623
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
356-577 |
1.28e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 60.96 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 356 MRfeNVSFTYPGTSraALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYqPD---QGRILLDG-----SDLQDwded 427
Cdd:NF040905 4 MR--GITKTFPGVK--ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGevcrfKDIRD---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 428 alRSRIGVIfqdfIRYQFL-------VGENLGVGDTHAFHDETRWREAAAQgmAAQFIEQ--LDKGYATQLGRWFAGGQE 498
Cdd:NF040905 75 --SEALGIV----IIHQELalipylsIAENIFLGNERAKRGVIDWNETNRR--ARELLAKvgLDESPDTLVTDIGVGKQQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 499 LSggqwqKI--ALSraymrRDADILILDEPTAALDAGAEAAVFEHFREY-AKGRMTLLISHRFSSVRN-AEHIVVLEHGR 574
Cdd:NF040905 147 LV-----EIakALS-----KDVKLLILDEPTAALNEEDSAALLDLLLELkAQGITSIIISHKLNEIRRvADSITVLRDGR 216
|
...
gi 488616976 575 VLE 577
Cdd:NF040905 217 TIE 219
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
356-586 |
1.65e-09 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 60.59 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 356 MRFENVSFTYPGTSRA---ALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRI-LLDGSDLQDWDEDALRS 431
Cdd:TIGR03269 280 IKVRNVSKRYISVDRGvvkAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnVRVGDEWVDMTKPGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 432 R------IGVIFQDFIRY-QFLVGENLGVGDTHAFHDETRWREAAAQGMAAQFIEQ-----LDKgYAtqlgrwfaggQEL 499
Cdd:TIGR03269 360 RgrakryIGILHQEYDLYpHRTVLDNLTEAIGLELPDELARMKAVITLKMVGFDEEkaeeiLDK-YP----------DEL 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 500 SGGQWQKIALSRAYMrRDADILILDEPTAALDAGAEAAVFE---HFREyAKGRMTLLISHRFSSVRN-AEHIVVLEHGRV 575
Cdd:TIGR03269 429 SEGERHRVALAQVLI-KEPRIVILDEPTGTMDPITKVDVTHsilKARE-EMEQTFIIVSHDMDFVLDvCDRAALMRDGKI 506
|
250
....*....|.
gi 488616976 576 LERGDHDSLIA 586
Cdd:TIGR03269 507 VKIGDPEEIVE 517
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
374-526 |
2.21e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 57.51 E-value: 2.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 374 ENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDALRSRIGVIFQDFIRYQFLVGENLGV 453
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYLGHQPGIKTELTALENLRF 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488616976 454 --GDTHAFHDETRWREAAAQGMAAQfiEQLDKGYatqlgrwfaggqeLSGGQWQKIALSRAYMrRDADILILDEP 526
Cdd:PRK13538 98 yqRLHGPGDDEALWEALAQVGLAGF--EDVPVRQ-------------LSAGQQRRVALARLWL-TRAPLWILDEP 156
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
290-573 |
2.29e-09 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 60.21 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 290 GRITLGQMTMYLVLFKQGQAAVS---SSLSAISGLYEDGLYLADLYIYLGQPVMPSAGSLTQGALPGDGMRFENVSFTYP 366
Cdd:COG4178 294 GEITLGGLMQAASAFGQVQGALSwfvDNYQSLAEWRATVDRLAGFEEALEAADALPEAASRIETSEDGALALEDLTLRTP 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 367 gTSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGsdlqdwDEDALrsrigvifqdfiryqFL 446
Cdd:COG4178 374 -DGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPA------GARVL---------------FL 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 447 -------VG---ENLGVGDTHAFHDETRWREAAAQ-GMAAqFIEQLDkgyatQLGRWfagGQELSGGQWQKIALSRAYMR 515
Cdd:COG4178 432 pqrpylpLGtlrEALLYPATAEAFSDAELREALEAvGLGH-LAERLD-----EEADW---DQVLSLGEQQRLAFARLLLH 502
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 488616976 516 RdADILILDEPTAALDAGAEAAVFEHFREYAKGRMTLLISHRFSSVRNAEHIVVLEHG 573
Cdd:COG4178 503 K-PDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
359-600 |
2.58e-09 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 57.98 E-value: 2.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 359 ENVSFTYPGtsRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSD--LQDWDEDALRSrIGVI 436
Cdd:PRK10895 7 KNLAKAYKG--RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDisLLPLHARARRG-IGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 437 FQDFIRYQFL-VGENLgVGDTHAFHDETR-WREAAAQGMAAQF-IEQLDKGYatqlgrwfagGQELSGGQWQKIALSRAy 513
Cdd:PRK10895 84 PQEASIFRRLsVYDNL-MAVLQIRDDLSAeQREDRANELMEEFhIEHLRDSM----------GQSLSGGERRRVEIARA- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 514 MRRDADILILDEP---TAALDAGAEAAVFEHFREYAKGrmTLLISHrfsSVRnaEHIVVLEHGRVLERGDhdsLIAAAGR 590
Cdd:PRK10895 152 LAANPKFILLDEPfagVDPISVIDIKRIIEHLRDSGLG--VLITDH---NVR--ETLAVCERAYIVSQGH---LIAHGTP 221
|
250
....*....|
gi 488616976 591 YAALFDLQAQ 600
Cdd:PRK10895 222 TEILQDEHVK 231
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
359-579 |
3.56e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 58.28 E-value: 3.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 359 ENVSFTYPGtSRAALENIDLhLAPGRS-VALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDALRSRIGVIF 437
Cdd:PRK13652 7 RDLCYSYSG-SKEALNNINF-IAPRNSrIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 438 Q--DFIRYQFLVGENLGVGDTHAFHDETRWREAAAQGMAAQFIEQLDKGYAtqlgrwfaggQELSGGQWQKIALSrAYMR 515
Cdd:PRK13652 85 QnpDDQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVP----------HHLSGGEKKRVAIA-GVIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488616976 516 RDADILILDEPTAALDAGAEAAVFEHFREYAKGR-MTLLIS-HRFSSVRN-AEHIVVLEHGRVLERG 579
Cdd:PRK13652 154 MEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYgMTVIFStHQLDLVPEmADYIYVMDKGRIVAYG 220
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
373-580 |
4.32e-09 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 57.54 E-value: 4.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 373 LENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYqPDQGRILLDGSDLQDWDEDALRSRIGVIFQD----FIR--YQFL 446
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHRAYLSQQqsppFAMpvFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 447 vgenlgvgdthAFHDETRWREAAAQGMAAQFIEQLdkGYATQLGRWFaggQELSGGQWQKIALSRAYMRRDADI------ 520
Cdd:COG4138 91 -----------ALHQPAGASSEAVEQLLAQLAEAL--GLEDKLSRPL---TQLSGGEWQRVRLAAVLLQVWPTInpegql 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488616976 521 LILDEPTAALDAGAEAAVFEHFREYA-KGRMTLLISHRFS-SVRNAEHIVVLEHGRVLERGD 580
Cdd:COG4138 155 LLLDEPMNSLDVAQQAALDRLLRELCqQGITVVMSSHDLNhTLRHADRVWLLKQGKLVASGE 216
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
360-526 |
4.54e-09 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 57.85 E-value: 4.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 360 NVSFTYpgTSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDAL---RSRIGVI 436
Cdd:PRK11831 12 GVSFTR--GNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRMSML 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 437 FQDFIRYQflvgeNLGVGDTHAF--HDETRWREAAAQGMAAQFIEQLDKGYATQLgrwfaGGQELSGGQWQKIALSRAyM 514
Cdd:PRK11831 90 FQSGALFT-----DMNVFDNVAYplREHTQLPAPLLHSTVMMKLEAVGLRGAAKL-----MPSELSGGMARRAALARA-I 158
|
170
....*....|..
gi 488616976 515 RRDADILILDEP 526
Cdd:PRK11831 159 ALEPDLIMFDEP 170
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
370-586 |
5.09e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 59.37 E-value: 5.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 370 RAALENIDLHLAPGRSVALVGENGSGKTTLIK-LLTRLYQPDQGRILLDGSdlqdwdeDALRSRIGVIFQDFIRYQFLVG 448
Cdd:PLN03130 630 RPTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGT-------VAYVPQVSWIFNATVRDNILFG 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 449 enlgvgdthAFHDETRWREAAAQGMAAQFIEQLDKGYATQLGRwfaGGQELSGGQWQKIALSRAyMRRDADILILDEPTA 528
Cdd:PLN03130 703 ---------SPFDPERYERAIDVTALQHDLDLLPGGDLTEIGE---RGVNISGGQKQRVSMARA-VYSNSDVYIFDDPLS 769
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488616976 529 ALDAGAEAAVFEH-FREYAKGRMTLLISHRFSSVRNAEHIVVLEHGRVLERGDHDSLIA 586
Cdd:PLN03130 770 ALDAHVGRQVFDKcIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSN 828
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
358-579 |
6.36e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 59.41 E-value: 6.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 358 FENVSFTYPGTSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDALRSRIGVIF 437
Cdd:PTZ00243 1311 FEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIP 1390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 438 QDFIRYQFLVGENLgvgdtHAFHDETR---WREAAAQGM---AAQFIEQLDkgyatqlGRWFAGGQELSGGQWQKIALSR 511
Cdd:PTZ00243 1391 QDPVLFDGTVRQNV-----DPFLEASSaevWAALELVGLrerVASESEGID-------SRVLEGGSNYSVGQRQLMCMAR 1458
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488616976 512 AYMRRDADILILDEPTA----ALDAGAEAAVFEHFREYAkgrmTLLISHRFSSVRNAEHIVVLEHGRVLERG 579
Cdd:PTZ00243 1459 ALLKKGSGFILMDEATAnidpALDRQIQATVMSAFSAYT----VITIAHRLHTVAQYDKIIVMDHGAVAEMG 1526
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
359-424 |
6.47e-09 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 56.96 E-value: 6.47e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488616976 359 ENVSFTYPGtsRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDW 424
Cdd:COG1137 7 ENLVKSYGK--RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHL 70
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
356-527 |
6.79e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 57.05 E-value: 6.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 356 MRFENVSFTYpgTSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGsdlqdwdedalRSRIGV 435
Cdd:PRK09544 5 VSLENVSVSF--GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG-----------KLRIGY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 436 IFQDFIRYQFLvgeNLGVGDTHAFHDETRWRE---AAAQGMAAQFIEQldkgyatqlgrwfaGGQELSGGQWQKIALSRA 512
Cdd:PRK09544 72 VPQKLYLDTTL---PLTVNRFLRLRPGTKKEDilpALKRVQAGHLIDA--------------PMQKLSGGETQRVLLARA 134
|
170
....*....|....*
gi 488616976 513 YMRRdADILILDEPT 527
Cdd:PRK09544 135 LLNR-PQLLVLDEPT 148
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
372-439 |
8.32e-09 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 56.72 E-value: 8.32e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488616976 372 ALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDALRSRIGVIFQD 439
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQD 95
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
370-527 |
1.25e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 57.73 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 370 RAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWD-EDALRSRIGVIFQDFIRY----Q 444
Cdd:COG3845 271 VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSpRERRRLGVAYIPEDRLGRglvpD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 445 FLVGENLGVGDTHAFHDETRW--REAAAQGMAAQFIEQLD---KGYATQLGRwfaggqeLSGGQWQKIALSRAyMRRDAD 519
Cdd:COG3845 351 MSVAENLILGRYRRPPFSRGGflDRKAIRAFAEELIEEFDvrtPGPDTPARS-------LSGGNQQKVILARE-LSRDPK 422
|
....*...
gi 488616976 520 ILILDEPT 527
Cdd:COG3845 423 LLIAAQPT 430
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
357-527 |
1.48e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 57.83 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 357 RFENVSFTYPGTsrAALENIDLHLAPGRSVALVGENGSGKTTLIKLLT--RLYQpdQGRILLDGSDLQDWDE-DALRSRI 433
Cdd:NF033858 3 RLEGVSHRYGKT--VALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAgaRKIQ--QGRVEVLGGDMADARHrRAVCPRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 434 GVIFQDFIR--YQFL-VGENLgvgDTHA--F-HD--ETRWReaaaqgmaaqfIEQLDKgyATQLGRwF----AGgqELSG 501
Cdd:NF033858 79 AYMPQGLGKnlYPTLsVFENL---DFFGrlFgQDaaERRRR-----------IDELLR--ATGLAP-FadrpAG--KLSG 139
|
170 180
....*....|....*....|....*.
gi 488616976 502 GQWQKIALSRAYMrRDADILILDEPT 527
Cdd:NF033858 140 GMKQKLGLCCALI-HDPDLLILDEPT 164
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
373-580 |
1.74e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 57.87 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 373 LENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRIlldgsdlqdWDEdalRSRIGVIFQDFIRyqflvgeNLG 452
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV---------WAE---RSIAYVPQQAWIM-------NAT 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 453 VGDTHAFHDETRWREAAAQGMAAQF---IEQLDKGYATQLGRwfaGGQELSGGQWQKIALSRA-YMRRDadILILDEPTA 528
Cdd:PTZ00243 737 VRGNILFFDEEDAARLADAVRVSQLeadLAQLGGGLETEIGE---KGVNLSGGQKARVSLARAvYANRD--VYLLDDPLS 811
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488616976 529 ALDAGAEAAVFEH-FREYAKGRMTLLISHRFSSVRNAEHIVVLEHGRVLERGD 580
Cdd:PTZ00243 812 ALDAHVGERVVEEcFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGS 864
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
316-527 |
2.33e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 56.94 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 316 SAISGLYEDGLY-------LADLYIYLGQPvmPSAGSLTQGALPGDGMrfENVSFTypgtsraalenidlhLAPGRSVAL 388
Cdd:PRK10762 223 REVADLTEDSLIemmvgrkLEDQYPRLDKA--PGEVRLKVDNLSGPGV--NDVSFT---------------LRKGEILGV 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 389 VGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQ-DWDEDALRSRIGVIFQDFIRYQFLVG----ENLGVGDTHAF-HDE 462
Cdd:PRK10762 284 SGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVtRSPQDGLANGIVYISEDRKRDGLVLGmsvkENMSLTALRYFsRAG 363
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488616976 463 TRWREAAAQGMAAQFIE-------QLDKgyatQLGrwfaggqELSGGQWQKIALSRAYMRRdADILILDEPT 527
Cdd:PRK10762 364 GSLKHADEQQAVSDFIRlfniktpSMEQ----AIG-------LLSGGNQQKVAIARGLMTR-PKVLILDEPT 423
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
356-526 |
2.33e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 55.56 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 356 MRFENVSFTYpgTSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQ-----PDQGRILLDGSDLQDWDED--A 428
Cdd:PRK14243 11 LRTENLNVYY--GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLYAPDVDpvE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 429 LRSRIGVIFQDFIRYQFLVGENLGVGdthafhdetrwreAAAQGMAAQFIEQLDKGYaTQLGRW-------FAGGQELSG 501
Cdd:PRK14243 89 VRRRIGMVFQKPNPFPKSIYDNIAYG-------------ARINGYKGDMDELVERSL-RQAALWdevkdklKQSGLSLSG 154
|
170 180
....*....|....*....|....*
gi 488616976 502 GQWQKIALSRAyMRRDADILILDEP 526
Cdd:PRK14243 155 GQQQRLCIARA-IAVQPEVILMDEP 178
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
381-527 |
3.45e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 54.68 E-value: 3.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 381 APGRSVALVGENGSGKTTLIKLLTRLYQPDQGRI--------LLD---GSDLQDWDEDALRSRIGVI----FQDFIRYQF 445
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeILDefrGSELQNYFTKLLEGDVKVIvkpqYVDLIPKAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 446 --LVGENLGVGDTHAFHDEtrwreaaaqgmaaqFIEQLDkgYATQLGRWFaggQELSGGQWQKIALSRAYMrRDADILIL 523
Cdd:cd03236 104 kgKVGELLKKKDERGKLDE--------------LVDQLE--LRHVLDRNI---DQLSGGELQRVAIAAALA-RDADFYFF 163
|
....
gi 488616976 524 DEPT 527
Cdd:cd03236 164 DEPS 167
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
372-579 |
3.70e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 56.40 E-value: 3.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 372 ALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDG---SDLQDWDEDALRSRIGVIFQDfiRYQFLvG 448
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGqriDTLSPGKLQALRRDIQFIFQD--PYASL-D 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 449 ENLGVGDT-------HAFHDETrwreaAAQGMAAQFIEQLdkGYATQLGRWFAggQELSGGQWQKIALSRAyMRRDADIL 521
Cdd:PRK10261 416 PRQTVGDSimeplrvHGLLPGK-----AAAARVAWLLERV--GLLPEHAWRYP--HEFSGGQRQRICIARA-LALNPKVI 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488616976 522 ILDEPTAALDAGAEAAVFEHFREYAK--GRMTLLISHRFSSVRNAEH-IVVLEHGRVLERG 579
Cdd:PRK10261 486 IADEAVSALDVSIRGQIINLLLDLQRdfGIAYLFISHDMAVVERISHrVAVMYLGQIVEIG 546
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
30-301 |
4.40e-08 |
|
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: 54.86 E-value: 4.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 30 VGLIVATLVAGLLPALAAWLGQRIVDAVVSAmqlhastgeaplwPVLRYVLLEAGVLALLAGAQRGLSVQQALLRVLLGQ 109
Cdd:cd07346 2 LLALLLLLLATALGLALPLLTKLLIDDVIPA-------------GDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 110 KVNTLI----LEKAQTLSLSQFEDSEFYDKLVRVRREASTRPLALVTKSLGLLQNLISLISFAVLLVHFSpWALLILVLG 185
Cdd:cd07346 69 RVVFDLrrdlFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLN-WKLTLVALL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 186 ALPVFFAEAHFSGDAFRLFTRRAPETRRQ---NYIETLLShegyIKEVKLFGFAPLLLKRYRDTFERLYAEDRRLTVRRD 262
Cdd:cd07346 148 LLPLYVLILRYFRRRIRKASREVRESLAElsaFLQESLSG----IRVVKAFAAEEREIERFREANRDLRDANLRAARLSA 223
|
250 260 270
....*....|....*....|....*....|....*....
gi 488616976 263 GWGFLLGLLGTASFYLAYAWVVVDAVHGRITLGQMTMYL 301
Cdd:cd07346 224 LFSPLIGLLTALGTALVLLYGGYLVLQGSLTIGELVAFL 262
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
382-556 |
6.06e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.59 E-value: 6.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 382 PGRSVALVGENGSGKTTLIKLLTRLYQPDQGRI--------LLD---GSDLQDWDEDALRSRIGVIFQ----DFIRYQFL 446
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNLGDYeeepswdeVLKrfrGTELQNYFKKLYNGEIKVVHKpqyvDLIPKVFK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 447 --VGENLgvgdthafhdetrwREAAAQGMAAQFIEQLDKGYAtqLGRWFaggQELSGGQWQKIALSRAYMRrDADILILD 524
Cdd:PRK13409 178 gkVRELL--------------KKVDERGKLDEVVERLGLENI--LDRDI---SELSGGELQRVAIAAALLR-DADFYFFD 237
|
170 180 190
....*....|....*....|....*....|..
gi 488616976 525 EPTAALDAGAEAAVFEHFREYAKGRMTLLISH 556
Cdd:PRK13409 238 EPTSYLDIRQRLNVARLIRELAEGKYVLVVEH 269
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
370-457 |
6.76e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 54.16 E-value: 6.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 370 RAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDAL---------RSRIGVIFQ-- 438
Cdd:PRK11701 19 RKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaerrrllRTEWGFVHQhp 98
|
90 100
....*....|....*....|....*
gi 488616976 439 -DFIRYQFLVGENLG-----VGDTH 457
Cdd:PRK11701 99 rDGLRMQVSAGGNIGerlmaVGARH 123
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
350-416 |
7.70e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 55.18 E-value: 7.70e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488616976 350 ALPGDGMRFENVSFTYpgTSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILL 416
Cdd:PRK10636 307 SLPNPLLKMEKVSAGY--GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL 371
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
373-556 |
8.24e-08 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 53.28 E-value: 8.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 373 LENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDEDA---LRSR-IGVIFQ------DF-- 440
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRNQkLGFIYQfhhllpDFta 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 441 ---IRYQFLVGenlGVGDTHAfhdetrwREAAAQGMAAQFIEQldkgyatqlgRWFAGGQELSGGQWQKIALSRAYMRRD 517
Cdd:PRK11629 105 lenVAMPLLIG---KKKPAEI-------NSRALEMLAAVGLEH----------RANHRPSELSGGERQRVAIARALVNNP 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488616976 518 ADILIlDEPTAALDAGAEAAVFEHFREY--AKGRMTLLISH 556
Cdd:PRK11629 165 RLVLA-DEPTGNLDARNADSIFQLLGELnrLQGTAFLVVTH 204
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
383-527 |
1.45e-07 |
|
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: 54.41 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 383 GRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLD----------GSDLQDWDEDALRSRIGVIFqdfiryqflvgenlg 452
Cdd:COG1245 366 GEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDlkisykpqyiSPDYDGTVEEFLRSANTDDF--------------- 430
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488616976 453 vgdthafhDETRWREAAAQGMaaqfieQLDKGYATQLGrwfaggqELSGGQWQKIALSrAYMRRDADILILDEPT 527
Cdd:COG1245 431 --------GSSYYKTEIIKPL------GLEKLLDKNVK-------DLSGGELQRVAIA-ACLSRDADLYLLDEPS 483
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
373-579 |
1.59e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 52.92 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 373 LENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQ-----GRILLDGSDLQDWDEDAL--RSRIGVIFQDFIRYQF 445
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNIYSPDVDPIevRREVGMVFQYPNPFPH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 446 L-VGENLGVG--------DTHAFHDETRWreaaAQGMAAQFIEQLD--KGYATQLgrwfaggqelSGGQWQKIALSRAYM 514
Cdd:PRK14267 100 LtIYDNVAIGvklnglvkSKKELDERVEW----ALKKAALWDEVKDrlNDYPSNL----------SGGQRQRLVIARALA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488616976 515 RRdADILILDEPTAALDAGAEAAVFEHFREYAKGRMTLLISHR-FSSVRNAEHIVVLEHGRVLERG 579
Cdd:PRK14267 166 MK-PKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVG 230
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
360-526 |
1.59e-07 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 53.88 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 360 NVSFTYPGT--SRaaleNIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWdEDALRSrIGVIF 437
Cdd:PRK11000 8 NVTKAYGDVviSK----DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDV-PPAERG-VGMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 438 QDFIRYQFL-VGENLGVGDTHAFHDET----RWREAAAQGMAAQFIEQLDKgyatqlgrwfaggqELSGGQWQKIALSRA 512
Cdd:PRK11000 82 QSYALYPHLsVAENMSFGLKLAGAKKEeinqRVNQVAEVLQLAHLLDRKPK--------------ALSGGQRQRVAIGRT 147
|
170
....*....|....
gi 488616976 513 yMRRDADILILDEP 526
Cdd:PRK11000 148 -LVAEPSVFLLDEP 160
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
372-580 |
1.63e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 53.32 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 372 ALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRI----LLDGSDLQDWDEDA------------LRSRIGV 435
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNHELITnpyskkiknfkeLRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 436 IFQdFIRYQF---------LVGE-NLGVGdthafhdetrwREAAAQgMAAQFIEQLDKGYaTQLGRwfaGGQELSGGQWQ 505
Cdd:PRK13631 121 VFQ-FPEYQLfkdtiekdiMFGPvALGVK-----------KSEAKK-LAKFYLNKMGLDD-SYLER---SPFGLSGGQKR 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488616976 506 KIALSrAYMRRDADILILDEPTAALDAGAEAAVFEHFREY-AKGRMTLLISHRFSSVRN-AEHIVVLEHGRVLERGD 580
Cdd:PRK13631 184 RVAIA-GILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAkANNKTVFVITHTMEHVLEvADEVIVMDKGKILKTGT 259
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
354-593 |
3.15e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 52.01 E-value: 3.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 354 DGMRFENVSFTypgTSRAALENIDLHLAPGRSVALVGENGSGKT----TLIKLLTRLYQPDQGRILLDGSDLQdwdEDAL 429
Cdd:PRK10418 3 QQIELRNIALQ---AAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVA---PCAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 430 RSR-IGVIFQDfIRYQFLVGENLGvgdTHAFhdETrWREAAAQGMAAQFIEQLDK---GYATQLGRWFAGgqELSGGQWQ 505
Cdd:PRK10418 77 RGRkIATIMQN-PRSAFNPLHTMH---THAR--ET-CLALGKPADDATLTAALEAvglENAARVLKLYPF--EMSGGMLQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 506 KIALSRAYMRrDADILILDEPTAALDAGAEAAVFEHFREYAKGRM--TLLISHRFSSV-RNAEHIVVLEHGRVLERGDHD 582
Cdd:PRK10418 148 RMMIALALLC-EAPFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVaRLADDVAVMSHGRIVEQGDVE 226
|
250
....*....|.
gi 488616976 583 SLIAAAGRYAA 593
Cdd:PRK10418 227 TLFNAPKHAVT 237
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
382-527 |
3.69e-07 |
|
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: 53.25 E-value: 3.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 382 PGRSVALVGENGSGKTTLIKLLTRLYQPDQGRI--------LLD---GSDLQDWDEDALRSRIGVIFQ----DFIRYQF- 445
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDYdeepswdeVLKrfrGTELQDYFKKLANGEIKVAHKpqyvDLIPKVFk 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 446 -LVGENLgvgdthafhdetrwREAAAQGMAAQFIEQLDKGYAtqLGRWFaggQELSGGQWQKIALSRAYMRrDADILILD 524
Cdd:COG1245 178 gTVRELL--------------EKVDERGKLDELAEKLGLENI--LDRDI---SELSGGELQRVAIAAALLR-DADFYFFD 237
|
...
gi 488616976 525 EPT 527
Cdd:COG1245 238 EPS 240
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
354-588 |
3.75e-07 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 51.81 E-value: 3.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 354 DGMRFENVSFTYPgTSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRIlldgSDLQDWDEDALRSRI 433
Cdd:PRK15056 5 AGIVVNDVTVTWR-NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKI----SILGQPTRQALQKNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 434 --------------GVIFQDFI---RYQflvgeNLGVGDTHAFHDETRWREAAAQgmaaqfIEQLDKGYaTQLGrwfagg 496
Cdd:PRK15056 80 vayvpqseevdwsfPVLVEDVVmmgRYG-----HMGWLRRAKKRDRQIVTAALAR------VDMVEFRH-RQIG------ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 497 qELSGGQWQKIALSRAyMRRDADILILDEPTAALDAGAEAAVFEHFREY-AKGRMTLLISHRFSSVRNAEHIVVLEHGRV 575
Cdd:PRK15056 142 -ELSGGQKKRVFLARA-IAQQGQVILLDEPFTGVDVKTEARIISLLRELrDEGKTMLVSTHNLGSVTEFCDYTVMVKGTV 219
|
250
....*....|...
gi 488616976 576 LERGDHDSLIAAA 588
Cdd:PRK15056 220 LASGPTETTFTAE 232
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
356-572 |
4.54e-07 |
|
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: 49.84 E-value: 4.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 356 MRFENVSFTYPgTSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDgsdlqdWDEDALrsrigv 435
Cdd:cd03223 1 IELENLSLATP-DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMP------EGEDLL------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 436 ifqdFI-RYQFLVGENLgvgdthafhdetrwREAAAqgmaaqfieqldkgYAtqlgrWfagGQELSGGQWQKIALSRAYM 514
Cdd:cd03223 68 ----FLpQRPYLPLGTL--------------REQLI--------------YP-----W---DDVLSGGEQQRLAFARLLL 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488616976 515 RRdADILILDEPTAALDAGAEAAVFEHFREYakgRMTLL-ISHRFSSVRNAEHIVVLEH 572
Cdd:cd03223 108 HK-PKFVFLDEATSALDEESEDRLYQLLKEL---GITVIsVGHRPSLWKFHDRVLDLDG 162
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
369-579 |
5.12e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 51.37 E-value: 5.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 369 SRAALENIDLHLAPGRSVALVGENGSGKTTLIKL----LTRLYQPD----QGRILLDGSDLQDWDEDALRSRIGVIFQDF 440
Cdd:PRK13547 13 HRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKAlagdLTGGGAPRgarvTGDVTLNGEPLAAIDAPRLARLRAVLPQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 441 IR-YQFLVGENLGVGD-THAFH---DETRWREAAAQGMAAQFIEQLDKGYATQlgrwfaggqeLSGGQWQKIALSRAYMR 515
Cdd:PRK13547 93 QPaFAFSAREIVLLGRyPHARRagaLTHRDGEIAWQALALAGATALVGRDVTT----------LSGGELARVQFARVLAQ 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488616976 516 --------RDADILILDEPTAALDAGAEAAVFEHFREYAKG-RMTLL-ISHRFS-SVRNAEHIVVLEHGRVLERG 579
Cdd:PRK13547 163 lwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLaIVHDPNlAARHADRIAMLADGAIVAHG 237
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
356-527 |
1.01e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 52.05 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 356 MRFENvsFTypgtsraALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILL-----DGSDLqdwdedALR 430
Cdd:NF033858 274 MRFGD--FT-------AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLfgqpvDAGDI------ATR 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 431 SRIGVIFQDFIRYQFL-VGENLgvgDTHA--FH-DETRWREAAAQgMAAQFieQLdKGYATQLgrwfagGQELSGGQWQK 506
Cdd:NF033858 339 RRVGYMSQAFSLYGELtVRQNL---ELHArlFHlPAAEIAARVAE-MLERF--DL-ADVADAL------PDSLPLGIRQR 405
|
170 180
....*....|....*....|.
gi 488616976 507 IALSRAyMRRDADILILDEPT 527
Cdd:NF033858 406 LSLAVA-VIHKPELLILDEPT 425
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
356-527 |
1.08e-06 |
|
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: 51.36 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 356 MRFENVSFTYP-GTSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPD-QGRILLDGSDLQDWD-EDALRSR 432
Cdd:TIGR02633 258 LEARNLTCWDViNPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNpAQAIRAG 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 433 IGVIFQDFIRY----QFLVGENLGVGDTHAFHDETRWREAAAQGMAAQFIEQLDKGYATQlgrwFAGGQELSGGQWQKIA 508
Cdd:TIGR02633 338 IAMVPEDRKRHgivpILGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASP----FLPIGRLSGGNQQKAV 413
|
170
....*....|....*....
gi 488616976 509 LSRAYMRrDADILILDEPT 527
Cdd:TIGR02633 414 LAKMLLT-NPRVLILDEPT 431
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
363-573 |
1.21e-06 |
|
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: 49.64 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 363 FTYpGTSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGS--DLQDWDEDALRSRIGVIF--Q 438
Cdd:cd03290 8 FSW-GSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKneSEPSFEATRSRNRYSVAYaaQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 439 DFIRYQFLVGENLGVGDThafHDETRWREAAAQGMAAQFIEQLDKGYATQLGRwfaGGQELSGGQWQKIALSRAyMRRDA 518
Cdd:cd03290 87 KPWLLNATVEENITFGSP---FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGE---RGINLSGGQRQRICVARA-LYQNT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 519 DILILDEP-----TAALDAGAEAAVFEHFREyaKGRMTLLISHRFSSVRNAEHIVVLEHG 573
Cdd:cd03290 160 NIVFLDDPfsaldIHLSDHLMQEGILKFLQD--DKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
357-555 |
1.92e-06 |
|
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: 49.19 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 357 RFENVS--FTYPGTSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPD---QGRILLDGSDLqdwDEDALRS 431
Cdd:cd03234 5 PWWDVGlkAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPR---KPDQFQK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 432 RIGVIFQDfiryQFLVgENLGVGDTHAFHDETRWREAAAQGMAAQFIEQLDKGYA--TQLGRWFAGGqeLSGGQWQKIAL 509
Cdd:cd03234 82 CVAYVRQD----DILL-PGLTVRETLTYTAILRLPRKSSDAIRKKRVEDVLLRDLalTRIGGNLVKG--ISGGERRRVSI 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488616976 510 SRAyMRRDADILILDEPTAALDAGAEAAVFEHFREYAKGRMTLLIS 555
Cdd:cd03234 155 AVQ-LLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILT 199
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
382-430 |
2.36e-06 |
|
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: 47.75 E-value: 2.36e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 488616976 382 PGRSVALVGENGSGKTTLIKLLTRLYQPDQGR-ILLDGSDLQDWDEDALR 430
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLL 50
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
353-414 |
3.89e-06 |
|
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: 49.93 E-value: 3.89e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488616976 353 GDGMRFENVSFTYPgtsraalenidlhlaPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRI 414
Cdd:TIGR03719 333 GDKLLIDDLSFKLP---------------PGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTI 379
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
373-442 |
4.04e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 48.48 E-value: 4.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 373 LENIDLHLAPGRSVALVGENGSGKTTLIKLLT--RLYQPDQGRILLDGSDLQDWDEDAlRSRIGVI--FQ---------- 438
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAghPAYKILEGDILFKGESILDLEPEE-RAHLGIFlaFQypieipgvsn 101
|
....*
gi 488616976 439 -DFIR 442
Cdd:CHL00131 102 aDFLR 106
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
364-526 |
4.21e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 47.92 E-value: 4.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 364 TYPGTSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDED---ALRSRIGVIFQDF 440
Cdd:PRK13543 18 AFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSrfmAYLGHLPGLKADL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 441 IRYqflvgENLG-VGDTHAFHDETRWREA-AAQGMAaqfieqldkGYATQLGRwfaggqELSGGQWQKIALSRAYMrRDA 518
Cdd:PRK13543 98 STL-----ENLHfLCGLHGRRAKQMPGSAlAIVGLA---------GYEDTLVR------QLSAGQKKRLALARLWL-SPA 156
|
....*...
gi 488616976 519 DILILDEP 526
Cdd:PRK13543 157 PLWLLDEP 164
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
359-414 |
4.80e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.56 E-value: 4.80e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 488616976 359 ENVSFTYPGtsRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRI 414
Cdd:PRK11147 323 ENVNYQIDG--KQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI 376
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
360-580 |
5.05e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 49.47 E-value: 5.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 360 NVSFTYPGTSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGS----------DLQDWDEDAL 429
Cdd:PRK10261 19 NIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrsrqviELSEQSAAQM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 430 R----SRIGVIFQD---FIRYQFLVGENlgVGDTHAFHDETRWREAAAQgmAAQFIEQLDKGYA-TQLGRWfagGQELSG 501
Cdd:PRK10261 99 RhvrgADMAMIFQEpmtSLNPVFTVGEQ--IAESIRLHQGASREEAMVE--AKRMLDQVRIPEAqTILSRY---PHQLSG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 502 GQWQKIALSRAYMRRDAdILILDEPTAALDAGAEAAVFEHFR----EYAKGrmTLLISHRFSSVRN-AEHIVVLEHGRVL 576
Cdd:PRK10261 172 GMRQRVMIAMALSCRPA-VLIADEPTTALDVTIQAQILQLIKvlqkEMSMG--VIFITHDMGVVAEiADRVLVMYQGEAV 248
|
....
gi 488616976 577 ERGD 580
Cdd:PRK10261 249 ETGS 252
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
360-527 |
6.20e-06 |
|
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: 49.16 E-value: 6.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 360 NVSFTYPGTsRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLD-----GSDLQDWDEDALRSRIG 434
Cdd:TIGR03719 9 RVSKVVPPK-KEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQpgikvGYLPQEPQLDPTKTVRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 435 VIFQDfiryqflVGENLGVGD-----THAFHDETRWREAAAQGMAaQFIEQLDKGYATQLGR-------------WFAGG 496
Cdd:TIGR03719 88 NVEEG-------VAEIKDALDrfneiSAKYAEPDADFDKLAAEQA-ELQEIIDAADAWDLDSqleiamdalrcppWDADV 159
|
170 180 190
....*....|....*....|....*....|.
gi 488616976 497 QELSGGQWQKIALSRAYMRRdADILILDEPT 527
Cdd:TIGR03719 160 TKLSGGERRRVALCRLLLSK-PDMLLLDEPT 189
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
386-527 |
7.69e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 49.04 E-value: 7.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 386 VALVGENGSGKTTLIKLLTRLYQPDQGRIlldgsdlqDWDEDA------LRSRIGVIFQDFIRYqflVGENLgvgdthaf 459
Cdd:PRK13409 368 IGIVGPNGIGKTTFAKLLAGVLKPDEGEV--------DPELKIsykpqyIKPDYDGTVEDLLRS---ITDDL-------- 428
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488616976 460 hDETRWREAAAQGMaaqfieQLDKGYATQLGrwfaggqELSGGQWQKIALSrAYMRRDADILILDEPT 527
Cdd:PRK13409 429 -GSSYYKSEIIKPL------QLERLLDKNVK-------DLSGGELQRVAIA-ACLSRDADLYLLDEPS 481
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
373-442 |
9.15e-06 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 48.07 E-value: 9.15e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488616976 373 LENIDLHLAPGRSVaLVGENGSGKTTLIKLLTRLYQPDQGRIlLDGSDLQDWDEDALRS-RIGVIFQDFIR 442
Cdd:COG3593 14 IKDLSIELSDDLTV-LVGENNSGKSSILEALRLLLGPSSSRK-FDEEDFYLGDDPDLPEiEIELTFGSLLS 82
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
353-414 |
1.38e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.19 E-value: 1.38e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488616976 353 GDGMRFENVSFTYPgtsraalenidlhlaPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRI 414
Cdd:PRK11819 335 GDRLLIDDLSFSLP---------------PGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI 381
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
380-527 |
1.43e-05 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 46.85 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 380 LAPGRSVALVGENGSGKTTLIKLLTRLYqPDQGRILLDGSDLQDWDEDALRSRIGVIFQD----FIR--YQFLvgenlgv 453
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLSQQqtppFAMpvFQYL------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 454 gdthAFHDETRWREAAAQGMAAQFIEQLdkGYATQLGRWFaggQELSGGQWQKIALSRAYMRRDADI------LILDEPT 527
Cdd:PRK03695 91 ----TLHQPDKTRTEAVASALNEVAEAL--GLDDKLGRSV---NQLSGGEWQRVRLAAVVLQVWPDInpagqlLLLDEPM 161
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
356-403 |
1.74e-05 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 45.70 E-value: 1.74e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 488616976 356 MRFENVSFTY--PGTSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLL 403
Cdd:cd03232 4 LTWKNLNYTVpvKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVL 53
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
360-527 |
1.99e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 47.03 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 360 NVSFTYPGTSRAALENIDLHLAPGRSVALVGENGSGKT----TLIKLLTRlyqpdQGRI----LLDGSDLQDWDEDAL-R 430
Cdd:PRK09473 19 RVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAA-----NGRIggsaTFNGREILNLPEKELnK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 431 SR---IGVIFQD-------FIRyqflVGENL--------GVGDTHAFHDETRWREAAAQGMAAQFIeqldKGYAtqlgrw 492
Cdd:PRK09473 94 LRaeqISMIFQDpmtslnpYMR----VGEQLmevlmlhkGMSKAEAFEESVRMLDAVKMPEARKRM----KMYP------ 159
|
170 180 190
....*....|....*....|....*....|....*
gi 488616976 493 faggQELSGGQWQKIALSRAYMRRdADILILDEPT 527
Cdd:PRK09473 160 ----HEFSGGMRQRVMIAMALLCR-PKLLIADEPT 189
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
377-588 |
2.59e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.93 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 377 DLHLAPGRSVALVGENGSGKTTLIKLLTrlyqpdQGRILLDGSDLQDWDEDALRSrigvifqdFIRYQFLVGEN------ 450
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALA------GELPLLSGERQSQFSHITRLS--------FEQLQKLVSDEwqrnnt 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 451 --LGVG--DT-----HAFHDETRWREAAAQgMAAQF-IEQLdkgyatqLGRWFaggQELSGGQWQKIALSRAYMRrDADI 520
Cdd:PRK10938 89 dmLSPGedDTgrttaEIIQDEVKDPARCEQ-LAQQFgITAL-------LDRRF---KYLSTGETRKTLLCQALMS-EPDL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 521 LILDEPTAALDAGAEAAVFEHFREYAKGRMTL-LISHRFSSVRN-AEHIVVLEHGRVLERGDHDSLIAAA 588
Cdd:PRK10938 157 LILDEPFDGLDVASRQQLAELLASLHQSGITLvLVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQQA 226
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
373-579 |
2.93e-05 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 46.96 E-value: 2.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 373 LENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPD---QGRILLDGSDLqdwDEDALRSRIGVIFQDFIryqfLVGe 449
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPI---DAKEMRAISAYVQQDDL----FIP- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 450 NLGVGDTHAFHDETRW--REAAAQGMAA--QFIEQLDKGYA--TQLGrwfAGGQE--LSGGQWQKIALSRAYMRrDADIL 521
Cdd:TIGR00955 113 TLTVREHLMFQAHLRMprRVTKKEKRERvdEVLQALGLRKCanTRIG---VPGRVkgLSGGERKRLAFASELLT-DPPLL 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488616976 522 ILDEPTAALDAGAEAAVFEHFREYAKGRMTLLIS-HRFSS--VRNAEHIVVLEHGRVLERG 579
Cdd:TIGR00955 189 FCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTiHQPSSelFELFDKIILMAEGRVAYLG 249
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
361-579 |
3.57e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 46.27 E-value: 3.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 361 VSFTYPGTSRAALENIDLHLAPGRSVALVGENGSGKTT-------LIKLLTRLYQPdqgRILLDGSDLQDWDEDALRSRI 433
Cdd:PRK11022 11 VHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVsslaimgLIDYPGRVMAE---KLEFNGQDLQRISEKERRNLV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 434 G----VIFQD---------FIRYQFLVGENLGVGDTHafhdetRWREAAAqgmaaqfIEQLdkgyaTQLG------RWFA 494
Cdd:PRK11022 88 GaevaMIFQDpmtslnpcyTVGFQIMEAIKVHQGGNK------KTRRQRA-------IDLL-----NQVGipdpasRLDV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 495 GGQELSGGQWQKIALSRAYMRRdADILILDEPTAALDAGAEAAVFEHFREYA-KGRMTL-LISHRFSSV-RNAEHIVVLE 571
Cdd:PRK11022 150 YPHQLSGGMSQRVMIAMAIACR-PKLLIADEPTTALDVTIQAQIIELLLELQqKENMALvLITHDLALVaEAAHKIIVMY 228
|
....*...
gi 488616976 572 HGRVLERG 579
Cdd:PRK11022 229 AGQVVETG 236
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
370-429 |
6.07e-05 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 44.56 E-value: 6.07e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488616976 370 RAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLY--QPDQGRILLDgsDLQDWDEDAL 429
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVP--DNQFGREASL 102
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
356-527 |
7.18e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 45.69 E-value: 7.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 356 MRFENVSFTYP-GTSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQ-PDQGRILLDGSDLQ-DWDEDALRSR 432
Cdd:PRK13549 260 LEVRNLTAWDPvNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKiRNPQQAIAQG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 433 IGVIFQDFIRY----QFLVGENLGVGDTHAFHDETRWREAAAQGMAAQFIEQLDKGYAT---QLGRwfaggqeLSGGQWQ 505
Cdd:PRK13549 340 IAMVPEDRKRDgivpVMGVGKNITLAALDRFTGGSRIDDAAELKTILESIQRLKVKTASpelAIAR-------LSGGNQQ 412
|
170 180
....*....|....*....|..
gi 488616976 506 KIALSRAYMRrDADILILDEPT 527
Cdd:PRK13549 413 KAVLAKCLLL-NPKILILDEPT 433
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
354-404 |
9.60e-05 |
|
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: 45.77 E-value: 9.60e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 488616976 354 DGMRFENVSFTYPGTSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLT 404
Cdd:TIGR01257 1936 DILRLNELTKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLT 1986
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
375-527 |
1.17e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 45.04 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 375 NIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDwDEDALRSRIGVIFQDFIRYQ---FL---VG 448
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINA-LSTAQRLARGLVYLPEDRQSsglYLdapLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 449 ENLgVGDTHafHDETRWREAAAQgmAAQFieqldKGYATQLGRWFAGGQE----LSGGQWQKIALSRAyMRRDADILILD 524
Cdd:PRK15439 360 WNV-CALTH--NRRGFWIKPARE--NAVL-----ERYRRALNIKFNHAEQaartLSGGNQQKVLIAKC-LEASPQLLIVD 428
|
...
gi 488616976 525 EPT 527
Cdd:PRK15439 429 EPT 431
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
355-526 |
2.48e-04 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 43.68 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 355 GMRFENVSFTYPGtSRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWdEDALRSrIG 434
Cdd:PRK11650 3 GLKLQAVRKSYDG-KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNEL-EPADRD-IA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 435 VIFQDFIRYQFL-VGENL-------GVGDTHAfhdETRWREAAAqgmaAQFIEQLdkgyatqLGRwfaGGQELSGGQWQK 506
Cdd:PRK11650 80 MVFQNYALYPHMsVRENMayglkirGMPKAEI---EERVAEAAR----ILELEPL-------LDR---KPRELSGGQRQR 142
|
170 180
....*....|....*....|
gi 488616976 507 IALSRAyMRRDADILILDEP 526
Cdd:PRK11650 143 VAMGRA-IVREPAVFLFDEP 161
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
27-261 |
3.65e-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: 349994 [Multi-domain] Cd Length: 294 Bit Score: 42.85 E-value: 3.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 27 ALSVGLIVATLVAGLLPALaawLGQRIVDavvsamqlhastgEAPLWPVLRYVLLEAGVLALLAGAQRGLSVQQALLRVL 106
Cdd:cd18550 2 ALVLLLILLSALLGLLPPL---LLREIID-------------DALPQGDLGLLVLLALGMVAVAVASALLGVVQTYLSAR 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 107 LGQKV----NTLILEKAQTLSLSQFedsefydklvrvrreASTRPLALVTK---------------SLGLLQNLISLISF 167
Cdd:cd18550 66 IGQGVmydlRVQLYAHLQRMSLAFF---------------TRTRTGEIQSRlnndvggaqsvvtgtLTSVVSNVVTLVAT 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 168 AVLLVHFSpWALLILVLGALPVFFAEAHFSGDAFRLFTRrapetRRQNYIETLLSHegyIKE---------VKLFGFAPL 238
Cdd:cd18550 131 LVAMLALD-WRLALLSLVLLPLFVLPTRRVGRRRRKLTR-----EQQEKLAELNSI---MQEtlsvsgallVKLFGREDD 201
|
250 260
....*....|....*....|...
gi 488616976 239 LLKRYRDTFERLyaedRRLTVRR 261
Cdd:cd18550 202 EAARFARRSREL----RDLGVRQ 220
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
28-215 |
4.55e-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: 350008 [Multi-domain] Cd Length: 307 Bit Score: 42.50 E-value: 4.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 28 LSVGLiVATLVAGLLPALAAWLGQRIVDAVVSAMQLHASTGEAPLWP--VLRYVLLEAGVLALLAGAQRGLSVQQALLRV 105
Cdd:cd18564 1 LALAL-LALLLETALRLLEPWPLKVVIDDVLGDKPLPGLLGLAPLLGpdPLALLLLAAAALVGIALLRGLASYAGTYLTA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 106 LLGQKV-NTL---ILEKAQTLSLSQFEDSEFYDKLVRVRREASTRPLALVTKSLGLLQNLISLISFAVLLVHFSpWALLI 181
Cdd:cd18564 80 LVGQRVvLDLrrdLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLD-WQLAL 158
|
170 180 190
....*....|....*....|....*....|....*
gi 488616976 182 LVLGALPVFF-AEAHFSgdafRLFTRRAPETRRQN 215
Cdd:cd18564 159 IALAVAPLLLlAARRFS----RRIKEASREQRRRE 189
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
28-304 |
1.02e-03 |
|
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: 41.47 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 28 LSVGLIVATLVAGLLPALAAWLGqRIVDAVVSamqlhasTGEAPLWPVLRYVLLeagVLALLAGAQRGLSVQQALLRVLL 107
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLG-RILDVLLP-------DGDPETQALNVYSLA---LLLLGLAQFILSFLQSYLLNHTG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 108 GQ---KVNTLILEKAQTLSLSQFEDSEFYDKLVRVRREASTRPLALVTKSLGLLQNLISLISFAVLLVHFSPWALLILVL 184
Cdd:pfam00664 70 ERlsrRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 185 GALPVFFAEAHFSGdAFRLFTRRAPETR--RQNYIETLLSHegyIKEVKLFGFAPLLLKRYRDTFERLYAEDRRLTVRRD 262
Cdd:pfam00664 150 VLPLYILVSAVFAK-ILRKLSRKEQKAVakASSVAEESLSG---IRTVKAFGREEYELEKYDKALEEALKAGIKKAVANG 225
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 488616976 263 GWGFLLGLLGTASFYLAYAWVVVDAVHGRITLGQMTMYLVLF 304
Cdd:pfam00664 226 LSFGITQFIGYLSYALALWFGAYLVISGELSVGDLVAFLSLF 267
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
370-602 |
1.05e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 41.32 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 370 RAALENIDLHLAPGRSVALVGENGSGKTTLIKLLT--RLYQPDQGRILLDGSDLQDWDEDAlRSRIGVifqdFIRYQFLV 447
Cdd:PRK09580 14 KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPED-RAGEGI----FMAFQYPV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 448 gENLGVGDTHAFHD------ETRWREAAAQGMAAQFIE---QLDKGYATQLGR----WFAGGQELSGGQWQKIALsraym 514
Cdd:PRK09580 89 -EIPGVSNQFFLQTalnavrSYRGQEPLDRFDFQDLMEekiALLKMPEDLLTRsvnvGFSGGEKKRNDILQMAVL----- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 515 rrDADILILDEPTAALDAGAEAAVFEHFREYAKGRMTLLISHRFSSVRN---AEHIVVLEHGRVLERGDHdSLIAaagry 591
Cdd:PRK09580 163 --EPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDyikPDYVHVLYQGRIVKSGDF-TLVK----- 234
|
250
....*....|.
gi 488616976 592 aalfDLQAQGY 602
Cdd:PRK09580 235 ----QLEEQGY 241
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
372-419 |
1.28e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 41.80 E-value: 1.28e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 488616976 372 ALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGS 419
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS 86
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
375-414 |
1.37e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 41.14 E-value: 1.37e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 488616976 375 NIDLHLAPGRSVaLVGENGSGKTTLIKLLTRLYQPDQGRI 414
Cdd:COG3950 18 EIDFDNPPRLTV-LVGENGSGKTTLLEAIALALSGLLSRL 56
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
499-527 |
1.89e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.93 E-value: 1.89e-03
10 20
....*....|....*....|....*....
gi 488616976 499 LSGGQWQKIALSRaYMRRDADILILDEPT 527
Cdd:NF040905 405 LSGGNQQKVVLSK-WLFTDPDVLILDEPT 432
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
30-322 |
1.95e-03 |
|
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: 40.54 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 30 VGLIVATLVAGLLPalaaWLGQRIVDAVvsamqlhasTGEAPLWPVLRYVLLEAGVLALlagaQRGLSVQQALLRVLLGQ 109
Cdd:cd18576 3 ILLLLSSAIGLVFP----LLAGQLIDAA---------LGGGDTASLNQIALLLLGLFLL----QAVFSFFRIYLFARVGE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 110 KVNTLI----LEKAQTLSLSQFEDSEFYDKLVRVRREASTRPLALVTKSLGLLQNLISLISFAVLLVHFSpWALLILVLG 185
Cdd:cd18576 66 RVVADLrkdlYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFIS-WKLTLLMLA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 186 ALPVFFAEAHFSGDAFRLFTRRA-PETRRQNYI--ETLLShegyIKEVKLFGFAPLLLKRYRDTFERLYaedrRLTVRRD 262
Cdd:cd18576 145 TVPVVVLVAVLFGRRIRKLSKKVqDELAEANTIveETLQG----IRVVKAFTREDYEIERYRKALERVV----KLALKRA 216
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488616976 263 GWGFLLGLLGTASFYLAYAWVVVDAVH----GRITLGQMTMYLVLfkqgQAAVSSSLSAISGLY 322
Cdd:cd18576 217 RIRALFSSFIIFLLFGAIVAVLWYGGRlvlaGELTAGDLVAFLLY----TLFIAGSIGSLADLY 276
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
338-527 |
2.38e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.00 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 338 PVMPSAGSLTQGALPGDgMRFENVSFTYPGtsRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLT-----------RL 406
Cdd:PLN03073 161 GVYVNHDGNGGGPAIKD-IHMENFSISVGG--RDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAmhaidgipkncQI 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 407 YQPDQGRILLDGSDLQ-DWDEDALRSRIGVIFQDFIRYQFLVGENLGVGDTHAFHDETRWREAAAQGMAAQF--IEQLDK 483
Cdd:PLN03073 238 LHVEQEVVGDDTTALQcVLNTDIERTQLLEEEAQLVAQQRELEFETETGKGKGANKDGVDKDAVSQRLEEIYkrLELIDA 317
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488616976 484 GYA-TQLGRWFAG-----------GQELSGGQWQKIALSRAyMRRDADILILDEPT 527
Cdd:PLN03073 318 YTAeARAASILAGlsftpemqvkaTKTFSGGWRMRIALARA-LFIEPDLLLLDEPT 372
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
370-419 |
4.57e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 40.15 E-value: 4.57e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 488616976 370 RAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGS 419
Cdd:PRK10636 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGN 63
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
358-414 |
5.95e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 39.84 E-value: 5.95e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 488616976 358 FENVSFTYPGTSrAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRI 414
Cdd:PLN03073 511 FSDASFGYPGGP-LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV 566
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
370-577 |
8.60e-03 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 39.00 E-value: 8.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 370 RAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGRILLDGSDLQDWDE-DALRSRIGVI---------FQD 439
Cdd:PRK09700 276 RKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPlDAVKKGMAYItesrrdngfFPN 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 440 F-IRYQFLVGENL---GVGDTHAF---HDETRWREAAAQGMAAQ--FIEQldkgyatqlgrwfaGGQELSGGQWQKIALS 510
Cdd:PRK09700 356 FsIAQNMAISRSLkdgGYKGAMGLfheVDEQRTAENQRELLALKchSVNQ--------------NITELSGGNQQKVLIS 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488616976 511 RaYMRRDADILILDEPTAALDAGAEAAVFEHFREYA-KGRMTLLISHRFSSVRNA-EHIVVLEHGRVLE 577
Cdd:PRK09700 422 K-WLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLAdDGKVILMVSSELPEIITVcDRIAVFCEGRLTQ 489
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
360-527 |
8.80e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 38.95 E-value: 8.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 360 NVSFTYPGTsRAALENIDLHLAPGRSVALVGENGSGKTTLIKLLTRLYQPDQGR-ILLDGsdlqdwdedalrSRIGVIFQ 438
Cdd:PRK11819 11 RVSKVVPPK-KQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEaRPAPG------------IKVGYLPQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488616976 439 DfiryQFL-----VGENL--GVGDTHAFHDetRWREAAAQgMA-------------AQFIEQLDKGYATQLGR------- 491
Cdd:PRK11819 78 E----PQLdpektVRENVeeGVAEVKAALD--RFNEIYAA-YAepdadfdalaaeqGELQEIIDAADAWDLDSqleiamd 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488616976 492 ------WFAGGQELSGGQWQKIALSRAYMRRdADILILDEPT 527
Cdd:PRK11819 151 alrcppWDAKVTKLSGGERRRVALCRLLLEK-PDMLLLDEPT 191
|
|
| |
