|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1-547 |
0e+00 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 1081.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 1 MELLVLVWRQYRWPFISVMALSLASAALGIGLIAFINQRLIETADTSLLVLPEFLGLLLLLMAVTLGSQLALTTLGHHFV 80
Cdd:PRK10522 1 MELLRLVWRQYRWPFISVMALSLASAALGIGLIAFINQRLIETADTSLLVLPEFLGLLLLLMAVTLGSQLALTTLGHHFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 81 YRLRSEFIKRILDTHVERIEQLGSASLLAGLTSDVRNITIAFVRLPELVQGIILTIGSAAYLWMLSGKMLLVTAIWMAIT 160
Cdd:PRK10522 81 YRLRSEFIKRILDTHVERIEQLGSASLLASLTSDVRNITIAFVRLPELVQGIILTLGSAAYLAWLSPKMLLVTAIWMAVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 161 IWGGFVLVARVYKHMATLRETEDKLYTDFQTVLEGRKELTLNRERAEYVFNNLYIPDAQEYRHHIIRADTFHLSAVNWSN 240
Cdd:PRK10522 161 IWGGFVLVARVYKHMATLRETEDKLYNDYQTVLEGRKELTLNRERAEYVFENEYEPDAQEYRHHIIRADTFHLSAVNWSN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 241 IMMLGAIGLVFWMANSLGWADTNVAATYSLTLLFLRTPLLSAVGALPTLLTAQVAFNKLNKFALAPFKAEFPRPQAFPNW 320
Cdd:PRK10522 241 IMMLGAIGLVFYMANSLGWADTNVAATYSLTLLFLRTPLLSAVGALPTLLSAQVAFNKLNKLALAPYKAEFPRPQAFPDW 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 321 QTLELRNVTFAYQDNAFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKLFS 400
Cdd:PRK10522 321 QTLELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 401 AVFTDVWLFDQLLGPEGKPANPQLVEKWLAQLKMAHKLELSNGRIVNLKLSKGQKKRVALLLALAEERDIILLDEWAADQ 480
Cdd:PRK10522 401 AVFTDFHLFDQLLGPEGKPANPALVEKWLERLKMAHKLELEDGRISNLKLSKGQKKRLALLLALAEERDILLLDEWAADQ 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130148 481 DPHFRREFYQVLLPLMQEMGKTIFAISHDDHYFIHADRLLEMRNGQLSELTGEERDAASRDAVARTA 547
Cdd:PRK10522 481 DPHFRREFYQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQLSELTGEERDAASRDAVARTA 547
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
1-539 |
0e+00 |
|
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: 751.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 1 MELLVLVWRQYRWPFISVMALSLASAALGIGLIAFINQRLIETADTSLLVLPEFLGLLLLLMAVTLGSQLALTTLGHHFV 80
Cdd:COG4615 1 MNLLRLLLRESRWLLLLALLLGLLSGLANAGLIALINQALNATGAALARLLLLFAGLLVLLLLSRLASQLLLTRLGQHAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 81 YRLRSEFIKRILDTHVERIEQLGSASLLAGLTSDVRNITIAFVRLPELVQGIILTIGSAAYLWMLSGKMLLVTAIWMAIT 160
Cdd:COG4615 81 ARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFVRLPELLQSVALVLGCLAYLAWLSPPLFLLTLVLLGLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 161 IWGGFVLVARVYKHMATLRETEDKLYTDFQTVLEGRKELTLNRERAEYVFNNLYIPDAQEYRHHIIRADTFHLSAVNWSN 240
Cdd:COG4615 161 VAGYRLLVRRARRHLRRAREAEDRLFKHFRALLEGFKELKLNRRRRRAFFDEDLQPTAERYRDLRIRADTIFALANNWGN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 241 IMMLGAIGLVFWMANSLGWADTNVAATYSLTLLFLRTPLLSAVGALPTLLTAQVAFNKLNKFALA-----PFKAEFPRPQ 315
Cdd:COG4615 241 LLFFALIGLILFLLPALGWADPAVLSGFVLVLLFLRGPLSQLVGALPTLSRANVALRKIEELELAlaaaePAAADAAAPP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 316 AFPNWQTLELRNVTFAYQ----DNAFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQ 391
Cdd:COG4615 321 APADFQTLELRGVTYRYPgedgDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 392 PEDYRKLFSAVFTDVWLFDQLLGPEGkPANPQLVEKWLAQLKMAHKLELSNGRIVNLKLSKGQKKRVALLLALAEERDII 471
Cdd:COG4615 401 REAYRQLFSAVFSDFHLFDRLLGLDG-EADPARARELLERLELDHKVSVEDGRFSTTDLSQGQRKRLALLVALLEDRPIL 479
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130148 472 LLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDHYFIHADRLLEMRNGQLSELTGEERDAAS 539
Cdd:COG4615 480 VFDEWAADQDPEFRRVFYTELLPELKARGKTVIAISHDDRYFDLADRVLKMDYGKLVELTGPAALAAS 547
|
|
| cyc_pep_trnsptr |
TIGR01194 |
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. ... |
2-527 |
1.75e-104 |
|
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. Bacteria have elaborate pathways for the production of toxins and secondary metabolites. Many such compounds, including syringomycin and pyoverdine are synthesized on non-ribosomal templates consisting of a multienzyme complex. On several occasions the proteins of the complex and transporter protein are present on the same operon. Often times these compounds cross the biological membrane by specific transporters. Syringomycin is an amphipathic, cylclic lipodepsipeptide when inserted into host causes formation of channels, permeable to variety of cations. On the other hand, pyoverdine is a cyclic octa-peptidyl dihydroxyquinoline, which is efficient in sequestering iron for uptake. [Transport and binding proteins, Amino acids, peptides and amines, Transport and binding proteins, Other]
Pssm-ID: 130262 [Multi-domain] Cd Length: 555 Bit Score: 324.60 E-value: 1.75e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 2 ELLVLVWRQYRWPFISVMALSLASAALGIGLIAFINQRLIETADTSLLVLPEFLGLLLLLMAVTLGSQLALTTLGHHFVY 81
Cdd:TIGR01194 7 EILALLRSPFPAITAFSIALGLAGGLAIIALLASINNAIHEENFLGQGSLFSFGGLCLLALLFRIGADIFPAYAGMHIIA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 82 RLRSEFIKRILDTHVERIEQLGSASLLAGLTSDVRNITIAFVRLPELVQGIILTIGSAAYLWMLSGKMLLVTAIWMAITI 161
Cdd:TIGR01194 87 NLRIALCEKILGAPIEEIDRRGAHNLIPLLTHDIDQINAFLFIFPPIAIALAIFFFCIAYLAYLSVPMFAITISAIIIGT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 162 WGGFVLVARVYKHMATLRETEDKLYTDFQTVLEGRKELTLNRERAEYVFNNLYIPDAQEYRHHIIRADTFHLSAVNWSNI 241
Cdd:TIGR01194 167 AAQLLAFMGGFKFFHAARDEEDAFNEHTHAIAFGAKELKIHGIRRLSFAHGAIQESANNIADLHIIEILIFIAAENFGQL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 242 MMLGAIGLVFWMANSLGWADTNVAATYSLTLLFLRTPLLSAVGALPTLLTAQVAFNKLNKFAlapFKAEFPRPQAF---- 317
Cdd:TIGR01194 247 LFFLLIGCALFAAAMFASIDAAAISAFVLALLYIKGPLEMLVSALPILAQAQIACQRLADFG---ERFNEPEPELElsda 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 318 ---------PNWQTLELRNVTFAYQD----NAFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDG 384
Cdd:TIGR01194 324 dnvlllahdKSVDSIELKDVHMNPKApegsEGFALGPIDLRIAQGDIVFIVGENGCGKSTLAKLFCGLYIPQEGEILLDG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 385 KPVSGEQPEDYRKLFSAVFTDVWLFDQLLGP-EGKPANPQLVEKWLAQLKMAHKLELSNGRI-VNLKLSKGQKKRVALLL 462
Cdd:TIGR01194 404 AAVSADSRDDYRDLFSAIFADFHLFDDLIGPdEGEHASLDNAQQYLQRLEIADKVKIEDGGFsTTTALSTGQQKRLALIC 483
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130148 463 ALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDHYFIHADRLLEMRNGQL 527
Cdd:TIGR01194 484 AWLEDRPILLFDEWAADQDPAFKRFFYEELLPDLKRQGKTIIIISHDDQYFELADQIIKLAAGCI 548
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
8-529 |
2.54e-57 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 201.16 E-value: 2.54e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 8 WRQYRWPFISVMALSLASAALGIGLIAFINQ---RLIETADTSLLVLpeflgLLLLLMAVTLGSQLA-------LTTLGH 77
Cdd:COG1132 16 LRPYRGLLILALLLLLLSALLELLLPLLLGRiidALLAGGDLSALLL-----LLLLLLGLALLRALLsylqrylLARLAQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 78 HFVYRLRSEFIKRILDTHVERIEQLGSASLLAGLTSDVRNITIAFVR-LPELVQGIILTIGSAAYLWMLSGKMLLVTAIW 156
Cdd:COG1132 91 RVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHgLPQLVRSVVTLIGALVVLFVIDWRLALIVLLV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 157 MAITIWGGFVLVARVYKHMATLRETEDKLYTDFQTVLEGRKEL-TLNRERAEY-VFNNLyipdAQEYRHHIIRAdtFHLS 234
Cdd:COG1132 171 LPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVkAFGREERELeRFREA----NEELRRANLRA--ARLS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 235 AVNWSNIMMLGAIGLVF------WMANSlGWADTNVAATYSLTLLFLRTPLLSAVGALPTLLTAQVAFNKLNKF-ALAPF 307
Cdd:COG1132 245 ALFFPLMELLGNLGLALvllvggLLVLS-GSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELlDEPPE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 308 KAEFPRPQAFPNWQ-TLELRNVTFAYQDNAFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKP 386
Cdd:COG1132 324 IPDPPGAVPLPPVRgEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVD 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 387 VSGEQPEDYRKLFSAVFTDVWLFDQ------LLGPEGkpANPQLVEKWlaqLKMAHKLELsngrIVNL------------ 448
Cdd:COG1132 404 IRDLTLESLRRQIGVVPQDTFLFSGtireniRYGRPD--ATDEEVEEA---AKAAQAHEF----IEALpdgydtvvgerg 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 449 -KLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQemGKTIFAISHDDHYFIHADRLLEMRNGQL 527
Cdd:COG1132 475 vNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRNADRILVLDDGRI 552
|
..
gi 16130148 528 SE 529
Cdd:COG1132 553 VE 554
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
323-526 |
1.14e-48 |
|
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: 166.02 E-value: 1.14e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDN-AFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKLFSA 401
Cdd:cd03228 1 IEFKNVSFSYPGRpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 402 VFTDVWLFDQLLGPegkpanpqlvekwlaqlkmahklelsngrivNLkLSKGQKKRVALLLALAEERDIILLDEWAADQD 481
Cdd:cd03228 81 VPQDPFLFSGTIRE-------------------------------NI-LSGGQRQRIAIARALLRDPPILILDEATSALD 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 16130148 482 PHFRREFYQVLLPLMQemGKTIFAISHDDHYFIHADRLLEMRNGQ 526
Cdd:cd03228 129 PETEALILEALRALAK--GKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
323-527 |
1.47e-45 |
|
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: 159.81 E-value: 1.47e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKLFSAV 402
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 403 FTDVwlFDQL----------LGPE--GKPAN--PQLVEKWLAQLKMAHKLElsngRIVNlKLSKGQKKRVALLLALAEER 468
Cdd:COG1122 81 FQNP--DDQLfaptveedvaFGPEnlGLPREeiRERVEEALELVGLEHLAD----RPPH-ELSGGQKQRVAIAGVLAMEP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 469 DIILLDEWAADQDPHFRREFYQVLLPLmQEMGKTIFAISHD-DHYFIHADRLLEMRNGQL 527
Cdd:COG1122 154 EVLVLDEPTAGLDPRGRRELLELLKRL-NKEGKTVIIVTHDlDLVAELADRVIVLDDGRI 212
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
82-529 |
4.90e-42 |
|
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: 158.78 E-value: 4.90e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 82 RLRSEFIKRILDTHVERIEQLGSASLLAGLTSDVRNITIAFVRL--PELVqGIILTIGSAAYLWMLSGKMLLVTAIWMAI 159
Cdd:COG4987 89 DLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRVllPLLV-ALLVILAAVAFLAFFSPALALVLALGLLL 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 160 TIWGGFVLVARVYKHM-ATLRETEDKLYTDFQTVLEGRKELTLN------RERAEYVFNNLyipDAQEYRHHIIRADTfh 232
Cdd:COG4987 168 AGLLLPLLAARLGRRAgRRLAAARAALRARLTDLLQGAAELAAYgaldraLARLDAAEARL---AAAQRRLARLSALA-- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 233 lSAVNWsnIMMLGAIGLVFWMAnSLGWADTNVAATYSLTLLFLRTPLLSAVGALPT----LLTAQVAFNKLNKFALAPFK 308
Cdd:COG4987 243 -QALLQ--LAAGLAVVAVLWLA-APLVAAGALSGPLLALLVLAALALFEALAPLPAaaqhLGRVRAAARRLNELLDAPPA 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 309 AEFPR-PQAFPNWQTLELRNVTFAYQDNAFSV-GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKP 386
Cdd:COG4987 319 VTEPAePAPAPGGPSLELEDVSFRYPGAGRPVlDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVD 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 387 VSGEQPEDYRKLFSAVFTDVWLFDQ------LLgpegkpANP-----QLVE--------KWLAQLKmaHKLEL---SNGR 444
Cdd:COG4987 399 LRDLDEDDLRRRIAVVPQRPHLFDTtlrenlRL------ARPdatdeELWAalervglgDWLAALP--DGLDTwlgEGGR 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 445 ivnlKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQemGKTIFAISHDDHYFIHADRLLEMRN 524
Cdd:COG4987 471 ----RLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGLERMDRILVLED 544
|
....*
gi 16130148 525 GQLSE 529
Cdd:COG4987 545 GRIVE 549
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
324-526 |
1.12e-41 |
|
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: 148.77 E-value: 1.12e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 324 ELRNVTFAYQDNAFSVG-PINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKLFSAV 402
Cdd:cd03225 1 ELKNLSFSYPDGARPALdDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 403 FTDVwlFDQLLGP------------EGKPAN--PQLVEKWLAQLKMAHKLELSngrivNLKLSKGQKKRVALLLALAEER 468
Cdd:cd03225 81 FQNP--DDQFFGPtveeevafglenLGLPEEeiEERVEEALELVGLEGLRDRS-----PFTLSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16130148 469 DIILLDEWAADQDPHFRREFYQVLLPLmQEMGKTIFAISHDDHYFI-HADRLLEMRNGQ 526
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKL-KAEGKTIIIVTHDLDLLLeLADRVIVLEDGK 211
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
9-529 |
8.04e-41 |
|
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: 156.92 E-value: 8.04e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 9 RQYRWPFISVMALSLASAALGIGLIAFINQ---RLIETADTSLLVLpeflglLLLLMAVTLGSQLALTTLGHHFV----- 80
Cdd:COG2274 152 RRYRRLLLQVLLASLLINLLALATPLFTQVvidRVLPNQDLSTLWV------LAIGLLLALLFEGLLRLLRSYLLlrlgq 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 81 ---YRLRSEFIKRILDTHVERIEQLGSASLLAGLtSDVRNITIAFV-RLPELVQGIILTIGSAAYLWMLSGKMLLVTAIW 156
Cdd:COG2274 226 ridLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIREFLTgSLLTALLDLLFVLIFLIVLFFYSPPLALVVLLL 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 157 MAITIWGGFVLVARVYKHMATLRETEDKLYTDFQTVLEGRKEL-TLNRE-RAEYVFNNLYIpdaqEYRHHIIRADTFHLS 234
Cdd:COG2274 305 IPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIkALGAEsRFRRRWENLLA----KYLNARFKLRRLSNL 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 235 AVNWSN-IMMLGAIGLVFWMAN-------SLGwadTNVAAtYSLTLLFLrTPLLSAVGALPTLLTAQVAFNKLNKFALAP 306
Cdd:COG2274 381 LSTLSGlLQQLATVALLWLGAYlvidgqlTLG---QLIAF-NILSGRFL-APVAQLIGLLQRFQDAKIALERLDDILDLP 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 307 fkAEFPRPQAFPNWQTL----ELRNVTFAY-QDNAFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEIL 381
Cdd:COG2274 456 --PEREEGRSKLSLPRLkgdiELENVSFRYpGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRIL 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 382 LDGKPVSGEQPEDYRKLFSAVFTDVWLF-----DQLLGpegkpANPQLVEKWLAQ-LKMAHKLELsngrIVNLK------ 449
Cdd:COG2274 534 IDGIDLRQIDPASLRRQIGVVLQDVFLFsgtirENITL-----GDPDATDEEIIEaARLAGLHDF----IEALPmgydtv 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 450 -------LSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQemGKTIFAISHDDHYFIHADRLLEM 522
Cdd:COG2274 605 vgeggsnLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIRLADRIIVL 682
|
....*..
gi 16130148 523 RNGQLSE 529
Cdd:COG2274 683 DKGRIVE 689
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
323-527 |
4.58e-38 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 139.18 E-value: 4.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKLFSAV 402
Cdd:COG4619 1 LELEGLSFRVGGKPI-LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 403 FTDVWLF-----DQLLGP---EGKPANPQLVEKWLAQLKMAHK-LELSNGRivnlkLSKGQKKRVALLLALAEERDIILL 473
Cdd:COG4619 80 PQEPALWggtvrDNLPFPfqlRERKFDRERALELLERLGLPPDiLDKPVER-----LSGGERQRLALIRALLLQPDVLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16130148 474 DEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDHYF-IHADRLLEMRNGQL 527
Cdd:COG4619 155 DEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIeRVADRVLTLEAGRL 209
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
323-527 |
3.68e-37 |
|
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: 135.22 E-value: 3.68e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAfSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVsGEQPEDYRKLFSAV 402
Cdd:cd03230 1 IEVRNLSKRYGKKT-ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDI-KKEPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 403 FTDVWLFDQLLGPEgkpanpqlvekwlaqlkmahklelsngrivNLKLSKGQKKRVALLLALAEERDIILLDEWAADQDP 482
Cdd:cd03230 79 PEEPSLYENLTVRE------------------------------NLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDP 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 16130148 483 HFRREFYQVLLPLMQEmGKTIFAISHD-DHYFIHADRLLEMRNGQL 527
Cdd:cd03230 129 ESRREFWELLRELKKE-GKTILLSSHIlEEAERLCDRVAILNNGRI 173
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
324-527 |
5.09e-35 |
|
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: 129.86 E-value: 5.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 324 ELRNVTFAYQDNaFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKLFSAVf 403
Cdd:cd03214 1 EVENLSVGYGGR-TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYV- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 404 tdvwlfdqllgpegkpanPQLvekwLAQLKMAHKLElsngRIVNlKLSKGQKKRVALLLALAEERDIILLDEWAADQDPH 483
Cdd:cd03214 79 ------------------PQA----LELLGLAHLAD----RPFN-ELSGGERQRVLLARALAQEPPILLLDEPTSHLDIA 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 16130148 484 FRREFYQVLLPLMQEMGKTIFAISHD-DHYFIHADRLLEMRNGQL 527
Cdd:cd03214 132 HQIELLELLRRLARERGKTVVMVLHDlNLAARYADRVILLKDGRI 176
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
323-527 |
5.61e-35 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 132.55 E-value: 5.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNA-FSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDG-KPVSGEQPEDYRKLFS 400
Cdd:TIGR04520 1 IEVENVSFSYPESEkPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGlDTLDEENLWEIRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 401 AVFT--DvwlfDQLL----------GPE--GKPAN--PQLVEKWLAQLKMAHKLELSNGRivnlkLSKGQKKRVALLLAL 464
Cdd:TIGR04520 81 MVFQnpD----NQFVgatveddvafGLEnlGVPREemRKRVDEALKLVGMEDFRDREPHL-----LSGGQKQRVAIAGVL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130148 465 AEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDHYFIHADRLLEMRNGQL 527
Cdd:TIGR04520 152 AMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVLADRVIVMNKGKI 214
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
323-527 |
1.28e-34 |
|
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: 130.50 E-value: 1.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKLFSAV 402
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 403 FTDVWLFDQLLGPEGKPANPQLvEKWLAQLKMAHKLELSngRIVNL-----------KLSKGQKKRVALLLALAEERDII 471
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKL-LKWPKEKIRERADELL--ALVGLdpaefadryphELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16130148 472 LLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHD-DHYFIHADRLLEMRNGQL 527
Cdd:cd03295 158 LMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDiDEAFRLADRIAIMKNGEI 214
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
324-526 |
5.91e-34 |
|
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: 125.82 E-value: 5.91e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 324 ELRNVTFAYQDNaFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKLFSAVF 403
Cdd:cd00267 1 EIENLSFRYGGR-TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 404 tdvwlfdQllgpegkpanpqlvekwlaqlkmahklelsngrivnlkLSKGQKKRVALLLALAEERDIILLDEWAADQDPH 483
Cdd:cd00267 80 -------Q--------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPA 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 16130148 484 FRREFYQVLLPLMQEmGKTIFAISHDDHYFIHA-DRLLEMRNGQ 526
Cdd:cd00267 115 SRERLLELLRELAEE-GRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
9-529 |
1.18e-33 |
|
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: 134.50 E-value: 1.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 9 RQYRWPFISVMALSLASAALGIG---LIAFINQRLIETADTSLLVLPEFLGlllllMAVTLGSQLALTTLGHHFVYR--- 82
Cdd:COG4988 13 RGARRWLALAVLLGLLSGLLIIAqawLLASLLAGLIIGGAPLSALLPLLGL-----LLAVLLLRALLAWLRERAAFRaaa 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 83 -----LRSEFIKRILDTHVERIEQLGSASLLAGLTSDVRNITIAFVR-LPELVQGIILTIGSAAYLWML---SGKMLLVT 153
Cdd:COG4988 88 rvkrrLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARyLPQLFLAALVPLLILVAVFPLdwlSGLILLVT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 154 A----IWMAITiwgGFVLVARVYKHMATLRetedKLYTDFQTVLEGRKELTL-NRERAEyvfnnlyipdAQEYRHhiiRA 228
Cdd:COG4988 168 AplipLFMILV---GKGAAKASRRQWRALA----RLSGHFLDRLRGLTTLKLfGRAKAE----------AERIAE---AS 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 229 DTFHLS-------AVNWSNIMMLGAIGLVFWMANSLGWA--DTNVAATYSLTLLFLR----TPL--LSA---VGAlptll 290
Cdd:COG4988 228 EDFRKRtmkvlrvAFLSSAVLEFFASLSIALVAVYIGFRllGGSLTLFAALFVLLLApeffLPLrdLGSfyhARA----- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 291 TAQVAFNKLNKFALAPFKAEFPRPQAFPNWQ--TLELRNVTFAYQDNAFSVGPINLTIKRGELLFLIGGNGSGKSTLAML 368
Cdd:COG4988 303 NGIAAAEKIFALLDAPEPAAPAGTAPLPAAGppSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 369 LTGLYQPQSGEILLDGKPVSGEQPEDYRKLFSAVFTDVWLF-----DQLLGpeGKP-ANPQLVEKWLAQLKMAHKLEL-- 440
Cdd:COG4988 383 LLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFagtirENLRL--GRPdASDEELEAALEAAGLDEFVAAlp 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 441 --------SNGRivnlKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQemGKTIFAISHDDHY 512
Cdd:COG4988 461 dgldtplgEGGR----GLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLAL 534
|
570
....*....|....*..
gi 16130148 513 FIHADRLLEMRNGQLSE 529
Cdd:COG4988 535 LAQADRILVLDDGRIVE 551
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
323-527 |
1.40e-33 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 126.84 E-value: 1.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAFSV----GpINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSG----EQPED 394
Cdd:cd03255 1 IELKNLSKTYGGGGEKVqalkG-VSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKlsekELAAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 395 YRKLFSAVFTDVWLFDQL-----------LGPEGKPANPQLVEKWLAQLKMAHKLElsngRIVNlKLSKGQKKRVALLLA 463
Cdd:cd03255 80 RRRHIGFVFQSFNLLPDLtalenvelpllLAGVPKKERRERAEELLERVGLGDRLN----HYPS-ELSGGQQQRVAIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130148 464 LAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDHYFIHADRLLEMRNGQL 527
Cdd:cd03255 155 LANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
341-478 |
9.89e-33 |
|
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: 122.37 E-value: 9.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 341 PINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKLFSAVFTDVWLFDQLLGPE---- 416
Cdd:pfam00005 3 NVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVREnlrl 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130148 417 -------GKPANPQLVEKWLAQLKMAHKLELSNGRIVNlKLSKGQKKRVALLLALAEERDIILLDEWAA 478
Cdd:pfam00005 83 glllkglSKREKDARAEEALEKLGLGDLADRPVGERPG-TLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
324-527 |
3.97e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 124.72 E-value: 3.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 324 ELRNVTFAYQDN-AFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKLFSAV 402
Cdd:PRK13632 9 KVENVSFSYPNSeNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGII 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 403 FT------------DvwlfDQLLGPEGKPANPQ----LVEKWLAQLKMAHKLELSngrivNLKLSKGQKKRVALLLALAE 466
Cdd:PRK13632 89 FQnpdnqfigatveD----DIAFGLENKKVPPKkmkdIIDDLAKKVGMEDYLDKE-----PQNLSGGQKQRVAIASVLAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130148 467 ERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDHYFIHADRLLEMRNGQL 527
Cdd:PRK13632 160 NPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKL 220
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
323-527 |
4.18e-32 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 123.64 E-value: 4.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNaFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVsGEQPEDYRKLFSAV 402
Cdd:COG1131 1 IEVRGLTKRYGDK-TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDV-ARDPAEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 403 FTDVWLFDQLLGPE-----------GKPANPQLVEKWLAQLKMAHKLelsnGRIVNlKLSKGQKKRVALLLALAEERDII 471
Cdd:COG1131 79 PQEPALYPDLTVREnlrffarlyglPRKEARERIDELLELFGLTDAA----DRKVG-TLSGGMKQRLGLALALLHDPELL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 472 LLDEWAADQDPHFRREFYQVLLPLMQEmGKTIFAISHD----DHYfihADRLLEMRNGQL 527
Cdd:COG1131 154 ILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYleeaERL---CDRVAIIDKGRI 209
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
323-527 |
3.83e-31 |
|
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: 120.68 E-value: 3.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAFSVGpINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKL---- 398
Cdd:cd03261 1 IELRGLTKSFGGRTVLKG-VDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLrrrm 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 399 -----FSAVFTDVWLFDQLLGP--EgkpaNPQLVEKWLAQLKMaHKLELsngriVNLK---------LSKGQKKRVALLL 462
Cdd:cd03261 80 gmlfqSGALFDSLTVFENVAFPlrE----HTRLSEEEIREIVL-EKLEA-----VGLRgaedlypaeLSGGMKKRVALAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130148 463 ALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDH--YFIhADRLLEMRNGQL 527
Cdd:cd03261 150 ALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDtaFAI-ADRIAVLYDGKI 215
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
324-529 |
3.63e-30 |
|
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: 117.71 E-value: 3.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 324 ELRNVTFAYQDNAFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKLFSAVF 403
Cdd:cd03254 4 EFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 404 TDVWLF-----DQLLgpEGKPANPQLVEKWLAQLKMAHKL--ELSNGRIVNLK-----LSKGQKKRVALLLALAEERDII 471
Cdd:cd03254 84 QDTFLFsgtimENIR--LGRPNATDEEVIEAAKEAGAHDFimKLPNGYDTVLGenggnLSQGERQLLAIARAMLRDPKIL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16130148 472 LLDEWAADQDPHFRREFYQVLLPLMQemGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
Cdd:cd03254 162 ILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKNADKILVLDDGKIIE 217
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
323-535 |
4.09e-30 |
|
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: 118.04 E-value: 4.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNaFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSgEQPEDYRKLFSAV 402
Cdd:COG4555 2 IEVENLSKKYGKV-PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVR-KEPREARRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 403 FTDVWLFDQL-----------LGPEGKPANPQLVEKWLAQLKMahkLELSNGRIvnLKLSKGQKKRVALLLALAEERDII 471
Cdd:COG4555 80 PDERGLYDRLtvreniryfaeLYGLFDEELKKRIEELIELLGL---EEFLDRRV--GELSTGMKKKVALARALVHDPKVL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130148 472 LLDEWAADQDPHFRREFYQVLLPLMQEmGKTIFAISHD--------DH-YFIHADRLLEM-RNGQLSELTGEER 535
Cdd:COG4555 155 LLDEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHImqevealcDRvVILHKGKVVAQgSLDELREEIGEEN 227
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
323-527 |
7.44e-30 |
|
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: 116.46 E-value: 7.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEdyRKLFSAV 402
Cdd:cd03259 1 LELKGLSKTYGSVRA-LDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 403 FTDVWLFDQL---------LGPEGKPAnPQLVEKWLAQLKMAHKLELSNGRIvnLKLSKGQKKRVALLLALAEERDIILL 473
Cdd:cd03259 78 FQDYALFPHLtvaeniafgLKLRGVPK-AEIRARVRELLELVGLEGLLNRYP--HELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16130148 474 DEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHD--DHYFIhADRLLEMRNGQL 527
Cdd:cd03259 155 DEPLSALDAKLREELREELKELQRELGITTIYVTHDqeEALAL-ADRIAVMNEGRI 209
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
323-527 |
8.30e-30 |
|
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: 117.45 E-value: 8.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKLFSAV 402
Cdd:COG1120 2 LEAENLSVGYGGRPV-LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 403 FTDV------------------WLfdQLLGPEGKpANPQLVEKWLAQLKMAHKLElsngRIVNlKLSKGQKKRVALLLAL 464
Cdd:COG1120 81 PQEPpapfgltvrelvalgrypHL--GLFGRPSA-EDREAVEEALERTGLEHLAD----RPVD-ELSGGERQRVLIARAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130148 465 AEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHD-DHYFIHADRLLEMRNGQL 527
Cdd:COG1120 153 AQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDlNLAARYADRLVLLKDGRI 216
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
323-524 |
6.04e-29 |
|
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: 114.11 E-value: 6.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAFSV---GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEdyrklF 399
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVtalEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 400 SAVFTDVWLFDQL-------LGPEGK-PANPQLVEKWLAQLKMahklelsngriVNLK---------LSKGQKKRVALLL 462
Cdd:cd03293 76 GYVFQQDALLPWLtvldnvaLGLELQgVPKAEARERAEELLEL-----------VGLSgfenayphqLSGGMRQRVALAR 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130148 463 ALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDHYFIH-ADRLLEMRN 524
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFlADRVVVLSA 207
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
323-529 |
6.29e-29 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 114.37 E-value: 6.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAFSV---GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSG---EQPEDYR 396
Cdd:COG1136 5 LELRNLTKSYGTGEGEVtalRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSlseRELARLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 397 -KLFSAVFTDVWLFD-----------QLLGPEGKPANPQLVEKWLAQLKMAHKLELSNGrivnlKLSKGQKKRVALLLAL 464
Cdd:COG1136 85 rRHIGFVFQFFNLLPeltalenvalpLLLAGVSRKERRERARELLERVGLGDRLDHRPS-----QLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130148 465 AEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
Cdd:COG1136 160 VNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
323-526 |
1.40e-28 |
|
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: 111.90 E-value: 1.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDnAFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVS--GEQPEDYRKLFS 400
Cdd:cd03229 1 LELKNVSKRYGQ-KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTdlEDELPPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 401 AVFTDVWLFdqllgpegkpanpqlvekwlaqlkmAHKLELSNgriVNLKLSKGQKKRVALLLALAEERDIILLDEWAADQ 480
Cdd:cd03229 80 MVFQDFALF-------------------------PHLTVLEN---IALGLSGGQQQRVALARALAMDPDVLLLDEPTSAL 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16130148 481 DPHFRREFYQVLLPLMQEMGKTIFAISHDDHYFIH-ADRLLEMRNGQ 526
Cdd:cd03229 132 DPITRREVRALLKSLQAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
324-527 |
1.68e-28 |
|
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: 112.35 E-value: 1.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 324 ELRNVTFAYQDNAFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGE----------QPE 393
Cdd:cd03226 1 RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKerrksigyvmQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 394 DYRKLFSAVFTDVWLFDQLLGPEGKPANPQLVEKWLAQLKMAHKLELSNGrivnlklskgQKKRVALLLALAEERDIILL 473
Cdd:cd03226 81 DYQLFTDSVREELLLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGG----------QKQRLAIAAALLSGKDLLIF 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16130148 474 DEWAADQDPHFRREFYQVLLPLmQEMGKTIFAISHDDHyFIH--ADRLLEMRNGQL 527
Cdd:cd03226 151 DEPTSGLDYKNMERVGELIREL-AAQGKAVIVITHDYE-FLAkvCDRVLLLANGAI 204
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
323-546 |
2.99e-28 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 112.97 E-value: 2.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAFS---VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKLF 399
Cdd:COG1124 2 LEVRNLSVSYGQGGRRvpvLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 400 SAVFTDvwlfdqllgPEGKpANPQL-VEKWLAQLKMAHKLELSNGRIVNL----------------KLSKGQKKRVALLL 462
Cdd:COG1124 82 QMVFQD---------PYAS-LHPRHtVDRILAEPLRIHGLPDREERIAELleqvglppsfldryphQLSGGQRQRVAIAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 463 ALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDHYFIH-ADRLLEMRNGQLSE-LTGEERDAASR 540
Cdd:COG1124 152 ALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEeLTVADLLAGPK 231
|
....*.
gi 16130148 541 DAVART 546
Cdd:COG1124 232 HPYTRE 237
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
323-529 |
3.96e-28 |
|
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: 117.70 E-value: 3.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAFS----VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPV---SGEQPEDY 395
Cdd:COG1123 261 LEVRNLSKRYPVRGKGgvraVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLtklSRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 396 RKLFSAVFTDVwlFDQLlgpegkpaNPQL-VEKWLAQ-LKMAHKLELSNGR--------IVNLK----------LSKGQK 455
Cdd:COG1123 341 RRRVQMVFQDP--YSSL--------NPRMtVGDIIAEpLRLHGLLSRAERRervaelleRVGLPpdladrypheLSGGQR 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130148 456 KRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHD----DHYfihADRLLEMRNGQLSE 529
Cdd:COG1123 411 QRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDlavvRYI---ADRVAVMYDGRIVE 485
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
323-546 |
8.21e-28 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 111.72 E-value: 8.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDN-AFSvgPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGE--------QPE 393
Cdd:COG1121 7 IELENLTVSYGGRpVLE--DVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRArrrigyvpQRA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 394 DYRKLFSA-VFtDV----------WLfdQLLGPEGKpanpQLVEKWLAQLKMAHkleLSNGRIVNlkLSKGQKKRVALLL 462
Cdd:COG1121 85 EVDWDFPItVR-DVvlmgrygrrgLF--RRPSRADR----EAVDEALERVGLED---LADRPIGE--LSGGQQQRVLLAR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 463 ALAEERDIILLDEWAADQDPHFRREFYQVLLPLmQEMGKTIFAISHDDHyFI--HADRLLEMRNGQLSEltGEERDAASR 540
Cdd:COG1121 153 ALAQDPDLLLLDEPFAGVDAATEEALYELLREL-RREGKTILVVTHDLG-AVreYFDRVLLLNRGLVAH--GPPEEVLTP 228
|
....*.
gi 16130148 541 DAVART 546
Cdd:COG1121 229 ENLSRA 234
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
323-534 |
1.76e-27 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 111.65 E-value: 1.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNA-FSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKLFSA 401
Cdd:PRK13635 6 IRVEHISFRYPDAAtYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 402 VFT--DvwlfDQLLGP------------EGKPaNPQLVEK--W-LAQLKMAHKLELSNGRivnlkLSKGQKKRVALLLAL 464
Cdd:PRK13635 86 VFQnpD----NQFVGAtvqddvafglenIGVP-REEMVERvdQaLRQVGMEDFLNREPHR-----LSGGQKQRVAIAGVL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130148 465 AEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDHYFIHADRLLEMRNGQL-SELTGEE 534
Cdd:PRK13635 156 ALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEIlEEGTPEE 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
323-529 |
3.90e-27 |
|
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: 115.00 E-value: 3.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNA-FSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQ---SGEILLDGKPVSGEQPEDYRKL 398
Cdd:COG1123 5 LEVRDLSVRYPGGDvPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 399 FSAVFTD-------VWLFDQL-----LGPEGKPANPQLVEKWLAQLKMAHKLELSNGRivnlkLSKGQKKRVALLLALAE 466
Cdd:COG1123 85 IGMVFQDpmtqlnpVTVGDQIaealeNLGLSRAEARARVLELLEAVGLERRLDRYPHQ-----LSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130148 467 ERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHD-DHYFIHADRLLEMRNGQLSE 529
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDlGVVAEIADRVVVMDDGRIVE 223
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
324-522 |
5.20e-27 |
|
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: 108.39 E-value: 5.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 324 ELRNVTFAYqDNAFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGE--------QPEDY 395
Cdd:cd03235 1 EVEDLTVSY-GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKErkrigyvpQRRSI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 396 RKLFSAVFTDV-----WLFDQLLGPEGKpANPQLVEKWLAQLKMAHkleLSNGRIVNlkLSKGQKKRVALLLALAEERDI 470
Cdd:cd03235 80 DRDFPISVRDVvlmglYGHKGLFRRLSK-ADKAKVDEALERVGLSE---LADRQIGE--LSGGQQQRVLLARALVQDPDL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16130148 471 ILLDEWAADQDPHFRREFYQVLLPLmQEMGKTIFAISHD-DHYFIHADRLLEM 522
Cdd:cd03235 154 LLLDEPFAGVDPKTQEDIYELLREL-RREGMTILVVTHDlGLVLEYFDRVLLL 205
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
342-534 |
5.77e-27 |
|
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: 110.04 E-value: 5.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKL----FSAVFTDVWLFDQL----- 412
Cdd:cd03294 43 VSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrrkkISMVFQSFALLPHRtvlen 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 413 --LGPEGKPANPQLVEKwlaqlKMAHKLELsngriVNLK---------LSKGQKKRVALLLALAEERDIILLDEWAADQD 481
Cdd:cd03294 123 vaFGLEVQGVPRAEREE-----RAAEALEL-----VGLEgwehkypdeLSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16130148 482 PHFRREFYQVLLPLMQEMGKTIFAISHD-DHYFIHADRLLEMRNGQLSEL-TGEE 534
Cdd:cd03294 193 PLIRREMQDELLRLQAELQKTIVFITHDlDEALRLGDRIAIMKDGRLVQVgTPEE 247
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
323-529 |
5.92e-27 |
|
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: 108.75 E-value: 5.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAFS---VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPV---SGEQPEDYR 396
Cdd:cd03257 2 LEVKNLSVSFPTGGGSvkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLlklSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 397 KLFSAVFTD-------VW-LFDQLLGP---EGKPANPQlvEKWLAQLKMAHKLELSNgRIVNLK---LSKGQKKRVALLL 462
Cdd:cd03257 82 KEIQMVFQDpmsslnpRMtIGEQIAEPlriHGKLSKKE--ARKEAVLLLLVGVGLPE-EVLNRYpheLSGGQRQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130148 463 ALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDH--YFIhADRLLEMRNGQLSE 529
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGvvAKI-ADRVAVMYAGKIVE 226
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
323-529 |
1.00e-26 |
|
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: 108.47 E-value: 1.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKLFSAV 402
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 403 FTDVWLFDQLLGPE---GKP-ANPQLVEKwLAQLKMAHK--LELSNG--RIV---NLKLSKGQKKRVALLLALAEERDII 471
Cdd:cd03253 81 PQDTVLFNDTIGYNiryGRPdATDEEVIE-AAKAAQIHDkiMRFPDGydTIVgerGLKLSGGEKQRVAIARAILKNPPIL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16130148 472 LLDEWAADQDPHFRREFYQVLLPLMQemGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
Cdd:cd03253 160 LLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVNADKIIVLKDGRIVE 215
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
323-529 |
1.55e-26 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 106.24 E-value: 1.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAFSV-GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQpEDYRKLFSA 401
Cdd:cd03247 1 LSINNVSFSYPEQEQQVlKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 402 VFTDVWLFDQLLgpegkpanpqlvekwlaqlkmahkleLSNgriVNLKLSKGQKKRVALLLALAEERDIILLDEWAADQD 481
Cdd:cd03247 80 LNQRPYLFDTTL--------------------------RNN---LGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLD 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16130148 482 PHFRREfyqvLLPLMQEM--GKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
Cdd:cd03247 131 PITERQ----LLSLIFEVlkDKTLIWITHHLTGIEHMDKILFLENGKIIM 176
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
323-526 |
4.44e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 108.01 E-value: 4.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPV--SGEQPEDYRKLFS 400
Cdd:PRK13636 6 LKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdySRKGLMKLRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 401 AVFT--DVWLF------DQLLGpegkPANPQLVEKWLaQLKMAHKLELSNgrIVNLK------LSKGQKKRVALLLALAE 466
Cdd:PRK13636 86 MVFQdpDNQLFsasvyqDVSFG----AVNLKLPEDEV-RKRVDNALKRTG--IEHLKdkpthcLSFGQKKRVAIAGVLVM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130148 467 ERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHD-DHYFIHADRLLEMRNGQ 526
Cdd:PRK13636 159 EPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDiDIVPLYCDNVFVMKEGR 219
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
323-527 |
5.65e-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: 106.22 E-value: 5.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAY-----QDNafsvgpINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRK 397
Cdd:COG1127 6 IEVRNLTKSFgdrvvLDG------VSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 398 L---------FSAVFTDVWLFDQLLGP--EgkpaNPQLVEKWLAQLKMAhKLELsngriVNLK---------LSKGQKKR 457
Cdd:COG1127 80 LrrrigmlfqGGALFDSLTVFENVAFPlrE----HTDLSEAEIRELVLE-KLEL-----VGLPgaadkmpseLSGGMRKR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130148 458 VALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDH--YFIhADRLLEMRNGQL 527
Cdd:COG1127 150 VALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDsaFAI-ADRVAVLADGKI 220
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
323-522 |
6.48e-26 |
|
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: 105.25 E-value: 6.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNA-FSvgPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSgEQPEDYRKLFSA 401
Cdd:COG4133 3 LEAENLSCRRGERLlFS--GLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIR-DAREDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 402 VFTDVWLFDQLLGPE---------GKPANPQLVEKWLAQLKMAHKLELSNGrivnlKLSKGQKKRVALLLALAEERDIIL 472
Cdd:COG4133 80 LGHADGLKPELTVREnlrfwaalyGLRADREAIDEALEAVGLAGLADLPVR-----QLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16130148 473 LDEWAADQDPHFRREFYQvllpLMQEM---GKTIFAISHDDhYFIHADRLLEM 522
Cdd:COG4133 155 LDEPFTALDAAGVALLAE----LIAAHlarGGAVLLTTHQP-LELAAARVLDL 202
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
75-509 |
9.30e-26 |
|
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: 110.91 E-value: 9.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 75 LGHHFVYR----LRSEFIKRILDTHVERIEQLGSASLLAGLTSDVRNITIAFVR--LP---ELVQGIILTIGSAAYLWML 145
Cdd:TIGR02868 76 VGHDAALRslgaLRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRviVPagvALVVGAAAVAAIAVLSVPA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 146 sgkmLLVTAIWMAITIWGGFVLVARVYK-HMATLRETEDKLYTDFQTVLEGRKELTLNRERAEYVfnnlyiPDAQEYRHH 224
Cdd:TIGR02868 156 ----ALILAAGLLLAGFVAPLVSLRAARaAEQALARLRGELAAQLTDALDGAAELVASGALPAAL------AQVEEADRE 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 225 IIRADTFHLSAVNWSNIMMLGAIGLVFWMANSLG---WADTNVAATYSLTLLFLRTPLLSAVGALP----TLLTAQVAFN 297
Cdd:TIGR02868 226 LTRAERRAAAATALGAALTLLAAGLAVLGALWAGgpaVADGRLAPVTLAVLVLLPLAAFEAFAALPaaaqQLTRVRAAAE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 298 KLNKFALAPFK---AEFPRPQAFPNWQ-TLELRNVTFAYQDNAFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLY 373
Cdd:TIGR02868 306 RIVEVLDAAGPvaeGSAPAAGAVGLGKpTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLL 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 374 QPQSGEILLDGKPVSGEQPEDYRKLFSAVFTDVWLFDQLLGPE---GKP-ANPQLVEKWLAQLKMAHKLE-LSNGRIVNL 448
Cdd:TIGR02868 386 DPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENlrlARPdATDEELWAALERVGLADWLRaLPDGLDTVL 465
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16130148 449 -----KLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQemGKTIFAISHD 509
Cdd:TIGR02868 466 geggaRLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALS--GRTVVLITHH 529
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
323-529 |
1.65e-25 |
|
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: 105.01 E-value: 1.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAFSVGP-INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKLFSA 401
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRdISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 402 VFTDVWLFDQLLGPE---GKP-ANPQLVEKwLAQLKMAHKL--ELSNGRIVNL-----KLSKGQKKRVALLLALAEERDI 470
Cdd:cd03251 81 VSQDVFLFNDTVAENiayGRPgATREEVEE-AARAANAHEFimELPEGYDTVIgergvKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16130148 471 ILLDEWAADQDPHFRREFYQVLLPLMQemGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIENADRIVVLEDGKIVE 216
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
323-527 |
2.16e-25 |
|
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: 102.68 E-value: 2.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNA-FSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKLFSA 401
Cdd:cd03246 1 LEVENVSFRYPGAEpPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 402 VFTDVWLFDqllgpegkpanpqlvekwlaqlkmahklelsnGRIVNLKLSKGQKKRVALLLALAEERDIILLDEWAADQD 481
Cdd:cd03246 81 LPQDDELFS--------------------------------GSIAENILSGGQRQRLGLARALYGNPRILVLDEPNSHLD 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 16130148 482 PHFRREFYQVLLpLMQEMGKTIFAISHDDHYFIHADRLLEMRNGQL 527
Cdd:cd03246 129 VEGERALNQAIA-ALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
323-540 |
6.22e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 104.43 E-value: 6.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNA--FSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKLFS 400
Cdd:PRK13650 5 IEVKNLTFKYKEDQekYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 401 AVFT------------DvwlfDQLLGPEGKPANPQL----VEKWLAQLKMAHKLELSNGRivnlkLSKGQKKRVALLLAL 464
Cdd:PRK13650 85 MVFQnpdnqfvgatveD----DVAFGLENKGIPHEEmkerVNEALELVGMQDFKEREPAR-----LSGGQKQRVAIAGAV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16130148 465 AEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDHYFIHADRLLEMRNGQLsELTGEERDAASR 540
Cdd:PRK13650 156 AMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQV-ESTSTPRELFSR 230
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
323-509 |
1.65e-24 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 102.14 E-value: 1.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAFSvgpINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPedYRKLFSAV 402
Cdd:COG3840 2 LRLDDLTYRYGDFPLR---FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP--AERPVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 403 FTDVWLFDQL---------LGPEGKPANPQ--LVEKWLAQLKMAHKLELSNGrivnlKLSKGQKKRVALLLALAEERDII 471
Cdd:COG3840 77 FQENNLFPHLtvaqniglgLRPGLKLTAEQraQVEQALERVGLAGLLDRLPG-----QLSGGQRQRVALARCLVRKRPIL 151
|
170 180 190
....*....|....*....|....*....|....*...
gi 16130148 472 LLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHD 509
Cdd:COG3840 152 LLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHD 189
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
323-525 |
1.83e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 102.91 E-value: 1.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQ-DNAFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKLFSA 401
Cdd:PRK13648 8 IVFKNVSFQYQsDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 402 VFTD--------VWLFDQLLGPEGKpANP-----QLVEKWLAQLKMAHKLELSNGrivnlKLSKGQKKRVALLLALAEER 468
Cdd:PRK13648 88 VFQNpdnqfvgsIVKYDVAFGLENH-AVPydemhRRVSEALKQVDMLERADYEPN-----ALSGGQKQRVAIAGVLALNP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16130148 469 DIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDHYFIHADRLLEMRNG 525
Cdd:PRK13648 162 SVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKG 218
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
323-509 |
1.99e-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: 102.48 E-value: 1.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAFSV---GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPE------ 393
Cdd:COG1116 8 LELRGVSKRFPTGGGGVtalDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPDrgvvfq 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 394 DYRkLFSavftdvWL--FDQ-LLGPE----GKPANPQLVEKWLAQLKMAHKL-----ELSnGrivnlklskGQKKRVALL 461
Cdd:COG1116 88 EPA-LLP------WLtvLDNvALGLElrgvPKAERRERARELLELVGLAGFEdayphQLS-G---------GMRQRVAIA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16130148 462 LALAEERDIILLDEwaadqdPhF-------RREFYQVLLPLMQEMGKTIFAISHD 509
Cdd:COG1116 151 RALANDPEVLLMDE------P-FgaldaltRERLQDELLRLWQETGKTVLFVTHD 198
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
323-527 |
5.29e-24 |
|
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: 98.27 E-value: 5.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAfSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKL-FSA 401
Cdd:cd03216 1 LELRGITKRFGGVK-ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAgIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 402 VFtdvwlfdQllgpegkpanpqlvekwlaqlkmahklelsngrivnlkLSKGQKKRVALLLALAEERDIILLDEWAADQD 481
Cdd:cd03216 80 VY-------Q--------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALT 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16130148 482 PHFRREFYQVLLPLmQEMGKTIFAISHD-DHYFIHADRLLEMRNGQL 527
Cdd:cd03216 115 PAEVERLFKVIRRL-RAQGVAVIFISHRlDEVFEIADRVTVLRDGRV 160
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
267-536 |
6.95e-24 |
|
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: 105.98 E-value: 6.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 267 TYSLTLLFLRTPLLSAVGALPTLLTAQVAFNKLNKFALAPfkAEFPRPQAFPNWQTL----ELRNVTFAYQDNAFSVGPI 342
Cdd:TIGR01193 416 TFNALLSYFLTPLENIINLQPKLQAARVANNRLNEVYLVD--SEFINKKKRTELNNLngdiVINDVSYSYGYGSNILSDI 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 343 NLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKLFSAVFTDVWLFDQ------LLGPE 416
Cdd:TIGR01193 494 SLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGsilenlLLGAK 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 417 GKPANPQL--------VEKWLAQLKMAHKLELSNGrivNLKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREF 488
Cdd:TIGR01193 574 ENVSQDEIwaaceiaeIKDDIENMPLGYQTELSEE---GSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKI 650
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 16130148 489 YQVLLPLMQemgKTIFAISHDDHYFIHADRLLEMRNGQLSElTGEERD 536
Cdd:TIGR01193 651 VNNLLNLQD---KTIIFVAHRLSVAKQSDKIIVLDHGKIIE-QGSHDE 694
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
323-527 |
1.06e-23 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 99.20 E-value: 1.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAY--QDNAfSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKLFS 400
Cdd:cd03245 3 IEFRNVSFSYpnQEIP-ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 401 AVFTDVWLF-----DQLL--GPEG------KPANPQLVEKWLAQLKMAHKLELS-NGRivnlKLSKGQKKRVALLLALAE 466
Cdd:cd03245 82 YVPQDVTLFygtlrDNITlgAPLAdderilRAAELAGVTDFVNKHPNGLDLQIGeRGR----GLSGGQRQAVALARALLN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130148 467 ERDIILLDEWAADQDPHFRREFYQVLlplmQEM--GKTIFAISHDDHYFIHADRLLEMRNGQL 527
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERLKERL----RQLlgDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
323-527 |
1.53e-23 |
|
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: 99.23 E-value: 1.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYqDNAFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPedYRKLFSAV 402
Cdd:cd03300 1 IELENVSKFY-GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPP--HKRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 403 FTDVWLFDQL-------LGPEGKPANPQLVEKWLA-QLKMAHKLELSNGRIVnlKLSKGQKKRVALLLALAEERDIILLD 474
Cdd:cd03300 78 FQNYALFPHLtvfeniaFGLRLKKLPKAEIKERVAeALDLVQLEGYANRKPS--QLSGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16130148 475 EWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHD-DHYFIHADRLLEMRNGQL 527
Cdd:cd03300 156 EPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDqEEALTMSDRIAVMNKGKI 209
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
323-527 |
2.70e-23 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 101.33 E-value: 2.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNaFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDyRKlFSAV 402
Cdd:COG3842 6 LELENVSKRYGDV-TALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEK-RN-VGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 403 FTDVWLFDQL---------LGPEGKPAN--PQLVEKWLAQLKMAHKLElsngRIVNlKLSKGQKKRVALLLALAEERDII 471
Cdd:COG3842 83 FQDYALFPHLtvaenvafgLRMRGVPKAeiRARVAELLELVGLEGLAD----RYPH-QLSGGQQQRVALARALAPEPRVL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16130148 472 LLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHD-DHYFIHADRLLEMRNGQL 527
Cdd:COG3842 158 LLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDqEEALALADRIAVMNDGRI 214
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
332-509 |
6.07e-23 |
|
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: 96.34 E-value: 6.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 332 YQDNAFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPV----SG------------EQPEDy 395
Cdd:TIGR01166 1 YPGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLdysrKGllerrqrvglvfQDPDD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 396 rKLFSA-VFTDVWLFDQLLGPEGKPANPQlVEKWLAQLKMAHKLElsngRIVNLkLSKGQKKRVALLLALAEERDIILLD 474
Cdd:TIGR01166 80 -QLFAAdVDQDVAFGPLNLGLSEAEVERR-VREALTAVGASGLRE----RPTHC-LSGGEKKRVAIAGAVAMRPDVLLLD 152
|
170 180 190
....*....|....*....|....*....|....*
gi 16130148 475 EWAADQDPHFRREFYQVLLPLMQEmGKTIFAISHD 509
Cdd:TIGR01166 153 EPTAGLDPAGREQMLAILRRLRAE-GMTVVISTHD 186
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
323-530 |
6.34e-23 |
|
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: 97.65 E-value: 6.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAFS---VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRK-- 397
Cdd:cd03258 2 IELKNVSKVFGDTGGKvtaLKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 398 -----------LFSA--VFTDVWLFDQLLGpEGKPANPQLVEKWLAQLKMAHKLEL--SNgrivnlkLSKGQKKRVALLL 462
Cdd:cd03258 82 rrigmifqhfnLLSSrtVFENVALPLEIAG-VPKAEIEERVLELLELVGLEDKADAypAQ-------LSGGQKQRVGIAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130148 463 ALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDdhyfIH-----ADRLLEMRNGQLSEL 530
Cdd:cd03258 154 ALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHE----MEvvkriCDRVAVMEKGEVVEE 222
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
323-527 |
7.80e-23 |
|
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: 96.79 E-value: 7.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAFSvgpINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDyrKLFSAV 402
Cdd:cd03298 1 VRLDKIRFSYGEQPMH---FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD--RPVSML 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 403 FTDVWLFDQL---------LGPEGK--PANPQLVEKWLAQLKMAHKLELSNGrivnlKLSKGQKKRVALLLALAEERDII 471
Cdd:cd03298 76 FQENNLFAHLtveqnvglgLSPGLKltAEDRQAIEVALARVGLAGLEKRLPG-----ELSGGERQRVALARVLVRDKPVL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16130148 472 LLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISH--DDHYFIhADRLLEMRNGQL 527
Cdd:cd03298 151 LLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHqpEDAKRL-AQRVVFLDNGRI 207
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
323-527 |
1.08e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 97.95 E-value: 1.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAF-SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGE---ILLDGKPVSGEQPEDYRKL 398
Cdd:PRK13640 6 VEFKHVSFTYPDSKKpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 399 FSAVF------------TDvwlfDQLLGPEGK----PANPQLVEKWLAQLKMAH--KLELSNgrivnlkLSKGQKKRVAL 460
Cdd:PRK13640 86 VGIVFqnpdnqfvgatvGD----DVAFGLENRavprPEMIKIVRDVLADVGMLDyiDSEPAN-------LSGGQKQRVAI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130148 461 LLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDHYFIHADRLLEMRNGQL 527
Cdd:PRK13640 155 AGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKL 221
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
323-539 |
1.51e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 97.37 E-value: 1.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSG-EQPEDYRKLFSA 401
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDfSKLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 402 VFTD--------VWLFDQLLGPEGKPANP----QLVEKWLAQLKMAHKLELSNGrivnlKLSKGQKKRVALLLALAEERD 469
Cdd:PRK13644 82 VFQNpetqfvgrTVEEDLAFGPENLCLPPieirKRVDRALAEIGLEKYRHRSPK-----TLSGGQGQCVALAGILTMEPE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 470 IILLDEWAADQDPHFRREFYQVLLPLmQEMGKTIFAISHDDHYFIHADRLLEMRNGQLSeLTGEERDAAS 539
Cdd:PRK13644 157 CLIFDEVTSMLDPDSGIAVLERIKKL-HEKGKTIVYITHNLEELHDADRIIVMDRGKIV-LEGEPENVLS 224
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
323-526 |
2.46e-22 |
|
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: 95.04 E-value: 2.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAfSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVS-------GEQPED- 394
Cdd:cd03269 1 LEVENVTKRFGRVT-ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDiaarnriGYLPEEr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 395 --YRKLfsAVFTDVWLFDQLLGPEGKPANPQlVEKWLaqlkmaHKLELSNGRIVNL-KLSKGQKKRVALLLALAEERDII 471
Cdd:cd03269 80 glYPKM--KVIDQLVYLAQLKGLKKEEARRR-IDEWL------ERLELSEYANKRVeELSKGNQQKVQFIAAVIHDPELL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16130148 472 LLDEWAADQDPHFRREFYQVLLPLmQEMGKTIFAISHD-DHYFIHADRLLEMRNGQ 526
Cdd:cd03269 151 ILDEPFSGLDPVNVELLKDVIREL-ARAGKTVILSTHQmELVEELCDRVLLLNKGR 205
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
323-527 |
5.00e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 95.91 E-value: 5.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPE--DYRKLFS 400
Cdd:PRK13639 2 LETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSllEVRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 401 AVFTDVwlFDQLLGPEGK------PANPQL----VEKWLAQLKMAHKLELSNGRIVNlKLSKGQKKRVALLLALAEERDI 470
Cdd:PRK13639 82 IVFQNP--DDQLFAPTVEedvafgPLNLGLskeeVEKRVKEALKAVGMEGFENKPPH-HLSGGQKKRVAIAGILAMKPEI 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16130148 471 ILLDEWAADQDPHFRREFYQVLLPLMQEmGKTIFAISHD-DHYFIHADRLLEMRNGQL 527
Cdd:PRK13639 159 IVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDvDLVPVYADKVYVMSDGKI 215
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
323-509 |
1.20e-21 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 94.34 E-value: 1.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVT--F----AYQDnafsvgpINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYR 396
Cdd:COG0411 5 LEVRGLTkrFgglvAVDD-------VSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 397 KL-----F--SAVFTD----------------VWLFDQLLGP----EGKPANPQLVEKWLAQLKMAHKLELSNGRivnlk 449
Cdd:COG0411 78 RLgiartFqnPRLFPEltvlenvlvaaharlgRGLLAALLRLprarREEREARERAEELLERVGLADRADEPAGN----- 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 450 LSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHD 509
Cdd:COG0411 153 LSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHD 212
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
323-527 |
1.23e-21 |
|
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: 93.24 E-value: 1.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVS---GEQPEDYRKLF 399
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSdlrGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 400 SAVFTDVWLFDQLLGPE---------GKPanPQLVEK----WLAQLKMAHKlelsnGRIVNLKLSKGQKKRVALLLALAE 466
Cdd:cd03292 81 GVVFQDFRLLPDRNVYEnvafalevtGVP--PREIRKrvpaALELVGLSHK-----HRALPAELSGGEQQRVAIARAIVN 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130148 467 ERDIILLDEWAADQDPHFRREFYQvLLPLMQEMGKTIFAISHDDHYF-IHADRLLEMRNGQL 527
Cdd:cd03292 154 SPTILIADEPTGNLDPDTTWEIMN-LLKKINKAGTTVVVATHAKELVdTTRHRVIALERGKL 214
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
323-529 |
1.31e-21 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 93.70 E-value: 1.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQ-DNAFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKLFSA 401
Cdd:cd03252 1 ITFEHVRFRYKpDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 402 VFTDVWLFDQLLGPE---GKPANPQLVEKWLAQLKMAH----KLELSNGRIVNLK---LSKGQKKRVALLLALAEERDII 471
Cdd:cd03252 81 VLQENVLFNRSIRDNialADPGMSMERVIEAAKLAGAHdfisELPEGYDTIVGEQgagLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130148 472 LLDEWAADQDphfrrefYQVLLPLMQEM-----GKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
Cdd:cd03252 161 IFDEATSALD-------YESEHAIMRNMhdicaGRTVIIIAHRLSTVKNADRIIVMEKGRIVE 216
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
312-533 |
1.35e-21 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 96.83 E-value: 1.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 312 PRPQAFPNWQT---LELRNVTFAYqDNAFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVS 388
Cdd:PRK11607 6 PRPQAKTRKALtplLEIRNLTKSF-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 389 GEQPedYRKLFSAVFTDVWLFDQL-------LG-PEGKPANPQLVEKWLAQLKMAHKLELSNGRivNLKLSKGQKKRVAL 460
Cdd:PRK11607 85 HVPP--YQRPINMMFQSYALFPHMtveqniaFGlKQDKLPKAEIASRVNEMLGLVHMQEFAKRK--PHQLSGGQRQRVAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130148 461 LLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHD-DHYFIHADRLLEMRNGQLSELtGE 533
Cdd:PRK11607 161 ARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDqEEAMTMAGRIAIMNRGKFVQI-GE 233
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
323-527 |
1.36e-21 |
|
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: 93.34 E-value: 1.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAF-SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKL--- 398
Cdd:cd03263 1 LQIRNLTKTYKKGTKpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLgyc 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 399 --FSAVFTD------VWLFDQLLGPEGKPANpQLVEKWLAQLKMAHKLelsNGRIVNlkLSKGQKKRVALLLALAEERDI 470
Cdd:cd03263 81 pqFDALFDEltvrehLRFYARLKGLPKSEIK-EEVELLLRVLGLTDKA---NKRART--LSGGMKRKLSLAIALIGGPSV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16130148 471 ILLDEWAADQDPHFRREFYQVLLPLMQemGKTIFAISHD-DHYFIHADRLLEMRNGQL 527
Cdd:cd03263 155 LLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSmDEAEALCDRIAIMSDGKL 210
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
323-529 |
1.55e-21 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 93.19 E-value: 1.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPED---YRKLF 399
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipyLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 400 SAVFTDVWLFD------------QLLGPEGKPANpQLVEKWLAQLKMAHKLElsngRIVNlKLSKGQKKRVALLLALAEE 467
Cdd:COG2884 82 GVVFQDFRLLPdrtvyenvalplRVTGKSRKEIR-RRVREVLDLVGLSDKAK----ALPH-ELSGGEQQRVAIARALVNR 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130148 468 RDIILLDEWAADQDPHFRREFYQVLLPLmQEMGKTIFAISHDDHyFIHA--DRLLEMRNGQLSE 529
Cdd:COG2884 156 PELLLADEPTGNLDPETSWEIMELLEEI-NRRGTTVLIATHDLE-LVDRmpKRVLELEDGRLVR 217
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
323-527 |
2.54e-21 |
|
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: 92.89 E-value: 2.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVT--F----AYQDnafsvgpINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYR 396
Cdd:cd03219 1 LEVRGLTkrFgglvALDD-------VSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 397 KL-----F--SAVFTDVWLFDQLL---------------GPEGKPANPQLVEKWLAQLKMAHKLELSNGRivnlkLSKGQ 454
Cdd:cd03219 74 RLgigrtFqiPRLFPELTVLENVMvaaqartgsglllarARREEREARERAEELLERVGLADLADRPAGE-----LSYGQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130148 455 KKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLmQEMGKTIFAISHD-DHYFIHADRLLEMRNGQL 527
Cdd:cd03219 149 QRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDmDVVMSLADRVTVLDQGRV 221
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
323-547 |
3.10e-21 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 93.33 E-value: 3.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAFS--------VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVS---GEQ 391
Cdd:TIGR02769 3 LEVRDVTHTYRTGGLFgakqrapvLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYqldRKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 392 PEDYRKLFSAVFTDVWlfdqllgpegKPANPQLVEKWLAQLKMAHKLELSNG----RIVNL----------------KLS 451
Cdd:TIGR02769 83 RRAFRRDVQLVFQDSP----------SAVNPRMTVRQIIGEPLRHLTSLDESeqkaRIAELldmvglrsedadklprQLS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 452 KGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHD---DHYFihADRLLEMRNGQLS 528
Cdd:TIGR02769 153 GGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDlrlVQSF--CQRVAVMDKGQIV 230
|
250
....*....|....*....
gi 16130148 529 eltgEERDAASRDAVARTA 547
Cdd:TIGR02769 231 ----EECDVAQLLSFKHPA 245
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
11-522 |
3.94e-21 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 96.59 E-value: 3.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 11 YRWPFISVMALSLASAALGIG---LIAFINQRLIETADTSLLVLPEFLGLLLllmAVTLGSQLALTT--LGHHFVYRLRS 85
Cdd:TIGR02857 1 ARRALALLALLGVLGALLIIAqawLLARVVDGLISAGEPLAELLPALGALAL---VLLLRALLGWLQerAAARAAAAVKS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 86 EFIKRILdthvERIEQLG--------SASLLAGLTSDVRNITIAFVR-LPELVQGIILT-IGSAAYLWM--LSGKMLLVT 153
Cdd:TIGR02857 78 QLRERLL----EAVAALGprwlqgrpSGELATLALEGVEALDGYFARyLPQLVLAVIVPlAILAAVFPQdwISGLILLLT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 154 A----IWMAITIWGGfvlVARVYKHMATLreteDKLYTDFQTVLEGRKEL-TLNRERAEYvfNNLYiPDAQEYRHHIIRA 228
Cdd:TIGR02857 154 AplipIFMILIGWAA---QAAARKQWAAL----SRLSGHFLDRLRGLPTLkLFGRAKAQA--AAIR-RSSEEYRERTMRV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 229 dtfhlsavnwSNIMMLGAIGLVFWMANSLGWadtnVAATYSLTLLFLRTPLLSAvgaLPTLLTAQVAFNKLNKF------ 302
Cdd:TIGR02857 224 ----------LRIAFLSSAVLELFATLSVAL----VAVYIGFRLLAGDLDLATG---LFVLLLAPEFYLPLRQLgaqyha 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 303 ---------ALAPFKAEFPRPQ-------AFPNWQtLELRNVTFAYQDNAFSVGPINLTIKRGELLFLIGGNGSGKSTLA 366
Cdd:TIGR02857 287 radgvaaaeALFAVLDAAPRPLagkapvtAAPASS-LEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLL 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 367 MLLTGLYQPQSGEILLDGKPVSGEQPEDYRKLFSAVFTDVWLFDQ------LLG-PEGKPAnpQLVEKwlAQLKMAHKLE 439
Cdd:TIGR02857 366 NLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGtiaeniRLArPDASDA--EIREA--LERAGLDEFV 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 440 LSNGRIVNLK-------LSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQemGKTIFAISHDDHY 512
Cdd:TIGR02857 442 AALPQGLDTPigeggagLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLAL 519
|
570
....*....|
gi 16130148 513 FIHADRLLEM 522
Cdd:TIGR02857 520 AALADRIVVL 529
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
323-527 |
5.57e-21 |
|
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: 91.44 E-value: 5.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAFSVGpINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPE--DYRKLFS 400
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKG-IDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 401 AVFTDVWLFDQL-------LGP---EGKPANP--QLVEKWLAQLKMAHKLELSNGRivnlkLSKGQKKRVALLLALAEER 468
Cdd:cd03262 80 MVFQQFNLFPHLtvlenitLAPikvKGMSKAEaeERALELLEKVGLADKADAYPAQ-----LSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130148 469 DIILLDEWAADQDPHFRREFYQVLLPLMQEmGKTIFAISHdDHYFIH--ADRLLEMRNGQL 527
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTH-EMGFARevADRVIFMDDGRI 213
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
323-527 |
6.02e-21 |
|
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: 91.76 E-value: 6.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAY---------QDNAFSVGPinltikrGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPE 393
Cdd:cd03248 12 VKFQNVTFAYptrpdtlvlQDVSFTLHP-------GEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 394 DYRKLFSAVFTDVWLFDQLLGPE---GKPANPQLVEKWLAQLKMAHKL--ELSNGRIVNL-----KLSKGQKKRVALLLA 463
Cdd:cd03248 85 YLHSKVSLVGQEPVLFARSLQDNiayGLQSCSFECVKEAAQKAHAHSFisELASGYDTEVgekgsQLSGGQKQRVAIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130148 464 LAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEmgKTIFAISHDDHYFIHADRLLEMRNGQL 527
Cdd:cd03248 165 LIRNPQVLILDEATSALDAESEQQVQQALYDWPER--RTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
322-527 |
8.94e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 92.00 E-value: 8.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 322 TLELRNVTFAYQDNAFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKLFSa 401
Cdd:PRK11231 2 TLRTENLTVGYGTKRI-LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 402 vftdvWLFDQLLGPEG---------------------KPANPQLVEKWLAQLkmaHKLELSNGRIVNlkLSKGQKKRVAL 460
Cdd:PRK11231 80 -----LLPQHHLTPEGitvrelvaygrspwlslwgrlSAEDNARVNQAMEQT---RINHLADRRLTD--LSGGQRQRAFL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130148 461 LLALAEERDIILLDEWAADQDPHfrrefYQV-LLPLMQEM---GKTIFAISHD-DHYFIHADRLLEMRNGQL 527
Cdd:PRK11231 150 AMVLAQDTPVVLLDEPTTYLDIN-----HQVeLMRLMRELntqGKTVVTVLHDlNQASRYCDHLVVLANGHV 216
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
342-525 |
1.06e-20 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 90.99 E-value: 1.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPE------DYRKL-FSAVFTDVWL-FDQLL 413
Cdd:TIGR01184 4 VNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDrmvvfqNYSLLpWLTVRENIALaVDRVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 414 GPEGKPANPQLVEKWLAQLKMAHKLELSNGrivnlKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLL 493
Cdd:TIGR01184 84 PDLSKSERRAIVEEHIALVGLTEAADKRPG-----QLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELM 158
|
170 180 190
....*....|....*....|....*....|...
gi 16130148 494 PLMQEMGKTIFAISHD-DHYFIHADRLLEMRNG 525
Cdd:TIGR01184 159 QIWEEHRVTVLMVTHDvDEALLLSDRVVMLTNG 191
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
323-526 |
2.88e-20 |
|
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: 89.93 E-value: 2.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKLFS-- 400
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRqi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 401 -AVFTDVWLFDQLLGPE----GKPANPQLVEKWLAQLKMAHKLE-LSNGRIVNL---------KLSKGQKKRVALLLALA 465
Cdd:cd03256 81 gMIFQQFNLIERLSVLEnvlsGRLGRRSTWRSLFGLFPKEEKQRaLAALERVGLldkayqradQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130148 466 EERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDHYFI-HADRLLEMRNGQ 526
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAReYADRIVGLKDGR 222
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
323-527 |
3.44e-20 |
|
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: 89.24 E-value: 3.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYqDNAFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDyRKLfSAV 402
Cdd:cd03301 1 VELENVTKRF-GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD-RDI-AMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 403 FTDVWL------FDQLLGP-----EGKPANPQLVEKWLAQLKMAHKLElsngRIVNlKLSKGQKKRVALLLALAEERDII 471
Cdd:cd03301 78 FQNYALyphmtvYDNIAFGlklrkVPKDEIDERVREVAELLQIEHLLD----RKPK-QLSGGQRQRVALGRAIVREPKVF 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16130148 472 LLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHD-DHYFIHADRLLEMRNGQL 527
Cdd:cd03301 153 LMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDqVEAMTMADRIAVMNDGQI 209
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
323-533 |
3.53e-20 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 89.39 E-value: 3.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKLFS-- 400
Cdd:PRK10247 8 LQLQNVGYLAGDAKI-LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSyc 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 401 ----AVFTDVwLFDQLLGP---EGKPANPQLVEKWLAQLKMAhkLELSNGRIVnlKLSKGQKKRVALLLALAEERDIILL 473
Cdd:PRK10247 87 aqtpTLFGDT-VYDNLIFPwqiRNQQPDPAIFLDDLERFALP--DTILTKNIA--ELSGGEKQRISLIRNLQFMPKVLLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130148 474 DEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDHYFIHADRL--LEMRNGQLSELTGE 533
Cdd:PRK10247 162 DEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVitLQPHAGEMQEARYE 223
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
322-527 |
3.74e-20 |
|
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: 89.71 E-value: 3.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 322 TLELRNVTFAYqDNAFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKLFsa 401
Cdd:cd03296 2 SIEVRNVSKRF-GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGF-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 402 VFTDVWLFDQL-------LGPEGKPANP-----QLVEKWLAQLKMAHkLELSNGRIVNlKLSKGQKKRVALLLALAEERD 469
Cdd:cd03296 79 VFQHYALFRHMtvfdnvaFGLRVKPRSErppeaEIRAKVHELLKLVQ-LDWLADRYPA-QLSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16130148 470 IILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDHYFIH-ADRLLEMRNGQL 527
Cdd:cd03296 157 VLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEvADRVVVMNKGRI 215
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
323-527 |
3.77e-20 |
|
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: 89.70 E-value: 3.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDnaFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEdyRKLFSAV 402
Cdd:cd03299 1 LKVENLSKDWKE--FKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 403 FTDVWLFDQL-----------LGPEGKPANPQLVEKWLAQLKMAHKLELSNGRivnlkLSKGQKKRVALLLALAEERDII 471
Cdd:cd03299 77 PQNYALFPHMtvykniayglkKRKVDKKEIERKVLEIAEMLGIDHLLNRKPET-----LSGGEQQRVAIARALVVNPKIL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16130148 472 LLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHD-DHYFIHADRLLEMRNGQL 527
Cdd:cd03299 152 LLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDfEEAWALADKVAIMLNGKL 208
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
323-525 |
3.91e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 90.57 E-value: 3.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKLFSAV 402
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 403 FTD---------VWLfDQLLGPEGKPANPQLVEKwlaqlKMAHKLelsngRIVNLK---------LSKGQKKRVALLLAL 464
Cdd:PRK13647 85 FQDpddqvfsstVWD-DVAFGPVNMGLDKDEVER-----RVEEAL-----KAVRMWdfrdkppyhLSYGQKKRVAIAGVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130148 465 AEERDIILLDEWAADQDPHFRREFYQVLLPLMQEmGKTIFAISHD-DHYFIHADRLLEMRNG 525
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDvDLAAEWADQVIVLKEG 214
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
324-527 |
8.90e-20 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 88.99 E-value: 8.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 324 ELRNVTFAYQDNAfSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDY-RKL---- 398
Cdd:COG4604 3 EIKNVSKRYGGKV-VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELaKRLailr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 399 ----FSAVFTdVwlfDQLLG----PEGK----PANPQLVEKWLAQLKMAhklELSNgRIVNlKLSKGQKKRVALLLALAE 466
Cdd:COG4604 82 qenhINSRLT-V---RELVAfgrfPYSKgrltAEDREIIDEAIAYLDLE---DLAD-RYLD-ELSGGQRQRAFIAMVLAQ 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16130148 467 ERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDdhyfI-----HADRLLEMRNGQL 527
Cdd:COG4604 153 DTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHD----InfascYADHIVAMKDGRV 214
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
321-543 |
1.04e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 89.38 E-value: 1.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 321 QTLELRNVTFAYQ--DNAFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKL 398
Cdd:PRK13642 3 KILEVENLVFKYEkeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 399 FSAVFTDVwlFDQLLGP------------EGKPaNPQLVEKWLAQLKMAHKLELSNGRIVnlKLSKGQKKRVALLLALAE 466
Cdd:PRK13642 83 IGMVFQNP--DNQFVGAtveddvafgmenQGIP-REEMIKRVDEALLAVNMLDFKTREPA--RLSGGQKQRVAVAGIIAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130148 467 ERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDHYFIHADRLLEMRNGQ-LSELTGEERDAASRDAV 543
Cdd:PRK13642 158 RPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEiIKEAAPSELFATSEDMV 235
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
323-527 |
1.12e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 89.38 E-value: 1.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDN-----AFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPE-DYR 396
Cdd:PRK13633 5 IKCKNVSYKYESNeesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLwDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 397 KLFSAVFT--DVWLF------DQLLGPEGKPANPQ----LVEKWLAQLKMA----HKLELsngrivnlkLSKGQKKRVAL 460
Cdd:PRK13633 85 NKAGMVFQnpDNQIVativeeDVAFGPENLGIPPEeireRVDESLKKVGMYeyrrHAPHL---------LSGGQKQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130148 461 LLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDHYFIHADRLLEMRNGQL 527
Cdd:PRK13633 156 AGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKV 222
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
342-536 |
2.75e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 88.18 E-value: 2.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPE--DYRKLFSAVFT--DVWLF------DQ 411
Cdd:PRK13637 26 VNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKlsDIRKKVGLVFQypEYQLFeetiekDI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 412 LLGPEGKPANPQLVEKwlaQLKMAHKlelsngrIVNLK-----------LSKGQKKRVALLLALAEERDIILLDEWAADQ 480
Cdd:PRK13637 106 AFGPINLGLSEEEIEN---RVKRAMN-------IVGLDyedykdkspfeLSGGQKRRVAIAGVVAMEPKILILDEPTAGL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16130148 481 DPHFRREFYQVLLPLMQEMGKTIFAISH--DDHYFIhADRLLEMRNGQLsELTGEERD 536
Cdd:PRK13637 176 DPKGRDEILNKIKELHKEYNMTIILVSHsmEDVAKL-ADRIIVMNKGKC-ELQGTPRE 231
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
323-526 |
3.24e-19 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 89.62 E-value: 3.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEdyRKLFSAV 402
Cdd:PRK09452 15 VELRGISKSFDGKEV-ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 403 FTDVWLFDQLLGPEG--------KPANPQLVEKWLAQLKMAHKLELSNGRIvnLKLSKGQKKRVALLLALAEERDIILLD 474
Cdd:PRK09452 92 FQSYALFPHMTVFENvafglrmqKTPAAEITPRVMEALRMVQLEEFAQRKP--HQLSGGQQQRVAIARAVVNKPKVLLLD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16130148 475 EWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHD-DHYFIHADRLLEMRNGQ 526
Cdd:PRK09452 170 ESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDqEEALTMSDRIVVMRDGR 222
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
342-529 |
3.34e-19 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 87.43 E-value: 3.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVS---GEQPEDYRKLFSAVFTDVwlfdqlLGpegk 418
Cdd:PRK10419 31 VSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAklnRAQRKAFRRDIQMVFQDS------IS---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 419 PANPQLVEKWLAQLKMAHKLELSNG----------RIVNL----------KLSKGQKKRVALLLALAEERDIILLDEWAA 478
Cdd:PRK10419 101 AVNPRKTVREIIREPLRHLLSLDKAerlarasemlRAVDLddsvldkrppQLSGGQLQRVCLARALAVEPKLLILDEAVS 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16130148 479 DQDPHFRREFYQVLLPLMQEMGKTIFAISHD---DHYFIHadRLLEMRNGQLSE 529
Cdd:PRK10419 181 NLDLVLQAGVIRLLKKLQQQFGTACLFITHDlrlVERFCQ--RVMVMDNGQIVE 232
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
323-529 |
5.16e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 90.27 E-value: 5.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAFSV-GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKLFSA 401
Cdd:PRK11160 339 LTLNNVSFTYPDQPQPVlKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 402 VFTDVWLFDQLLGPEGKPANPQLVEKWLAQlkMAHKLELSN---------------GRivnlKLSKGQKKRVALLLALAE 466
Cdd:PRK11160 419 VSQRVHLFSATLRDNLLLAAPNASDEALIE--VLQQVGLEKlleddkglnawlgegGR----QLSGGEQRRLGIARALLH 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130148 467 ERDIILLDEWAADQDPHFRREFYQVLLPLMQemGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
Cdd:PRK11160 493 DAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQFDRICVMDNGQIIE 553
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
323-529 |
7.76e-19 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 85.91 E-value: 7.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAFSVGpINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSG--EQPEDYRKLFS 400
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHN-IDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 401 AVFTDVWLFDQLLGPEGKPANPQLVEKwlAQLKMAHKLELSNGRIVNL---------KLSKGQKKRVALLLALAEERDII 471
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVMFGPLRVRG--ASKEEAEKQARELLAKVGLaerahhypsELSGGQQQRVAIARALAVKPKLM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 472 LLDEWAADQDPHFRREFYQVLLPLMQEmGKTIFAISHDDHyFIH--ADRLLEMRNGQLSE 529
Cdd:PRK09493 159 LFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIG-FAEkvASRLIFIDKGRIAE 216
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
342-540 |
1.30e-18 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 87.45 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKLFS----AVFTDVWLFDQL----- 412
Cdd:PRK10851 21 ISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVfqhyALFRHMTVFDNIafglt 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 413 -LGPEGKPANPQLVEKWLAQLKMAHKLELSNgRIVNlKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQV 491
Cdd:PRK10851 101 vLPRRERPNAAAIKAKVTQLLEMVQLAHLAD-RYPA-QLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRW 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16130148 492 LLPLMQEMGKTIFAISHDDHYFIH-ADRLLEMRNGQLSEL-TGEE--RDAASR 540
Cdd:PRK10851 179 LRQLHEELKFTSVFVTHDQEEAMEvADRVVVMSQGNIEQAgTPDQvwREPATR 231
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
323-529 |
1.60e-18 |
|
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: 84.47 E-value: 1.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDN-AFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKLFSA 401
Cdd:cd03244 3 IEFKNVSLRYRPNlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 402 VFTDVWLFD----QLLGPEGKPANPQLVE--------KWLAQLKMAHKLELSNGrivNLKLSKGQKKRVALLLALAEERD 469
Cdd:cd03244 83 IPQDPVLFSgtirSNLDPFGEYSDEELWQalervglkEFVESLPGGLDTVVEEG---GENLSVGQRQLLCLARALLRKSK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16130148 470 IILLDEWAADQDPHFRRefyqvllpLMQEM------GKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
Cdd:cd03244 160 ILVLDEATASVDPETDA--------LIQKTireafkDCTVLTIAHRLDTIIDSDRILVLDKGRVVE 217
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
342-527 |
1.80e-18 |
|
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: 84.51 E-value: 1.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVS------GEQPE----DY-----------RKLFS 400
Cdd:cd03220 41 VSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSllglggGFNPEltgrENiylngrllglsRKEID 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 401 AVFTDVWLFDQLlgpegkpanpqlvekwlaqlkmahklelsnGRIVNLKL---SKGQKKRVALLLALAEERDIILLDEWA 477
Cdd:cd03220 121 EKIDEIIEFSEL------------------------------GDFIDLPVktySSGMKARLAFAIATALEPDILLIDEVL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16130148 478 ADQDPHFRREFYQVLLPlMQEMGKTIFAISHDDHYFI-HADRLLEMRNGQL 527
Cdd:cd03220 171 AVGDAAFQEKCQRRLRE-LLKQGKTVILVSHDPSSIKrLCDRALVLEKGKI 220
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
323-526 |
1.88e-18 |
|
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: 83.67 E-value: 1.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAFSVGP----INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKP--VSgEQPEdyr 396
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFtlkdINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIayVS-QEPW--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 397 kLFSAVFTDVWLFdqllgpeGKPANPQLVEKWL--AQLK-----MAHKLEL---SNGriVNLklSKGQKKRVALLLALAE 466
Cdd:cd03250 77 -IQNGTIRENILF-------GKPFDEERYEKVIkaCALEpdleiLPDGDLTeigEKG--INL--SGGQKQRISLARAVYS 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130148 467 ERDIILLDEWAADQDPHFRRE-FYQVLLPLMQEmGKTIFAISHDDHYFIHADRLLEMRNGQ 526
Cdd:cd03250 145 DADIYLLDDPLSAVDAHVGRHiFENCILGLLLN-NKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
323-527 |
2.20e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 85.24 E-value: 2.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKLFSAV 402
Cdd:PRK13652 4 IETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 403 FTDVwlFDQLLGPEGK------PANPQLVEKWLAQL--KMAHKLELSNGRI-VNLKLSKGQKKRVALLLALAEERDIILL 473
Cdd:PRK13652 84 FQNP--DDQIFSPTVEqdiafgPINLGLDEETVAHRvsSALHMLGLEELRDrVPHHLSGGEKKRVAIAGVIAMEPQVLVL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16130148 474 DEWAADQDPHFRREFYQVLLPLMQEMGKT-IFAISHDDHYFIHADRLLEMRNGQL 527
Cdd:PRK13652 162 DEPTAGLDPQGVKELIDFLNDLPETYGMTvIFSTHQLDLVPEMADYIYVMDKGRI 216
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
323-529 |
3.41e-18 |
|
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: 83.77 E-value: 3.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAfSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLY-----QPQSGEILLDGKPVSGEQ--PEDY 395
Cdd:cd03260 1 IELRDLNVYYGDKH-ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLDvdVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 396 RK----------LFSA-VFTDVWLFDQLLGPEGKPANPQLVEKwlaQLKMAHKLELSNGRIVNLKLSKGQKKRVALLLAL 464
Cdd:cd03260 80 RRrvgmvfqkpnPFPGsIYDNVAYGLRLHGIKLKEELDERVEE---ALRKAALWDEVKDRLHALGLSGGQQQRLCLARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 465 AEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMgkTIFAISHDdhyfIH-----ADRLLEMRNGQLSE 529
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHN----MQqaarvADRTAFLLNGRLVE 220
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
342-509 |
4.12e-18 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 83.98 E-value: 4.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDyrklfSAVFTDVWL-----------FD 410
Cdd:PRK11248 20 INLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----GVVFQNEGLlpwrnvqdnvaFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 411 QLLGPEGKPANPQLVEKWLAQLKMAhklELSNGRIvnLKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQ 490
Cdd:PRK11248 95 LQLAGVEKMQRLEIAHQMLKKVGLE---GAEKRYI--WQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQT 169
|
170
....*....|....*....
gi 16130148 491 VLLPLMQEMGKTIFAISHD 509
Cdd:PRK11248 170 LLLKLWQETGKQVLLITHD 188
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
342-527 |
4.49e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 84.88 E-value: 4.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQP----EDYRKLFSAVF--TDVWLF------ 409
Cdd:PRK13641 26 ISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGnknlKKLRKKVSLVFqfPEAQLFentvlk 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 410 DQLLGPEGKPANPQLVE----KWLAQLKMAHKLELSNgrivNLKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFR 485
Cdd:PRK13641 106 DVEFGPKNFGFSEDEAKekalKWLKKVGLSEDLISKS----PFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGR 181
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 16130148 486 REFYQVLLPlMQEMGKTIFAISHD-DHYFIHADRLLEMRNGQL 527
Cdd:PRK13641 182 KEMMQLFKD-YQKAGHTVILVTHNmDDVAEYADDVLVLEHGKL 223
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
323-545 |
8.19e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 86.23 E-value: 8.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAY-----QDNafsvgpINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRK 397
Cdd:COG3845 6 LELRGITKRFggvvaNDD------VSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 398 L--------FSavftdvwLFDQL-------LGPEGKPA---NPQLVEKWLAQLKMAHKLELSNGRIVNlKLSKGQKKRVA 459
Cdd:COG3845 80 LgigmvhqhFM-------LVPNLtvaenivLGLEPTKGgrlDRKAARARIRELSERYGLDVDPDAKVE-DLSVGEQQRVE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 460 LLLALAEERDIILLDEWAADQDPHFRREFYQVLLpLMQEMGKTIFAISHDdhyfIH-----ADRLLEMRNGqlsELTGE- 533
Cdd:COG3845 152 ILKALYRGARILILDEPTAVLTPQEADELFEILR-RLAAEGKSIIFITHK----LRevmaiADRVTVLRRG---KVVGTv 223
|
250
....*....|..
gi 16130148 534 ERDAASRDAVAR 545
Cdd:COG3845 224 DTAETSEEELAE 235
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
322-529 |
9.71e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 83.68 E-value: 9.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 322 TLELRNVTFAYQDNA----FSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDY-- 395
Cdd:PRK13646 2 TIRFDNVSYTYQKGTpyehQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYir 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 396 --RKLFSAVFT--DVWLFDQ------LLGPEGKPANPQLVEKWLAQLKMahklELSNGRIV----NLKLSKGQKKRVALL 461
Cdd:PRK13646 82 pvRKRIGMVFQfpESQLFEDtvereiIFGPKNFKMNLDEVKNYAHRLLM----DLGFSRDVmsqsPFQMSGGQMRKIAIV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130148 462 LALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHD-DHYFIHADRLLEMRNGQLSE 529
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDmNEVARYADEVIVMKEGSIVS 226
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
323-535 |
1.98e-17 |
|
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: 81.71 E-value: 1.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAFSVG---PINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGeQPEDYRKLF 399
Cdd:COG4181 9 IELRGLTKTVGTGAGELTilkGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFA-LDEDARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 400 SA-----VFTDvwlFdQLLG----------P---EGKPANPQLVEKWLAQLKMAHKLELSNGRivnlkLSKGQKKRVALL 461
Cdd:COG4181 88 RArhvgfVFQS---F-QLLPtltalenvmlPlelAGRRDARARARALLERVGLGHRLDHYPAQ-----LSGGEQQRVALA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130148 462 LALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDHYFIHADRLLEMRNGQLSELTGEER 535
Cdd:COG4181 159 RAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLRAGRLVEDTAATA 232
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
322-527 |
2.36e-17 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 83.58 E-value: 2.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 322 TLELRNVTFAYqDNAFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDyRKLfSA 401
Cdd:COG3839 3 SLELENVSKSY-GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD-RNI-AM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 402 VFTDVWLFDQL-----------LGPEGKPANPQLVEKWLAQLKMAHKLElsngRivnlK---LSKGQKKRVALLLALAEE 467
Cdd:COG3839 80 VFQSYALYPHMtvyeniafplkLRKVPKAEIDRRVREAAELLGLEDLLD----R----KpkqLSGGQRQRVALGRALVRE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130148 468 RDIILLDEWAADQDPH----FRREFYQvllpLMQEMGKTIFAISHDdhy-fihADRLLEMRNGQL 527
Cdd:COG3839 152 PKVFLLDEPLSNLDAKlrveMRAEIKR----LHRRLGTTTIYVTHDqveamtlADRIAVMNDGRI 212
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
3-530 |
2.52e-17 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 85.54 E-value: 2.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 3 LLVLVWRQyrWPFISVMALSLASAALGIGLIAFINQRLIETADTSLLVlPEFLGLLLLLMAVTLGSQLALTTLGHHFVY- 81
Cdd:TIGR00958 152 LLGLSGRD--WPWLISAFVFLTLSSLGEMFIPFYTGRVIDTLGGDKGP-PALASAIFFMCLLSIASSVSAGLRGGSFNYt 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 82 ------RLRSEFIKRILDTHVERIEQLGSASLLAGLTSDVRNI--TIAFvRLPELVQGIILTIGSAAYLWMLSGKMLLVT 153
Cdd:TIGR00958 229 marinlRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMsrSLSL-NVNVLLRNLVMLLGLLGFMLWLSPRLTMVT 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 154 AIWMAITIwggfvLVARVY--KHMATLRETEDKLYTDFQTVLEGRKEL-TLNRERAEYVfnnlyipDAQEYRH------H 224
Cdd:TIGR00958 308 LINLPLVF-----LAEKVFgkRYQLLSEELQEAVAKANQVAEEALSGMrTVRSFAAEEG-------EASRFKEaleetlQ 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 225 IIRADTFHLSAVNWSN-IMMLGAIGLVFW------MANSLGWADTNVAATYSL-------TLLFLRTPLLSAVGAlptll 290
Cdd:TIGR00958 376 LNKRKALAYAGYLWTTsVLGMLIQVLVLYyggqlvLTGKVSSGNLVSFLLYQEqlgeavrVLSYVYSGMMQAVGA----- 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 291 tAQVAFNKLNKfalapfKAEFPRP--QAFPNWQTL-ELRNVTFAY--QDNAFSVGPINLTIKRGELLFLIGGNGSGKSTL 365
Cdd:TIGR00958 451 -SEKVFEYLDR------KPNIPLTgtLAPLNLEGLiEFQDVSFSYpnRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTV 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 366 AMLLTGLYQPQSGEILLDGKPVS--------------GEQPEdyrkLFSAVFTDVWLFDQLLGPEGKPANpqlvekwLAQ 431
Cdd:TIGR00958 524 AALLQNLYQPTGGQVLLDGVPLVqydhhylhrqvalvGQEPV----LFSGSVRENIAYGLTDTPDEEIMA-------AAK 592
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 432 LKMAHKL--ELSNGRIVNL-----KLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQvllpLMQEMGKTIF 504
Cdd:TIGR00958 593 AANAHDFimEFPNGYDTEVgekgsQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE----SRSRASRTVL 668
|
570 580
....*....|....*....|....*.
gi 16130148 505 AISHDDHYFIHADRLLEMRNGQLSEL 530
Cdd:TIGR00958 669 LIAHRLSTVERADQILVLKKGSVVEM 694
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
319-531 |
2.55e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 81.40 E-value: 2.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 319 NWQTLELRNVTFAyqdnafsvgpinltIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKL 398
Cdd:PRK11629 19 SVQTDVLHNVSFS--------------IGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 399 FSAVFTDVWLFDQLLgPE-------------GKPANPQLVEKWLAQLKMAHKLELSNGRivNLKLSKGQKKRVALLLALA 465
Cdd:PRK11629 85 RNQKLGFIYQFHHLL-PDftalenvamplliGKKKPAEINSRALEMLAAVGLEHRANHR--PSELSGGERQRVAIARALV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130148 466 EERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDHYFIHADRLLEMRNGQLS-ELT 531
Cdd:PRK11629 162 NNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTaELS 228
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
323-510 |
2.83e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 82.10 E-value: 2.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAFSVGP----INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPV-SGEQPEDYRK 397
Cdd:PRK13649 3 INLQNVSYTYQAGTPFEGRalfdVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItSTSKNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 398 L-------F----SAVFTDVWLFDQLLGPE----GKPANPQLVEKWLAQLKMAHKLELSNgrivNLKLSKGQKKRVALLL 462
Cdd:PRK13649 83 IrkkvglvFqfpeSQLFEETVLKDVAFGPQnfgvSQEEAEALAREKLALVGISESLFEKN----PFELSGGQMRRVAIAG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16130148 463 ALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEmGKTIFAISH--DD 510
Cdd:PRK13649 159 ILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQS-GMTIVLVTHlmDD 207
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
322-529 |
5.93e-17 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 82.50 E-value: 5.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 322 TLELRNVTFAYqdNAFSV-GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKpvsgeqpedyrklfs 400
Cdd:COG1118 2 SIEVRNISKRF--GSFTLlDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGR--------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 401 AVFTDV--------WLF-DQLL------------GPEGKPANP----QLVEKWLAQLKMAHkLElsnGRIVNlKLSKGQK 455
Cdd:COG1118 65 DLFTNLpprerrvgFVFqHYALfphmtvaeniafGLRVRPPSKaeirARVEELLELVQLEG-LA---DRYPS-QLSGGQR 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130148 456 KRVALLLALAEERDIILLDE-WAAdQDPHFRREFYQVLLPLMQEMG-KTIFaISHD--DHYFIhADRLLEMRNGQLSE 529
Cdd:COG1118 140 QRVALARALAVEPEVLLLDEpFGA-LDAKVRKELRRWLRRLHDELGgTTVF-VTHDqeEALEL-ADRVVVMNQGRIEQ 214
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
323-527 |
6.06e-17 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 82.46 E-value: 6.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPV--SGEQPEDYRKLFS 400
Cdd:PRK11432 7 VVLKNITKRFGSNTV-IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVthRSIQQRDICMVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 401 --AVFTDVWLFD------QLLGpEGKPANPQLVEKWLAQLKMAHKLElsngRIVNlKLSKGQKKRVALLLALAEERDIIL 472
Cdd:PRK11432 86 syALFPHMSLGEnvgyglKMLG-VPKEERKQRVKEALELVDLAGFED----RYVD-QISGGQQQRVALARALILKPKVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16130148 473 LDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDD-HYFIHADRLLEMRNGQL 527
Cdd:PRK11432 160 FDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQsEAFAVSDTVIVMNKGKI 215
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
278-527 |
6.90e-17 |
|
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: 83.64 E-value: 6.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 278 PLLSAVGALPTLLTAQVAFNKLNKFaLAPFKAEF-----PRPQAfpnwqTLELRNVTFAYQ-DNAFSVGPINLTIKRGEL 351
Cdd:COG4618 287 PIEQAIGGWKQFVSARQAYRRLNEL-LAAVPAEPermplPRPKG-----RLSVENLTVVPPgSKRPILRGVSFSLEPGEV 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 352 LFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKLFSAVFTDVWLFDqllG---------PEgkpANP 422
Cdd:COG4618 361 LGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFD---GtiaeniarfGD---ADP 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 423 QLVEKwLAQLKMAHKLELS-----------NGRIvnlkLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQV 491
Cdd:COG4618 435 EKVVA-AAKLAGVHEMILRlpdgydtrigeGGAR----LSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAA 509
|
250 260 270
....*....|....*....|....*....|....*.
gi 16130148 492 LLpLMQEMGKTIFAISHDDHYFIHADRLLEMRNGQL 527
Cdd:COG4618 510 IR-ALKARGATVVVITHRPSLLAAVDKLLVLRDGRV 544
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
324-529 |
7.72e-17 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 79.89 E-value: 7.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 324 ELRNVTFAY---QDNafsvgPI----NLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYR 396
Cdd:cd03249 2 EFKNVSFRYpsrPDV-----PIlkglSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 397 KLFSAVFTDVWLFDQLLGPE---GKPANPQLVEKWLAQLKMAHKLelsngrIVNL-------------KLSKGQKKRVAL 460
Cdd:cd03249 77 SQIGLVSQEPVLFDGTIAENiryGKPDATDEEVEEAAKKANIHDF------IMSLpdgydtlvgergsQLSGGQKQRIAI 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130148 461 LLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMqeMGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
Cdd:cd03249 151 ARALLRNPKILLLDEATSALDAESEKLVQEALDRAM--KGRTTIVIAHRLSTIRNADLIAVLQNGQVVE 217
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
322-488 |
8.54e-17 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 79.06 E-value: 8.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 322 TLELRNVTFAYQDNAFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQ---SGEILLDGKPVSGEQPEDyRKL 398
Cdd:COG4136 1 MLSLENLTITLGGRPL-LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAEQ-RRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 399 fSAVFTDVWLFDQL-----LG---PE--GKPANPQLVEKWLAQLKMAHKLElsngRIVNlKLSKGQKKRVALLLALAEER 468
Cdd:COG4136 79 -GILFQDDLLFPHLsvgenLAfalPPtiGRAQRRARVEQALEEAGLAGFAD----RDPA-TLSGGQRARVALLRALLAEP 152
|
170 180
....*....|....*....|
gi 16130148 469 DIILLDEWAADQDPHFRREF 488
Cdd:COG4136 153 RALLLDEPFSKLDAALRAQF 172
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
323-526 |
1.08e-16 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 79.74 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSG-EILLDGKPVSGEQPEDYRK---L 398
Cdd:COG1119 4 LELRNVTVRRGGKTI-LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKrigL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 399 FSAVFTD-------VW------LFDQL-LGPEGKPANPQLVEKWLAQLKMAHKLELSNGRivnlkLSKGQKKRVALLLAL 464
Cdd:COG1119 83 VSPALQLrfprdetVLdvvlsgFFDSIgLYREPTDEQRERARELLELLGLAHLADRPFGT-----LSQGEQRRVLIARAL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130148 465 AEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHddhyfiHA-------DRLLEMRNGQ 526
Cdd:COG1119 158 VKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTH------HVeeippgiTHVLLLKDGR 220
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
339-527 |
1.13e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 79.88 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 339 VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYqPQSGEILLDGKPVSGEQPED---YRKLFS-----AVFTDVWLFD 410
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAElarHRAYLSqqqspPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 411 QLLGPEGkpANPQLVEKWLAQLkmAHKLELSN--GRIVNlKLSKGQKKRV---ALLL----ALAEERDIILLDEWAADQD 481
Cdd:COG4138 91 ALHQPAG--ASSEAVEQLLAQL--AEALGLEDklSRPLT-QLSGGEWQRVrlaAVLLqvwpTINPEGQLLLLDEPMNSLD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16130148 482 PHFRREFYQvLLPLMQEMGKTIFAISHD-DHYFIHADRLLEMRNGQL 527
Cdd:COG4138 166 VAQQAALDR-LLRELCQQGITVVMSSHDlNHTLRHADRVWLLKQGKL 211
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
322-529 |
1.14e-16 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 83.23 E-value: 1.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 322 TLELRNVTFAYQDNAFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKLFSA 401
Cdd:PRK10790 340 RIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 402 VFTD-VWLFDQLLG--PEGKPANPQLVEKWLAQLKMAHKL-ELSNGRIVNL-----KLSKGQKKRVALLLALAEERDIIL 472
Cdd:PRK10790 420 VQQDpVVLADTFLAnvTLGRDISEEQVWQALETVQLAELArSLPDGLYTPLgeqgnNLSVGQKQLLALARVLVQTPQILI 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16130148 473 LDEWAADQDPHFRREFYQVLLPLMQEmgKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
Cdd:PRK10790 500 LDEATANIDSGTEQAIQQALAAVREH--TTLVVIAHRLSTIVEADTILVLHRGQAVE 554
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
323-534 |
1.16e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 82.76 E-value: 1.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYqdnafsvGP------INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYR 396
Cdd:COG1129 5 LEMRGISKSF-------GGvkaldgVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 397 KL-FSAVFTDVWLFDQL-------LGPEgkPANPQLV---------EKWLAQLkmahKLELSNGRIVNlKLSKGQKKRVA 459
Cdd:COG1129 78 AAgIAIIHQELNLVPNLsvaenifLGRE--PRRGGLIdwramrrraRELLARL----GLDIDPDTPVG-DLSVAQQQLVE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 460 LLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLmQEMGKTIFAISHD-DHYFIHADRLLEMRNGQL------SELTG 532
Cdd:COG1129 151 IARALSRDARVLILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISHRlDEVFEIADRVTVLRDGRLvgtgpvAELTE 229
|
..
gi 16130148 533 EE 534
Cdd:COG1129 230 DE 231
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
323-534 |
2.01e-16 |
|
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: 78.18 E-value: 2.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAfSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEqPEDYRKLFSAV 402
Cdd:cd03265 1 IEVENLVKKYGDFE-AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVRE-PREVRRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 403 FTDVWLFDQLLGPE---------GKPaNPQLVEKWLAQLKMAHKLELSNgRIVNlKLSKGQKKRVALLLALAEERDIILL 473
Cdd:cd03265 79 FQDLSVDDELTGWEnlyiharlyGVP-GAERRERIDELLDFVGLLEAAD-RLVK-TYSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130148 474 DEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHD-DHYFIHADRLLEMRNGQL-SELTGEE 534
Cdd:cd03265 156 DEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYmEEAEQLCDRVAIIDHGRIiAEGTPEE 218
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
323-529 |
2.97e-16 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 81.60 E-value: 2.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQD-NAFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKLFSA 401
Cdd:PRK11176 342 IEFRNVTFTYPGkEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 402 VFTDVWLFDQLLG------PEGKPANPQLVEKwlaqLKMAHKLE----LSNG--RIV---NLKLSKGQKKRVALLLALAE 466
Cdd:PRK11176 422 VSQNVHLFNDTIAnniayaRTEQYSREQIEEA----ARMAYAMDfinkMDNGldTVIgenGVLLSGGQRQRIAIARALLR 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130148 467 ERDIILLDEWAADQDPHFRREFYQVLLPLMQEmgKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
Cdd:PRK11176 498 DSPILILDEATSALDTESERAIQAALDELQKN--RTSLVIAHRLSTIEKADEILVVEDGEIVE 558
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
323-518 |
3.94e-16 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 78.65 E-value: 3.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNA-FSvgPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPV---SGEQPEDYRKL 398
Cdd:PRK11831 8 VDMRGVSFTRGNRCiFD--NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamSRSRLYTVRKR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 399 FS------AVFTDVWLFDQLLGPEGKpaNPQLVEKWLAQLKMAhKLELSNGR-IVNLK---LSKGQKKRVALLLALAEER 468
Cdd:PRK11831 86 MSmlfqsgALFTDMNVFDNVAYPLRE--HTQLPAPLLHSTVMM-KLEAVGLRgAAKLMpseLSGGMARRAALARAIALEP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130148 469 DIILLDEWAADQDPhfrrEFYQVLLPLMQE----MGKTIFAISHD--------DHYFIHADR 518
Cdd:PRK11831 163 DLIMFDEPFVGQDP----ITMGVLVKLISElnsaLGVTCVVVSHDvpevlsiaDHAYIVADK 220
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
323-475 |
6.04e-16 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 77.41 E-value: 6.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFayqdnafSVGP------INLTIKRGELLFLIGGNGSGKSTLAMLLTGL--YQPQSGEILLDGKPVSGEQPED 394
Cdd:COG0396 1 LEIKNLHV-------SVEGkeilkgVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELSPDE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 395 YRK--LFSAvFTD------VWLFD--------QLLGPEGKPANPQLVEKWLAQLKMAHKLeLSngRIVNLKLSKGQKKRV 458
Cdd:COG0396 74 RARagIFLA-FQYpveipgVSVSNflrtalnaRRGEELSAREFLKLLKEKMKELGLDEDF-LD--RYVNEGFSGGEKKRN 149
|
170
....*....|....*..
gi 16130148 459 ALLLALAEERDIILLDE 475
Cdd:COG0396 150 EILQMLLLEPKLAILDE 166
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
336-530 |
7.21e-16 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 79.69 E-value: 7.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 336 AFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDG----KPVSGEQPEDYRKLFSAVFTDVWLFDQ 411
Cdd:PRK10070 41 SLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiaKISDAELREVRRKKIAMVFQSFALMPH 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 412 L-------LGPE--GKPANPQLvEKWLAQLKMAHKLELSNGriVNLKLSKGQKKRVALLLALAEERDIILLDEWAADQDP 482
Cdd:PRK10070 121 MtvldntaFGMElaGINAEERR-EKALDALRQVGLENYAHS--YPDELSGGMRQRVGLARALAINPDILLMDEAFSALDP 197
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16130148 483 HFRREFYQVLLPLMQEMGKTIFAISHD-DHYFIHADRLLEMRNGQLSEL 530
Cdd:PRK10070 198 LIRTEMQDELVKLQAKHQRTIVFISHDlDEAMRIGDRIAIMQNGEVVQV 246
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
342-527 |
7.64e-16 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 77.04 E-value: 7.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVS------GEQPEdyrklfsavFT---DVWLFDQL 412
Cdd:COG1134 45 VSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSAllelgaGFHPE---------LTgreNIYLNGRL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 413 LGpegkpANPQLVEKwlaqlKMAHKLELSN-GRIVNLKL---SKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREF 488
Cdd:COG1134 116 LG-----LSRKEIDE-----KFDEIVEFAElGDFIDQPVktySSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKC 185
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 16130148 489 YQVLLPLMQEmGKTIFAISHdDHYFI--HADRLLEMRNGQL 527
Cdd:COG1134 186 LARIRELRES-GRTVIFVSH-SMGAVrrLCDRAIWLEKGRL 224
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
323-536 |
7.94e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 78.14 E-value: 7.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNA-F---SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVS-GEQPEDYRK 397
Cdd:PRK13634 3 ITFQKVEHRYQYKTpFerrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITaGKKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 398 LFSAV-----FTDVWLFDQLL------GP--------EGKpanpQLVEKWLAQLKMAHK-LELSngrivNLKLSKGQKKR 457
Cdd:PRK13634 83 LRKKVgivfqFPEHQLFEETVekdicfGPmnfgvseeDAK----QKAREMIELVGLPEElLARS-----PFELSGGQMRR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 458 VALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISH--DD--HYfihADRLLEMRNGQLsELTGE 533
Cdd:PRK13634 154 VAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHsmEDaaRY---ADQIVVMHKGTV-FLQGT 229
|
...
gi 16130148 534 ERD 536
Cdd:PRK13634 230 PRE 232
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
323-508 |
8.98e-16 |
|
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: 76.25 E-value: 8.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAF---SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKL- 398
Cdd:cd03266 2 ITADALTKRFRDVKKtvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 399 -FSA---------VFTDVWLFDQLLGPEGKPANPQLveKWLAQ-LKMAHKLELSNGrivnlKLSKGQKKRVALLLALAEE 467
Cdd:cd03266 82 fVSDstglydrltARENLEYFAGLYGLKGDELTARL--EELADrLGMEELLDRRVG-----GFSTGMRQKVAIARALVHD 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 16130148 468 RDIILLDEWAADQDPHFRREFYQVLLPLmQEMGKTIFAISH 508
Cdd:cd03266 155 PPVLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTH 194
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
307-527 |
1.57e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 77.58 E-value: 1.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 307 FKAEFPRPQAFPNWQTLELRNVTFAY---QDNAFSV-GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEI-- 380
Cdd:PRK13631 6 MKKKLKVPNPLSDDIILRVKNLYCVFdekQENELVAlNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 381 --LLDGKPVSGEQPEDY------------RKLFSAVFT--DVWLF------DQLLGP----EGKPANPQLVEKWLAQLKM 434
Cdd:PRK13631 86 gdIYIGDKKNNHELITNpyskkiknfkelRRRVSMVFQfpEYQLFkdtiekDIMFGPvalgVKKSEAKKLAKFYLNKMGL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 435 AHK-LELSNgrivnLKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEmGKTIFAISHD-DHY 512
Cdd:PRK13631 166 DDSyLERSP-----FGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTmEHV 239
|
250
....*....|....*
gi 16130148 513 FIHADRLLEMRNGQL 527
Cdd:PRK13631 240 LEVADEVIVMDKGKI 254
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
342-511 |
1.59e-15 |
|
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: 76.22 E-value: 1.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKpVSGEQPEDYRKLFSAVF---TDVWlFDqLLGPEGK 418
Cdd:cd03267 40 ISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL-VPWKRRKKFLRRIGVVFgqkTQLW-WD-LPVIDSF 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 419 PANPQL--VEKWLAQLKMAHKLELSN-GRIVNL---KLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVL 492
Cdd:cd03267 117 YLLAAIydLPPARFKKRLDELSELLDlEELLDTpvrQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFL 196
|
170
....*....|....*....
gi 16130148 493 LPLMQEMGKTIFAISHDDH 511
Cdd:cd03267 197 KEYNRERGTTVLLTSHYMK 215
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
322-475 |
4.92e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 75.92 E-value: 4.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 322 TLELRNVTFAYQDNAfSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQ-------PED 394
Cdd:COG4152 1 MLELKGLTKRFGDKT-AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDrrrigylPEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 395 ---YRKLfsavftDVWlfDQLL------GPEGKPANPQLvEKWLAQLKMAH----KLElsngrivnlKLSKGQKKRVALL 461
Cdd:COG4152 80 rglYPKM------KVG--EQLVylarlkGLSKAEAKRRA-DEWLERLGLGDrankKVE---------ELSKGNQQKVQLI 141
|
170
....*....|....
gi 16130148 462 LALAEERDIILLDE 475
Cdd:COG4152 142 AALLHDPELLILDE 155
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
325-529 |
6.48e-15 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 73.60 E-value: 6.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 325 LRNVTFayqdnafsvgpinlTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKLFSAVFT 404
Cdd:cd03369 24 LKNVSF--------------KVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTIIPQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 405 DVWLFDQL----LGPEGKPANPQLVEkwlaqlkmahKLELSNGrivNLKLSKGQKKRVALLLALAEERDIILLDEWAADQ 480
Cdd:cd03369 90 DPTLFSGTirsnLDPFDEYSDEEIYG----------ALRVSEG---GLNLSQGQRQLLCLARALLKRPRVLVLDEATASI 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16130148 481 DPHFRREFYQVLLPLMQemGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
Cdd:cd03369 157 DYATDALIQKTIREEFT--NSTILTIAHRLRTIIDYDKILVMDAGEVKE 203
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
342-527 |
7.80e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 74.42 E-value: 7.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKLfSAV----------FT--DVWLF 409
Cdd:PRK13548 21 VSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARR-RAVlpqhsslsfpFTveEVVAM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 410 DQLLGPEGKPANPQLVEKWLAQLKMAHkleLSNGRIvnLKLSKGQKKRVALLLALA------EERDIILLDEWAADQDPH 483
Cdd:PRK13548 100 GRAPHGLSRAEDDALVAAALAQVDLAH---LAGRDY--PQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16130148 484 FRREFYQVLLPLMQEMGKTIFAISHD----DHYfihADRLLEMRNGQL 527
Cdd:PRK13548 175 HQHHVLRLARQLAHERGLAVIVVLHDlnlaARY---ADRIVLLHQGRL 219
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
323-526 |
8.48e-15 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 71.71 E-value: 8.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNA-FSvgPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEIlldgkpvsgeqpedyrklfsa 401
Cdd:cd03221 1 IELENLSKTYGGKLlLK--DISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV--------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 402 vftdvwlfdqllgpegkpanpqlveKWLAQLKMAHkLElsngrivnlKLSKGQKKRVALLLALAEERDIILLDEwaadqd 481
Cdd:cd03221 58 -------------------------TWGSTVKIGY-FE---------QLSGGEKMRLALAKLLLENPNLLLLDE------ 96
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16130148 482 P--HFRREFYQVLLPLMQEMGKTIFAISHdDHYFIH--ADRLLEMRNGQ 526
Cdd:cd03221 97 PtnHLDLESIEALEEALKEYPGTVILVSH-DRYFLDqvATKIIELEDGK 144
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
349-527 |
9.53e-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: 73.48 E-value: 9.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 349 GELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKP-VSGEQ----PEDYRKLfSAVFTDVWLFDQL-------LGPE 416
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlFDSRKkinlPPQQRKI-GLVFQQYALFPHLnvrenlaFGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 417 GKPANP--QLVEKWLAQLKMAHKLELSNGrivnlKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREfyqvLLP 494
Cdd:cd03297 102 RKRNREdrISVDELLDLLGLDHLLNRYPA-----QLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQ----LLP 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 16130148 495 LMQEMGK-----TIFaISHD-DHYFIHADRLLEMRNGQL 527
Cdd:cd03297 173 ELKQIKKnlnipVIF-VTHDlSEAEYLADRIVVMEDGRL 210
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
340-527 |
9.73e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 74.20 E-value: 9.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 340 GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYqPQSGEILLDGKPVSGEQPED---YRKLFS----AVFT-DVWLFDQ 411
Cdd:PRK03695 13 GPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAElarHRAYLSqqqtPPFAmPVFQYLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 412 LLGPEGkpANPQLVEKWL----AQLKMAHKLelsnGRIVNlKLSKGQKKRV---ALLL----ALAEERDIILLDEWAADQ 480
Cdd:PRK03695 92 LHQPDK--TRTEAVASALnevaEALGLDDKL----GRSVN-QLSGGEWQRVrlaAVVLqvwpDINPAGQLLLLDEPMNSL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16130148 481 DPHFRREFYQvLLPLMQEMGKTIFAISHD-DHYFIHADRLLEMRNGQL 527
Cdd:PRK03695 165 DVAQQAALDR-LLSELCQQGIAVVMSSHDlNHTLRHADRVWLLKQGKL 211
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
323-527 |
1.09e-14 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 77.07 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAFSV---GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKL- 398
Cdd:PRK10535 5 LELKDIRRSYPSGEEQVevlKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 399 ---FSAVFTDVWLFDQLLGPE-----------GKPANPQLVEKWLAQLKMAHKLELSNGrivnlKLSKGQKKRVALLLAL 464
Cdd:PRK10535 85 rehFGFIFQRYHLLSHLTAAQnvevpavyaglERKQRLLRAQELLQRLGLEDRVEYQPS-----QLSGGQQQRVSIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130148 465 AEERDIILLDEWAADQDPHFRREFYQVLLPLmQEMGKTIFAISHDDHYFIHADRLLEMRNGQL 527
Cdd:PRK10535 160 MNGGQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
323-527 |
1.21e-14 |
|
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: 73.00 E-value: 1.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYqDNAFSVGPINLTIKRGeLLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSgEQPEDYRKLFSAV 402
Cdd:cd03264 1 LQLENLTKRY-GKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVL-KQPQKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 403 FTDVWLFDQLlgpegkPANPQLveKWLAQLK-MAHK---------LELsngriVNL---------KLSKGQKKRVALLLA 463
Cdd:cd03264 78 PQEFGVYPNF------TVREFL--DYIAWLKgIPSKevkarvdevLEL-----VNLgdrakkkigSLSGGMRRRVGIAQA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130148 464 LAEERDIILLDEWAADQDPHFRREFYQVLlplmQEMGKT-IFAIS-H--DDHYFIhADRLLEMRNGQL 527
Cdd:cd03264 145 LVGDPSILIVDEPTAGLDPEERIRFRNLL----SELGEDrIVILStHivEDVESL-CNQVAVLNKGKL 207
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
325-527 |
1.48e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 74.27 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 325 LRNVTFAY-QDNAFSVGPIN---LTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGE-ILLDGKPVSG----EQPEDY 395
Cdd:PRK13645 9 LDNVSYTYaKKTPFEFKALNntsLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQtIVGDYAIPANlkkiKEVKRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 396 RKLFSAVFT--DVWLF------DQLLGPEGKPANPQLVEKWLAQLKMAHKLELSNGRIVNLKLSKGQKKRVALLLALAEE 467
Cdd:PRK13645 89 RKEIGLVFQfpEYQLFqetiekDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130148 468 RDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHD-DHYFIHADRLLEMRNGQL 527
Cdd:PRK13645 169 GNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNmDQVLRIADEVIVMHEGKV 229
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
330-527 |
1.49e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 73.89 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 330 FAYQDNAFSVGpINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVsgeqpeDY--------RKLFSA 401
Cdd:PRK13638 9 FRYQDEPVLKG-LNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL------DYskrgllalRQQVAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 402 VFTD----VWLFDQLLGPEGKPANPQLVEKWLAQlKMAHKLELSNGRIVNLK----LSKGQKKRVALLLALAEERDIILL 473
Cdd:PRK13638 82 VFQDpeqqIFYTDIDSDIAFSLRNLGVPEAEITR-RVDEALTLVDAQHFRHQpiqcLSHGQKKRVAIAGALVLQARYLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16130148 474 DEWAADQDPHFRREFYQVLLPLMQEmGKTIFAISHD-DHYFIHADRLLEMRNGQL 527
Cdd:PRK13638 161 DEPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDiDLIYEISDAVYVLRQGQI 214
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
305-532 |
1.72e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 75.87 E-value: 1.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 305 APFKAEFPRPQAFPNwQTLELRNVTFAYQDNA-FSvgPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLd 383
Cdd:COG0488 299 KTVEIRFPPPERLGK-KVLELEGLSKSYGDKTlLD--DLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL- 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 384 GKPVS-------GEQ-PEDYRklfsavftdvwLFDQL--LGPEGKPANP-QLVEKWLAQLKMAHKLelsngriVNlKLSK 452
Cdd:COG0488 375 GETVKigyfdqhQEElDPDKT-----------VLDELrdGAPGGTEQEVrGYLGRFLFSGDDAFKP-------VG-VLSG 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 453 GQKKRVALLLALAEERDIILLDEWAADQDPHFRrefyQVLLPLMQEMGKTIFAISHdDHYFI--HADRLLEMRNGQLSEL 530
Cdd:COG0488 436 GEKARLALAKLLLSPPNVLLLDEPTNHLDIETL----EALEEALDDFPGTVLLVSH-DRYFLdrVATRILEFEDGGVREY 510
|
..
gi 16130148 531 TG 532
Cdd:COG0488 511 PG 512
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
323-527 |
1.73e-14 |
|
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: 72.25 E-value: 1.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAfSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVsGEQPEDYRKLfSAV 402
Cdd:cd03268 1 LKTNDLTKTYGKKR-VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY-QKNIEALRRI-GAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 403 FTDVWLFDQLLGPE---------GKPANpqLVEKWLAQLKMAHklelSNGRIVNlKLSKGQKKRVALLLALAEERDIILL 473
Cdd:cd03268 78 IEAPGFYPNLTAREnlrllarllGIRKK--RIDEVLDVVGLKD----SAKKKVK-GFSLGMKQRLGIALALLGNPDLLIL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16130148 474 DEWAADQDPHFRREFYQVLLPLMQEmGKTIFAISHddhyFIH-----ADRLLEMRNGQL 527
Cdd:cd03268 151 DEPTNGLDPDGIKELRELILSLRDQ-GITVLISSH----LLSeiqkvADRIGIINKGKL 204
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
324-529 |
1.85e-14 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 76.15 E-value: 1.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 324 ELRNVTFAYQDNAFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKLFSAVF 403
Cdd:PRK13657 336 EFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVF 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 404 TDVWLFDQLLGPE---GKP-ANPqlvEKWLAQLKMAHKLELSNGRIVNL---------KLSKGQKKRVALLLALAEERDI 470
Cdd:PRK13657 416 QDAGLFNRSIEDNirvGRPdATD---EEMRAAAERAQAHDFIERKPDGYdtvvgergrQLSGGERQRLAIARALLKDPPI 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16130148 471 ILLDEWAADQDPHFRREFYQVLLPLMQemGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
Cdd:PRK13657 493 LILDEATSALDVETEAKVKAALDELMK--GRTTFIIAHRLSTVRNADRILVFDNGRVVE 549
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
342-527 |
2.06e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 73.97 E-value: 2.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEIL-------LDGKPVSGE-----------------QPEDYRK 397
Cdd:PRK13651 26 VSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwifkdekNKKKTKEKEkvleklviqktrfkkikKIKEIRR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 398 LFSAVF--TDVWLFDQ------LLGPEGKPANPQLVEKWLAQ-LKMAhKLELSNGRIVNLKLSKGQKKRVALLLALAEER 468
Cdd:PRK13651 106 RVGVVFqfAEYQLFEQtiekdiIFGPVSMGVSKEEAKKRAAKyIELV-GLDESYLQRSPFELSGGQKRRVALAGILAMEP 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 469 DIILLDEWAADQDPHFRREFYQVLLPLmQEMGKTIFAISHD-DHYFIHADRLLEMRNGQL 527
Cdd:PRK13651 185 DFLVFDEPTAGLDPQGVKEILEIFDNL-NKQGKTIILVTHDlDNVLEWTKRTIFFKDGKI 243
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
339-509 |
2.13e-14 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 73.10 E-value: 2.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 339 VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGeQP--EDYRKLFSAVFTDVWLFDQLL--- 413
Cdd:PRK11300 21 VNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEG-LPghQIARMGVVRTFQHVRLFREMTvie 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 414 --------------------GPEGKPANPQLVEK---WLAQLKMahkLELSNGRIVNlkLSKGQKKRVALLLALAEERDI 470
Cdd:PRK11300 100 nllvaqhqqlktglfsgllkTPAFRRAESEALDRaatWLERVGL---LEHANRQAGN--LAYGQQRRLEIARCMVTQPEI 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 16130148 471 ILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHD 509
Cdd:PRK11300 175 LMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHD 213
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
323-527 |
2.22e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 73.61 E-value: 2.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNA----FSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILL------------DGKP 386
Cdd:PRK13643 2 IKFEKVNYTYQPNSpfasRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgdivvsstskqkEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 387 VSGEQPEDYRKLFSAVFTDVWLFDQLLGPEGKPANPQLVEKWLAQLKMAHKLELSNGRIVNLKLSKGQKKRVALLLALAE 466
Cdd:PRK13643 82 VRKKVGVVFQFPESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130148 467 ERDIILLDEWAADQDPHFRREFYQvLLPLMQEMGKTIFAISH-DDHYFIHADRLLEMRNGQL 527
Cdd:PRK13643 162 EPEVLVLDEPTAGLDPKARIEMMQ-LFESIHQSGQTVVLVTHlMDDVADYADYVYLLEKGHI 222
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
325-520 |
2.72e-14 |
|
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: 72.83 E-value: 2.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 325 LRNVTFAYQDNAFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDG-----KP--VSGEQPEDYRK 397
Cdd:cd03237 1 YTYPTMKKTLGEFTLEVEGGSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELdtvsyKPqyIKADYEGTVRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 398 LFSAVFTDVWLFDQLlgpEGKPANPQLVEKWLAQlkmahklELSNgrivnlkLSKGQKKRVALLLALAEERDIILLDEWA 477
Cdd:cd03237 81 LLSSITKDFYTHPYF---KTEIAKPLQIEQILDR-------EVPE-------LSGGELQRVAIAACLSKDADIYLLDEPS 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 16130148 478 ADQDPHFRREFYQVLLPLMQEMGKTIFAISHdDHYFIH--ADRLL 520
Cdd:cd03237 144 AYLDVEQRLMASKVIRRFAENNEKTAFVVEH-DIIMIDylADRLI 187
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
342-529 |
3.79e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 71.73 E-value: 3.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKL-----------FSAVFT-----D 405
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLrakhvgfvfqsFMLIPTlnaleN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 406 VWLFDQLLGPEGKPANPQLVEkWLAQLKMAHKLelsngRIVNLKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFR 485
Cdd:PRK10584 109 VELPALLRGESSRQSRNGAKA-LLEQLGLGKRL-----DHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTG 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 16130148 486 REFYQVLLPLMQEMGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
Cdd:PRK10584 183 DKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
322-529 |
4.16e-14 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 72.09 E-value: 4.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 322 TLELRNVTFAYQDNAFSVGpINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQS-----GEILLDG-KPVSGEQP--E 393
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHG-IDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAgtirvGDITIDTaRSLSQQKGliR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 394 DYRKLFSAVFTDVWLFDQ-------LLGP-----EGKPANPQLVEKWLAQLKMAHKlELSNGRivnlKLSKGQKKRVALL 461
Cdd:PRK11264 82 QLRQHVGFVFQNFNLFPHrtvleniIEGPvivkgEPKEEATARARELLAKVGLAGK-ETSYPR----RLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130148 462 LALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMgKTIFAISHDDHYFIH-ADRLLEMRNGQLSE 529
Cdd:PRK11264 157 RALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDvADRAIFMDQGRIVE 224
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
323-529 |
4.85e-14 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 72.51 E-value: 4.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNV--TFAYQDNAF------SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVS----GE 390
Cdd:PRK15112 5 LEVRNLskTFRYRTGWFrrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgdySY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 391 QPEDYRKLFSAVFTDvwlfdqlLGPEGKPAnpQLVEkwlAQLKMAHKLELSNG--------RIVNLK----------LSK 452
Cdd:PRK15112 85 RSQRIRMIFQDPSTS-------LNPRQRIS--QILD---FPLRLNTDLEPEQRekqiietlRQVGLLpdhasyyphmLAP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130148 453 GQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDHYFIH-ADRLLEMRNGQLSE 529
Cdd:PRK15112 153 GQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVE 230
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
323-527 |
5.56e-14 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 71.54 E-value: 5.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAFSvgpINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEdyRKLFSAV 402
Cdd:PRK10771 2 LKLTDITWLYHHLPMR---FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 403 FTDVWLFDQL-------LGpegkpANP--QLVEKWLAQLK-MAHKLELSN--GRIVNlKLSKGQKKRVALLLALAEERDI 470
Cdd:PRK10771 77 FQENNLFSHLtvaqnigLG-----LNPglKLNAAQREKLHaIARQMGIEDllARLPG-QLSGGQRQRVALARCLVREQPI 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16130148 471 ILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISH--DDHYFIhADRLLEMRNGQL 527
Cdd:PRK10771 151 LLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHslEDAARI-APRSLVVADGRI 208
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
323-475 |
6.46e-14 |
|
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: 70.63 E-value: 6.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAFSVGpINLTIKRGELLFLIGGNGSGKSTLAMLLTGL--YQPQSGEILLDGKPVSGEQPEDYRKLfs 400
Cdd:cd03217 1 LEIKDLHVSVGGKEILKG-VNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERARL-- 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130148 401 AVFtdvwlfdqlLGPEGKPANPqlvekwlaQLKMAHKLelsngRIVNLKLSKGQKKRVALLLALAEERDIILLDE 475
Cdd:cd03217 78 GIF---------LAFQYPPEIP--------GVKNADFL-----RYVNEGFSGGEKKRNEILQLLLLEPDLAILDE 130
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
307-519 |
8.32e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 72.56 E-value: 8.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 307 FKAEFPRPQAFPNwQTLELRNVTFAYQDNAFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKP 386
Cdd:PRK13536 27 SEAKASIPGSMST-VAIDLAGVSKSYGDKAV-VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 387 VSGeQPEDYRKLFSAV---------FT---DVWLFDQLLG---PEGKPANPQLVEkwLAQLKMAhklelSNGRIVNlkLS 451
Cdd:PRK13536 105 VPA-RARLARARIGVVpqfdnldleFTvreNLLVFGRYFGmstREIEAVIPSLLE--FARLESK-----ADARVSD--LS 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130148 452 KGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEmGKTIFAIShddHYFIHADRL 519
Cdd:PRK13536 175 GGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTT---HFMEEAERL 238
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
323-527 |
1.11e-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: 69.38 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQdnafsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKL-FSA 401
Cdd:cd03215 5 LEVRGLSVKGA-----VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 402 VftdvwlfdqllgPEGKpanpqlvekwlaqLKMAHKLELS---NGRIVNLkLSKGQKKRVALLLALAEERDIILLDEWAA 478
Cdd:cd03215 80 V------------PEDR-------------KREGLVLDLSvaeNIALSSL-LSGGNQQKVVLARWLARDPRVLILDEPTR 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16130148 479 DQDPHFRREFYQVLLPLMQEmGKTIFAISHDDHYFIH-ADRLLEMRNGQL 527
Cdd:cd03215 134 GVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
342-522 |
2.27e-13 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 68.80 E-value: 2.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSG---EQPEDYRKL----FSAVFTDVWLFDQLLG 414
Cdd:NF040873 11 VDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAyvpQRSEVPDSLpltvRDLVAMGRWARRGLWR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 415 PEGKpANPQLVEKWLAQLKMAhklELSNGRIVnlKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLP 494
Cdd:NF040873 91 RLTR-DDRAAVDDALERVGLA---DLAGRQLG--ELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAE 164
|
170 180
....*....|....*....|....*...
gi 16130148 495 LMQEmGKTIFAISHDDHYFIHADRLLEM 522
Cdd:NF040873 165 EHAR-GATVVVVTHDLELVRRADPCVLL 191
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
330-525 |
3.06e-13 |
|
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: 68.90 E-value: 3.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 330 FAYQDNAFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDY--RKLFSAVFT--D 405
Cdd:cd03290 8 FSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATrsRNRYSVAYAaqK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 406 VWLFDQLLGPE---GKPANPQ----LVEKWLAQ-----LKMAHKLELSNgRIVNLklSKGQKKRVALLLALAEERDIILL 473
Cdd:cd03290 88 PWLLNATVEENitfGSPFNKQrykaVTDACSLQpdidlLPFGDQTEIGE-RGINL--SGGQRQRICVARALYQNTNIVFL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16130148 474 DEWAADQDPHFRREFYQV-LLPLMQEMGKTIFAISHDDHYFIHADRLLEMRNG 525
Cdd:cd03290 165 DDPFSALDIHLSDHLMQEgILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
323-509 |
3.21e-13 |
|
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: 70.85 E-value: 3.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAFSV----GpINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQ---SGEILLDGKPVSGEQPEDY 395
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVkavdG-VSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 396 RKL----FSAVFTDvwlfdqllgpegkPA---NP------QLVEKWLAQLKMAHK---------LELsngriVNLK---- 449
Cdd:COG0444 81 RKIrgreIQMIFQD-------------PMtslNPvmtvgdQIAEPLRIHGGLSKAeareraielLER-----VGLPdper 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130148 450 --------LSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHD 509
Cdd:COG0444 143 rldrypheLSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHD 210
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
342-535 |
6.01e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 68.96 E-value: 6.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGeQPEDYR-KLFSAVFTDVwlfdqLLG--PE-- 416
Cdd:COG1101 25 LNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTK-LPEYKRaKYIGRVFQDP-----MMGtaPSmt 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 417 -----------GKP---------ANPQLVEKWLAQLKMAhkLElsnGRI---VNLkLSKGQKKRVALLLALAEERDIILL 473
Cdd:COG1101 99 ieenlalayrrGKRrglrrgltkKRRELFRELLATLGLG--LE---NRLdtkVGL-LSGGQRQALSLLMATLTKPKLLLL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130148 474 DEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDHYFI-HADRLLEMRNGQ-LSELTGEER 535
Cdd:COG1101 173 DEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALdYGNRLIMMHEGRiILDVSGEEK 236
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
325-509 |
9.00e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 69.67 E-value: 9.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 325 LRNVTFAYQDNAFSvGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDyrKLFSAVFT 404
Cdd:PRK11000 6 LRNVTKAYGDVVIS-KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE--RGVGMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 405 DVWLFDQL-----------LGPEGKPANPQLVEKWLAQLKMAHKLELSNGrivnlKLSKGQKKRVALLLALAEERDIILL 473
Cdd:PRK11000 83 SYALYPHLsvaenmsfglkLAGAKKEEINQRVNQVAEVLQLAHLLDRKPK-----ALSGGQRQRVAIGRTLVAEPSVFLL 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 16130148 474 DEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHD 509
Cdd:PRK11000 158 DEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHD 193
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
323-527 |
2.14e-12 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 67.40 E-value: 2.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQpEDYRKLFSAV 402
Cdd:PRK11247 13 LLLNAVSKRYGERTV-LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAR-EDTRLMFQDA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 403 FTDVW--LFDQL-LGPEG--KPANPQLVE---------KWLAqlkmahklelsngrivnlKLSKGQKKRVALLLALAEER 468
Cdd:PRK11247 91 RLLPWkkVIDNVgLGLKGqwRDAALQALAavgladranEWPA------------------ALSGGQKQRVALARALIHRP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 469 DIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDHYFIH-ADRLLEMRNGQL 527
Cdd:PRK11247 153 GLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAmADRVLLIEEGKI 212
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
342-527 |
2.91e-12 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 66.96 E-value: 2.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 342 INLTIKRGELLFLIGGNGSGKSTL----AMLLTGLYQPQSgEILLDGKPV--SGEQPEDYRK----------LFSAVFTD 405
Cdd:PRK09984 23 VDLNIHHGEMVALLGPSGSGKSTLlrhlSGLITGDKSAGS-HIELLGRTVqrEGRLARDIRKsrantgyifqQFNLVNRL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 406 VWLFDQLLGPEG------------KPANPQLVEKWLAQLKMAHkleLSNGRIVNLklSKGQKKRVALLLALAEERDIILL 473
Cdd:PRK09984 102 SVLENVLIGALGstpfwrtcfswfTREQKQRALQALTRVGMVH---FAHQRVSTL--SGGQQQRVAIARALMQQAKVILA 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16130148 474 DEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHD-DHYFIHADRLLEMRNGQL 527
Cdd:PRK09984 177 DEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQvDYALRYCERIVALRQGHV 231
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
342-509 |
4.15e-12 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 67.94 E-value: 4.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKLFSAVFTDVWL---FD-------- 410
Cdd:PRK09536 22 VDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsfeFDvrqvvemg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 411 -----QLLGPEGkPANPQLVEKWLAQLKMAHKLElsngRIVNlKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHfr 485
Cdd:PRK09536 102 rtphrSRFDTWT-ETDRAAVERAMERTGVAQFAD----RPVT-SLSGGERQRVLLARALAQATPVLLLDEPTASLDIN-- 173
|
170 180
....*....|....*....|....*...
gi 16130148 486 refYQV-LLPLMQEM---GKTIFAISHD 509
Cdd:PRK09536 174 ---HQVrTLELVRRLvddGKTAVAAIHD 198
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
321-527 |
4.49e-12 |
|
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: 64.88 E-value: 4.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 321 QTLELRNVTFAYQDNAFSVGP-----INLTIKRGELLFLIGGNGSGKSTLAMLLTGL--YQPQSGEILLDGKPVSgeqPE 393
Cdd:cd03213 2 VTLSFRNLTVTVKSSPSKSGKqllknVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPLD---KR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 394 DYRKLFSAVFTDvwlfDQLLgpegkpanPQL-VEKWL---AQLKmahklelsngrivnlKLSKGQKKRVALLLALAEERD 469
Cdd:cd03213 79 SFRKIIGYVPQD----DILH--------PTLtVRETLmfaAKLR---------------GLSGGERKRVSIALELVSNPS 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 470 IILLDEWAADQDPhFRREFYQVLLPLMQEMGKTIFAISHDDHYFIHA--DRLLEMRNGQL 527
Cdd:cd03213 132 LLFLDEPTSGLDS-SSALQVMSLLRRLADTGRTIICSIHQPSSEIFElfDKLLLLSQGRV 190
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
323-526 |
5.41e-12 |
|
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: 65.53 E-value: 5.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAY------QDnafsvgpINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPED-- 394
Cdd:cd03224 1 LEVENLNAGYgksqilFG-------VSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHEra 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 395 -----Y----RKLFSA--VFTDVWLFDQLLGPEGKPAN--------PQLVEKW--LAQLkmahklelsngrivnlkLSKG 453
Cdd:cd03224 74 ragigYvpegRRIFPEltVEENLLLGAYARRRAKRKARlervyelfPRLKERRkqLAGT-----------------LSGG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 454 QKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLmQEMGKTI--------FAISHDDHYFIhadrlleMRNG 525
Cdd:cd03224 137 EQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIREL-RDEGVTIllveqnarFALEIADRAYV-------LERG 208
|
.
gi 16130148 526 Q 526
Cdd:cd03224 209 R 209
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
323-519 |
5.75e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 66.75 E-value: 5.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKL---- 398
Cdd:PRK13537 8 IDFRNVEKRYGDKLV-VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVgvvp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 399 --------FSaVFTDVWLFDQLLGPEGKPANpQLVEKWLAQLKMAHKLELSNGrivnlKLSKGQKKRVALLLALAEERDI 470
Cdd:PRK13537 87 qfdnldpdFT-VRENLLVFGRYFGLSAAAAR-ALVPPLLEFAKLENKADAKVG-----ELSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16130148 471 ILLDEWAADQDPHFRREFYQVLLPLMQEmGKTIFAIShddHYFIHADRL 519
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTT---HFMEEAERL 204
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
325-545 |
5.79e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 68.17 E-value: 5.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 325 LRNVTFAYQDNA-FSvgPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSG----EQPED-YRKL 398
Cdd:COG0488 1 LENLSKSFGGRPlLD--DVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGylpqEPPLDdDLTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 399 FSAV---FTDVW-LFDQLLGPEGKPANPQLVEKWLAQL-----------------KMAHKLELSN---GRIVNlKLSKGQ 454
Cdd:COG0488 79 LDTVldgDAELRaLEAELEELEAKLAEPDEDLERLAELqeefealggweaearaeEILSGLGFPEedlDRPVS-ELSGGW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 455 KKRVALLLALAEERDIILLDE-----------WAADqdpHFRRefYQvllplmqemgKTIFAISHdDHYFIH--ADRLLE 521
Cdd:COG0488 158 RRRVALARALLSEPDLLLLDEptnhldlesieWLEE---FLKN--YP----------GTVLVVSH-DRYFLDrvATRILE 221
|
250 260 270
....*....|....*....|....*....|...
gi 16130148 522 MRNGQLSELTG---------EERDAASRDAVAR 545
Cdd:COG0488 222 LDRGKLTLYPGnysayleqrAERLEQEAAAYAK 254
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
342-547 |
6.22e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 67.77 E-value: 6.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKLfsavftDVWLFDQ---------- 411
Cdd:PRK15439 30 IDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQL------GIYLVPQepllfpnlsv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 412 ----LLGPEGKPANPQLVEKWLAQLKMAHKLELSNGrivnlKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRRE 487
Cdd:PRK15439 104 keniLFGLPKRQASMQKMKQLLAALGCQLDLDSSAG-----SLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETER 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130148 488 FYQVLLPLMQEmGKTIFAISHDDHYFIH-ADRLLEMRNGQ--LSELTGEERDAASRDAVARTA 547
Cdd:PRK15439 179 LFSRIRELLAQ-GVGIVFISHKLPEIRQlADRISVMRDGTiaLSGKTADLSTDDIIQAITPAA 240
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
342-527 |
6.35e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 66.16 E-value: 6.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPV----SGEQPEDYRKLFSAVFTDVWLFDQLLGPEG 417
Cdd:PRK10253 26 LTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIqhyaSKEVARRIGLLAQNATTPGDITVQELVARG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 418 KPANPQLVEKWLAQLKMAHKLELSNGRIVNL------KLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQV 491
Cdd:PRK10253 106 RYPHQPLFTRWRKEDEEAVTKAMQATGITHLadqsvdTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLEL 185
|
170 180 190
....*....|....*....|....*....|....*..
gi 16130148 492 LLPLMQEMGKTIFAISHD-DHYFIHADRLLEMRNGQL 527
Cdd:PRK10253 186 LSELNREKGYTLAAVLHDlNQACRYASHLIALREGKI 222
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
322-527 |
7.29e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 65.96 E-value: 7.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 322 TLELRNVTFAYQDNAFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDY-RKLfs 400
Cdd:PRK10575 11 TFALRNVSFRVPGRTL-LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFaRKV-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 401 avftdVWLFDQLLGPEG---------------------KPANPQLVEKW--LAQLK-MAHKLELSngrivnlkLSKGQKK 456
Cdd:PRK10575 88 -----AYLPQQLPAAEGmtvrelvaigrypwhgalgrfGAADREKVEEAisLVGLKpLAHRLVDS--------LSGGERQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130148 457 RVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDHYFI-HADRLLEMRNGQL 527
Cdd:PRK10575 155 RAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAArYCDYLVALRGGEM 226
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
341-543 |
7.40e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 67.63 E-value: 7.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 341 PINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDyrklfsAVFTDVwlfdqLLGPEGK-- 418
Cdd:PRK11288 271 PISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRD------AIRAGI-----MLCPEDRka 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 419 ----------------------PANPQLVEKWLAQLKMAHKLELS----NGR--IVNlkLSKGQKKRVALLLALAEERDI 470
Cdd:PRK11288 340 egiipvhsvadninisarrhhlRAGCLINNRWEAENADRFIRSLNiktpSREqlIMN--LSGGNQQKAILGRWLSEDMKV 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130148 471 ILLDEWAADQDPHFRREFYQVLLPLmQEMGKTIFAISHDDHYFIH-ADRLLEMRNGQLS-ELTgeeRDAASRDAV 543
Cdd:PRK11288 418 ILLDEPTRGIDVGAKHEIYNVIYEL-AAQGVAVLFVSSDLPEVLGvADRIVVMREGRIAgELA---REQATERQA 488
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
322-509 |
9.88e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 65.67 E-value: 9.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 322 TLELRNVTFAYQDNAFSVgpinltiKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGE----------Q 391
Cdd:PRK15056 13 TVTWRNGHTALRDASFTV-------PGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQAlqknlvayvpQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 392 PEDYRKLFSAVFTDVWLFDQlLGPEG-----KPANPQLVEKWLAQLKMahkLELSNGRIVnlKLSKGQKKRVALLLALAE 466
Cdd:PRK15056 86 SEEVDWSFPVLVEDVVMMGR-YGHMGwlrraKKRDRQIVTAALARVDM---VEFRHRQIG--ELSGGQKKRVFLARAIAQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 16130148 467 ERDIILLDEWAADQDPHFRREFYQVLLPLMQEmGKTIFAISHD 509
Cdd:PRK15056 160 QGQVILLDEPFTGVDVKTEARIISLLRELRDE-GKTMLVSTHN 201
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
345-520 |
1.04e-11 |
|
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: 67.50 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 345 TIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDG----KP--VSGEQP---EDY-RKLFSAVFTDVWLFDQLLG 414
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLkisyKPqyISPDYDgtvEEFlRSANTDDFGSSYYKTEIIK 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 415 PEGkpanpqlVEKWLAQlkmahklELSNgrivnlkLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLP 494
Cdd:COG1245 442 PLG-------LEKLLDK-------NVKD-------LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRR 500
|
170 180
....*....|....*....|....*...
gi 16130148 495 LMQEMGKTIFAISHdDHYFIH--ADRLL 520
Cdd:COG1245 501 FAENRGKTAMVVDH-DIYLIDyiSDRLM 527
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
338-527 |
1.35e-11 |
|
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: 66.75 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEI----------------LLDG--KPVSGEQPEDYrklf 399
Cdd:TIGR03269 299 AVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdewvdmtkpgpDGRGraKRYIGILHQEY---- 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 400 sAVFTDVWLFDQLLGPEGKPANPQL-VEKWLAQLKMAHKLELSNGRIVNL---KLSKGQKKRVALLLALAEERDIILLDE 475
Cdd:TIGR03269 375 -DLYPHRTVLDNLTEAIGLELPDELaRMKAVITLKMVGFDEEKAEEILDKypdELSEGERHRVALAQVLIKEPRIVILDE 453
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16130148 476 WAADQDPHFRREFYQVLLPLMQEMGKTIFAISHD-DHYFIHADRLLEMRNGQL 527
Cdd:TIGR03269 454 PTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDmDFVLDVCDRAALMRDGKI 506
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
342-475 |
1.44e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 63.67 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKLFsavftdvWL-----FDQLLGPE 416
Cdd:PRK13538 20 LSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLL-------YLghqpgIKTELTAL 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130148 417 ---------GKPANPQLVEKWLAQLKMAHKLELSNGRivnlkLSKGQKKRVALL-LALAeERDIILLDE 475
Cdd:PRK13538 93 enlrfyqrlHGPGDDEALWEALAQVGLAGFEDVPVRQ-----LSAGQQRRVALArLWLT-RAPLWILDE 155
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
342-482 |
1.51e-11 |
|
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: 64.49 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSgEQPEDYRKLF--------SAVFTDVWLFDQLL 413
Cdd:cd03218 19 VSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDIT-KLPMHKRARLgigylpqeASIFRKLTVEENIL 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130148 414 G-----PEGKPANPQLVEKWLAQLKMAHkLELSNGrivnLKLSKGQKKRVALLLALAEERDIILLDEWAADQDP 482
Cdd:cd03218 98 AvleirGLSKKEREEKLEELLEEFHITH-LRKSKA----SSLSGGERRRVEIARALATNPKFLLLDEPFAGVDP 166
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
233-529 |
1.80e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 67.07 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 233 LSAVNwsnIMMLGAIGLV-----FWMANSLGWADTNVAATYSLTLL-FLRTPLLsavgALPTLLT----AQVAFNKLNKF 302
Cdd:PLN03130 522 LSAFN---SFILNSIPVLvtvvsFGVFTLLGGDLTPARAFTSLSLFaVLRFPLF----MLPNLITqavnANVSLKRLEEL 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 303 ALAPFKAEFPRPQAFPNWQTLELRNVTFAYQDNA--FSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQS-GE 379
Cdd:PLN03130 595 LLAEERVLLPNPPLEPGLPAISIKNGYFSWDSKAerPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdAS 674
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 380 ILLDGKPVSGEQpedYRKLFSAVFTDVWLFdqllgpeGKPANPQLVEKWLAQLKMAHKLELSNG--------RIVNlkLS 451
Cdd:PLN03130 675 VVIRGTVAYVPQ---VSWIFNATVRDNILF-------GSPFDPERYERAIDVTALQHDLDLLPGgdlteigeRGVN--IS 742
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130148 452 KGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPlmQEM-GKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
Cdd:PLN03130 743 GGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIK--DELrGKTRVLVTNQLHFLSQVDRIILVHEGMIKE 819
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
345-520 |
2.36e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 66.37 E-value: 2.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 345 TIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLD----GKP--VSGEQPEDYRKLFSAV---FTDVWLFDQLLGP 415
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPElkisYKPqyIKPDYDGTVEDLLRSItddLGSSYYKSEIIKP 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 416 egkpanpqlvekwlaqLKMAHKLElsngRIVNlKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPL 495
Cdd:PRK13409 441 ----------------LQLERLLD----KNVK-DLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRI 499
|
170 180
....*....|....*....|....*..
gi 16130148 496 MQEMGKTIFAISHdDHYFIH--ADRLL 520
Cdd:PRK13409 500 AEEREATALVVDH-DIYMIDyiSDRLM 525
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
322-529 |
2.41e-11 |
|
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: 66.38 E-value: 2.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 322 TLELRNVTFAYQDNAFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKLFSA 401
Cdd:COG5265 357 EVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGI 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 402 VFTDVWLFDQLLGPE---GKP-ANPQLVEkwlAQLKMAHKLE----LSNG-------RivNLKLSKGQKKRVALLLALAE 466
Cdd:COG5265 437 VPQDTVLFNDTIAYNiayGRPdASEEEVE---AAARAAQIHDfiesLPDGydtrvgeR--GLKLSGGEKQRVAIARTLLK 511
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130148 467 ERDIILLDEWAADQDPHFRREFYQVLLPLMQemGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
Cdd:COG5265 512 NPPILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAHRLSTIVDADEILVLEAGRIVE 572
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
282-529 |
2.57e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 66.02 E-value: 2.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 282 AVGA---LPTLLTAQVAFNKLNKFALAPFKAEfprpqafpnwqTLELRN-VTFAYQDNAFsVGPINLTIKRGELLFLIGG 357
Cdd:PRK11174 317 AVGAaesLVTFLETPLAHPQQGEKELASNDPV-----------TIEAEDlEILSPDGKTL-AGPLNFTLPAGQRIALVGP 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 358 NGSGKSTLAMLLTGlYQPQSGEILLDGKPVSGEQPEDYRKLFSAVFTDVWLFDQLLGPEGKPANPQLVEKWLAQ-LKMAH 436
Cdd:PRK11174 385 SGAGKTSLLNALLG-FLPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQaLENAW 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 437 KLE----LSNG--RIV---NLKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQemGKTIFAIS 507
Cdd:PRK11174 464 VSEflplLPQGldTPIgdqAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASR--RQTTLMVT 541
|
250 260
....*....|....*....|..
gi 16130148 508 HDDHYFIHADRLLEMRNGQLSE 529
Cdd:PRK11174 542 HQLEDLAQWDQIWVMQDGQIVQ 563
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
15-173 |
4.75e-11 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 63.61 E-value: 4.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 15 FISVMALSLASAALGIGLIAFInQRLIETADTSLLVLPeflglLLLLMAVTLGSQLALTTL--------GHHFVYRLRSE 86
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLV-KNLIDALSAGGSSGG-----LLALLVALFLLQAVLSALssyllgrtGERVVLDLRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 87 FIKRILDTHVERIEQLGSASLLAGLTSD---VRN-ITIAfvrLPELVQGIILTIGSAAYLWMLSGKMLLVTAIWMAITIW 162
Cdd:cd18551 75 LWRRLLRLPVSFFDRRRSGDLVSRVTNDttlLRElITSG---LPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFL 151
|
170
....*....|.
gi 16130148 163 GGFVLVARVYK 173
Cdd:cd18551 152 IILPLGRRIRK 162
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
323-529 |
1.08e-10 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 63.17 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAFSV---GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRK-- 397
Cdd:COG1135 2 IELENLSKTFPTKGGPVtalDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 398 -----------LFSA--VFTDVwlfdqllgpegkpANPqlvekwlaqLKMAHK------------LELsngriVNLK--- 449
Cdd:COG1135 82 rkigmifqhfnLLSSrtVAENV-------------ALP---------LEIAGVpkaeirkrvaelLEL-----VGLSdka 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 450 ------LSKGQKKRVALLLALAEERDIILLDEwaADQ--DPHFRREFYQVLLPLMQEMGKTIFAISHDdhyfIH-----A 516
Cdd:COG1135 135 daypsqLSGGQKQRVGIARALANNPKVLLCDE--ATSalDPETTRSILDLLKDINRELGLTIVLITHE----MDvvrriC 208
|
250
....*....|...
gi 16130148 517 DRLLEMRNGQLSE 529
Cdd:COG1135 209 DRVAVLENGRIVE 221
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
338-527 |
1.35e-10 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 64.65 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSgEQPEDYRKLFSAVFTDVWLFDQLLGPEG 417
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIE-TNLDAVRQSLGMCPQHNILFHHLTVAEH 1023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 418 KPANPQLVEK-W-LAQLKMAHKLE---LSNGRIVNLK-LSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQV 491
Cdd:TIGR01257 1024 ILFYAQLKGRsWeEAQLEMEAMLEdtgLHHKRNEEAQdLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDL 1103
|
170 180 190
....*....|....*....|....*....|....*..
gi 16130148 492 LLPLMQemGKTIFAISHD-DHYFIHADRLLEMRNGQL 527
Cdd:TIGR01257 1104 LLKYRS--GRTIIMSTHHmDEADLLGDRIAIISQGRL 1138
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
257-529 |
1.70e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 64.23 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 257 LGWADTNVAATYSLTLL-FLRTPLLSAVGALPTLLTAQVAFNKLNKFALAPFKAEFPRPQAFPNWQTLELRNVTFAYQDN 335
Cdd:PLN03232 548 LGGDLTPARAFTSLSLFaVLRSPLNMLPNLLSQVVNANVSLQRIEELLLSEERILAQNPPLQPGAPAISIKNGYFSWDSK 627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 336 AF--SVGPINLTIKRGELLFLIGGNGSGKSTL-AMLLTGLYQPQSGEILLDGKPVSGEQpedYRKLFSAVFTDVWLFdql 412
Cdd:PLN03232 628 TSkpTLSDINLEIPVGSLVAIVGGTGEGKTSLiSAMLGELSHAETSSVVIRGSVAYVPQ---VSWIFNATVRENILF--- 701
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 413 lgpeGKPANPQLVEKWLAQLKMAHKLELSNGRIVN------LKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRR 486
Cdd:PLN03232 702 ----GSDFESERYWRAIDVTALQHDLDLLPGRDLTeigergVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAH 777
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 16130148 487 efyQVLLPLMQE--MGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
Cdd:PLN03232 778 ---QVFDSCMKDelKGKTRVLVTNQLHFLPLMDRIILVSEGMIKE 819
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
321-546 |
2.12e-10 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 61.25 E-value: 2.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 321 QTLELRNVTfAYQDNAFsVGPINLTIKRGELLFLIGGNGSGKS-----TLAMLLTGLYQpQSGEILLDGKPVSGEQ---- 391
Cdd:PRK10418 3 QQIELRNIA-LQAAQPL-VHGVSLTLQRGRVLALVGGSGSGKSltcaaALGILPAGVRQ-TAGRVLLDGKPVAPCAlrgr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 392 -----PEDYRKLFSAVFTDVWLFDQLLGPEGKPANPQLvekwlaqlkMAHKLE---LSN-GRIVNL---KLSKGQKKRVA 459
Cdd:PRK10418 80 kiatiMQNPRSAFNPLHTMHTHARETCLALGKPADDAT---------LTAALEavgLENaARVLKLypfEMSGGMLQRMM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 460 LLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDHYFIH-ADRLLEMRNGQLSElTGEERD-- 536
Cdd:PRK10418 151 IALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARlADDVAVMSHGRIVE-QGDVETlf 229
|
250
....*....|
gi 16130148 537 AASRDAVART 546
Cdd:PRK10418 230 NAPKHAVTRS 239
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
342-510 |
2.54e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 60.36 E-value: 2.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLY--QPQSGEILLDGKPVSGEQPedyrklfsavftdvwLFDQLlGPEGKP 419
Cdd:COG2401 49 LNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFGREAS---------------LIDAI-GRKGDF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 420 -------ANPQLVEKWLAQLKMAHklelsngrivnlkLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVL 492
Cdd:COG2401 113 kdavellNAVGLSDAVLWLRRFKE-------------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNL 179
|
170
....*....|....*...
gi 16130148 493 LPLMQEMGKTIFAISHDD 510
Cdd:COG2401 180 QKLARRAGITLVVATHHY 197
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
324-508 |
2.61e-10 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 62.13 E-value: 2.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 324 ELRNVTFAYQDNAFSV---GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRK--- 397
Cdd:PRK11153 3 ELKNISKVFPQGGRTIhalNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKarr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 398 ----------LFSA--VFTDVWLFDQLlgpEGKPANpqLVEKWLAQLkmahkLELsngriVNL---------KLSKGQKK 456
Cdd:PRK11153 83 qigmifqhfnLLSSrtVFDNVALPLEL---AGTPKA--EIKARVTEL-----LEL-----VGLsdkadrypaQLSGGQKQ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16130148 457 RVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISH 508
Cdd:PRK11153 148 RVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITH 199
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
342-536 |
2.73e-10 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 62.81 E-value: 2.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKLFSAVFTDVWLFDQLLGPE---GK 418
Cdd:PRK10789 334 VNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNialGR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 419 P-ANPQLVEKwLAQLKMAHK--LELSNG-------RIVnlKLSKGQKKRVALLLALAEERDIILLDEWAADQDPhfrREF 488
Cdd:PRK10789 414 PdATQQEIEH-VARLASVHDdiLRLPQGydtevgeRGV--MLSGGQKQRISIARALLLNAEILILDDALSAVDG---RTE 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16130148 489 YQVLLPLMQ-EMGKTIFAISHDDHYFIHADRLLEMRNG---------QLSELTGEERD 536
Cdd:PRK10789 488 HQILHNLRQwGEGRTVIISAHRLSALTEASEILVMQHGhiaqrgnhdQLAQQSGWYRD 545
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
342-529 |
2.77e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 61.14 E-value: 2.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVS-------------GEQPEDYRKLFSAVFT--DV 406
Cdd:PRK10619 24 VSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadKNQLRLLRTRLTMVFQhfNL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 407 WLFD-----------QLLGPEGKPANPQLVeKWLAQLKMAhklELSNGRiVNLKLSKGQKKRVALLLALAEERDIILLDE 475
Cdd:PRK10619 104 WSHMtvlenvmeapiQVLGLSKQEARERAV-KYLAKVGID---ERAQGK-YPVHLSGGQQQRVSIARALAMEPEVLLFDE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16130148 476 WAADQDPHFRREFYQVLLPLMQEmGKTIFAISHDDHYFIH-ADRLLEMRNGQLSE 529
Cdd:PRK10619 179 PTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHvSSHVIFLHQGKIEE 232
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
266-530 |
3.50e-10 |
|
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: 63.04 E-value: 3.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 266 ATYSLTLL-FLRTPLLSAVGALPTLLTAQVAFNKLNKF----ALAPFKAEfPRPQAFPNWQTLELRNVTFAY-QDNAFSV 339
Cdd:TIGR00957 576 AFVSLALFnILRFPLNILPMVISSIVQASVSLKRLRIFlsheELEPDSIE-RRTIKPGEGNSITVHNATFTWaRDLPPTL 654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 340 GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKpvsgeqpedyrklFSAVFTDVWLFDQLLGPE--- 416
Cdd:TIGR00957 655 NGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-------------VAYVPQQAWIQNDSLRENilf 721
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 417 GKPANPQLVEKWLAQLKMAHKLELSNG--------RIVNlkLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRRE- 487
Cdd:TIGR00957 722 GKALNEKYYQQVLEACALLPDLEILPSgdrteigeKGVN--LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHi 799
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 16130148 488 FYQVLLPLMQEMGKTIFAISHDDHYFIHADRLLEMRNGQLSEL 530
Cdd:TIGR00957 800 FEHVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEM 842
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
323-475 |
4.57e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 59.19 E-value: 4.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKLF--- 399
Cdd:PRK13540 2 LDVIELDFDYHDQPL-LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCfvg 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130148 400 --SAVFTDVWLFDQLLGPEGKPANPQLVEKWLAQLKMAHKLELSNGRivnlkLSKGQKKRVALLLALAEERDIILLDE 475
Cdd:PRK13540 81 hrSGINPYLTLRENCLYDIHFSPGAVGITELCRLFSLEHLIDYPCGL-----LSSGQKRQVALLRLWMSKAKLWLLDE 153
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
322-529 |
5.40e-10 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 60.03 E-value: 5.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 322 TLELRNVTFAYQDNAfSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDG------KPVSGEQPEDY 395
Cdd:PRK11124 2 SIQLNGINCFYGAHQ-ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 396 RKLFSAVFTDVWLFDQL-------------LGPEGKPANPQlVEKWLAQLKMAHKLELsngriVNLKLSKGQKKRVALLL 462
Cdd:PRK11124 81 RRNVGMVFQQYNLWPHLtvqqnlieapcrvLGLSKDQALAR-AEKLLERLRLKPYADR-----FPLHLSGGQQQRVAIAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130148 463 ALAEERDIILLDEWAADQDPHFRREFYQVLLPLmQEMGKTIFAISHD-DHYFIHADRLLEMRNGQLSE 529
Cdd:PRK11124 155 ALMMEPQVLLFDEPTAALDPEITAQIVSIIREL-AETGITQVIVTHEvEVARKTASRVVYMENGHIVE 221
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
339-535 |
7.57e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 60.36 E-value: 7.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 339 VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKLFSAVftdvwlfdQLL--GPE 416
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLRQKI--------QIVfqNPY 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 417 GKpANP-----QLVEKWLA---QLKMAHKLE--LSNGRIVNLK----------LSKGQKKRVALLLALAEERDIILLDEW 476
Cdd:PRK11308 103 GS-LNPrkkvgQILEEPLLintSLSAAERREkaLAMMAKVGLRpehydryphmFSGGQRQRIAIARALMLDPDVVVADEP 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 477 AADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDHYFIH-ADRLLEMRNGQLSELTGEER 535
Cdd:PRK11308 182 VSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQ 241
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
323-547 |
9.84e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 60.80 E-value: 9.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYqdnafSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQP---------- 392
Cdd:COG1129 257 LEVEGLSVGG-----VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPrdairagiay 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 393 --EDyRK-----LFSAVFTDVWL--FDQL--LGPEGKPANPQLVEKWLAQL--KMAH-KLELSNgrivnlkLSKG--QKk 456
Cdd:COG1129 332 vpED-RKgeglvLDLSIRENITLasLDRLsrGGLLDRRRERALAEEYIKRLriKTPSpEQPVGN-------LSGGnqQK- 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 457 rVALLLALAEERDIILLDEwaadqdPhFR-------REFYQvllpLMQEM---GKTIFAISHDDHYFIH-ADRLLEMRNG 525
Cdd:COG1129 403 -VVLAKWLATDPKVLILDE------P-TRgidvgakAEIYR----LIRELaaeGKAVIVISSELPELLGlSDRILVMREG 470
|
250 260
....*....|....*....|...
gi 16130148 526 QLS-ELTGEErdaASRDAVARTA 547
Cdd:COG1129 471 RIVgELDREE---ATEEAIMAAA 490
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
342-543 |
1.31e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 60.57 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKL-FSAVFTDVWLFDQLLGPEGKPA 420
Cdd:PRK09700 24 VNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGIIYQELSVIDELTVLENLYI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 421 NPQLVEK--------WLAQLKMAHKLELSNGRIVNL-----KLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRRE 487
Cdd:PRK09700 104 GRHLTKKvcgvniidWREMRVRAAMMLLRVGLKVDLdekvaNLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDY 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16130148 488 FYQVLLPLMQEmGKTIFAISHDDHYFIH-ADRLLEMRNGQlSELTGEERDAASRDAV 543
Cdd:PRK09700 184 LFLIMNQLRKE-GTAIVYISHKLAEIRRiCDRYTVMKDGS-SVCSGMVSDVSNDDIV 238
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
322-394 |
1.33e-09 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 59.86 E-value: 1.33e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130148 322 TLELRNVTFAYQDNAFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPED 394
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD 75
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
339-529 |
2.04e-09 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 60.08 E-value: 2.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 339 VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLyQPQSGEILLDGKPVSGEQPEDYRKLFSA---VFTDvwlfdqllgP 415
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSRRALRPLRRRmqvVFQD---------P 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 416 EGKpANP-----QLVEKWLAqlkmAHKLELS----NGRI------VNLK----------LSKGQKKRVALLLALAEERDI 470
Cdd:COG4172 372 FGS-LSPrmtvgQIIAEGLR----VHGPGLSaaerRARVaealeeVGLDpaarhrypheFSGGQRQRIAIARALILEPKL 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130148 471 ILLDEWAADQDPHFRREFYQVLLPLMQEMGKT-IFaISHDdhyfIH-----ADRLLEMRNGQLSE 529
Cdd:COG4172 447 LVLDEPTSALDVSVQAQILDLLRDLQREHGLAyLF-ISHD----LAvvralAHRVMVMKDGKVVE 506
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
323-398 |
3.31e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 59.27 E-value: 3.31e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16130148 323 LELRNVTFAYQDNAFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKL 398
Cdd:COG3845 258 LEVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRL 333
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
322-482 |
5.26e-09 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 56.83 E-value: 5.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 322 TLELRNVTFAYQDNAFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVS------------G 389
Cdd:PRK10895 3 TLTAKNLAKAYKGRRV-VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllplhararrgiG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 390 EQPED---YRKLfsAVFTDVWLFDQLLGPEGKPANPQLVEKWLAQLKMAHkLELSNGRivnlKLSKGQKKRVALLLALAE 466
Cdd:PRK10895 82 YLPQEasiFRRL--SVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEH-LRDSMGQ----SLSGGERRRVEIARALAA 154
|
170
....*....|....*.
gi 16130148 467 ERDIILLDEWAADQDP 482
Cdd:PRK10895 155 NPKFILLDEPFAGVDP 170
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
342-511 |
5.42e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 57.05 E-value: 5.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRkLFSAVFTDVWLFdQLLGPEGKPAN 421
Cdd:PRK09544 23 VSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLY-LDTTLPLTVNRF-LRLRPGTKKED 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 422 pqlVEKWLAQLKMAHKLELSNGrivnlKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGK 501
Cdd:PRK09544 101 ---ILPALKRVQAGHLIDAPMQ-----KLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDC 172
|
170
....*....|
gi 16130148 502 TIFAISHDDH 511
Cdd:PRK09544 173 AVLMVSHDLH 182
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
323-475 |
6.16e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 56.72 E-value: 6.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAFSVGpINLTIKRGELLFLIGGNGSGKSTLAMLLTGL--YQPQSGEILLDGKPVSGEQPED------ 394
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRG-LNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDragegi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 395 -----YRKLFSAVFTDVWLFDQL--------LGPEGKPANPQLVEKWLAQLKMAHKLeLSngRIVNLKLSKGQKKRVALL 461
Cdd:PRK09580 81 fmafqYPVEIPGVSNQFFLQTALnavrsyrgQEPLDRFDFQDLMEEKIALLKMPEDL-LT--RSVNVGFSGGEKKRNDIL 157
|
170
....*....|....
gi 16130148 462 LALAEERDIILLDE 475
Cdd:PRK09580 158 QMAVLEPELCILDE 171
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
323-508 |
6.29e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 56.84 E-value: 6.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAFSVGpINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQ--PQ---SGEILLDGKPVSGEQPEDYRK 397
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDG-VNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvSGEVYLDGQDIFKMDVIELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 398 LFSAVFT------DVWLFDQL-LGPE------GKPANPQLVEKWL--AQL--KMAHKLELSNGrivnlKLSKGQKKRVAL 460
Cdd:PRK14247 83 RVQMVFQipnpipNLSIFENVaLGLKlnrlvkSKKELQERVRWALekAQLwdEVKDRLDAPAG-----KLSGGQQQRLCI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16130148 461 LLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMgkTIFAISH 508
Cdd:PRK14247 158 ARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTH 203
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
323-387 |
8.94e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 58.00 E-value: 8.94e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130148 323 LELRN--VTF----AYQDNAFSVgpinltiKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPV 387
Cdd:PRK11288 5 LSFDGigKTFpgvkALDDISFDC-------RAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEM 68
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
255-481 |
9.71e-09 |
|
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: 58.42 E-value: 9.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 255 NSLGWADTNVAATYSLTLLFLRTPLLSAVGALPTLLtaqVAFNKLNKFAL----APFKAEFPRP-QAFPNWQTLELRNVT 329
Cdd:TIGR00957 1215 HSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNI---VAVERLKEYSEtekeAPWQIQETAPpSGWPPRGRVEFRNYC 1291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 330 FAY-QDNAFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKLFSAVFTDVWL 408
Cdd:TIGR00957 1292 LRYrEDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVL 1371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 409 FDQLLGPEGKPANPQLVEKWLAQLKMAHKLELSNGRIVNL---------KLSKGQKKRVALLLALAEERDIILLDEWAAD 479
Cdd:TIGR00957 1372 FSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLdhecaeggeNLSVGQRQLVCLARALLRKTKILVLDEATAA 1451
|
..
gi 16130148 480 QD 481
Cdd:TIGR00957 1452 VD 1453
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
342-547 |
1.05e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 57.75 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQ------------PEDYRKlfSAVFTDV--- 406
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALStaqrlarglvylPEDRQS--SGLYLDApla 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 407 WLFDQLL-GPEGKPANPQLVEKWLAQLKMAHKLELSNGRIVNLKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFR 485
Cdd:PRK15439 360 WNVCALThNRRGFWIKPARENAVLERYRRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSAR 439
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130148 486 REFYQVLLPLMQEMGKTIFaISHDDHYFIH-ADRLLEMRNGQLS-ELTGEerdAASRDAVARTA 547
Cdd:PRK15439 440 NDIYQLIRSIAAQNVAVLF-ISSDLEEIEQmADRVLVMHQGEISgALTGA---AINVDTIMRLA 499
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
323-508 |
1.29e-08 |
|
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: 57.50 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAfSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGL--YQPQSGEIL----------------LDG 384
Cdd:TIGR03269 1 IEVKNLTKKFDGKE-VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpsKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 385 K--PVSGE--QPED---------YRKLFS-----------AVFTDVWLFDQLL------GPEGKPANPQLVEkWLAQLKM 434
Cdd:TIGR03269 80 EpcPVCGGtlEPEEvdfwnlsdkLRRRIRkriaimlqrtfALYGDDTVLDNVLealeeiGYEGKEAVGRAVD-LIEMVQL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16130148 435 AHklelsngRIVNL--KLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISH 508
Cdd:TIGR03269 159 SH-------RITHIarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSH 227
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
342-475 |
1.37e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 56.63 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGK-PVsgEQPEDYRKLFSAVF---TDVWlFD------- 410
Cdd:COG4586 41 ISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYvPF--KRRKEFARRIGVVFgqrSQLW-WDlpaidsf 117
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130148 411 QLLG-----PEgkpanpQLVEKWLAQLkmAHKLELsnGRIVNL---KLSKGQKKRVALLLALAEERDIILLDE 475
Cdd:COG4586 118 RLLKaiyriPD------AEYKKRLDEL--VELLDL--GELLDTpvrQLSLGQRMRCELAAALLHRPKILFLDE 180
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
342-475 |
1.44e-08 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 54.81 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKLFSA-----------VFTDVWLFD 410
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLghapgikttlsVLENLRFWH 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130148 411 QLLGPEGkpanpqlVEKWLAQLKMAhKLElsnGRIVNlKLSKGQKKRVALLLALAEERDIILLDE 475
Cdd:cd03231 99 ADHSDEQ-------VEEALARVGLN-GFE---DRPVA-QLSAGQQRRVALARLLLSGRPLWILDE 151
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
323-475 |
1.76e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 56.86 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYqDNAFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYqPQ---SGEILLDGKPVSGEQPEDY-RKL 398
Cdd:PRK13549 6 LEMKNITKTF-GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNIRDTeRAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 399 FSAVFTDVWLFDQL-------LGPEGKP-------ANPQLVEKWLAQLKMAHKLELsngRIVNLKLskGQKKRVALLLAL 464
Cdd:PRK13549 84 IAIIHQELALVKELsvlenifLGNEITPggimdydAMYLRAQKLLAQLKLDINPAT---PVGNLGL--GQQQLVEIAKAL 158
|
170
....*....|.
gi 16130148 465 AEERDIILLDE 475
Cdd:PRK13549 159 NKQARLLILDE 169
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
316-511 |
2.34e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 56.64 E-value: 2.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 316 AFPNWQTLELRNVtfayqDNAFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQsGEILLDGKPVSG---EQP 392
Cdd:PRK15134 284 AFPIRKGILKRTV-----DHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQ-GEIWFDGQPLHNlnrRQL 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 393 EDYRKLFSAVFTDvwlfdqllgPEGKpANPQL-VEKWLAQLKMAHKLELSNG----RIVNL----------------KLS 451
Cdd:PRK15134 358 LPVRHRIQVVFQD---------PNSS-LNPRLnVLQIIEEGLRVHQPTLSAAqreqQVIAVmeevgldpetrhrypaEFS 427
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 452 KGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDH 511
Cdd:PRK15134 428 GGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLH 487
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
342-475 |
2.38e-08 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 54.58 E-value: 2.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQ---SGEILLDGKPVSgeqPEDYRKLFSAVFTDVWLFD-------- 410
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRK---PDQFQKCVAYVRQDDILLPgltvretl 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130148 411 ----QLLGPEGKPaNPQLVEKWlAQLKMAHkleLSNGRIVNLK---LSKGQKKRVALLLALAEERDIILLDE 475
Cdd:cd03234 103 tytaILRLPRKSS-DAIRKKRV-EDVLLRD---LALTRIGGNLvkgISGGERRRVSIAVQLLWDPKVLILDE 169
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
342-475 |
3.55e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 53.72 E-value: 3.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGK----PVSGEQ-----PEDYRKLFSAVFTDVWLFDQL 412
Cdd:PRK13539 21 LSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGdiddPDVAEAchylgHRNAMKPALTVAENLEFWAAF 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130148 413 LGpegkpANPQLVEKWLAQLKMAHKLELSNGrivnlKLSKGQKKRVALLLALAEERDIILLDE 475
Cdd:PRK13539 101 LG-----GEELDIAAALEAVGLAPLAHLPFG-----YLSAGQKRRVALARLLVSNRPIWILDE 153
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
342-536 |
3.73e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 56.33 E-value: 3.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILldgkpvsGEQ-----PEDYRKLFSAVFTDVWLFDqllgpE 416
Cdd:PTZ00243 679 VSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-------AERsiayvPQQAWIMNATVRGNILFFD-----E 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 417 GKPANPQLV------EKWLAQLKMAHKLELSNgRIVNlkLSKGQKKRVALLLALAEERDIILLDEWAADQDPHF-RREFY 489
Cdd:PTZ00243 747 EDAARLADAvrvsqlEADLAQLGGGLETEIGE-KGVN--LSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVgERVVE 823
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16130148 490 QVLLPLMQemGKTIFAISHDDHYFIHADRLLEMRNGQLsELTGEERD 536
Cdd:PTZ00243 824 ECFLGALA--GKTRVLATHQVHVVPRADYVVALGDGRV-EFSGSSAD 867
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
342-540 |
3.82e-08 |
|
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: 54.86 E-value: 3.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGK-----PVSGEQPEDYRK-LFSAVFTDVWLFDQLLgp 415
Cdd:cd03291 56 INLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRisfssQFSWIMPGTIKEnIIFGVSYDEYRYKSVV-- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 416 egkpANPQLVEKwLAQLKMAHKLELSNGRIVnlkLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRRE-FYQVLLP 494
Cdd:cd03291 134 ----KACQLEED-ITKFPEKDNTVLGEGGIT---LSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEiFESCVCK 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16130148 495 LMQEmgKTIFAISHDDHYFIHADRLLEMRNGQ------LSELTGEERDAASR 540
Cdd:cd03291 206 LMAN--KTRILVTSKMEHLKKADKILILHEGSsyfygtFSELQSLRPDFSSK 255
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
323-522 |
4.18e-08 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 52.93 E-value: 4.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEIlldgkpvsgEQPEDYRKLF--- 399
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---------GMPEGEDLLFlpq 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 400 SAVFTDVWLFDQLLGPEGKpanpqlvekwlaqlkmahklelsngrivnlKLSKGQKKRVALLLALAEERDIILLDEWAAD 479
Cdd:cd03223 72 RPYLPLGTLREQLIYPWDD------------------------------VLSGGEQQRLAFARLLLHKPKFVFLDEATSA 121
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 16130148 480 QDPHFRREFYQVLlplmQEMGKTIFAISHDDHYFIHADRLLEM 522
Cdd:cd03223 122 LDEESEDRLYQLL----KELGITVISVGHRPSLWKFHDRVLDL 160
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
349-509 |
4.54e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 56.02 E-value: 4.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 349 GELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPV---SGEQPEDYRKLFSAVFTDVW--------LFDQLLGP-- 415
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlSPGKLQALRRDIQFIFQDPYasldprqtVGDSIMEPlr 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 416 -----EGKPANPQLVekWLAQ---LKMAHKLELSNgrivnlKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRRE 487
Cdd:PRK10261 430 vhgllPGKAAAARVA--WLLErvgLLPEHAWRYPH------EFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQ 501
|
170 180
....*....|....*....|..
gi 16130148 488 FYQVLLPLMQEMGKTIFAISHD 509
Cdd:PRK10261 502 IINLLLDLQRDFGIAYLFISHD 523
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
323-398 |
4.84e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 54.26 E-value: 4.84e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130148 323 LELRNVTFAYQDNAFSVGpINLTIKRGELLFLIGGNGSGKSTLAMLLTG--LYQPQSGEILLDGKPVSGEQPEDYRKL 398
Cdd:CHL00131 8 LEIKNLHASVNENEILKG-LNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEERAHL 84
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
323-526 |
5.58e-08 |
|
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: 55.22 E-value: 5.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYqDNAFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYqPQ---SGEILLDGKPVSGEQPEDY-RKL 398
Cdd:TIGR02633 2 LEMKGIVKTF-GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHgtwDGEIYWSGSPLKASNIRDTeRAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 399 FS------------AVFTDVWLFDQLLGPEGKPANPQLV---EKWLAQLKMAhklELSNGRIVNlKLSKGQKKRVALLLA 463
Cdd:TIGR02633 80 IViihqeltlvpelSVAENIFLGNEITLPGGRMAYNAMYlraKNLLRELQLD---ADNVTRPVG-DYGGGQQQLVEIAKA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130148 464 LAEERDIILLDEWAADqdphFRREFYQVLLPLMQEM---GKTIFAISHD-DHYFIHADRLLEMRNGQ 526
Cdd:TIGR02633 156 LNKQARLLILDEPSSS----LTEKETEILLDIIRDLkahGVACVYISHKlNEVKAVCDTICVIRDGQ 218
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
342-540 |
7.31e-08 |
|
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: 55.69 E-value: 7.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGK-----PVSGEQPEDYRK--LFSAVFtDVWLFDQLLg 414
Cdd:TIGR01271 445 ISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRisfspQTSWIMPGTIKDniIFGLSY-DEYRYTSVI- 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 415 pegkpaNPQLVEKWLAQLKMAHKLELSNGRIVnlkLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRRE-FYQVLL 493
Cdd:TIGR01271 523 ------KACQLEEDIALFPEKDKTVLGEGGIT---LSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEiFESCLC 593
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16130148 494 PLMqeMGKTIFAISHDDHYFIHADRLLEMRN------GQLSELTGEERDAASR 540
Cdd:TIGR01271 594 KLM--SNKTRILVTSKLEHLKKADKILLLHEgvcyfyGTFSELQAKRPDFSSL 644
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
331-482 |
8.83e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 52.93 E-value: 8.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 331 AYQDNAFSV-GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQpedyRKLFSAVFTDVwlf 409
Cdd:PRK13543 18 AFSRNEEPVfGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD----RSRFMAYLGHL--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 410 dqllgPEGKPAnpqlvekwLAQLKMAHKLELSNGR-----------IVNL---------KLSKGQKKRVALLLALAEERD 469
Cdd:PRK13543 91 -----PGLKAD--------LSTLENLHFLCGLHGRrakqmpgsalaIVGLagyedtlvrQLSAGQKKRLALARLWLSPAP 157
|
170
....*....|...
gi 16130148 470 IILLDEWAADQDP 482
Cdd:PRK13543 158 LWLLDEPYANLDL 170
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
323-475 |
1.02e-07 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 53.12 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDN-AFSvgPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLY--QPQ---SGEILLDGKPVSGEQ--PED 394
Cdd:COG1117 12 IEVRNLNVYYGDKqALK--DINLDIPENKVTALIGPSGCGKSTLLRCLNRMNdlIPGarvEGEILLDGEDIYDPDvdVVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 395 YRKLFSAVFtdvwlfdQllgpegKPaNP-------------------------QLVEKwlaQLKMA-------HKLElSN 442
Cdd:COG1117 90 LRRRVGMVF-------Q------KP-NPfpksiydnvayglrlhgikskseldEIVEE---SLRKAalwdevkDRLK-KS 151
|
170 180 190
....*....|....*....|....*....|...
gi 16130148 443 GrivnLKLSKGQKKRVALLLALAEERDIILLDE 475
Cdd:COG1117 152 A----LGLSGGQQQRLCIARALAVEPEVLLMDE 180
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
322-537 |
1.08e-07 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 54.43 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 322 TLELRNVTFAYQDNAFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLdgkpvsgeqPEDYRKLF-- 399
Cdd:COG4178 362 ALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR---------PAGARVLFlp 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 400 -SAVFTDVWLFDQLLGPEGKPA-NPQLVEKWLAQLKMAH---KLELSN--GRIvnlkLSKGQKKRVALLLALAEERDIIL 472
Cdd:COG4178 433 qRPYLPLGTLREALLYPATAEAfSDAELREALEAVGLGHlaeRLDEEAdwDQV----LSLGEQQRLAFARLLLHKPDWLF 508
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130148 473 LDEWAADQDPHFRREFYQVLLPLMQEMgkTIFAISHDDHYFIHADRLLEMRNGQLSELTGEERDA 537
Cdd:COG4178 509 LDEATSALDEENEAALYQLLREELPGT--TVISVGHRSTLAAFHDRVLELTGDGSWQLLPAEAPA 571
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
15-253 |
1.58e-07 |
|
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: 52.94 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 15 FISVMALSLASAALGIgLIAFINQRLIE----TADTSLLVLPE--FLGLLLLLMAVTLGSQLALTTLGHHFVYRLRSEFI 88
Cdd:cd07346 1 LLLALLLLLLATALGL-ALPLLTKLLIDdvipAGDLSLLLWIAllLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 89 KRILDTHVERIEQLGSASLLAGLTSDVRNITIAFVR-LPELVQGIILTIGSAAYLWMLSGKMLLVTAIWMAITIWGGFVL 167
Cdd:cd07346 80 RHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSgLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 168 VARVYKHMATLRETEDKLYTDFQTVLEGRKEL-TLNRERAEY-VFNNLyipdAQEYRHHIIRADTfhLSAVNWSNIMMLG 245
Cdd:cd07346 160 RRRIRKASREVRESLAELSAFLQESLSGIRVVkAFAAEEREIeRFREA----NRDLRDANLRAAR--LSALFSPLIGLLT 233
|
250
....*....|
gi 16130148 246 AIG--LVFWM 253
Cdd:cd07346 234 ALGtaLVLLY 243
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
323-543 |
1.85e-07 |
|
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: 52.60 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAFSV-GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKLFSA 401
Cdd:cd03288 20 IKIHDLCVRYENNLKPVlKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 402 VFTDVWLFDQL----LGPEGKPANPQLVEKW-LAQLK-MAHKLELSNGRIVN---LKLSKGQKKRVALLLALAEERDIIL 472
Cdd:cd03288 100 ILQDPILFSGSirfnLDPECKCTDDRLWEALeIAQLKnMVKSLPGGLDAVVTeggENFSVGQRQLFCLARAFVRKSSILI 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130148 473 LDEWAADQDPHFRREFYQVLLPLMQEmgKTIFAISHDDHYFIHADRLLEMRNGQLSELTGEERDAASRDAV 543
Cdd:cd03288 180 MDEATASIDMATENILQKVVMTAFAD--RTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGV 248
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
290-493 |
2.99e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.09 E-value: 2.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 290 LTAQVAFN-KLNKFALaPFKAEFPRPQAFPNWQTL-ELRNVTFAYQDNafsvgPI----NLTIKRGELLFLIGGNGSGKS 363
Cdd:PRK10938 227 LVAQLAHSeQLEGVQL-PEPDEPSARHALPANEPRiVLNNGVVSYNDR-----PIlhnlSWQVNPGEHWQIVGPNGAGKS 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 364 TLAMLLTGLYqPQ--------------SGEILLDGKP----VSGEQPEDYR-------KLFSAVFTDVWLFDQLlgpegK 418
Cdd:PRK10938 301 TLLSLITGDH-PQgysndltlfgrrrgSGETIWDIKKhigyVSSSLHLDYRvstsvrnVILSGFFDSIGIYQAV-----S 374
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130148 419 PANPQLVEKWLAQLKMAHKLELSNGRivnlKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFR---REFYQVLL 493
Cdd:PRK10938 375 DRQQKLAQQWLDILGIDKRTADAPFH----SLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRqlvRRFVDVLI 448
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
342-526 |
3.45e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 52.57 E-value: 3.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKP-VSGEQ----PEDYRKLfSAVFTDVWLFdqllgPE 416
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVlFDAEKgiclPPEKRRI-GYVFQDARLF-----PH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 417 GKpanpqlVEKWLaQLKMAHKLELSNGRIVNL------------KLSKGQKKRVALLLALAEERDIILLDEWAADQDPHF 484
Cdd:PRK11144 91 YK------VRGNL-RYGMAKSMVAQFDKIVALlgieplldrypgSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPR 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16130148 485 RREfyqvLLPLMQEMGKT----IFAISHDDHYFIH-ADRLLEMRNGQ 526
Cdd:PRK11144 164 KRE----LLPYLERLAREinipILYVSHSLDEILRlADRVVVLEQGK 206
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
348-525 |
4.46e-07 |
|
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: 49.68 E-value: 4.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 348 RGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLdgkpVSGEQPEDYrklfsavftdvwlfdqllgpegkpanpqlvek 427
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY----IDGEDILEE-------------------------------- 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 428 wlaqlkmaHKLELSNGRIVNLKLSKGQKKRVALLLALAEER--DIILLDEWAADQDPHFRR-----EFYQVLLPLMQEMG 500
Cdd:smart00382 45 --------VLDQLLLIIVGGKKASGSGELRLRLALALARKLkpDVLILDEITSLLDAEQEAlllllEELRLLLLLKSEKN 116
|
170 180 190
....*....|....*....|....*....|.
gi 16130148 501 KTIFAISHDDHYFIHA------DRLLEMRNG 525
Cdd:smart00382 117 LTVILTTNDEKDLGPAllrrrfDRRIVLLLI 147
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
342-387 |
5.19e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.42 E-value: 5.19e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 16130148 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPV 387
Cdd:PRK10982 17 VNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI 62
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
344-475 |
5.73e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 52.31 E-value: 5.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 344 LTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKL-FSAVFTDVWLFDQL-------LGP 415
Cdd:PRK10762 25 LNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAgIGIIHQELNLIPQLtiaenifLGR 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 416 EgkPANP----------QLVEKWLAQLKMAHklelSNGRIVNlKLSKGQKKRVALLLALAEERDIILLDE 475
Cdd:PRK10762 105 E--FVNRfgridwkkmyAEADKLLARLNLRF----SSDKLVG-ELSIGEQQMVEIAKVLSFESKVIIMDE 167
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
323-387 |
6.81e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 51.71 E-value: 6.81e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130148 323 LELRNVT--F----AYQDnafsvgpINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYqPQ---SGEILLDGKPV 387
Cdd:NF040905 2 LEMRGITktFpgvkALDD-------VNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGEVC 67
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
306-382 |
6.87e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 52.09 E-value: 6.87e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130148 306 PFKAEFPRPQAFPNwQTLELRNVTFAYQDNAFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILL 382
Cdd:PRK10636 297 PFHFSFRAPESLPN-PLLKMEKVSAGYGDRII-LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL 371
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
62-544 |
7.43e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 52.29 E-value: 7.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 62 MAVTLGSQLALTTLGHHFVYRLRSEFIKRILDTHVERIEQLGSASLLAGLTSDVRNITIAFVRLPELVQGIiltigsaay 141
Cdd:PLN03232 964 VAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQ--------- 1034
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 142 LWMLSGKMLLVTAIwMAITIWGGFVLVARVYK----HMATLRE-------TEDKLYTDFQTVLEGrkeltLNRERAEYVF 210
Cdd:PLN03232 1035 LWQLLSTFALIGTV-STISLWAIMPLLILFYAaylyYQSTSREvrrldsvTRSPIYAQFGEALNG-----LSSIRAYKAY 1108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 211 NNLYIPDAQeYRHHIIRADTFHLSAVNWSNIMMLGAIGLVFWMANS---LGWADTNVAATYSLTLLFLR------TPLLS 281
Cdd:PLN03232 1109 DRMAKINGK-SMDNNIRFTLANTSSNRWLTIRLETLGGVMIWLTATfavLRNGNAENQAGFASTMGLLLsytlniTTLLS 1187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 282 AVgalptLLTAQVAFNKLNKF----------ALAPFKAEFPRP-QAFPNWQTLELRNVTFAYQDN--------AFSVGPi 342
Cdd:PLN03232 1188 GV-----LRQASKAENSLNSVervgnyidlpSEATAIIENNRPvSGWPSRGSIKFEDVHLRYRPGlppvlhglSFFVSP- 1261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 343 nltikrGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKLFSAVFTDVWLFDQL----LGPEGK 418
Cdd:PLN03232 1262 ------SEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTvrfnIDPFSE 1335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 419 PANPQLvekWLAqLKMAHKLELSNGRIVNL---------KLSKGQKKRVALLLALAEERDIILLDEWAADQDPH------ 483
Cdd:PLN03232 1336 HNDADL---WEA-LERAHIKDVIDRNPFGLdaevseggeNFSVGQRQLLSLARALLRRSKILVLDEATASVDVRtdsliq 1411
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130148 484 --FRREFYQVllplmqemgkTIFAISHDDHYFIHADRLLEMRNGQLSELTGEErDAASRDAVA 544
Cdd:PLN03232 1412 rtIREEFKSC----------TMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQ-ELLSRDTSA 1463
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
338-530 |
7.79e-07 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 51.25 E-value: 7.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDY---RKLFSAVFTDvwlfdqllg 414
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravRSDIQMIFQD--------- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 415 pegkP---ANPQL-VEKWLAQLKMAHKLELSN--------------GRIVNL------KLSKGQKKRVALLLALAEERDI 470
Cdd:PRK15079 107 ----PlasLNPRMtIGEIIAEPLRTYHPKLSRqevkdrvkammlkvGLLPNLinryphEFSGGQCQRIGIARALILEPKL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130148 471 ILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDHYFIH-ADRLLEMRNGQLSEL 530
Cdd:PRK15079 183 IICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVEL 243
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
342-527 |
1.13e-06 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 49.88 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKLFSAVFtdvwlfdqllgPEGKPAN 421
Cdd:PRK11614 24 VSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVAIV-----------PEGRRVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 422 PQL-VEKWLAQLKMAHKLELSNGRIVNL----------------KLSKGQKKRVALLLALAEERDIILLDEWAADQDPHF 484
Cdd:PRK11614 93 SRMtVEENLAMGGFFAERDQFQERIKWVyelfprlherriqragTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPII 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 16130148 485 RREFYQVLLPLMQEmGKTIFAISHDDHYFIH-ADRLLEMRNGQL 527
Cdd:PRK11614 173 IQQIFDTIEQLREQ-GMTIFLVEQNANQALKlADRGYVLENGHV 215
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
377-524 |
1.29e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.57 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 377 SGEILLDGKPVSGEQPEDYRKLFSAVFTDVWLFDQLLGPEGKPANPQLVekwLAQLKMAHKL--------ELSNGRIVNL 448
Cdd:PTZ00265 1276 SGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDAT---REDVKRACKFaaidefieSLPNKYDTNV 1352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 449 -----KLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDHYFIHADRLLEMR 523
Cdd:PTZ00265 1353 gpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFN 1432
|
.
gi 16130148 524 N 524
Cdd:PTZ00265 1433 N 1433
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
346-519 |
1.47e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 48.72 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 346 IKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSgeqpedyrklfsavftdvwlfdqllgpegkpANPQLV 425
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPV-------------------------------YKPQYI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 426 ekwlaqlkmahklelsngrivnlKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFA 505
Cdd:cd03222 71 -----------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALV 127
|
170
....*....|....
gi 16130148 506 ISHDdhyFIHADRL 519
Cdd:cd03222 128 VEHD---LAVLDYL 138
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
323-482 |
1.88e-06 |
|
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: 49.47 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAFSV-GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQsGEILLDGKPVSGEQPEDYRKLFSA 401
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVlENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 402 VFTDVWLFD----QLLGPEGKPANPQL------------VEKWLAQLKmahkLELSNGRIVnlkLSKGQKKRVALLLALA 465
Cdd:cd03289 82 IPQKVFIFSgtfrKNLDPYGKWSDEEIwkvaeevglksvIEQFPGQLD----FVLVDGGCV---LSHGHKQLMCLARSVL 154
|
170
....*....|....*..
gi 16130148 466 EERDIILLDEWAADQDP 482
Cdd:cd03289 155 SKAKILLLDEPSAHLDP 171
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
324-547 |
2.60e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 50.17 E-value: 2.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 324 ELRNVTfaYQDNAfSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKLFSAVF 403
Cdd:PRK09700 267 EVRNVT--SRDRK-KVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMAYI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 404 T----DVWLFDQLLGPEGKPANPQL-VEKW-----LAQLKMAHKLELSNGRIVNLK----------LSKGQKKRVALLLA 463
Cdd:PRK09700 344 TesrrDNGFFPNFSIAQNMAISRSLkDGGYkgamgLFHEVDEQRTAENQRELLALKchsvnqniteLSGGNQQKVLISKW 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 464 LAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEmGKTIFAISHDDHYFIHA-DRLLEMRNGQLSELTgEERDAASRDA 542
Cdd:PRK09700 424 LCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVcDRIAVFCEGRLTQIL-TNRDDMSEEE 501
|
....*
gi 16130148 543 VARTA 547
Cdd:PRK09700 502 IMAWA 506
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
337-508 |
3.18e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 49.89 E-value: 3.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 337 FSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPvsgeqpedyrklfSAVFTDVWLFDQLLGPE 416
Cdd:PRK13545 38 YALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSA-------------ALIAISSGLNGQLTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 417 G---------------KPANPQLVEkwLAQLkmahklelsnGRIVNLKL---SKGQKKRVALLLALAEERDIILLDEWAA 478
Cdd:PRK13545 105 NielkglmmgltkekiKEIIPEIIE--FADI----------GKFIYQPVktySSGMKSRLGFAISVHINPDILVIDEALS 172
|
170 180 190
....*....|....*....|....*....|...
gi 16130148 479 DQDPHFRREfyqvLLPLM---QEMGKTIFAISH 508
Cdd:PRK13545 173 VGDQTFTKK----CLDKMnefKEQGKTIFFISH 201
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
323-508 |
4.54e-06 |
|
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: 50.01 E-value: 4.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAF-SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPV-----SGEQPEDYR 396
Cdd:TIGR01257 1938 LRLNELTKVYSGTSSpAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIltnisDVHQNMGYC 2017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 397 KLFSAV------FTDVWLFDQLlgpEGKPANP-QLVEKWLAQlkmAHKLELSNGRIVNlKLSKGQKKRVALLLALAEERD 469
Cdd:TIGR01257 2018 PQFDAIddlltgREHLYLYARL---RGVPAEEiEKVANWSIQ---SLGLSLYADRLAG-TYSGGNKRKLSTAIALIGCPP 2090
|
170 180 190
....*....|....*....|....*....|....*....
gi 16130148 470 IILLDEWAADQDPHFRREFYQVLLPLMQEmGKTIFAISH 508
Cdd:TIGR01257 2091 LVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSH 2128
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
323-508 |
6.75e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 47.91 E-value: 6.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAFSVGpINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQ-----SGEILLDGKPVSGEQ--PEDY 395
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKG-VDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDvdPIEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 396 RKLFSAVFTDVWLFDQL-------LG------PEGKPANPQLVEkWlaQLKMAHKLELSNGRIVNL--KLSKGQKKRVAL 460
Cdd:PRK14267 84 RREVGMVFQYPNPFPHLtiydnvaIGvklnglVKSKKELDERVE-W--ALKKAALWDEVKDRLNDYpsNLSGGQRQRLVI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16130148 461 LLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMgkTIFAISH 508
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTH 206
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
342-387 |
9.95e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 48.58 E-value: 9.95e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 16130148 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPV 387
Cdd:NF033858 285 VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV 330
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
324-380 |
1.03e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.41 E-value: 1.03e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130148 324 ELRNVTFAYQD----NAFSVgpinlTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEI 380
Cdd:PRK11147 321 EMENVNYQIDGkqlvKDFSA-----QVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI 376
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
346-540 |
1.06e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 48.62 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 346 IKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKLFSAVFTDVWLFD----QLLGP--EGKP 419
Cdd:PTZ00243 1333 IAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDgtvrQNVDPflEASS 1412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 420 AnpqlvEKWLA------QLKMAHKLELSNGRIVN--LKLSKGQKKRVALLLALAEE-RDIILLDEWAADQDPHFRRefyQ 490
Cdd:PTZ00243 1413 A-----EVWAAlelvglRERVASESEGIDSRVLEggSNYSVGQRQLMCMARALLKKgSGFILMDEATANIDPALDR---Q 1484
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16130148 491 VLLPLMQEMGK-TIFAISHDDHYFIHADRLLEMRNGQLSELtGEERDAASR 540
Cdd:PTZ00243 1485 IQATVMSAFSAyTVITIAHRLHTVAQYDKIIVMDHGAVAEM-GSPRELVMN 1534
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
311-394 |
1.35e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 47.62 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 311 FPRPQAFPNWQTLELRNVTFAYQDNAF--SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQS-GEILLDGKPV 387
Cdd:PRK13549 248 YPREPHTIGEVILEVRNLTAWDPVNPHikRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFIDGKPV 327
|
....*..
gi 16130148 388 SGEQPED 394
Cdd:PRK13549 328 KIRNPQQ 334
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
323-529 |
1.48e-05 |
|
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: 47.76 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAFS---VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQ----SGEILLDGKPVSGEQPEDY 395
Cdd:COG4172 7 LSVEDLSVAFGQGGGTveaVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPaahpSGSILFDGQDLLGLSEREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 396 RKL----FSAVFTDvwlfdqllgpegkPA---NP-QLVEKWLAQLKMAHKlELS----NGRIVNL--------------- 448
Cdd:COG4172 87 RRIrgnrIAMIFQE-------------PMtslNPlHTIGKQIAEVLRLHR-GLSgaaaRARALELlervgipdperrlda 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 449 ---KLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHD----DHYfihADRLLE 521
Cdd:COG4172 153 yphQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDlgvvRRF---ADRVAV 229
|
....*...
gi 16130148 522 MRNGQLSE 529
Cdd:COG4172 230 MRQGEIVE 237
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
326-509 |
1.60e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 46.73 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 326 RNVTFayqdnaFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKpvsgeqpedyrklFSAVFTD 405
Cdd:PRK13546 33 KNKTF------FALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE-------------VSVIAIS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 406 VWLFDQLLGPEG---KPANPQLVEKWLAQLkMAHKLELSN-GRIVNL---KLSKGQKKRVALLLALAEERDIILLDEWAA 478
Cdd:PRK13546 94 AGLSGQLTGIENiefKMLCMGFKRKEIKAM-TPKIIEFSElGEFIYQpvkKYSSGMRAKLGFSINITVNPDILVIDEALS 172
|
170 180 190
....*....|....*....|....*....|....
gi 16130148 479 DQDphfrREFYQVLLPLMQEM---GKTIFAISHD 509
Cdd:PRK13546 173 VGD----QTFAQKCLDKIYEFkeqNKTIFFVSHN 202
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
307-511 |
1.79e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.55 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 307 FKAEFPRPQAFPNWQTLELRNVTFAYQDNAFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGkp 386
Cdd:PLN03073 493 YKFEFPTPDDRPGPPIISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSA-- 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 387 vsgeqpedyrKLFSAVFT-------DVWLFDQLLGPEGKPANP-QLVEKWLAQLKMAHKLELSNgrivNLKLSKGQKKRV 458
Cdd:PLN03073 571 ----------KVRMAVFSqhhvdglDLSSNPLLYMMRCFPGVPeQKLRAHLGSFGVTGNLALQP----MYTLSGGQKSRV 636
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16130148 459 ALLLALAEERDIILLDEWAADQDPHFRREFYQVLLpLMQemgKTIFAISHDDH 511
Cdd:PLN03073 637 AFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLV-LFQ---GGVLMVSHDEH 685
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
321-410 |
1.87e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 47.19 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 321 QTLELRNVTFAYQDNA-FSvgPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKLF 399
Cdd:PRK15064 318 NALEVENLTKGFDNGPlFK--NLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQDHAYDF 395
|
90
....*....|.
gi 16130148 400 SavfTDVWLFD 410
Cdd:PRK15064 396 E---NDLTLFD 403
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
323-509 |
2.37e-05 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 45.64 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPED---YRKLF 399
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 400 SAVFTDVWL------FDQLLGPE--GKPANPQLVEKWLAQLKMAHKLElsNGRIVNLKLSKGQKKRVALLLALAEERDII 471
Cdd:PRK10908 82 GMIFQDHHLlmdrtvYDNVAIPLiiAGASGDDIRRRVSAALDKVGLLD--KAKNFPIQLSGGEQQRVGIARAVVNKPAVL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 16130148 472 LLDEWAADQDphfrREFYQVLLPLMQE---MGKTIFAISHD 509
Cdd:PRK10908 160 LADEPTGNLD----DALSEGILRLFEEfnrVGVTVLMATHD 196
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
323-380 |
3.70e-05 |
|
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: 46.47 E-value: 3.70e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 16130148 323 LELRNVTFAYQDNAFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEI 380
Cdd:TIGR03719 323 IEAENLTKAFGDKLL-IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTI 379
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
328-509 |
3.83e-05 |
|
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: 45.44 E-value: 3.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 328 VTFAYQDNAFSVgpINLTIKR-GELLFLIGGNGSGKSTLAMLLTGLYQPQSGEIlldgkpvsgEQPEDYRKLFSAvFTDV 406
Cdd:cd03236 6 PVHRYGPNSFKL--HRLPVPReGQVLGLVGPNGIGKSTALKILAGKLKPNLGKF---------DDPPDWDEILDE-FRGS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 407 WL---FDQLLGPEGKPA-NPQLVE--------KWLAQLKMAHK----------LELSNGRIVNL-KLSKGQKKRVALLLA 463
Cdd:cd03236 74 ELqnyFTKLLEGDVKVIvKPQYVDlipkavkgKVGELLKKKDErgkldelvdqLELRHVLDRNIdQLSGGELQRVAIAAA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 16130148 464 LAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEmGKTIFAISHD 509
Cdd:cd03236 154 LARDADFYFFDEPSSYLDIKQRLNAARLIRELAED-DNYVLVVEHD 198
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
79-253 |
4.83e-05 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 45.47 E-value: 4.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 79 FVYRLRSEFIKRILDTHVERIEQLGSASLLAGLTSDVRNI---TIAFVRLpeLVQGIILTIGSAAYLWMLSGKMLLVTAI 155
Cdd:cd18548 70 FGRDLRKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVqnfVMMLLRM--LVRAPIMLIGAIIMAFRINPKLALILLV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 156 WMAITIWGGFVLVARVYKHMATLRETEDKLYTDFQTVLEG----RkelTLNRERAEYV-FNNlyipDAQEYRHHIIRAdt 230
Cdd:cd18548 148 AIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGirviR---AFNREDYEEErFDK----ANDDLTDTSLKA-- 218
|
170 180
....*....|....*....|....*.
gi 16130148 231 FHLSAVNwSNIMML---GAIGLVFWM 253
Cdd:cd18548 219 GRLMALL-NPLMMLimnLAIVAILWF 243
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
312-529 |
4.85e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 46.00 E-value: 4.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 312 PRPQAFPNWQTLELRNVTFAYQDNAFSVGPI---NLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVS 388
Cdd:PRK10261 2 PHSDELDARDVLAVENLNIAFMQEQQKIAAVrnlSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 389 --GEQPEDYRKLFSAVFTDVWLFD--QLLGPEGKPANP------QLVEKWLAQLKMAHKLELSNG-RIVNL--------- 448
Cdd:PRK10261 82 rrSRQVIELSEQSAAQMRHVRGADmaMIFQEPMTSLNPvftvgeQIAESIRLHQGASREEAMVEAkRMLDQvripeaqti 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 449 ------KLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDHYFIH-ADRLLE 521
Cdd:PRK10261 162 lsryphQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEiADRVLV 241
|
....*...
gi 16130148 522 MRNGQLSE 529
Cdd:PRK10261 242 MYQGEAVE 249
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
15-251 |
6.87e-05 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 45.09 E-value: 6.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 15 FISVMALSLASAALGIgLIAFINQRLIETADTSLLVLPEFLGLLLLLMAVTLG------------SQLALTTLGHHFVYR 82
Cdd:cd18547 1 LILVIILAIISTLLSV-LGPYLLGKAIDLIIEGLGGGGGVDFSGLLRILLLLLglyllsalfsylQNRLMARVSQRTVYD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 83 LRSEFIKRI-------LDTHverieQLGSasLLAGLTSDVRNITIAFVR-LPELVQGIILTIGSAAYLWMLSGKMLLVTA 154
Cdd:cd18547 80 LRKDLFEKLqrlplsyFDTH-----SHGD--IMSRVTNDVDNISQALSQsLTQLISSILTIVGTLIMMLYISPLLTLIVL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 155 IWMAITIWGGFVLVARVYKHMATLRETEDKLYTDFQTVLEGRKELTL-NRE-RAEYVFNNLyipdAQEYRHHIIRADTFh 232
Cdd:cd18547 153 VTVPLSLLVTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAfNREeEAIEEFDEI----NEELYKASFKAQFY- 227
|
250 260
....*....|....*....|....
gi 16130148 233 lsavnwSNIMM-----LGAIGLVF 251
Cdd:cd18547 228 ------SGLLMpimnfINNLGYVL 245
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
354-514 |
7.99e-05 |
|
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: 45.31 E-value: 7.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 354 LIGGNGSGKSTLAMLLTGLYQPQSGEIL---------------LD-GKPVSGEQPEDYRKLFSAV--FTDVWL------- 408
Cdd:TIGR03719 36 VLGLNGAGKSTLLRIMAGVDKDFNGEARpqpgikvgylpqepqLDpTKTVRENVEEGVAEIKDALdrFNEISAkyaepda 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 409 -FDQLLGPEGKpanpqLVEKWLA--------QLKMA-HKLELSNGRIVNLKLSKGQKKRVALLLALAEERDIILLDEwaa 478
Cdd:TIGR03719 116 dFDKLAAEQAE-----LQEIIDAadawdldsQLEIAmDALRCPPWDADVTKLSGGERRRVALCRLLLSKPDMLLLDE--- 187
|
170 180 190
....*....|....*....|....*....|....*...
gi 16130148 479 dqdP--HFRREFYQVLLPLMQEMGKTIFAISHdDHYFI 514
Cdd:TIGR03719 188 ---PtnHLDAESVAWLERHLQEYPGTVVAVTH-DRYFL 221
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
226-529 |
1.03e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 45.50 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 226 IRADTFHLSAVNWSNIMMLGAIGLVFWMANSL-----GWADTNVAATYSLTLLFLR----TPLLSAVGALPTLltAQVAF 296
Cdd:PLN03130 1126 IRFTLVNMSSNRWLAIRLETLGGLMIWLTASFavmqnGRAENQAAFASTMGLLLSYalniTSLLTAVLRLASL--AENSL 1203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 297 NKLNKF-------ALAPFKAEFPRPQ-AFPNWQTLELRNVTFAYQDNAFSV-GPINLTIKRGELLFLIGGNGSGKSTLAM 367
Cdd:PLN03130 1204 NAVERVgtyidlpSEAPLVIENNRPPpGWPSSGSIKFEDVVLRYRPELPPVlHGLSFEISPSEKVGIVGRTGAGKSSMLN 1283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 368 LLTGLYQPQSGEILLDGKPVSGEQPEDYRKLFSAV------FTDVWLFDqlLGPEGKPANPQLVEkwlaQLKMAH----- 436
Cdd:PLN03130 1284 ALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIpqapvlFSGTVRFN--LDPFNEHNDADLWE----SLERAHlkdvi 1357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 437 -------KLELSNGrivNLKLSKGQKKRVALLLALAEERDIILLDEWAADQD--------PHFRREFYQVllplmqemgk 501
Cdd:PLN03130 1358 rrnslglDAEVSEA---GENFSVGQRQLLSLARALLRRSKILVLDEATAAVDvrtdaliqKTIREEFKSC---------- 1424
|
330 340
....*....|....*....|....*...
gi 16130148 502 TIFAISHDDHYFIHADRLLEMRNGQLSE 529
Cdd:PLN03130 1425 TMLIIAHRLNTIIDCDRILVLDAGRVVE 1452
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
317-482 |
1.38e-04 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 44.90 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 317 FPNWQTLELRNVTFAYQDNAFSV-GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQsGEILLDGKPVSGEQPEDY 395
Cdd:TIGR01271 1212 WPSGGQMDVQGLTAKYTEAGRAVlQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTW 1290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 396 RKLFSAVFTDVWL----FDQLLGPEGKPANPQL--------VEKWLAQLKMAHKLELSNGRIVnlkLSKGQKKRVALLLA 463
Cdd:TIGR01271 1291 RKAFGVIPQKVFIfsgtFRKNLDPYEQWSDEEIwkvaeevgLKSVIEQFPDKLDFVLVDGGYV---LSNGHKQLMCLARS 1367
|
170
....*....|....*....
gi 16130148 464 LAEERDIILLDEWAADQDP 482
Cdd:TIGR01271 1368 ILSKAKILLLDEPSAHLDP 1386
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
322-498 |
2.69e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.46 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 322 TLELRNVTFAYQDNAFSVGPiNLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKLFSA 401
Cdd:PRK10938 3 SLQISQGTFRLSDTKTLQLP-SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 402 VF----TDvwlfdqLLGPE----GKPA---------NPQLVEKWLAQLKMAHkleLSNGRIVnlKLSKGQKKRVALLLAL 464
Cdd:PRK10938 82 EWqrnnTD------MLSPGeddtGRTTaeiiqdevkDPARCEQLAQQFGITA---LLDRRFK--YLSTGETRKTLLCQAL 150
|
170 180 190
....*....|....*....|....*....|....
gi 16130148 465 AEERDIILLDEWAADQDPHFRREFYQVLLPLMQE 498
Cdd:PRK10938 151 MSEPDLLILDEPFDGLDVASRQQLAELLASLHQS 184
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
315-383 |
2.72e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 43.86 E-value: 2.72e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130148 315 QAFPNWQTLELRNVTFAY--QDNAFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLD 383
Cdd:PTZ00265 375 KKLKDIKKIQFKNVRFHYdtRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN 445
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
310-536 |
3.40e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 43.45 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 310 EFPRPQAFPNWQTLELRNVTFAYQDNafsvgpINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSG 389
Cdd:PRK10762 245 QYPRLDKAPGEVRLKVDNLSGPGVND------VSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVT 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 390 EQPED-------Y----RKlfsavftdvwlFDQL-LGPEGK-----PANPQLVEKWLAQLKMAHKLELSNG-RIVNLK-- 449
Cdd:PRK10762 319 RSPQDglangivYisedRK-----------RDGLvLGMSVKenmslTALRYFSRAGGSLKHADEQQAVSDFiRLFNIKtp 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 450 --------LSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEmGKTIFAISHDDHYFI-HADRLL 520
Cdd:PRK10762 388 smeqaiglLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLgMSDRIL 466
|
250
....*....|....*..
gi 16130148 521 EMRNGQLS-ELTGEERD 536
Cdd:PRK10762 467 VMHEGRISgEFTREQAT 483
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
323-539 |
3.41e-04 |
|
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: 43.27 E-value: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDNAF--SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQ-SGEILLDGKPVSGEQPEDYRKLF 399
Cdd:TIGR02633 258 LEARNLTCWDVINPHrkRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAQAIRAG 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 400 SAVFTDVWLFDQLLGPEGKPANPQL--VEKW--LAQLKMAHKLELSNGRIVNLK------------LSKGQKKRVALLLA 463
Cdd:TIGR02633 338 IAMVPEDRKRHGIVPILGVGKNITLsvLKSFcfKMRIDAAAELQIIGSAIQRLKvktaspflpigrLSGGNQQKAVLAKM 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 464 LAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEmGKTIFAISHDDHYFIH-ADRLLEMRNGQL------SELTGEERD 536
Cdd:TIGR02633 418 LLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGlSDRVLVIGEGKLkgdfvnHALTQEQVL 496
|
...
gi 16130148 537 AAS 539
Cdd:TIGR02633 497 AAA 499
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
63-279 |
3.97e-04 |
|
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: 42.24 E-value: 3.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 63 AVTLGSQLALTTLGHHFVYRLRSEFIKRILDTHVERIEQLGSASLLAGLTSDVRNI-TIAFVRLPELVQGIILTIGSAAY 141
Cdd:pfam00664 56 ILSFLQSYLLNHTGERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIrDGLGEKLGLLFQSLATIVGGIIV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 142 LWMLSGKMLLVTAIWMAITIWGGFVlvarVYKHMATLRETE----DKLYTDFQTVLEGRKEL-TLNRERAEYvfnnlyip 216
Cdd:pfam00664 136 MFYYGWKLTLVLLAVLPLYILVSAV----FAKILRKLSRKEqkavAKASSVAEESLSGIRTVkAFGREEYEL-------- 203
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130148 217 daQEYRHHIIRADTFHLSAVNWSNI-------MMLGAIGLVFWMANSL---GWADTNVAATYSLTLLFLRTPL 279
Cdd:pfam00664 204 --EKYDKALEEALKAGIKKAVANGLsfgitqfIGYLSYALALWFGAYLvisGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
342-526 |
4.49e-04 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 41.15 E-value: 4.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 342 INLTIKRGELLFLIGGNGSGKSTLamLLTGLYQpQSGEILLDGKPVSGEQPedyrklfsAVFtdvwlFDQLlgpegkpan 421
Cdd:cd03238 14 LDVSIPLNVLVVVTGVSGSGKSTL--VNEGLYA-SGKARLISFLPKFSRNK--------LIF-----IDQL--------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 422 PQLVEKWLAQLKMAHKLElsngrivnlKLSKGQKKRVALL--LALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEm 499
Cdd:cd03238 69 QFLIDVGLGYLTLGQKLS---------TLSGGELQRVKLAseLFSEPPGTLFILDEPSTGLHQQDINQLLEVIKGLIDL- 138
|
170 180
....*....|....*....|....*..
gi 16130148 500 GKTIFAISHDDHYFIHADRLLEMRNGQ 526
Cdd:cd03238 139 GNTVILIEHNLDVLSSADWIIDFGPGS 165
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
323-380 |
6.01e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.41 E-value: 6.01e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 16130148 323 LELRNVTFAYQDNAFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEI 380
Cdd:PRK11819 325 IEAENLSKSFGDRLL-IDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI 381
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
336-528 |
6.07e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 42.63 E-value: 6.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 336 AFSVGPI----NLTIKRGELLFLIGGNGSGKSTLAMLLtglyqpqSGEILLD-GK-------PVS--------------- 388
Cdd:PRK11147 12 SFSDAPLldnaELHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDdGRiiyeqdlIVArlqqdpprnvegtvy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 389 ----------GEQPEDYRKLFSAVFTDvwlfdqllgpegkpanPQlvEKWLAQL-KMAHKLELSNG-----RIV-NLK-- 449
Cdd:PRK11147 85 dfvaegieeqAEYLKRYHDISHLVETD----------------PS--EKNLNELaKLQEQLDHHNLwqlenRINeVLAql 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 450 ----------LSKGQKKRVALLLALAEERDIILLDEwaadqdP--HFRREFYQVLLPLMQEMGKTIFAISHdDHYFIH-- 515
Cdd:PRK11147 147 gldpdaalssLSGGWLRKAALGRALVSNPDVLLLDE------PtnHLDIETIEWLEGFLKTFQGSIIFISH-DRSFIRnm 219
|
250
....*....|...
gi 16130148 516 ADRLLEMRNGQLS 528
Cdd:PRK11147 220 ATRIVDLDRGKLV 232
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
15-253 |
7.40e-04 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 41.65 E-value: 7.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 15 FISVMALSLASAALGIG---LIAFINQRLIETADTSLLVLPeflglLLLLMAVTL-------GSQLALTTLGHHFVYRLR 84
Cdd:cd18542 1 YLLAILALLLATALNLLiplLIRRIIDSVIGGGLRELLWLL-----ALLILGVALlrgvfryLQGYLAEKASQKVAYDLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 85 SEFIKRIldthverieQLGSAS---------LLAGLTSDVRNI--TIAFVrLPELVQGIILTIGSAAYLWMLSGKMLLVT 153
Cdd:cd18542 76 NDLYDHL---------QRLSFSfhdkartgdLMSRCTSDVDTIrrFLAFG-LVELVRAVLLFIGALIIMFSINWKLTLIS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 154 AIWMAITIWGGFVLVARVYKHMATLRETEDKLYTDFQTVLEG-R--KelTLNRERAEYV-FNNLyipdAQEYRHHIIRAD 229
Cdd:cd18542 146 LAIIPFIALFSYVFFKKVRPAFEEIREQEGELNTVLQENLTGvRvvK--AFAREDYEIEkFDKE----NEEYRDLNIKLA 219
|
250 260
....*....|....*....|....*.
gi 16130148 230 tfHLSAVNWSNIMMLG--AIGLVFWM 253
Cdd:cd18542 220 --KLLAKYWPLMDFLSglQIVLVLWV 243
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
72-171 |
1.52e-03 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 40.62 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 72 LTTLGHHFVYRLRSEFIKRILDTHVERIEQLGSASLLAGLTSDVRNI-TIAFVRLPELVQGIILTIGSAAYLWMLSGKML 150
Cdd:cd18557 60 FNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLqSAVTDNLSQLLRNILQVIGGLIILFILSWKLT 139
|
90 100
....*....|....*....|.
gi 16130148 151 LVTAIWMAITIWGGFVLVARV 171
Cdd:cd18557 140 LVLLLVIPLLLIASKIYGRYI 160
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
323-385 |
2.64e-03 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 39.91 E-value: 2.64e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130148 323 LELRNVTFAYQD-NAFSvgPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGK 385
Cdd:PRK11701 7 LSVRGLTKLYGPrKGCR--DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMR 68
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
354-512 |
3.21e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 40.26 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 354 LIGGNGSGKSTLAMLLTGLYQPQSGEILLD-----GKpVSGEQ--PEDYRKLFSAVFTDVWLFDQLLGPEGKPANPQLVE 426
Cdd:PRK15064 32 LIGANGCGKSTFMKILGGDLEPSAGNVSLDpnerlGK-LRQDQfaFEEFTVLDTVIMGHTELWEVKQERDRIYALPEMSE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 427 K---WLAQLKMAH---------------------KLELSNGRIVNlkLSKGQKKRVALLLALAEERDIILLDEWAADQDP 482
Cdd:PRK15064 111 EdgmKVADLEVKFaemdgytaearagelllgvgiPEEQHYGLMSE--VAPGWKLRVLLAQALFSNPDILLLDEPTNNLDI 188
|
170 180 190
....*....|....*....|....*....|
gi 16130148 483 HFRREFYQVLlplmQEMGKTIFAISHDDHY 512
Cdd:PRK15064 189 NTIRWLEDVL----NERNSTMIIISHDRHF 214
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
327-509 |
3.45e-03 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 39.71 E-value: 3.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 327 NVTFAYQD-NAFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQ---SGEILLDGKPVSGEQPEDYRKL---- 398
Cdd:PRK09473 19 RVTFSTPDgDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPEKELNKLraeq 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 399 FSAVFTD--------VWLFDQLL-------GPEGKPANPQLVeKWLAQLKM--AHKlelsNGRIVNLKLSKGQKKRVALL 461
Cdd:PRK09473 99 ISMIFQDpmtslnpyMRVGEQLMevlmlhkGMSKAEAFEESV-RMLDAVKMpeARK----RMKMYPHEFSGGMRQRVMIA 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16130148 462 LALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHD 509
Cdd:PRK09473 174 MALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHD 221
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
323-534 |
3.64e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 39.79 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 323 LELRNVTFAYQDnafSVGP------INLTIKRGELLFLIGGNGSGKSTLAMLLTGL----YQPQSGEILLDGKPVSGEQP 392
Cdd:PRK15093 4 LDIRNLTIEFKT---SDGWvkavdrVSMTLTEGEIRGLVGESGSGKSLIAKAICGVtkdnWRVTADRMRFDDIDLLRLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 393 EDYRKLF----SAVFTDVwlfDQLLGPEGKPANpQLVE---------KWLAQLKMAHKLELSNGRIVNLK---------- 449
Cdd:PRK15093 81 RERRKLVghnvSMIFQEP---QSCLDPSERVGR-QLMQnipgwtykgRWWQRFGWRKRRAIELLHRVGIKdhkdamrsfp 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 450 --LSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDHYFIH-ADRLLEMRNGQ 526
Cdd:PRK15093 157 yeLTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQwADKINVLYCGQ 236
|
....*...
gi 16130148 527 LSELTGEE 534
Cdd:PRK15093 237 TVETAPSK 244
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
346-475 |
6.97e-03 |
|
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: 37.99 E-value: 6.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 346 IKRGELLFLIGGNGSGKSTLAMLL-----TGLYqpqSGEILLDGKPVsgeqPEDYRKLFSAVftdvwlfdqllgpegkpa 420
Cdd:cd03232 30 VKPGTLTALMGESGAGKTTLLDVLagrktAGVI---TGEILINGRPL----DKNFQRSTGYV------------------ 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 16130148 421 npQLVEKWLAQLKMAHKLELSngriVNLK-LSKGQKKRVALLLALAEERDIILLDE 475
Cdd:cd03232 85 --EQQDVHSPNLTVREALRFS----ALLRgLSVEQRKRLTIGVELAAKPSILFLDE 134
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
346-508 |
8.76e-03 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 38.87 E-value: 8.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 346 IKRGELLFLIGGNGSGKSTLAMLLTGlYQPQ----SGEILLDGKPVSGEQpedYRKLFSAVFTDVWLFDQLLGPE----- 416
Cdd:TIGR00955 48 AKPGELLAVMGSSGAGKTTLMNALAF-RSPKgvkgSGSVLLNGMPIDAKE---MRAISAYVQQDDLFIPTLTVREhlmfq 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130148 417 ---------GKPANPQLVEKWLAQL---KMAHKLELSNGRIVNlkLSKGQKKRVALLLALAEERDIILLDEWAADQDPHF 484
Cdd:TIGR00955 124 ahlrmprrvTKKEKRERVDEVLQALglrKCANTRIGVPGRVKG--LSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFM 201
|
170 180
....*....|....*....|....
gi 16130148 485 RREFYQVLLPLMQEmGKTIFAISH 508
Cdd:TIGR00955 202 AYSVVQVLKGLAQK-GKTIICTIH 224
|
|
| |
