|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
3-646 |
0e+00 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 842.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 3 PALSKLRENQSAIV---------GVTGISAALWIIAYGKMSSKRRKHGYEEKIQYTISEKKDKKSPKAHVNAVFFKQLRK 73
Cdd:TIGR00954 2 AVLSKYRLLRSTSNnktdkqdspAAVGMNKVIELKRERAADRRGDKSGKEELTIVGKHSTIEGAKKKAHVNGVFLGKLDF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 74 LLPILVPGFWSIESGLLFLVAASLIGRSVSDIWMIQNATVVESTIIHMNKAGFRTSLIKYLAALPMISVVTNILKWSLGE 153
Cdd:TIGR00954 82 LLKILIPRVFCKETGLLILIAFLLVSRTYLSVYVATLDGQIESSIVRRSPRNFAWILFKWFLIAPPASFINSAIKYLLKE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 154 LKLRFRTNLTHHLYNQYLTGYTYYKMSNLDNRIANADQLLTTDIDKFCESATELYSNISKPVLDIFIYVYRLTVNLGGKT 233
Cdd:TIGR00954 162 LKLRFRVRLTRYLYSKYLSGFTFYKVSNLDSRIQNPDQLLTQDVEKFCDSVVELYSNLTKPILDVILYSFKLLTALGSVG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 234 PSILMIYLLFAGVLLTRMRRPTGRLTVEEQKLEGEFRYVNSRLITNSEEVAFYQGNAREKLTLLASYSKLRSHLRKFLEF 313
Cdd:TIGR00954 242 PAGLFAYLFATGVVLTKLRPPIGKLTVEEQALEGEYRYVHSRLIMNSEEIAFYQGNKVEKETVMSSFYRLVEHLNLIIKF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 314 RVGMGIVDNIVGKYFASIVGFYAVSIPFFTPNHPLLSGENQGQRLQAYYTYGRMLIKLAEAIGRLVLAGREMTRLAGFTA 393
Cdd:TIGR00954 322 RFSYGFLDNIVAKYTWSAVGLVAVSIPIFDKTHPAFLEMSEEELMQEFYNNGRLLLKAADALGRLMLAGRDMTRLAGFTA 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 394 RMTELIKVLNDLNKGTYERTMVNNVVNG-----NSDFGPGKGAMEFVDNIIKFENVPLVTPNGDVLVKDLTFEVKSGTNV 468
Cdd:TIGR00954 402 RVDTLLQVLDDVKSGNFKRPRVEEIESGreggrNSNLVPGRGIVEYQDNGIKFENIPLVTPNGDVLIESLSFEVPSGNNL 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 469 LVCGPNGCGKSSLFRILGELWPTWGGKVTKPQRGKLFYIPQRPYMTLGSLRDQIIYPHTREDMRRNGKTDEDLMQYLDIV 548
Cdd:TIGR00954 482 LICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQRPYMTLGTLRDQIIYPDSSEDMKRRGLSDKDLEQILDNV 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 549 QLTYLEHRENGLDAIEDWIDVLSGGEKQRIAMARLFYHSPQFAILDECTSAVSVDVEGKMYSYCREAGITLFTVSHRKSL 628
Cdd:TIGR00954 562 QLTHILEREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFGITLFSVSHRKSL 641
|
650
....*....|....*...
gi 1678143030 629 WVHHDFFLQFDGRGNYEF 646
Cdd:TIGR00954 642 WKYHEYLLYMDGRGGYQF 659
|
|
| ABC_membrane_2 |
pfam06472 |
ABC transporter transmembrane region 2; This domain covers the transmembrane of a small family ... |
74-342 |
1.76e-119 |
|
ABC transporter transmembrane region 2; This domain covers the transmembrane of a small family of ABC transporters and shares sequence similarity with pfam00664. Mutations in this domain in Swiss:P28288 are believed responsible for Zellweger Syndrome-2; mutations in Swiss:P33897 are responsible for recessive X-linked adrenoleukodystrophy. A Saccharomyces cerevisiae homolog is involved in the import of long-chain fatty acids.
Pssm-ID: 399466 Cd Length: 269 Bit Score: 356.92 E-value: 1.76e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 74 LLPILVPGFWSIESGLLFLVAASLIGRSVSDIWMIQNATVVESTIIHMNKAGFRTSLIKYLAALPMISVVTNILKWSLGE 153
Cdd:pfam06472 1 LLKILFPRWFSKEAGLLLALAALLVLRTFLSVLVAQLDGQIVKALVAKNGRGFIRLLLKWALLAVPASFVNSALKYLTQR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 154 LKLRFRTNLTHHLYNQYLTGYTYYKMSNLDNRIANADQLLTTDIDKFCESATELYSNISKPVLDIFIYVYRLTVNLGGKT 233
Cdd:pfam06472 81 LALRFRTRLTRHLHDEYLKGRTYYKMSNLDGRIDNPDQRITQDVEKFCSSLSDLYSNLLKPILDIILFTFRLWRLSGWRG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 234 PSILMIYLLFAGVLLTRMRRPTGRLTVEEQKLEGEFRYVNSRLITNSEEVAFYQGNAREKLTLLASYSKLRSHLRKFLEF 313
Cdd:pfam06472 161 PAILFLYVLLSAVILRRLSPPFGKLVAEEQKLEGEFRYLHSRLITNAEEIAFYRGEKREKKQLQRSFKSLIDHMRRILRR 240
|
250 260
....*....|....*....|....*....
gi 1678143030 314 RVGMGIVDNIVGKYFASIVGFYAVSIPFF 342
Cdd:pfam06472 241 RLWYGFIEDFVLKYTWSILGYVLVALPIF 269
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
67-653 |
3.19e-98 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 312.51 E-value: 3.19e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 67 FFKQLRKLlpilVPGFWSIES-----GLLFLVAASLIGRSVSDIWMIQNATVVESTIIHMNKAGFRTSLIKYLAALPMIS 141
Cdd:COG4178 3 LLRQFWRL----ARPYWRSEEkwkawGLLALLLLLTLASVGLNVLLNFWNRDFYDALQARDAAAFWQQLGVFALLAAISI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 142 VVTNILKWSLGELKLRFRTNLTHHLYNQYLTGYTYYKMSNLDNRIANADQLLTTDIDKFCESATELYSNISKPVLDIFIY 221
Cdd:COG4178 79 LLAVYQTYLRQRLQIRWREWLTERLLDRWLSNRAYYRLQLSGGEIDNPDQRIAEDIRLFTETTLSLSLGLLSSVVTLISF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 222 VY-------RLTVNLGGKTPSI-------LMIYLLFAGVLLTRMRRPTGRLTVEEQKLEGEFRYVNSRLITNSEEVAFYQ 287
Cdd:COG4178 159 IGilwslsgSLTFTLGGYSITIpgymvwaALIYAIIGTLLTHLIGRPLIRLNFEQQRREADFRFALVRVRENAESIALYR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 288 GNAREKLTLLASYSKLRSHLRKFLEFRVGMGIVDNIVGkYFASIVGFYAVSIPFFtpnhpllSGEnqgqrlqayYTYGRM 367
Cdd:COG4178 239 GEAAERRRLRRRFDAVIANWRRLIRRQRNLTFFTTGYG-QLAVIFPILVAAPRYF-------AGE---------ITLGGL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 368 lIKLAEAIGRLVLAGR----EMTRLAGFTA---RMTELIKVLNDLNKgtyertmvnnvvngnsdFGPGKGAMEFV-DNII 439
Cdd:COG4178 302 -MQAASAFGQVQGALSwfvdNYQSLAEWRAtvdRLAGFEEALEAADA-----------------LPEAASRIETSeDGAL 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 440 KFENVPLVTPNGDVLVKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELWPtWG-GKVTKPQRGKLFYIPQRPYMTLGSL 518
Cdd:COG4178 364 ALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWP-YGsGRIARPAGARVLFLPQRPYLPLGTL 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 519 RDQIIYPHTREDMrrngkTDEDLMQYLDIVQLTYLEHRengLDAIEDWIDVLSGGEKQRIAMARLFYHSPQFAILDECTS 598
Cdd:COG4178 443 REALLYPATAEAF-----SDAELREALEAVGLGHLAER---LDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATS 514
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 1678143030 599 AVSVDVEGKMYSYCREA--GITLFTVSHRKSLWVHHDFFLQFDGRGNYEFGRIDQDK 653
Cdd:COG4178 515 ALDEENEAALYQLLREElpGTTVISVGHRSTLAAFHDRVLELTGDGSWQLLPAEAPA 571
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
439-644 |
3.32e-82 |
|
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: 256.70 E-value: 3.32e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 439 IKFENVPLVTPNGDVLVKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELWPTWGGKVTKPQRGKLFYIPQRPYMTLGSL 518
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQRPYLPLGTL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 519 RDQIIYPhtredmrrngktdedlmqyldivqltylehrengldaiedWIDVLSGGEKQRIAMARLFYHSPQFAILDECTS 598
Cdd:cd03223 81 REQLIYP----------------------------------------WDDVLSGGEQQRLAFARLLLHKPKFVFLDEATS 120
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1678143030 599 AVSVDVEGKMYSYCREAGITLFTVSHRKSLWVHHDFFLQFDGRGNY 644
Cdd:cd03223 121 ALDEESEDRLYQLLKELGITVISVGHRPSLWKFHDRVLDLDGEGGW 166
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
439-624 |
1.13e-29 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 116.45 E-value: 1.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 439 IKFENVPlVTPNGDVLVKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELWPTWGGKVT---KPQ--------RGKLFYI 507
Cdd:COG4619 1 LELEGLS-FRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYldgKPLsampppewRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 508 PQRPYMTLGSLRDQIIYPHTREDMRRNGKTDEDLMQYLdivqltylehrenGLDA-IEDW-IDVLSGGEKQRIAMARLFY 585
Cdd:COG4619 80 PQEPALWGGTVRDNLPFPFQLRERKFDRERALELLERL-------------GLPPdILDKpVERLSGGERQRLALIRALL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1678143030 586 HSPQFAILDECTSA---VSVD-VEGKMYSYCREAGITLFTVSH 624
Cdd:COG4619 147 LQPDVLLLDEPTSAldpENTRrVEELLREYLAEEGRAVLWVSH 189
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
64-625 |
1.02e-27 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 117.96 E-value: 1.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 64 NAVFFKQLRKLLPILVPGFWSIESGLLFLVAASLIGrsVSDIWMIQNatVVESTIIHMNKAGFRTSLIKYLAALPMISVV 143
Cdd:COG1132 2 SKSPRKLLRRLLRYLRPYRGLLILALLLLLLSALLE--LLLPLLLGR--IIDALLAGGDLSALLLLLLLLLGLALLRALL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 144 TNILKWSLGELKLRFRTNLTHHLYNQYLT-GYTYYK-------MSNLDNRIANADQLLTTdidkfceSATELYSNISKPV 215
Cdd:COG1132 78 SYLQRYLLARLAQRVVADLRRDLFEHLLRlPLSFFDrrrtgdlLSRLTNDVDAVEQFLAH-------GLPQLVRSVVTLI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 216 LdIFIYVYRLTVNLGGktpsILMIYLLFAGVLLTRMRRPTGRLTVEEQKLEGEfryVNSRL---ITNSEEVafyQGNARE 292
Cdd:COG1132 151 G-ALVVLFVIDWRLAL----IVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAE---LNGRLqesLSGIRVV---KAFGRE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 293 KltllASYSKLRSHLRKFLEFRVGMGIVDNIVGKYFASIVGF-YAVSIPFFTpnHPLLSGE-NQGQrLQAYYTYGRMLIK 370
Cdd:COG1132 220 E----RELERFREANEELRRANLRAARLSALFFPLMELLGNLgLALVLLVGG--LLVLSGSlTVGD-LVAFILYLLRLFG 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 371 LAEAIGRLVlagREMTRLAGFTARMTELIKVlndlnkgtyERTMVNnvvngnsdfGPGKGAMEFVDNIIKFENVPLVTPN 450
Cdd:COG1132 293 PLRQLANVL---NQLQRALASAERIFELLDE---------PPEIPD---------PPGAVPLPPVRGEIEFENVSFSYPG 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 451 GDVLVKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELWPTWGGKVT---------KPQ--RGKLFYIPQRPYMTLGSLR 519
Cdd:COG1132 352 DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILidgvdirdlTLEslRRQIGVVPQDTFLFSGTIR 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 520 DQIIYPhtredmrRNGKTDEDLMQYLDIVQLT-YLEHRENGLDAIedwidV------LSGGEKQRIAMARLFYHSPQFAI 592
Cdd:COG1132 432 ENIRYG-------RPDATDEEVEEAAKAAQAHeFIEALPDGYDTV-----VgergvnLSGGQRQRIAIARALLKDPPILI 499
|
570 580 590
....*....|....*....|....*....|....*
gi 1678143030 593 LDECTSAVSVDVEGKMYSYCRE--AGITLFTVSHR 625
Cdd:COG1132 500 LDEATSALDTETEALIQEALERlmKGRTTIVIAHR 534
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
439-625 |
2.26e-26 |
|
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: 113.70 E-value: 2.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 439 IKFENVPLVTPNGDVLVKDLTFEVKSGTNVLVCGPNGCGKSSLFR-ILGELWPTwGGKVT-----------KPQRGKLFY 506
Cdd:COG4988 337 IELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNlLLGFLPPY-SGSILingvdlsdldpASWRRQIAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 507 IPQRPYMTLGSLRDQIiyphtreDMRRNGKTDEDLMQYLDIVQLT-YLEHRENGLDAIedwidV------LSGGEKQRIA 579
Cdd:COG4988 416 VPQNPYLFAGTIRENL-------RLGRPDASDEELEAALEAAGLDeFVAALPDGLDTP-----LgeggrgLSGGQAQRLA 483
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1678143030 580 MARLFYHSPQFAILDECTSavSVDVEG------KMYSYCReaGITLFTVSHR 625
Cdd:COG4988 484 LARALLRDAPLLLLDEPTA--HLDAETeaeilqALRRLAK--GRTVILITHR 531
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
439-628 |
8.52e-26 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 104.39 E-value: 8.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 439 IKFENVPLVTPNGDVLV-KDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELWPtwggkvtkPQRGKLFY--IPQRPYmTL 515
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVlKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYD--------PTSGEILIdgVDLRDL-DL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 516 GSLRDQIIYphtredmrrngktdedlmqyldIVQLTYLEH---RENgldaiedwidVLSGGEKQRIAMARLFYHSPQFAI 592
Cdd:cd03228 72 ESLRKNIAY----------------------VPQDPFLFSgtiREN----------ILSGGQRQRIAIARALLRDPPILI 119
|
170 180 190
....*....|....*....|....*....|....*...
gi 1678143030 593 LDECTSAVSVDVEGKMYSYCRE--AGITLFTVSHRKSL 628
Cdd:cd03228 120 LDEATSALDPETEALILEALRAlaKGKTVIVIAHRLST 157
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
456-641 |
8.98e-25 |
|
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: 102.55 E-value: 8.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 456 KDLTFEVKSGTNVLVCGPNGCGKSSLFR-ILGELWPTwGGKVTKPqrGKLFYIPQRPYMTLGSLRDQIIYpHTREDMRRn 534
Cdd:cd03250 22 KDINLEVPKGELVAIVGPVGSGKSSLLSaLLGELEKL-SGSVSVP--GSIAYVSQEPWIQNGTIRENILF-GKPFDEER- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 535 gktdedlmqYLDIVQ-------LTYLEHR------ENGLDaiedwidvLSGGEKQRIAMARLFYHSPQFAILDECTSAVS 601
Cdd:cd03250 97 ---------YEKVIKacalepdLEILPDGdlteigEKGIN--------LSGGQKQRISLARAVYSDADIYLLDDPLSAVD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1678143030 602 VDVEGKMYSYC-REAGI---TLFTVSHRKSLWVHHDFFLQ-FDGR 641
Cdd:cd03250 160 AHVGRHIFENCiLGLLLnnkTRILVTHQLQLLPHADQIVVlDNGR 204
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
356-628 |
1.80e-24 |
|
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: 108.77 E-value: 1.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 356 QRLQAYYTYGRMLIKLAEAIG------RLVLAGrEMTR--------LAG-FTARMTELIKVLNDLN--KGTYERtmVNNV 418
Cdd:COG2274 375 RRLSNLLSTLSGLLQQLATVAllwlgaYLVIDG-QLTLgqliafniLSGrFLAPVAQLIGLLQRFQdaKIALER--LDDI 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 419 VNGNSDFGPGKGA--MEFVDNIIKFENV----PlvtPNGDVLVKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELWPTW 492
Cdd:COG2274 452 LDLPPEREEGRSKlsLPRLKGDIELENVsfryP---GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPT 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 493 GGKVT---------KPQ--RGKLFYIPQRPYMTLGSLRDQIIyphtredMRRNGKTDEDLMQYLDIVQLT-YLEHRENGL 560
Cdd:COG2274 529 SGRILidgidlrqiDPAslRRQIGVVLQDVFLFSGTIRENIT-------LGDPDATDEEIIEAARLAGLHdFIEALPMGY 601
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1678143030 561 DA-IEDWIDVLSGGEKQRIAMARLFYHSPQFAILDECTSAVSVDVEGKMYSYCRE--AGITLFTVSHRKSL 628
Cdd:COG2274 602 DTvVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRllKGRTVIIIAHRLST 672
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
439-627 |
1.72e-23 |
|
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: 99.61 E-value: 1.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 439 IKFENVPLVTPNGDVLVKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELWPTWGGKVT-----------KPQRGKLFYI 507
Cdd:cd03254 3 IEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILidgidirdisrKSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 508 PQRPYMTLGSLRDQIIYphtredmRRNGKTDEDLMQYLDIVQLTYL-EHRENGLDA-IEDWIDVLSGGEKQRIAMARLFY 585
Cdd:cd03254 83 LQDTFLFSGTIMENIRL-------GRPNATDEEVIEAAKEAGAHDFiMKLPNGYDTvLGENGGNLSQGERQLLAIARAML 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1678143030 586 HSPQFAILDECTSAVSVDVEGKMYSYCRE--AGITLFTVSHRKS 627
Cdd:cd03254 156 RDPKILILDEATSNIDTETEKLIQEALEKlmKGRTSIIIAHRLS 199
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
439-628 |
3.17e-23 |
|
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: 103.91 E-value: 3.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 439 IKFENVPLVTPNGDVLVKDLTFEVKSGTNVLVCGPNGCGKSSLFR-ILGELWPTWG----GKVTKPQ------RGKLFYI 507
Cdd:TIGR02857 322 LEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNlLLGFVDPTEGsiavNGVPLADadadswRDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 508 PQRPYMTLGSLRDQIIyphtredMRRNGKTDEDLMQYLDIVQL-TYLEHRENGLDA-IEDWIDVLSGGEKQRIAMARLFY 585
Cdd:TIGR02857 402 PQHPFLFAGTIAENIR-------LARPDASDAEIREALERAGLdEFVAALPQGLDTpIGEGGAGLSGGQAQRLALARAFL 474
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1678143030 586 HSPQFAILDECTSAVSVDVEGKMYSYCREA--GITLFTVSHRKSL 628
Cdd:TIGR02857 475 RDAPLLLLDEPTAHLDAETEAEVLEALRALaqGRTVLLVTHRLAL 519
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
450-624 |
2.04e-22 |
|
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: 97.04 E-value: 2.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 450 NGDVLVKDLTFEVKSGTNVLVCGPNGCGKSSLFR-ILGELWPTwGGKVT---KP-------QRGKLF-YIPQRPYMTLG- 516
Cdd:COG1120 12 GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRaLAGLLKPS-SGEVLldgRDlaslsrrELARRIaYVPQEPPAPFGl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 517 SLRDQII---YPHTReDMRRNGKTDEDL-MQYLDIVQLTYLEHREngldaiedwIDVLSGGEKQRIAMARLFYHSPQFAI 592
Cdd:COG1120 91 TVRELVAlgrYPHLG-LFGRPSAEDREAvEEALERTGLEHLADRP---------VDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 1678143030 593 LDECTSAV----SVDVEGKMYSYCREAGITLFTVSH 624
Cdd:COG1120 161 LDEPTSHLdlahQLEVLELLRRLARERGRTVVMVLH 196
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
440-624 |
4.92e-22 |
|
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: 94.91 E-value: 4.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 440 KFENVPlVTPNGDVLVKDLTFEVKSGTNVLVCGPNGCGKSSLFR-ILGELWPTWG-----GKVTKPQRGKLFYIPQRPYM 513
Cdd:cd03235 1 EVEDLT-VSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKaILGLLKPTSGsirvfGKPLEKERKRIGYVPQRRSI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 514 TLG---SLRDQI---IYPHTREDMRRNGKTDEDLMQYLDIVQLTYLEHREngldaiedwIDVLSGGEKQRIAMARLFYHS 587
Cdd:cd03235 80 DRDfpiSVRDVVlmgLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQ---------IGELSGGQQQRVLLARALVQD 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1678143030 588 PQFAILDECTsaVSVDVEGKMYSY-----CREAGITLFTVSH 624
Cdd:cd03235 151 PDLLLLDEPF--AGVDPKTQEDIYellreLRREGMTILVVTH 190
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
436-633 |
1.52e-21 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 94.39 E-value: 1.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 436 DNIIKFENVpLVTPNGDVLVKDLTFEVKSGTNVLVCGPNGCGKSSLFR-ILGELWPTWG-----GKVTKPQRGKLFYIPQ 509
Cdd:COG1121 4 MPAIELENL-TVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKaILGLLPPTSGtvrlfGKPPRRARRRIGYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 510 RPYMTLG---SLRDQI---IYPHTReDMRRNGKTDEDL-MQYLDIVQLTYLEHRengldaiedWIDVLSGGEKQRIAMAR 582
Cdd:COG1121 83 RAEVDWDfpiTVRDVVlmgRYGRRG-LFRRPSRADREAvDEALERVGLEDLADR---------PIGELSGGQQQRVLLAR 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1678143030 583 LFYHSPQFAILDECTSAVSVDVEGKMYSY---CREAGITLftvshrksLWVHHD 633
Cdd:COG1121 153 ALAQDPDLLLLDEPFAGVDAATEEALYELlreLRREGKTI--------LVVTHD 198
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
371-625 |
1.55e-21 |
|
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: 99.07 E-value: 1.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 371 LAEAIGRLVLAGREMTRLAGFTARMTELIkvlndlnkgtyerTMVNNVVNgnsdfgPGKGAMEFVDNIIKFENVPLVTPN 450
Cdd:COG4987 285 LFEALAPLPAAAQHLGRVRAAARRLNELL-------------DAPPAVTE------PAEPAPAPGGPSLELEDVSFRYPG 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 451 GDVLV-KDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELWPTWGGKVT---KP--------QRGKLFYIPQRPYMTLGSL 518
Cdd:COG4987 346 AGRPVlDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITlggVDlrdldeddLRRRIAVVPQRPHLFDTTL 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 519 RDQIIyphtredMRRNGKTDEDLMQYLDIVQL-TYLEHRENGLDAiedWIDV----LSGGEKQRIAMARLFYHSPQFAIL 593
Cdd:COG4987 426 RENLR-------LARPDATDEELWAALERVGLgDWLAALPDGLDT---WLGEggrrLSGGERRRLALARALLRDAPILLL 495
|
250 260 270
....*....|....*....|....*....|....
gi 1678143030 594 DECTSAVSVDVEGKMYSYCREA--GITLFTVSHR 625
Cdd:COG4987 496 DEPTEGLDAATEQALLADLLEAlaGRTVLLITHR 529
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
439-625 |
5.71e-21 |
|
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: 91.79 E-value: 5.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 439 IKFENVPL-VTPNGDVLVKDLTFEVKSGTNVLVCGPNGCGKSS----LFRILgelwPTWGGKVT-----------KPQRG 502
Cdd:cd03244 3 IEFKNVSLrYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLV----ELSSGSILidgvdiskiglHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 503 KLFYIPQRPYMTLGSLRDQiIYPHtredmrrNGKTDEDLMQYLDIVQLT-YLEHRENGLDA-IEDWIDVLSGGEKQRIAM 580
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSN-LDPF-------GEYSDEELWQALERVGLKeFVESLPGGLDTvVEEGGENLSVGQRQLLCL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1678143030 581 ARLFYHSPQFAILDECTSAVSVDVEGKMYSYCRE--AGITLFTVSHR 625
Cdd:cd03244 151 ARALLRKSKILVLDEATASVDPETDALIQKTIREafKDCTVLTIAHR 197
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
435-640 |
5.94e-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: 92.15 E-value: 5.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 435 VDNIIKFENVPLVTPN-GDVLV-KDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELWPTWGGKVT---KP--------QR 501
Cdd:cd03248 8 LKGIVKFQNVTFAYPTrPDTLVlQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLldgKPisqyehkyLH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 502 GKLFYIPQRPYMTLGSLRDQIIYphtredmrrnGKTDEDLMQYLDIVQlTYLEHRENGLDAIEDWIDV------LSGGEK 575
Cdd:cd03248 88 SKVSLVGQEPVLFARSLQDNIAY----------GLQSCSFECVKEAAQ-KAHAHSFISELASGYDTEVgekgsqLSGGQK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1678143030 576 QRIAMARLFYHSPQFAILDECTSAVSVDVEGKMYS--YCREAGITLFTVSHRKSLWVHHDFFLQFDG 640
Cdd:cd03248 157 QRVAIARALIRNPQVLILDEATSALDAESEQQVQQalYDWPERRTVLVIAHRLSTVERADQILVLDG 223
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
450-625 |
7.13e-21 |
|
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: 89.61 E-value: 7.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 450 NGDVLVKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELWPTWGGKVTkpqrgklFYIPQRPYMTLGSLRDQIIYphtre 529
Cdd:cd00267 10 GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEIL-------IDGKDIAKLPLEELRRRIGY----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 530 dmrrngktdedLMQyldivqltylehrengldaiedwidvLSGGEKQRIAMARLFYHSPQFAILDECTSAVSVDVEGKMY 609
Cdd:cd00267 78 -----------VPQ--------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLL 120
|
170
....*....|....*....
gi 1678143030 610 SYCREA---GITLFTVSHR 625
Cdd:cd00267 121 ELLRELaeeGRTVIIVTHD 139
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
440-625 |
2.27e-20 |
|
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: 89.83 E-value: 2.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 440 KFENVPLVTPNGDVLV-KDLTFEVKSGTNVLVCGPNGCGKSSLFRIL-GELWPT-----WGGKVTKPQ-----RGKLFYI 507
Cdd:cd03225 1 ELKNLSFSYPDGARPAlDDISLTIKKGEFVLIVGPNGSGKSTLLRLLnGLLGPTsgevlVDGKDLTKLslkelRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 508 PQRPymtlgslRDQIIYPHTREDM---RRNGKTDEDLM-----QYLDIVQLTYLEHREngldaiedwIDVLSGGEKQRIA 579
Cdd:cd03225 81 FQNP-------DDQFFGPTVEEEVafgLENLGLPEEEIeerveEALELVGLEGLRDRS---------PFTLSGGQKQRVA 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1678143030 580 MARLFYHSPQFAILDECTSavSVDVEG-----KMYSYCREAGITLFTVSHR 625
Cdd:cd03225 145 IAGVLAMDPDILLLDEPTA--GLDPAGrrellELLKKLKAEGKTIIIVTHD 193
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
450-624 |
7.62e-20 |
|
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: 88.30 E-value: 7.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 450 NGDVLVKDLTFEVKSGTNVLVCGPNGCGKSSLFRIL-GELWPT-----WGGKVTKPQ----RGKLFYIPQRP--YMTLgS 517
Cdd:COG4133 13 GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILaGLLPPSagevlWNGEPIRDAredyRRRLAYLGHADglKPEL-T 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 518 LRDQIIYpHTRedMRRNGKTDEDLMQYLDIVQLTYLEHREngldaiedwIDVLSGGEKQRIAMARLFYHSPQFAILDECT 597
Cdd:COG4133 92 VRENLRF-WAA--LYGLRADREAIDEALEAVGLAGLADLP---------VRQLSAGQKRRVALARLLLSPAPLWLLDEPF 159
|
170 180 190
....*....|....*....|....*....|...
gi 1678143030 598 SAvsVDVEGK------MYSYCREAGITLFTvSH 624
Cdd:COG4133 160 TA--LDAAGVallaelIAAHLARGGAVLLT-TH 189
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
455-598 |
1.44e-19 |
|
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: 85.78 E-value: 1.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 455 VKDLTFEVKSGTNVLVCGPNGCGKSSLFRIL-GELWPTwGGKVT-----------KPQRGKLFYIPQ----RPYMTLgsl 518
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIaGLLSPT-EGTILldgqdltdderKSLRKEIGYVFQdpqlFPRLTV--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 519 RDQIIYPHTREDMRRNGKtDEDLMQYLDIVQLTYLEHRengldAIEDWIDVLSGGEKQRIAMARLFYHSPQFAILDECTS 598
Cdd:pfam00005 77 RENLRLGLLLKGLSKREK-DARAEEALEKLGLGDLADR-----PVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
439-628 |
4.48e-19 |
|
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: 86.49 E-value: 4.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 439 IKFENVPLVTPNGDVL-VKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELWptwggkvtKPQRGKLF------------ 505
Cdd:cd03245 3 IEFRNVSFSYPNQEIPaLDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLY--------KPTSGSVLldgtdirqldpa 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 506 -------YIPQRPYMTLGSLRDQIIyphtredMRRNGKTDEDLMQYLDIVQLTYLEHRE-NGLD-AIEDWIDVLSGGEKQ 576
Cdd:cd03245 75 dlrrnigYVPQDVTLFYGTLRDNIT-------LGAPLADDERILRAAELAGVTDFVNKHpNGLDlQIGERGRGLSGGQRQ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1678143030 577 RIAMARLFYHSPQFAILDECTSAVSVDVEGKMYSYCRE--AGITLFTVSHRKSL 628
Cdd:cd03245 148 AVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQllGDKTLIIITHRPSL 201
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
439-628 |
5.95e-19 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 84.58 E-value: 5.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 439 IKFENVPLVTPNGD-VLVKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELWPTWGGKVTkpqrgkLFYIPQRPYmTLGS 517
Cdd:cd03246 1 LEVENVSFRYPGAEpPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVR------LDGADISQW-DPNE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 518 LRDQIIYphtredmrrngktdedLMQylDIVQLTylehrenglDAIEDWIdvLSGGEKQRIAMARLFYHSPQFAILDECT 597
Cdd:cd03246 74 LGDHVGY----------------LPQ--DDELFS---------GSIAENI--LSGGQRQRLGLARALYGNPRILVLDEPN 124
|
170 180 190
....*....|....*....|....*....|....
gi 1678143030 598 SAVSVDVEGKMYS---YCREAGITLFTVSHRKSL 628
Cdd:cd03246 125 SHLDVEGERALNQaiaALKAAGATRIVIAHRPET 158
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
455-624 |
6.85e-19 |
|
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: 86.40 E-value: 6.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 455 VKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELWPTWGGKVT-----------KPQRGKLFYIPQRPY------MTLgs 517
Cdd:COG1124 21 LKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTfdgrpvtrrrrKAFRRRVQMVFQDPYaslhprHTV-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 518 lrDQIIyphtREDMRRNGKTD--EDLMQYLDIVqltylehrenGLDaiEDWID----VLSGGEKQRIAMARLFYHSPQFA 591
Cdd:COG1124 99 --DRIL----AEPLRIHGLPDreERIAELLEQV----------GLP--PSFLDryphQLSGGQRQRVAIARALILEPELL 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 1678143030 592 ILDECTSAVSVDVEGKM----YSYCREAGITLFTVSH 624
Cdd:COG1124 161 LLDEPTSALDVSVQAEIlnllKDLREERGLTYLFVSH 197
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
427-637 |
6.90e-19 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 90.94 E-value: 6.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 427 PGKGAMEFVDNIIKFENVPLVTPN-GDVLV-KDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELW-PTwGGKVT------ 497
Cdd:TIGR00958 467 TGTLAPLNLEGLIEFQDVSFSYPNrPDVPVlKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYqPT-GGQVLldgvpl 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 498 -----KPQRGKLFYIPQRPYMTLGSLRDQIIYPHTRedmrrngKTDEDLMqylDIVQL----TYLEHRENGLDA-IEDWI 567
Cdd:TIGR00958 546 vqydhHYLHRQVALVGQEPVLFSGSVRENIAYGLTD-------TPDEEIM---AAAKAanahDFIMEFPNGYDTeVGEKG 615
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1678143030 568 DVLSGGEKQRIAMARLFYHSPQFAILDECTSAVSVDVEGKMYSYCREAGITLFTVSHRKSLW--VHHDFFLQ 637
Cdd:TIGR00958 616 SQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAHRLSTVerADQILVLK 687
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
450-624 |
7.12e-19 |
|
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: 84.79 E-value: 7.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 450 NGDVLVKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELWPTWGGKVtkpqrgklfYIPQRPYMTLGS--LRDQIIYpht 527
Cdd:cd03214 10 GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEI---------LLDGKDLASLSPkeLARKIAY--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 528 redmrrngktdedLMQYLDIVQLTYLEHREngldaiedwIDVLSGGEKQRIAMARLFYHSPQFAILDECTSAV----SVD 603
Cdd:cd03214 78 -------------VPQALELLGLAHLADRP---------FNELSGGERQRVLLARALAQEPPILLLDEPTSHLdiahQIE 135
|
170 180
....*....|....*....|.
gi 1678143030 604 VEGKMYSYCREAGITLFTVSH 624
Cdd:cd03214 136 LLELLRRLARERGKTVVMVLH 156
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
439-624 |
1.42e-18 |
|
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: 85.08 E-value: 1.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 439 IKFENVPLVTPNGDVLVKDLTFEVKSGTNVLVCGPNGCGKSSLFRIL--------GELWptWGGKVTKPQRGKLF----- 505
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLngllkptsGEVL--VDGKDITKKNLRELrrkvg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 506 YIPQRPymtlgslRDQIIYPHTRED----MRRNGKTDEDL----MQYLDIVQLTYLEHREngldaiedwIDVLSGGEKQR 577
Cdd:COG1122 79 LVFQNP-------DDQLFAPTVEEDvafgPENLGLPREEIrervEEALELVGLEHLADRP---------PHELSGGQKQR 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1678143030 578 IAMARLFYHSPQFAILDECTSavSVDVEGK--MYSYCRE---AGITLFTVSH 624
Cdd:COG1122 143 VAIAGVLAMEPEVLVLDEPTA--GLDPRGRreLLELLKRlnkEGKTVIIVTH 192
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
439-628 |
2.81e-18 |
|
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: 88.65 E-value: 2.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 439 IKFENVPLVTPNGD-VLVKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELWPTWGGKV----------TKPQRGKLF-Y 506
Cdd:COG4618 331 LSVENLTVVPPGSKrPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVrldgadlsqwDREELGRHIgY 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 507 IPQRPymTL--GSLRDQIiyphtredmRRNGKTDEDL------------MqyldIVQL-----TYLEhrENGLdaiedwi 567
Cdd:COG4618 411 LPQDV--ELfdGTIAENI---------ARFGDADPEKvvaaaklagvheM----ILRLpdgydTRIG--EGGA------- 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1678143030 568 dVLSGGEKQRIAMARLFYHSPQFAILDECTSavSVDVEG-----KMYSYCREAGITLFTVSHRKSL 628
Cdd:COG4618 467 -RLSGGQRQRIGLARALYGDPRLVVLDEPNS--NLDDEGeaalaAAIRALKARGATVVVITHRPSL 529
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
432-595 |
8.30e-18 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 83.60 E-value: 8.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 432 MEFVDNIIKFENVPLV--TPNGDVLV-KDLTFEVKSGTNVLVCGPNGCGKSSLFRIL--------GELwpTWGGKVTKPQ 500
Cdd:COG1116 1 MSAAAPALELRGVSKRfpTGGGGVTAlDDVSLTVAAGEFVALVGPSGCGKSTLLRLIaglekptsGEV--LVDGKPVTGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 501 RGKLFYIPQR----PYMTLgslRDQIIYPHTREDMRRnGKTDEDLMQYLDIVQLTYLEHRengldaiedWIDVLSGGEKQ 576
Cdd:COG1116 79 GPDRGVVFQEpallPWLTV---LDNVALGLELRGVPK-AERRERARELLELVGLAGFEDA---------YPHQLSGGMRQ 145
|
170
....*....|....*....
gi 1678143030 577 RIAMARLFYHSPQFAILDE 595
Cdd:COG1116 146 RVAIARALANDPEVLLMDE 164
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
427-641 |
8.30e-18 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 87.32 E-value: 8.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 427 PGKGAMEFVDNIIKFENVPLVTPNGDVLVKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGelwptwggKVTKPQRGKLFY 506
Cdd:PRK13657 323 PGAIDLGRVKGAVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQ--------RVFDPQSGRILI 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 507 --IPQRPyMTLGSLRDQI--------IYPHTREDMRRNGK---TDEDLMQYLDIVQ-LTYLEHRENGLDAIedwidV--- 569
Cdd:PRK13657 395 dgTDIRT-VTRASLRRNIavvfqdagLFNRSIEDNIRVGRpdaTDEEMRAAAERAQaHDFIERKPDGYDTV-----Vger 468
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678143030 570 ---LSGGEKQRIAMARLFYHSPQFAILDECTSAVSVDVEGKMYSYCREA--GITLFTVSHRKSLWVHHDFFLQFD-GR 641
Cdd:PRK13657 469 grqLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELmkGRTTFIIAHRLSTVRNADRILVFDnGR 546
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
450-633 |
2.41e-17 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 81.68 E-value: 2.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 450 NGDVLVKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELwptwggkvTKPQRGKLF-------------------YIPQR 510
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASL--------ISPTSGTLLfegedistlkpeiyrqqvsYCAQT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 511 PYMTLGSLRDQIIYPHtredMRRNGKTDEDLMQyldiVQLTYLEHRENGLDAIedwIDVLSGGEKQRIAMARLFYHSPQF 590
Cdd:PRK10247 90 PTLFGDTVYDNLIFPW----QIRNQQPDPAIFL----DDLERFALPDTILTKN---IAELSGGEKQRISLIRNLQFMPKV 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1678143030 591 AILDECTSAVSVD----VEGKMYSYCREAGITLftvshrksLWVHHD 633
Cdd:PRK10247 159 LLLDEITSALDESnkhnVNEIIHRYVREQNIAV--------LWVTHD 197
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
439-633 |
2.42e-17 |
|
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: 81.89 E-value: 2.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 439 IKFENVPL-VTPNGDVLvKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELWPTWGGKVT-----------KPQRGKLFY 506
Cdd:cd03253 1 IEFENVTFaYDPGRPVL-KDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILidgqdirevtlDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 507 IPQRPYMTLGSLRDQIIYPH---TREDMRRNGKT---DEDLMQ----YLDIVQltylehrENGLdaiedwidVLSGGEKQ 576
Cdd:cd03253 80 VPQDTVLFNDTIGYNIRYGRpdaTDEEVIEAAKAaqiHDKIMRfpdgYDTIVG-------ERGL--------KLSGGEKQ 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1678143030 577 RIAMARLFYHSPQFAILDECTSAVSVDVEGKMYSYCRE--AGITLFTVSHRKSLWVHHD 633
Cdd:cd03253 145 RVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDvsKGRTTIVIAHRLSTIVNAD 203
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
438-624 |
2.90e-17 |
|
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: 85.34 E-value: 2.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 438 IIKFENV----PLVTPNGDVLVKDLTFEVKSGTNVLVCGPNGCGKSSLFRIL--------------GELWPTWGGKVTKP 499
Cdd:COG1123 260 LLEVRNLskryPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLlgllrptsgsilfdGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 500 QRGKLFYIPQRPY------MTLGslrDQIIYPHTREDMRRNGKTDEDLMQYLDIVQLtylehrenGLDAIEDWIDVLSGG 573
Cdd:COG1123 340 LRRRVQMVFQDPYsslnprMTVG---DIIAEPLRLHGLLSRAERRERVAELLERVGL--------PPDLADRYPHELSGG 408
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1678143030 574 EKQRIAMARLFYHSPQFAILDECTSA--VSV--DVEGKMYSYCREAGITLFTVSH 624
Cdd:COG1123 409 QRQRVAIARALALEPKLLILDEPTSAldVSVqaQILNLLRDLQRELGLTYLFISH 463
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
442-628 |
5.18e-17 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 84.71 E-value: 5.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 442 ENVPLVTPNGD-VLVKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELWPTWGGKV----------TKPQRGK-LFYIPQ 509
Cdd:TIGR01842 320 ENVTIVPPGGKkPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVrldgadlkqwDRETFGKhIGYLPQ 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 510 RPYMTLGSLRDQIiyphTRedMRRNGkTDEDLMQYLDIVQLTYLEHR-ENGLD-AIEDWIDVLSGGEKQRIAMARLFYHS 587
Cdd:TIGR01842 400 DVELFPGTVAENI----AR--FGENA-DPEKIIEAAKLAGVHELILRlPDGYDtVIGPGGATLSGGQRQRIALARALYGD 472
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1678143030 588 PQFAILDECTSavSVDVEGKMYSY-----CREAGITLFTVSHRKSL 628
Cdd:TIGR01842 473 PKLVVLDEPNS--NLDEEGEQALAnaikaLKARGITVVVITHRPSL 516
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
439-624 |
6.66e-17 |
|
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: 80.21 E-value: 6.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 439 IKFENVPLVTPNGDVLVK---DLTFEVKSGTNVLVCGPNGCGKSSLFRILGELWPTWGGKVT---------KPQRGklfY 506
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTaleDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLvdgepvtgpGPDRG---Y 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 507 IPQR----PYMTlgsLRDQIIYPhtrEDMRRNGKTD--EDLMQYLDIVQLTYLEHRengldaiedWIDVLSGGEKQRIAM 580
Cdd:cd03293 78 VFQQdallPWLT---VLDNVALG---LELQGVPKAEarERAEELLELVGLSGFENA---------YPHQLSGGMRQRVAL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1678143030 581 ARLFYHSPQFAILDECTSAVSVDVEGKMYSY----CREAGITLFTVSH 624
Cdd:cd03293 143 ARALAVDPDVLLLDEPFSALDALTREQLQEElldiWRETGKTVLLVTH 190
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
439-624 |
1.10e-16 |
|
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: 79.46 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 439 IKFENVPLVTPNGDVLV---KDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELwptwggkvTKPQRGKLF---------- 505
Cdd:cd03255 1 IELKNLSKTYGGGGEKVqalKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGL--------DRPTSGEVRvdgtdiskls 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 506 -------------YIPQR----PYMTlgsLRDQIIYP------HTREDMRRNgktdEDLMQYLDivqltyLEHRENglda 562
Cdd:cd03255 73 ekelaafrrrhigFVFQSfnllPDLT---ALENVELPlllagvPKKERRERA----EELLERVG------LGDRLN---- 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1678143030 563 ieDWIDVLSGGEKQRIAMARLFYHSPQFAILDECTSAV----SVDVEGKMYSYCREAGITLFTVSH 624
Cdd:cd03255 136 --HYPSELSGGQQQRVAIARALANDPKIILADEPTGNLdsetGKEVMELLRELNKEAGTTIVVVTH 199
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
450-624 |
1.16e-16 |
|
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: 79.10 E-value: 1.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 450 NGDVLVKDLTFEVKSGTNVLVCGPNGCGKSSLFRIL--------GELWptWGGK-VTK--PQRGKLFYIPQR----PYMT 514
Cdd:cd03259 11 GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIaglerpdsGEIL--IDGRdVTGvpPERRNIGMVFQDyalfPHLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 515 lgsLRDQIIYPHTREDMRRnGKTDEDLMQYLDIVQLTYLEHRengldaiedWIDVLSGGEKQRIAMARLFYHSPQFAILD 594
Cdd:cd03259 89 ---VAENIAFGLKLRGVPK-AEIRARVRELLELVGLEGLLNR---------YPHELSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 1678143030 595 ECTSAvsVDVE------GKMYSYCREAGITLFTVSH 624
Cdd:cd03259 156 EPLSA--LDAKlreelrEELKELQRELGITTIYVTH 189
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
367-633 |
1.32e-16 |
|
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: 83.18 E-value: 1.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 367 MLIKLA--EAIGRLVLAGREMTRLAGFTARMTELIKvlndlnkgtyertmvNNVVNGNSDFgPGKGAMEFVDNIIKFENV 444
Cdd:TIGR02868 277 VLLPLAafEAFAALPAAAQQLTRVRAAAERIVEVLD---------------AAGPVAEGSA-PAAGAVGLGKPTLELRDL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 445 PLVTPNGDVLVKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELWPTWGGKVT-----------KPQRGKLFYIPQRPYM 513
Cdd:TIGR02868 341 SAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTldgvpvssldqDEVRRRVSVCAQDAHL 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 514 TLGSLRDQIIyphtredMRRNGKTDEDLMQYLDIVQL-TYLEHRENGLDAI--EDWIdVLSGGEKQRIAMARLFYHSPQF 590
Cdd:TIGR02868 421 FDTTVRENLR-------LARPDATDEELWAALERVGLaDWLRALPDGLDTVlgEGGA-RLSGGERQRLALARALLADAPI 492
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1678143030 591 AILDECTSAVSVDVEGKMYSycreagiTLFTVSHRKS-LWVHHD 633
Cdd:TIGR02868 493 LLLDEPTEHLDAETADELLE-------DLLAALSGRTvVLITHH 529
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
439-625 |
1.70e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 82.95 E-value: 1.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 439 IKFENVPLVTPNGDVLV-KDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELWPTWGGKVT---KP--------QRGKLFY 506
Cdd:PRK11160 339 LTLNNVSFTYPDQPQPVlKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILlngQPiadyseaaLRQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 507 IPQRPYMTLGSLRDQIIyphtredMRRNGKTDEDLMQYLDIVQLTYLEHRENGLDAiedWID----VLSGGEKQRIAMAR 582
Cdd:PRK11160 419 VSQRVHLFSATLRDNLL-------LAAPNASDEALIEVLQQVGLEKLLEDDKGLNA---WLGeggrQLSGGEQRRLGIAR 488
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1678143030 583 LFYHSPQFAILDECTSAVSVDVEGKMYSYCRE--AGITLFTVSHR 625
Cdd:PRK11160 489 ALLHDAPLLLLDEPTEGLDAETERQILELLAEhaQNKTVLMITHR 533
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
455-624 |
1.97e-16 |
|
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: 78.41 E-value: 1.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 455 VKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELWPTWGGKVTkpQRGKLFYIPQRPYMTLGSLRD-QIIYPH--TREDM 531
Cdd:cd03268 16 LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEIT--FDGKSYQKNIEALRRIGALIEaPGFYPNltARENL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 532 RRN----GKTDEDLMQYLDIVQLTYLEHRENGLdaiedwidvLSGGEKQRIAMARLFYHSPQFAILDECTSAvsVDVEG- 606
Cdd:cd03268 94 RLLarllGIRKKRIDEVLDVVGLKDSAKKKVKG---------FSLGMKQRLGIALALLGNPDLLILDEPTNG--LDPDGi 162
|
170 180
....*....|....*....|..
gi 1678143030 607 ----KMYSYCREAGITLFTVSH 624
Cdd:cd03268 163 kelrELILSLRDQGITVLISSH 184
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
436-625 |
2.21e-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: 79.36 E-value: 2.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 436 DNIIKFENVpLVTPNGDVLVKDLTFEVKSGTNVLVCGPNGCGKSSLFRIL-GELWPTWGGKVT---KpQRGK--LFYIPQ 509
Cdd:COG1119 1 DPLLELRNV-TVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLItGDLPPTYGNDVRlfgE-RRGGedVWELRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 510 RpymtLG----SLRDQIIYPHTREDMRRNGK----------TDEDL---MQYLDIVQLTYLEHREngldaiedwIDVLSG 572
Cdd:COG1119 79 R----IGlvspALQLRFPRDETVLDVVLSGFfdsiglyrepTDEQReraRELLELLGLAHLADRP---------FGTLSQ 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1678143030 573 GEKQRIAMARLFYHSPQFAILDECTSavSVDVEGK------MYSYCREAGITLFTVSHR 625
Cdd:COG1119 146 GEQRRVLIARALVKDPELLILDEPTA--GLDLGARelllalLDKLAAEGAPTLVLVTHH 202
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
437-624 |
3.52e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 78.62 E-value: 3.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 437 NIIKFENVPLVTPNGDVLvKDLTFEVKSGTNVLVCGPNGCGKSSLFR-ILGELWPTwGGKVTKPQRGKLFYIPQRPYM-- 513
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVL-SDVSLELKPGKILTLLGPNGAGKSTLVRvVLGLVAPD-EGVIKRNGKLRIGYVPQKLYLdt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 514 TLgslrdqiiyPHT--REDMRRNGKTDEDLMQYLDIVQLTYLehrengldaIEDWIDVLSGGEKQRIAMARLFYHSPQFA 591
Cdd:PRK09544 81 TL---------PLTvnRFLRLRPGTKKEDILPALKRVQAGHL---------IDAPMQKLSGGETQRVLLARALLNRPQLL 142
|
170 180 190
....*....|....*....|....*....|....*....
gi 1678143030 592 ILDECTSAvsVDVEGKMYSY------CREAGITLFTVSH 624
Cdd:PRK09544 143 VLDEPTQG--VDVNGQVALYdlidqlRRELDCAVLMVSH 179
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
455-624 |
1.20e-15 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 76.64 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 455 VKDLTFEVKSGTnvLVC--GPNGCGKSSLFRIL-GELWPTwGGKVT----------KPQRGKLFYIPQRP--YMTLgSLR 519
Cdd:COG1131 16 LDGVSLTVEPGE--IFGllGPNGAGKTTTIRMLlGLLRPT-SGEVRvlgedvardpAEVRRRIGYVPQEPalYPDL-TVR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 520 DQI-----IYPHTREDMRrngktdEDLMQYLDIVQLTylehrenglDAIEDWIDVLSGGEKQRIAMARLFYHSPQFAILD 594
Cdd:COG1131 92 ENLrffarLYGLPRKEAR------ERIDELLELFGLT---------DAADRKVGTLSGGMKQRLGLALALLHDPELLILD 156
|
170 180 190
....*....|....*....|....*....|....*
gi 1678143030 595 ECTSAvsVDVEG--KMYSYCRE---AGITLFTVSH 624
Cdd:COG1131 157 EPTSG--LDPEArrELWELLRElaaEGKTVLLSTH 189
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
449-624 |
1.42e-15 |
|
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: 75.54 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 449 PNGDVLVKDLTFEVKSGTNVLVCGPNGCGKSSLFRIL-GELWPT-----WGGKVTKPQRGKLFYIPQRPYMTLGSLRDQI 522
Cdd:TIGR01166 2 PGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLnGLLRPQsgavlIDGEPLDYSRKGLLERRQRVGLVFQDPDDQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 523 IYPHTREDMR---RN-GKTDEDLM----QYLDIVQLTYLEHREngldaiedwIDVLSGGEKQRIAMARLFYHSPQFAILD 594
Cdd:TIGR01166 82 FAADVDQDVAfgpLNlGLSEAEVErrvrEALTAVGASGLRERP---------THCLSGGEKKRVAIAGAVAMRPDVLLLD 152
|
170 180 190
....*....|....*....|....*....|....*
gi 1678143030 595 ECTSAvsVDVEG-----KMYSYCREAGITLFTVSH 624
Cdd:TIGR01166 153 EPTAG--LDPAGreqmlAILRRLRAEGMTVVISTH 185
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
438-624 |
1.57e-15 |
|
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: 76.39 E-value: 1.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 438 IIKFENVPLVTPNGD---VLVKDLTFEVKSGTNVLVCGPNGCGKSSLFRIL--------------GELWPTWGGKVTKPQ 500
Cdd:cd03257 1 LLEVKNLSVSFPTGGgsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAIlgllkptsgsiifdGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 501 RGKLFYIPQRPY------MTLGslrDQIiyphtREDMRRNGKTDEDlmQYLDIVQLTYLEHRenGLDaiEDWIDV----L 570
Cdd:cd03257 81 RKEIQMVFQDPMsslnprMTIG---EQI-----AEPLRIHGKLSKK--EARKEAVLLLLVGV--GLP--EEVLNRypheL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1678143030 571 SGGEKQRIAMARLFYHSPQFAILDECTSAVSVDVEGK----MYSYCREAGITLFTVSH 624
Cdd:cd03257 147 SGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQildlLKKLQEELGLTLLFITH 204
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
454-599 |
3.68e-15 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 75.92 E-value: 3.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 454 LVKDLTFEVKSGTNVLVCGPNGCGKSSLFRIL-GELWPTwGGKVT---------KPQ-----RGKLfyiPQRPYMTLGSL 518
Cdd:COG4559 16 LLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLtGELTPS-SGEVRlngrplaawSPWelarrRAVL---PQHSSLAFPFT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 519 RDQII----YPHTREdmrrNGKTDEDLMQYLDIVQLTYLEHREngldaiedwIDVLSGGEKQRIAMARLF-------YHS 587
Cdd:COG4559 92 VEEVValgrAPHGSS----AAQDRQIVREALALVGLAHLAGRS---------YQTLSGGEQQRVQLARVLaqlwepvDGG 158
|
170
....*....|..
gi 1678143030 588 PQFAILDECTSA 599
Cdd:COG4559 159 PRWLFLDEPTSA 170
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
451-595 |
3.74e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 78.57 E-value: 3.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 451 GDVLVKDLTFEVKSGTNVLVCGPNGCGKSSLFRIL-GELWPTwGGKVTKPQRGKLFYIPQRPYMTLG-SLRDQII--YPH 526
Cdd:COG0488 10 GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILaGELEPD-SGEVSIPKGLRIGYLPQEPPLDDDlTVLDTVLdgDAE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 527 TREDMRR-------NGKTDEDLMQYLDivqltyLEHRengLDAIEDW-----------------------IDVLSGGEKQ 576
Cdd:COG0488 89 LRALEAEleeleakLAEPDEDLERLAE------LQEE---FEALGGWeaearaeeilsglgfpeedldrpVSELSGGWRR 159
|
170
....*....|....*....
gi 1678143030 577 RIAMARLFYHSPQFAILDE 595
Cdd:COG0488 160 RVALARALLSEPDLLLLDE 178
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
439-625 |
5.26e-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: 74.37 E-value: 5.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 439 IKFENVPL-VTPNGDVLVKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELWPTWGGKVT-----------KPQRGKLFY 506
Cdd:cd03369 7 IEVENLSVrYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEidgidistiplEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 507 IPQRPYMTLGSLRDQIiyphTREDMrrngKTDEDLMQYLDIvqltylehRENGLDaiedwidvLSGGEKQRIAMARLFYH 586
Cdd:cd03369 87 IPQDPTLFSGTIRSNL----DPFDE----YSDEEIYGALRV--------SEGGLN--------LSQGQRQLLCLARALLK 142
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1678143030 587 SPQFAILDECTSAVSVDVEGKMYSYCRE--AGITLFTVSHR 625
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREefTNSTILTIAHR 183
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
438-597 |
5.43e-15 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 74.70 E-value: 5.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 438 IIKFENVPLVTPNGDVLVKDLTFEVKSGTNVLVCGPNGCGKSSLFR-ILGELWPT-----WGGK-VTKPQRGKLfyipqr 510
Cdd:COG2884 1 MIRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKlLYGEERPTsgqvlVNGQdLSRLKRREI------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 511 PYM--TLG------------SLRDQIIYP-----HTREDMRRngktdeDLMQYLDIVQLtylEHRENGLdaiedwIDVLS 571
Cdd:COG2884 75 PYLrrRIGvvfqdfrllpdrTVYENVALPlrvtgKSRKEIRR------RVREVLDLVGL---SDKAKAL------PHELS 139
|
170 180
....*....|....*....|....*.
gi 1678143030 572 GGEKQRIAMARLFYHSPQFAILDECT 597
Cdd:COG2884 140 GGEQQRVAIARALVNRPELLLADEPT 165
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
439-624 |
5.58e-15 |
|
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: 74.52 E-value: 5.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 439 IKFENVPLVTPNGDVLvKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELWP-----TWGGKVT---------------- 497
Cdd:cd03260 1 IELRDLNVYYGDKHAL-KDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLldgkdiydldvdvlel 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 498 KPQRGKLFyipQRPYMTLGSLRDQIIYPHTREDMRRNGKTDEDLMQYLDIVQLTYLEHREngLDAIEdwidvLSGGEKQR 577
Cdd:cd03260 80 RRRVGMVF---QKPNPFPGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKDR--LHALG-----LSGGQQQR 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1678143030 578 IAMARLFYHSPQFAILDECTSAV----SVDVEGKMYSYCREagITLFTVSH 624
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALdpisTAKIEELIAELKKE--YTIVIVTH 198
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
439-627 |
5.61e-15 |
|
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: 74.96 E-value: 5.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 439 IKFENVPL-VTPNGDVLVKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELWPTWGGKVT-----------KPQRGKLFY 506
Cdd:cd03251 1 VEFKNVTFrYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILidghdvrdytlASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 507 IPQRPYMTLGSLRDQIIYPhtredmrRNGKTDEDLMQYLDIVQLT-YLEHRENGLDA-IEDWIDVLSGGEKQRIAMARLF 584
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYG-------RPGATREEVEEAARAANAHeFIMELPEGYDTvIGERGVKLSGGQRQRIAIARAL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1678143030 585 YHSPQFAILDECTSAvsVDVEGKMysYCREA------GITLFTVSHRKS 627
Cdd:cd03251 154 LKDPPILILDEATSA--LDTESER--LVQAAlerlmkNRTTFVIAHRLS 198
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
439-627 |
8.51e-15 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 74.50 E-value: 8.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 439 IKFENVPLVTPN-GDVLV-KDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELWPTWGGKVT-----------KPQRGKLF 505
Cdd:cd03249 1 IEFKNVSFRYPSrPDVPIlKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILldgvdirdlnlRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 506 YIPQRPYMTLGSLRDQIIYPhtredmrRNGKTDEDLMQYLDIVqltylehreNGLDAIEDWID-----------VLSGGE 574
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYG-------KPDATDEEVEEAAKKA---------NIHDFIMSLPDgydtlvgergsQLSGGQ 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1678143030 575 KQRIAMARLFYHSPQFAILDECTSAVSVDVEGKMYSYCREA--GITLFTVSHRKS 627
Cdd:cd03249 145 KQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAmkGRTTIVIAHRLS 199
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
451-624 |
9.27e-15 |
|
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: 73.30 E-value: 9.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 451 GDVLVKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELWPTWGGKVTKPQRGKLFYIP--QRPYMTLGSLRDQIIYPHTR 528
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDsiARGLLYLGHAPGIKTTLSVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 529 EDMR--RNGKTDEDLMQYLDIVQLTYLEHRENGldaiedwidVLSGGEKQRIAMARLFYHSPQFAILDECTSAV---SVD 603
Cdd:cd03231 92 ENLRfwHADHSDEQVEEALARVGLNGFEDRPVA---------QLSAGQQRRVALARLLLSGRPLWILDEPTTALdkaGVA 162
|
170 180
....*....|....*....|..
gi 1678143030 604 -VEGKMYSYCREAGITLFTVSH 624
Cdd:cd03231 163 rFAEAMAGHCARGGMVVLTTHQ 184
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
439-624 |
9.70e-15 |
|
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: 74.20 E-value: 9.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 439 IKFENVPlVTPNGDVLVKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELwptwggkvTKPQRGKLFY---------IPQ 509
Cdd:cd03300 1 IELENVS-KFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGF--------ETPTSGEILLdgkditnlpPHK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 510 RPYMTLgsLRDQIIYPH-TRED-------MRRNGKTD--EDLMQYLDIVQLTYLEHREngldaiedwIDVLSGGEKQRIA 579
Cdd:cd03300 72 RPVNTV--FQNYALFPHlTVFEniafglrLKKLPKAEikERVAEALDLVQLEGYANRK---------PSQLSGGQQQRVA 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1678143030 580 MARLFYHSPQFAILDECTSAVSVDVEGKMY----SYCREAGITLFTVSH 624
Cdd:cd03300 141 IARALVNEPKVLLLDEPLGALDLKLRKDMQlelkRLQKELGITFVFVTH 189
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
455-603 |
2.54e-14 |
|
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: 72.97 E-value: 2.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 455 VKDLTFEVKSGTNVLVCGPNGCGKSSLFRIL-GELWPTWG-------GKVTKPQ--RGKLFYIPQRPYMTLG-SLRDQII 523
Cdd:COG4555 17 LKDVSFTAKDGEITGLLGPNGAGKTTLLRMLaGLLKPDSGsilidgeDVRKEPReaRRQIGVLPDERGLYDRlTVRENIR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 524 YphTREDMRRNGKTDEDLMQYLDivqltylehRENGLDAIEDW-IDVLSGGEKQRIAMARLFYHSPQFAILDECTSAVSV 602
Cdd:COG4555 97 Y--FAELYGLFDEELKKRIEELI---------ELLGLEEFLDRrVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDV 165
|
.
gi 1678143030 603 D 603
Cdd:COG4555 166 M 166
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
451-595 |
2.74e-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: 2.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 451 GDVLVKDLTFEVKSGTNVLVCGPNGCGKSSLFRIL-GELWPTwGGKVTKPQRGKLFYIPQRpymtLGSLR-DQIIYPHTR 528
Cdd:COG0488 327 DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLaGELEPD-SGTVKLGETVKIGYFDQH----QEELDpDKTVLDELR 401
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 529 EDMRrnGKTDEDLMQYLdivqltylehrENGL---DAIEDWIDVLSGGEKQRIAMARLFYHSPQFAILDE 595
Cdd:COG0488 402 DGAP--GGTEQEVRGYL-----------GRFLfsgDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDE 458
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
436-624 |
4.18e-14 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 72.00 E-value: 4.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 436 DNIIKFENVPLVTPNGDVLV---KDLTFEVKSGTNVLVCGPNGCGKSSLFRILGEL-WPTwGGKVT----------KPQR 501
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVtalRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLdRPT-SGEVLidgqdisslsEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 502 GKL------FyIPQR----PYMTLgslRDQIIYPHTREDMRRnGKTDEDLMQYLDIVQLT-YLEHRengldaiedwIDVL 570
Cdd:COG1136 81 ARLrrrhigF-VFQFfnllPELTA---LENVALPLLLAGVSR-KERRERARELLERVGLGdRLDHR----------PSQL 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1678143030 571 SGGEKQRIAMARLFYHSPQFAILDECTSAV----SVDVEGKMYSYCREAGITLFTVSH 624
Cdd:COG1136 146 SGGQQQRVAIARALVNRPKLILADEPTGNLdsktGEEVLELLRELNRELGTTIVMVTH 203
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
439-624 |
6.47e-14 |
|
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: 69.40 E-value: 6.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 439 IKFENVpLVTPNGDVLVKDLTFEVKSGTNVLVCGPNGCGKSSLFRIL-GELWPTwGGKVTKPQRGKLFYIPQrpymtlgs 517
Cdd:cd03221 1 IELENL-SKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIaGELEPD-EGIVTWGSTVKIGYFEQ-------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 518 lrdqiiyphtredmrrngktdedlmqyldivqltylehrengldaiedwidvLSGGEKQRIAMARLFYHSPQFAILDECT 597
Cdd:cd03221 71 ----------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPT 98
|
170 180
....*....|....*....|....*....
gi 1678143030 598 SavSVDVEGK--MYSYCREAGITLFTVSH 624
Cdd:cd03221 99 N--HLDLESIeaLEEALKEYPGTVILVSH 125
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
439-625 |
6.76e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 74.88 E-value: 6.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 439 IKFENVPLVTPNGDVLVKDLTFEVKSGTNVLVCGPNGCGKSSLFR-ILG----------------ELWPT-Wggkvtkpq 500
Cdd:PRK11174 350 IEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNaLLGflpyqgslkingielrELDPEsW-------- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 501 RGKLFYIPQRPYMTLGSLRDQIIyphtredMRRNGKTDEDLMQYLDIVQLT-YLEHRENGLD-AIEDWIDVLSGGEKQRI 578
Cdd:PRK11174 422 RKHLSWVGQNPQLPHGTLRDNVL-------LGNPDASDEQLQQALENAWVSeFLPLLPQGLDtPIGDQAAGLSVGQAQRL 494
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1678143030 579 AMARLFYHSPQFAILDECTSAVSVDVEGKMYSYCREA--GITLFTVSHR 625
Cdd:PRK11174 495 ALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAAsrRQTTLMVTHQ 543
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
439-655 |
1.19e-13 |
|
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: 70.98 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 439 IKFENVPL-VTPNGDVLVKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELWPTWGGKV-----------TKPQRGKLFY 506
Cdd:cd03252 1 ITFEHVRFrYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVlvdghdlaladPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 507 IPQRPYMTLGSLRDQIIYPHTREDMRRNGKTDEDLMQYLDIVQL-----TYLEHRENGLdaiedwidvlSGGEKQRIAMA 581
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELpegydTIVGEQGAGL----------SGGQRQRIAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678143030 582 RLFYHSPQFAILDECTSAVSVDVE----GKMYSYCreAGITLFTVSHRKSLWVHHDFFLQFDGrgnyefGRIDQDKEH 655
Cdd:cd03252 151 RALIHNPRILIFDEATSALDYESEhaimRNMHDIC--AGRTVIIIAHRLSTVKNADRIIVMEK------GRIVEQGSH 220
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
455-624 |
2.25e-13 |
|
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: 68.58 E-value: 2.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 455 VKDLTFEVKSGTNVLVCGPNGCGKSSLFRIL-GELWPTwGGKVT----------KPQRGKLFYIPQRPYmtlgslrdqiI 523
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIIlGLLKPD-SGEIKvlgkdikkepEEVKRRIGYLPEEPS----------L 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 524 YPHtredmrrngktdedlmqyldivqLTYLEHrengLDaiedwidvLSGGEKQRIAMARLFYHSPQFAILDECTSAvsVD 603
Cdd:cd03230 85 YEN-----------------------LTVREN----LK--------LSGGMKQRLALAQALLHDPELLILDEPTSG--LD 127
|
170 180
....*....|....*....|....*..
gi 1678143030 604 VEGK------MYSYcREAGITLFTVSH 624
Cdd:cd03230 128 PESRrefwelLREL-KKEGKTILLSSH 153
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
450-621 |
5.25e-13 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 68.15 E-value: 5.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 450 NGDVLVKDLTFEVKSGTNVLVCGPNGCGKSSLFRIL-GELWPT-----WGGKVTKPQRGK----LFYIPQRPYM-TLGSL 518
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILaGLLRPDsgevrWNGTPLAEQRDEphenILYLGHLPGLkPELSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 519 RDQIIYPHtredmRRNGKTDEDLMQYLDIVQLTYLEHRENGldaiedwidVLSGGEKQRIAMARLFYHSPQFAILDECTS 598
Cdd:TIGR01189 91 LENLHFWA-----AIHGGAQRTIEDALAAVGLTGFEDLPAA---------QLSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
170 180
....*....|....*....|....*..
gi 1678143030 599 AVSVD----VEGKMYSYCREAGITLFT 621
Cdd:TIGR01189 157 ALDKAgvalLAGLLRAHLARGGIVLLT 183
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
436-625 |
6.91e-13 |
|
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: 71.47 E-value: 6.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 436 DNIIKFENVPLVTPNGDV-LVKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELWP---TWGGKV----------TKPQR 501
Cdd:COG1123 2 TPLLEVRDLSVRYPGGDVpAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPhggRISGEVlldgrdllelSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 502 GKLF-YIPQRPYMTLGSLR--DQIIyphtreDMRRNGKTDEDLMQYLDIVQLtylehRENGLDAIED-WIDVLSGGEKQR 577
Cdd:COG1123 82 GRRIgMVFQDPMTQLNPVTvgDQIA------EALENLGLSRAEARARVLELL-----EAVGLERRLDrYPHQLSGGQRQR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1678143030 578 IAMARLFYHSPQFAILDECTSA----VSVDVEGKMYSYCREAGITLFTVSHR 625
Cdd:COG1123 151 VAIAMALALDPDLLIADEPTTAldvtTQAEILDLLRELQRERGTTVLLITHD 202
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
457-617 |
9.24e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 71.93 E-value: 9.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 457 DLTFEVKSGTNVLVCGPNGCGKSSLFR-ILGELWPTWGGKVTKpqRGKLFYIPQRPYMTLGSLRDQIIYPHTREDMRRNG 535
Cdd:PLN03232 635 DINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVI--RGSVAYVPQVSWIFNATVRENILFGSDFESERYWR 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 536 KTDEDLMQY-LDIV---QLTylEHRENGLDaiedwidvLSGGEKQRIAMARLFYHSPQFAILDECTSAVSVDVEGKMYSY 611
Cdd:PLN03232 713 AIDVTALQHdLDLLpgrDLT--EIGERGVN--------ISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDS 782
|
....*.
gi 1678143030 612 CREAGI 617
Cdd:PLN03232 783 CMKDEL 788
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
450-599 |
1.54e-12 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 67.87 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 450 NGDVLVKDLTFEVKSGTNVLVCGPNGCGKSSLFRIL-GELWPTwGGKVT---------KPQ-----RGKLfyiPQRPYMT 514
Cdd:PRK13548 13 GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALsGELSPD-SGEVRlngrpladwSPAelarrRAVL---PQHSSLS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 515 LGSLRDQII----YPHTredmRRNGKTDEDLMQYLDIVQLTYLEHREngldaiedwIDVLSGGEKQRIAMARLF------ 584
Cdd:PRK13548 89 FPFTVEEVVamgrAPHG----LSRAEDDALVAAALAQVDLAHLAGRD---------YPQLSGGEQQRVQLARVLaqlwep 155
|
170
....*....|....*
gi 1678143030 585 YHSPQFAILDECTSA 599
Cdd:PRK13548 156 DGPPRWLLLDEPTSA 170
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
156-604 |
1.80e-12 |
|
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: 71.13 E-value: 1.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 156 LRFRTNLTHHLYNQYLTGYTYYKMSNLDNRIANadqLLTTDIDKFCESATELYSNISKPvLDIFIYVYRLTVNLGgktPS 235
Cdd:TIGR00957 387 MRIKTAVMGAVYRKALVITNSARKSSTVGEIVN---LMSVDAQRFMDLATYINMIWSAP-LQVILALYFLWLNLG---PS 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 236 IL-----MIYLL-FAGVLLTRMRRptgrLTVEEQKLEgefryvNSRLITNSEEVafyqgnarEKLTLLASYSKLRSHLRK 309
Cdd:TIGR00957 460 VLagvavMVLMVpLNAVMAMKTKT----YQVAHMKSK------DNRIKLMNEIL--------NGIKVLKLYAWELAFLDK 521
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 310 FLEFRVG-MGIVDNivGKYFASIVGFYAVSIPFFT------------PNHpLLSGENQGQRLQAYYTYGRMLIKLAEAIG 376
Cdd:TIGR00957 522 VEGIRQEeLKVLKK--SAYLHAVGTFTWVCTPFLValitfavyvtvdENN-ILDAEKAFVSLALFNILRFPLNILPMVIS 598
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 377 RLVLAGREMTRLAGFTARmtelikvlNDLNKGTYERTMVNnvvngnsdfgPGKGamefvdNIIKFENVPLVTPNGDV-LV 455
Cdd:TIGR00957 599 SIVQASVSLKRLRIFLSH--------EELEPDSIERRTIK----------PGEG------NSITVHNATFTWARDLPpTL 654
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 456 KDLTFEVKSGTNVLVCGPNGCGKSSLFR-ILGELwPTWGGKVTkpQRGKLFYIPQRPYMTLGSLRDQIIYPHTREDmRRN 534
Cdd:TIGR00957 655 NGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEM-DKVEGHVH--MKGSVAYVPQQAWIQNDSLRENILFGKALNE-KYY 730
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 535 GKTDEDLMQYLDIVQLTYLEHRENGLDAIEdwidvLSGGEKQRIAMARLFYHSPQFAILDECTSAVSVDV 604
Cdd:TIGR00957 731 QQVLEACALLPDLEILPSGDRTEIGEKGVN-----LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHV 795
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
450-624 |
2.08e-12 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 66.10 E-value: 2.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 450 NGDVLVKDLTFEVKSGTNVLVCGPNGCGKSSLFRIL-GELWPTwGGKVTKPQRGKLFYIPQR-------PY-----MTLG 516
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLaGVLRPT-SGTVRRAGGARVAYVPQRsevpdslPLtvrdlVAMG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 517 SLRDQIIY-PHTREDMRRngktdedLMQYLDIVQLTYLEHREngldaiedwIDVLSGGEKQRIAMARLFYHSPQFAILDE 595
Cdd:NF040873 82 RWARRGLWrRLTRDDRAA-------VDDALERVGLADLAGRQ---------LGELSGGQRQRALLAQGLAQEADLLLLDE 145
|
170 180 190
....*....|....*....|....*....|..
gi 1678143030 596 CTSAVSVDVEGKMYSYCREA---GITLFTVSH 624
Cdd:NF040873 146 PTTGLDAESRERIIALLAEEharGATVVVVTH 177
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
439-597 |
2.99e-12 |
|
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: 66.28 E-value: 2.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 439 IKFENVPLVTPNGDVLVKDLTFEVKSGTNVLVCGPNGCGKSSLFR-ILGELWPTWG-----GK-VTKPQRGKLFYIPQRP 511
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKlIYKEELPTSGtirvnGQdVSDLRGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 512 YMTLGSLR---DQIIYPHTREDMRRNGKTDEDLMQYL-DIVQLTYLEHRENGLDAiedwidVLSGGEKQRIAMARLFYHS 587
Cdd:cd03292 81 GVVFQDFRllpDRNVYENVAFALEVTGVPPREIRKRVpAALELVGLSHKHRALPA------ELSGGEQQRVAIARAIVNS 154
|
170
....*....|
gi 1678143030 588 PQFAILDECT 597
Cdd:cd03292 155 PTILIADEPT 164
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
439-624 |
3.36e-12 |
|
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: 65.29 E-value: 3.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 439 IKFENVPlVTPNGDVLVKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELWPTWGGKVT-------------KPQRGKLF 505
Cdd:cd03229 1 LELKNVS-KRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILidgedltdledelPPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 506 YIPQRPymtlgslrdqIIYPHtredmrrngktdedlMQYLDIVQLtylehrengldaiedwidVLSGGEKQRIAMARLFY 585
Cdd:cd03229 80 MVFQDF----------ALFPH---------------LTVLENIAL------------------GLSGGQQQRVALARALA 116
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1678143030 586 HSPQFAILDECTSA----VSVDVEGKMYSYCREAGITLFTVSH 624
Cdd:cd03229 117 MDPDVLLLDEPTSAldpiTRREVRALLKSLQAQLGITVVLVTH 159
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
455-633 |
3.51e-12 |
|
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: 66.59 E-value: 3.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 455 VKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELWPTWGGKVT---------KPQRGKLFYIPQR----PYMTLgslRDQ 521
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILfggedatdvPVQERNVGFVFQHyalfRHMTV---FDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 522 IIYP-HTREDMRRNGKT--DEDLMQYLDIVQLTYLEHRengldaiedWIDVLSGGEKQRIAMARLFYHSPQFAILDECTS 598
Cdd:cd03296 95 VAFGlRVKPRSERPPEAeiRAKVHELLKLVQLDWLADR---------YPAQLSGGQRQRVALARALAVEPKVLLLDEPFG 165
|
170 180 190
....*....|....*....|....*....|....*
gi 1678143030 599 AVSVDVEGKMYSYCREagitLFTVSHRKSLWVHHD 633
Cdd:cd03296 166 ALDAKVRKELRRWLRR----LHDELHVTTVFVTHD 196
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
450-599 |
6.06e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 65.28 E-value: 6.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 450 NGDVLVKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELWPTWGGKVTKPQRGklfyipqrpyMTLGSLRDQIIYPHTRE 529
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD----------IDDPDVAEACHYLGHRN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 530 DMRRN--------------GKTDEDLMQYLDIVQLTYLEHRENGldaiedwidVLSGGEKQRIAMARLF-YHSPQFaILD 594
Cdd:PRK13539 83 AMKPAltvaenlefwaaflGGEELDIAAALEAVGLAPLAHLPFG---------YLSAGQKRRVALARLLvSNRPIW-ILD 152
|
....*
gi 1678143030 595 ECTSA 599
Cdd:PRK13539 153 EPTAA 157
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
454-624 |
9.08e-12 |
|
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: 64.59 E-value: 9.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 454 LVKDLTFEVKSGTNVLVCGPNGCGKSSLFRIL-GELWPT-----WGGKVTKP--QRGKLFYIPQRPYMTLG--SLRDQII 523
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILaGLIKESsgsilLNGKPIKAkeRRKSIGYVMQDVDYQLFtdSVREELL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 524 YphTREDMRRNGKTDEDLMQYLDIVQLtyleHRENGLDaiedwidvLSGGEKQRIAMARLFYHSPQFAILDECTSAV--- 600
Cdd:cd03226 95 L--GLKELDAGNEQAETVLKDLDLYAL----KERHPLS--------LSGGQKQRLAIAAALLSGKDLLIFDEPTSGLdyk 160
|
170 180
....*....|....*....|....
gi 1678143030 601 SVDVEGKMYSYCREAGITLFTVSH 624
Cdd:cd03226 161 NMERVGELIRELAAQGKAVIVITH 184
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
436-612 |
1.75e-11 |
|
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: 67.63 E-value: 1.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 436 DNIIKFENVPL-VTPngdvLVKDLTFEVKSGTNVLVCGPNGCGKSSLFR-ILGELWPTwGGKVTkpQRGKLFYIPQRPYM 513
Cdd:TIGR01271 426 DDGLFFSNFSLyVTP----VLKNISFKLEKGQLLAVAGSTGSGKSSLLMmIMGELEPS-EGKIK--HSGRISFSPQTSWI 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 514 TLGSLRDQIIYPHTREDMRrngktdedlmqYLDIVQLTYLEHR-----ENGLDAIEDWIDVLSGGEKQRIAMARLFYHSP 588
Cdd:TIGR01271 499 MPGTIKDNIIFGLSYDEYR-----------YTSVIKACQLEEDialfpEKDKTVLGEGGITLSGGQRARISLARAVYKDA 567
|
170 180
....*....|....*....|....
gi 1678143030 589 QFAILDECTSAVSVDVEGKMYSYC 612
Cdd:TIGR01271 568 DLYLLDSPFTHLDVVTEKEIFESC 591
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
451-625 |
1.76e-11 |
|
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: 62.83 E-value: 1.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 451 GDVLV-KDLTFEVKSGTNVLVCGPNGCGKSSLFRIL-GELWPTwGGKVTkpqrgklfyipqrpymtlgsLRDQIIYPHTR 528
Cdd:cd03216 11 GGVKAlDGVSLSVRRGEVHALLGENGAGKSTLMKILsGLYKPD-SGEIL--------------------VDGKEVSFASP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 529 EDMRRNGktdedlmqyldiVQLTYLehrengldaiedwidvLSGGEKQRIAMARLFYHSPQFAILDECTSAVSVDVEGKM 608
Cdd:cd03216 70 RDARRAG------------IAMVYQ----------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERL 121
|
170 180
....*....|....*....|
gi 1678143030 609 YSYCR---EAGITLFTVSHR 625
Cdd:cd03216 122 FKVIRrlrAQGVAVIFISHR 141
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
453-633 |
2.05e-11 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 65.90 E-value: 2.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 453 VLVKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELwptwggkvTKPQRGKLFY---------IPQR------------P 511
Cdd:PRK11432 20 TVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGL--------EKPTEGQIFIdgedvthrsIQQRdicmvfqsyalfP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 512 YMTLGslrDQIIYphtreDMRRNGKTDEDLMQY----LDIVQLTYLEHRengldaiedWIDVLSGGEKQRIAMARLFYHS 587
Cdd:PRK11432 92 HMSLG---ENVGY-----GLKMLGVPKEERKQRvkeaLELVDLAGFEDR---------YVDQISGGQQQRVALARALILK 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1678143030 588 PQFAILDECTSAVSVDVEGKMYSYCREA----GITlftvshrkSLWVHHD 633
Cdd:PRK11432 155 PKVLLFDEPLSNLDANLRRSMREKIRELqqqfNIT--------SLYVTHD 196
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
454-582 |
2.09e-11 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 65.94 E-value: 2.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 454 LVKDLTFEVKSGTNVLVCGPNGCGKSSLFRIL-GELWPTWG-----GKVTK----PQRGK---------LFyipqrPYMT 514
Cdd:COG1118 17 LLDDVSLEIASGELVALLGPSGSGKTTLLRIIaGLETPDSGrivlnGRDLFtnlpPRERRvgfvfqhyaLF-----PHMT 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1678143030 515 LgslRDQI-----IYPHTREDMRrngktdEDLMQYLDIVQLTYLEHR---EngldaiedwidvLSGGEKQRIAMAR 582
Cdd:COG1118 92 V---AENIafglrVRPPSKAEIR------ARVEELLELVQLEGLADRypsQ------------LSGGQRQRVALAR 146
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
455-636 |
2.14e-11 |
|
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: 63.89 E-value: 2.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 455 VKDLTFEVKSGTNVLVCGPNGCGKSSLF-RILGELwPTWGGKV---------------TKPQRGKLFYIPQRPYMTLGSL 518
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEM-QTLEGKVhwsnknesepsfeatRSRNRYSVAYAAQKPWLLNATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 519 RDQIIYPHTREDMRRNGKTDEDLMQyLDIVQLTYLEHRENGLDAIEdwidvLSGGEKQRIAMARLFYHSPQFAILDECTS 598
Cdd:cd03290 96 EENITFGSPFNKQRYKAVTDACSLQ-PDIDLLPFGDQTEIGERGIN-----LSGGQRQRICVARALYQNTNIVFLDDPFS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1678143030 599 AVSVDV------EGkMYSYCREAGITLFTVSHRKSLWVHHDFFL 636
Cdd:cd03290 170 ALDIHLsdhlmqEG-ILKFLQDDKRTLVLVTHKLQYLPHADWII 212
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
439-624 |
2.96e-11 |
|
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: 64.13 E-value: 2.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 439 IKFENVPLVTPNGDVLVKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELwptwggkvTKPQRGKLFY----IPQRPYMT 514
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGL--------VEPTSGSVLIdgtdINKLKGKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 515 LGSLRDQI--IYPHTREDMRRNGKTDEdLMQYLD-------IVQLTYLEHRENGLDAIEDW---------IDVLSGGEKQ 576
Cdd:cd03256 73 LRQLRRQIgmIFQQFNLIERLSVLENV-LSGRLGrrstwrsLFGLFPKEEKQRALAALERVglldkayqrADQLSGGQQQ 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1678143030 577 RIAMARLFYHSPQFAILDECTSAV----SVDVEGKMYSYCREAGITLFTVSH 624
Cdd:cd03256 152 RVAIARALMQQPKLILADEPVASLdpasSRQVMDLLKRINREEGITVIVSLH 203
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
455-624 |
3.50e-11 |
|
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: 63.64 E-value: 3.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 455 VKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGEL-WPTWGG------KVTKP--------QRGKLFyipqrPYMTLgslR 519
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLaQPTSGGvilegkQITEPgpdrmvvfQNYSLL-----PWLTV---R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 520 DQI------IYPHTREDMRRngktdEDLMQYLDIVQLTYLEHREngldaiedwIDVLSGGEKQRIAMARLFYHSPQFAIL 593
Cdd:TIGR01184 73 ENIalavdrVLPDLSKSERR-----AIVEEHIALVGLTEAADKR---------PGQLSGGMKQRVAIARALSIRPKVLLL 138
|
170 180 190
....*....|....*....|....*....|....*
gi 1678143030 594 DECTSAVSV----DVEGKMYSYCREAGITLFTVSH 624
Cdd:TIGR01184 139 DEPFGALDAltrgNLQEELMQIWEEHRVTVLMVTH 173
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
436-624 |
5.39e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 63.65 E-value: 5.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 436 DNIIKFENVPLVTPnGDVLVKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELWPTWGGKVTKPQR------GKLF---- 505
Cdd:PRK10575 9 DTTFALRNVSFRVP-GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQpleswsSKAFarkv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 506 -YIPQR-PY---MTLGSLRDQIIYP-HTRedMRRNGKTD-EDLMQYLDIVQLTYLEHRengldaiedWIDVLSGGEKQRI 578
Cdd:PRK10575 88 aYLPQQlPAaegMTVRELVAIGRYPwHGA--LGRFGAADrEKVEEAISLVGLKPLAHR---------LVDSLSGGERQRA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1678143030 579 AMARLFYHSPQFAILDECTSAV----SVDVEGKMYSYCREAGITLFTVSH 624
Cdd:PRK10575 157 WIAMLVAQDSRCLLLDEPTSALdiahQVDVLALVHRLSQERGLTVIAVLH 206
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
451-634 |
5.51e-11 |
|
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: 63.12 E-value: 5.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 451 GDVLVKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELWPTWGGKVT---------KPQRGKLFYIPQR----PYMTLgs 517
Cdd:cd03299 11 KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILlngkditnlPPEKRDISYVPQNyalfPHMTV-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 518 lRDQIIYPhTREDMRRNGKTDEDLMQYLDIVQLTYLEHRENGldaiedwidVLSGGEKQRIAMARLFYHSPQFAILDECT 597
Cdd:cd03299 89 -YKNIAYG-LKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPE---------TLSGGEQQRVAIARALVVNPKILLLDEPF 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 1678143030 598 SAVSVDVEGKMYSYCREAGITL-FTVSHrkslwVHHDF 634
Cdd:cd03299 158 SALDVRTKEKLREELKKIRKEFgVTVLH-----VTHDF 190
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
451-630 |
6.25e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 62.99 E-value: 6.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 451 GDVLVKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELWPTWGGKVT-------------KPQRGkLFYIPQRP--YMTL 515
Cdd:PRK10895 15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIiddedisllplhaRARRG-IGYLPQEAsiFRRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 516 GSLRDQIIYPHTREDMRRNGKTD--EDLMQYLDIvqltylEHRENGLDaiedwiDVLSGGEKQRIAMARLFYHSPQFAIL 593
Cdd:PRK10895 94 SVYDNLMAVLQIRDDLSAEQREDraNELMEEFHI------EHLRDSMG------QSLSGGERRRVEIARALAANPKFILL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1678143030 594 DECTSAVS----VDVEgKMYSYCREAGITLFTVSH--RKSLWV 630
Cdd:PRK10895 162 DEPFAGVDpisvIDIK-RIIEHLRDSGLGVLITDHnvRETLAV 203
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
436-612 |
6.33e-11 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 63.72 E-value: 6.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 436 DNIIKFENVPLVtpnGDVLVKDLTFEVKSGTNVLVCGPNGCGKSSLFR-ILGELWPTwGGKVTkpQRGKLFYIPQRPYMT 514
Cdd:cd03291 37 DNNLFFSNLCLV---GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMlILGELEPS-EGKIK--HSGRISFSSQFSWIM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 515 LGSLRDQIIYPHTREDMRrngktdedlmqYLDIVQLTYLEHR-------------ENGLdaiedwidVLSGGEKQRIAMA 581
Cdd:cd03291 111 PGTIKENIIFGVSYDEYR-----------YKSVVKACQLEEDitkfpekdntvlgEGGI--------TLSGGQRARISLA 171
|
170 180 190
....*....|....*....|....*....|.
gi 1678143030 582 RLFYHSPQFAILDECTSAVSVDVEGKMYSYC 612
Cdd:cd03291 172 RAVYKDADLYLLDSPFGYLDVFTEKEIFESC 202
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
388-608 |
8.73e-11 |
|
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: 65.15 E-value: 8.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 388 LAGFTARMTELIKVLNDLNKGTYERTMVNNVVNGNSDFGPGKGAMEfvdniikfenvpLVTPNGDVLVKDLTFEVKSGTN 467
Cdd:TIGR01193 421 LSYFLTPLENIINLQPKLQAARVANNRLNEVYLVDSEFINKKKRTE------------LNNLNGDIVINDVSYSYGYGSN 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 468 VL--------------VCGPNGCGKSSLFRILGELWPTWGGKVT-----------KPQRGKLFYIPQRPYMTLGSLRDQI 522
Cdd:TIGR01193 489 ILsdisltikmnskttIVGMSGSGKSTLAKLLVGFFQARSGEILlngfslkdidrHTLRQFINYLPQEPYIFSGSILENL 568
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 523 IYPHtredmrRNGKTDEDLMQYLDIVQL-TYLEHRENGLDA-IEDWIDVLSGGEKQRIAMARLFYHSPQFAILDECTSAV 600
Cdd:TIGR01193 569 LLGA------KENVSQDEIWAACEIAEIkDDIENMPLGYQTeLSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNL 642
|
....*...
gi 1678143030 601 SVDVEGKM 608
Cdd:TIGR01193 643 DTITEKKI 650
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
456-624 |
1.35e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 62.39 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 456 KDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELwptwggkvTKPQRGKLfyipqrpymtlgsLRDQIIYPHTREDMRrng 535
Cdd:PRK11247 29 NQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGL--------ETPSAGEL-------------LAGTAPLAEAREDTR--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 536 ktdedLM----------QYLDIVQLTYLEH-RENGLDAIE---------DWIDVLSGGEKQRIAMARLFYHSPQFAILDE 595
Cdd:PRK11247 85 -----LMfqdarllpwkKVIDNVGLGLKGQwRDAALQALAavgladranEWPAALSGGQKQRVALARALIHRPGLLLLDE 159
|
170 180 190
....*....|....*....|....*....|...
gi 1678143030 596 CTSAVS----VDVEGKMYSYCREAGITLFTVSH 624
Cdd:PRK11247 160 PLGALDaltrIEMQDLIESLWQQHGFTVLLVTH 192
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
453-624 |
2.10e-10 |
|
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: 61.01 E-value: 2.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 453 VLvKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELwptwggkvTKPQRGKLFY----IPQRPYmTLGSLRDQI------ 522
Cdd:cd03262 15 VL-KGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLL--------EEPDSGTIIIdglkLTDDKK-NINELRQKVgmvfqq 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 523 --IYPH-------TREDMRRNGKTDEDL----MQYLDIVQLtylehrengLDAIEDWIDVLSGGEKQRIAMARLFYHSPQ 589
Cdd:cd03262 85 fnLFPHltvleniTLAPIKVKGMSKAEAeeraLELLEKVGL---------ADKADAYPAQLSGGQQQRVAIARALAMNPK 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 1678143030 590 FAILDECTSA----VSVDVEGKMYSYCREaGITLFTVSH 624
Cdd:cd03262 156 VMLFDEPTSAldpeLVGEVLDVMKDLAEE-GMTMVVVTH 193
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
457-612 |
2.16e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 64.37 E-value: 2.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 457 DLTFEVKSGTNVLVCGPNGCGKSSLFR-ILGELWPTWGGKVTkpQRGKLFYIPQRPYMTLGSLRDQIIYPHTREDMRRNG 535
Cdd:PLN03130 635 NINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVV--IRGTVAYVPQVSWIFNATVRDNILFGSPFDPERYER 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 536 KTDEDLMQY-LDIV---QLTylEHRENGLDaiedwidvLSGGEKQRIAMARLFYHSPQFAILDECTSAVSVDVEGKMYSY 611
Cdd:PLN03130 713 AIDVTALQHdLDLLpggDLT--EIGERGVN--------ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDK 782
|
.
gi 1678143030 612 C 612
Cdd:PLN03130 783 C 783
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
455-625 |
2.24e-10 |
|
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: 60.76 E-value: 2.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 455 VKDLTFEVKSGTNVLVCGPNGCGKSSLFR-ILGELWPT-----WGGK-VTKPQRGKLFYIPQR----PYMTLgslRDQII 523
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRmILGIILPDsgevlFDGKpLDIAARNRIGYLPEErglyPKMKV---IDQLV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 524 Y-----PHTREDMRRngktdeDLMQYLDIVQLTylEHRENGLDAiedwidvLSGGEKQRIAMARLFYHSPQFAILDECTS 598
Cdd:cd03269 93 YlaqlkGLKKEEARR------RIDEWLERLELS--EYANKRVEE-------LSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190
....*....|....*....|....*....|
gi 1678143030 599 A---VSVDVEGKMYSYCREAGITLFTVSHR 625
Cdd:cd03269 158 GldpVNVELLKDVIRELARAGKTVILSTHQ 187
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
439-597 |
2.42e-10 |
|
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: 60.67 E-value: 2.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 439 IKFENVPLVTPNGDVLvKDLTFEVKSGTNVLVcGPNGCGKSSLFRILGELWPTWGGKVT--------KPQ--RGKLFYIP 508
Cdd:cd03264 1 LQLENLTKRYGKKRAL-DGVSLTLGPGMYGLL-GPNGAGKTTLMRILATLTPPSSGTIRidgqdvlkQPQklRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 509 QR----PYMTLgslRDQIIYPHTREDMRrNGKTDEDLMQYLDIVQLTYLEHREngldaiedwIDVLSGGEKQRIAMARLF 584
Cdd:cd03264 79 QEfgvyPNFTV---REFLDYIAWLKGIP-SKEVKARVDEVLELVNLGDRAKKK---------IGSLSGGMRRRVGIAQAL 145
|
170
....*....|...
gi 1678143030 585 YHSPQFAILDECT 597
Cdd:cd03264 146 VGDPSILIVDEPT 158
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
453-624 |
2.74e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 60.20 E-value: 2.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 453 VLVKDLTFEVKSGTNVLVCGPNGCGKSSLFRIL--------GELwpTWGGKVTKPQR----GKLFYIPQRP--------- 511
Cdd:PRK13538 15 ILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILaglarpdaGEV--LWQGEPIRRQRdeyhQDLLYLGHQPgikteltal 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 512 -----YMTLGSLRDqiiyphtredmrrngktDEDLMQYLDIVqltylehrenGLDAIEDW-IDVLSGGEKQRIAMARLFY 585
Cdd:PRK13538 93 enlrfYQRLHGPGD-----------------DEALWEALAQV----------GLAGFEDVpVRQLSAGQQRRVALARLWL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1678143030 586 HSPQFAILDECTSAVSV----DVEGKMYSYCREAGITLFTvSH 624
Cdd:PRK13538 146 TRAPLWILDEPFTAIDKqgvaRLEALLAQHAEQGGMVILT-TH 187
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
439-624 |
2.75e-10 |
|
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: 61.29 E-value: 2.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 439 IKFENVPLVTPNGDVLV-KDLTFEVKSGTNVLVCGPNGCGKSSLFRIL-GELWPTWG-----GKVTKpQRGKLFYIPQRP 511
Cdd:TIGR04520 1 IEVENVSFSYPESEKPAlKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLnGLLLPTSGkvtvdGLDTL-DEENLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 512 YMTLGSLRDQIIYPHTRED--------------MRRngKTDEdlmqYLDIVQLTYLEHRENGLdaiedwidvLSGGEKQR 577
Cdd:TIGR04520 80 GMVFQNPDNQFVGATVEDDvafglenlgvpreeMRK--RVDE----ALKLVGMEDFRDREPHL---------LSGGQKQR 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1678143030 578 IAMARLFYHSPQFAILDECTSAvsVDVEGK------MYSYCREAGITLFTVSH 624
Cdd:TIGR04520 145 VAIAGVLAMRPDIIILDEATSM--LDPKGRkevletIRKLNKEEGITVISITH 195
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
451-624 |
3.26e-10 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 62.04 E-value: 3.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 451 GDVL-VKDLTFEVKSGTnvLVC--GPNGCGKSSLFRIL-GELWPT-----WGGKV---TKPQRGKLFYIPQR----PYMT 514
Cdd:COG3842 16 GDVTaLDDVSLSIEPGE--FVAllGPSGCGKTTLLRMIaGFETPDsgrilLDGRDvtgLPPEKRNVGMVFQDyalfPHLT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 515 LG-----SLRdqiiyphtredMRRNGKTD--EDLMQYLDIVQLTYLEHREngldaiedwIDVLSGGEKQRIAMARLFYHS 587
Cdd:COG3842 94 VAenvafGLR-----------MRGVPKAEirARVAELLELVGLEGLADRY---------PHQLSGGQQQRVALARALAPE 153
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1678143030 588 PQFAILDECTSAVSVDVEGKM----YSYCREAGITLFTVSH 624
Cdd:COG3842 154 PRVLLLDEPLSALDAKLREEMreelRRLQRELGITFIYVTH 194
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
457-624 |
3.29e-10 |
|
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: 60.39 E-value: 3.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 457 DLTFEVKSGTNVLVcGPNGCGKSSLFRILGELWPTWGGKV---------------TKPQRGKLFYIPQR----PYMTLgs 517
Cdd:cd03297 16 KIDFDLNEEVTGIF-GASGAGKSTLLRCIAGLEKPDGGTIvlngtvlfdsrkkinLPPQQRKIGLVFQQyalfPHLNV-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 518 lRDQIIYPHTRedmRRNGKTDEDLMQYLDIVQLTYLEHRengldaiedWIDVLSGGEKQRIAMARLFYHSPQFAILDECT 597
Cdd:cd03297 93 -RENLAFGLKR---KRNREDRISVDELLDLLGLDHLLNR---------YPAQLSGGEKQRVALARALAAQPELLLLDEPF 159
|
170 180 190
....*....|....*....|....*....|.
gi 1678143030 598 SAVSVDVEGKMYSYCREA----GITLFTVSH 624
Cdd:cd03297 160 SALDRALRLQLLPELKQIkknlNIPVIFVTH 190
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
428-627 |
4.26e-10 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 62.73 E-value: 4.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 428 GKGAMEFVDNIIKFENVPLVTPNGDVL-VKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELWPTWGGKVTkpqrgkLFY 506
Cdd:PRK11176 331 GKRVIERAKGDIEFRNVTFTYPGKEVPaLRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEIL------LDG 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 507 IPQRPYmTLGSLRDQ------------------IIYP----HTREDMRRNGKtdedlMQYldivQLTYLEHRENGLDAI- 563
Cdd:PRK11176 405 HDLRDY-TLASLRNQvalvsqnvhlfndtiannIAYArteqYSREQIEEAAR-----MAY----AMDFINKMDNGLDTVi 474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678143030 564 -EDWIdVLSGGEKQRIAMAR-LFYHSPqFAILDECTSAVSVDVEGKMYSYCRE--AGITLFTVSHRKS 627
Cdd:PRK11176 475 gENGV-LLSGGQRQRIAIARaLLRDSP-ILILDEATSALDTESERAIQAALDElqKNRTSLVIAHRLS 540
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
427-625 |
4.38e-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: 4.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 427 PGKGAMEFVDNIIKFEnvplvtPNGDVLVKDLTFEVKSGTNVLVCGPNGCGKSS----LFRIL----GELWPTwGGKVTK 498
Cdd:TIGR00957 1280 PPRGRVEFRNYCLRYR------EDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSltlgLFRINesaeGEIIID-GLNIAK 1352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 499 ----PQRGKLFYIPQRPYMTLGSLRDQIiYPHTRedmrrngKTDEDLMQYLDIVQL-TYLEHRENGLD-AIEDWIDVLSG 572
Cdd:TIGR00957 1353 iglhDLRFKITIIPQDPVLFSGSLRMNL-DPFSQ-------YSDEEVWWALELAHLkTFVSALPDKLDhECAEGGENLSV 1424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1678143030 573 GEKQRIAMARLFYHSPQFAILDECTSAVSVDVEGKMYSYCREA--GITLFTVSHR 625
Cdd:TIGR00957 1425 GQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQfeDCTVLTIAHR 1479
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
439-599 |
4.73e-10 |
|
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: 62.53 E-value: 4.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 439 IKFENVPL-VTPNGDVLvKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELWPTWGGKVT---KPQRGklfyipqrpyMT 514
Cdd:COG5265 358 VRFENVSFgYDPERPIL-KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILidgQDIRD----------VT 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 515 LGSLRDQI-IYPH-T-------REDMR--RNGKTDEDLMQYLDIVQL-TYLEHRENGLDAIedwidV------LSGGEKQ 576
Cdd:COG5265 427 QASLRAAIgIVPQdTvlfndtiAYNIAygRPDASEEEVEAAARAAQIhDFIESLPDGYDTR-----VgerglkLSGGEKQ 501
|
170 180
....*....|....*....|...
gi 1678143030 577 RIAMARLFYHSPQFAILDECTSA 599
Cdd:COG5265 502 RVAIARTLLKNPPILIFDEATSA 524
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
455-625 |
5.31e-10 |
|
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: 60.14 E-value: 5.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 455 VKDLTFEVKSGTNVLVCGPNGCGKSSLFRIL-GELWPTwGGKV---------TKPQR------GKLFYIPqRPY--MT-- 514
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLIsGFLRPT-SGSVlfdgeditgLPPHEiarlgiGRTFQIP-RLFpeLTvl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 515 ----LGSLRDQIIYPHTREDMRRNGKTDEDLMQYLDIVQLTYLEHRENGLdaiedwidvLSGGEKQRIAMARLFYHSPQF 590
Cdd:cd03219 94 envmVAAQARTGSGLLLARARREEREARERAEELLERVGLADLADRPAGE---------LSYGQQRRLEIARALATDPKL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1678143030 591 AILDECTSAVS-------VDVEGKMysycREAGITLFTVSHR 625
Cdd:cd03219 165 LLLDEPAAGLNpeeteelAELIREL----RERGITVLLVEHD 202
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
454-628 |
5.84e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 59.59 E-value: 5.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 454 LVKDLTFEVKSGTNVLVCGPNGCGKSSLFRILgelwptWGGKVTKPQRGKlFYIPQRPYMTLGSLRDQIIyphtredmrR 533
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLL------AGALKGTPVAGC-VDVPDNQFGREASLIDAIG---------R 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 534 NGKTDeDLMQYLDIVQLTylehrenglDAIEdWI---DVLSGGEKQRIAMARLFYHSPQFAILDECTSAVSVD----VEG 606
Cdd:COG2401 109 KGDFK-DAVELLNAVGLS---------DAVL-WLrrfKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQtakrVAR 177
|
170 180
....*....|....*....|..
gi 1678143030 607 KMYSYCREAGITLFTVSHRKSL 628
Cdd:COG2401 178 NLQKLARRAGITLVVATHHYDV 199
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
435-633 |
5.94e-10 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 61.25 E-value: 5.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 435 VDNIIKFENvplvtpNGDVLvKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELWPTWGGKVT------------KPQRG 502
Cdd:PRK10851 5 IANIKKSFG------RTQVL-NDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRfhgtdvsrlharDRKVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 503 KLF--YIPQRpYMTLGslrDQIIYPHT----REdmRRNGKT-DEDLMQYLDIVQLTYLEHRengldaiedWIDVLSGGEK 575
Cdd:PRK10851 78 FVFqhYALFR-HMTVF---DNIAFGLTvlprRE--RPNAAAiKAKVTQLLEMVQLAHLADR---------YPAQLSGGQK 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1678143030 576 QRIAMARLFYHSPQFAILDECTSAVSVDVEGKMYSYCREAGITL-FTvshrkSLWVHHD 633
Cdd:PRK10851 143 QRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELkFT-----SVFVTHD 196
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
439-600 |
6.22e-10 |
|
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: 60.01 E-value: 6.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 439 IKFENVPLVTPNGDVLVKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELW-PTWG-----GKVTKPQ-----RGKLFYI 507
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIePTSGeifidGEDIREQdpvelRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 508 PQR----PYMTLG---SLRDQII-YPHTREDMRrngkTDEdLMQYLDIVQLTYLEHrengldaiedWIDVLSGGEKQRIA 579
Cdd:cd03295 81 IQQiglfPHMTVEeniALVPKLLkWPKEKIRER----ADE-LLALVGLDPAEFADR----------YPHELSGGQQQRVG 145
|
170 180
....*....|....*....|.
gi 1678143030 580 MARLFYHSPQFAILDECTSAV 600
Cdd:cd03295 146 VARALAADPPLLLMDEPFGAL 166
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
457-624 |
7.18e-10 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 60.03 E-value: 7.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 457 DLTFEVKSGTNVLVCGPNGCGKSSLFRILGELwptwggkvTKPQRGKL------FYIPQRPYMTLG-SLRDQI------- 522
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKSSLLRVLNLL--------EMPRSGTLniagnhFDFSKTPSDKAIrELRRNVgmvfqqy 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 523 -IYPH-------TREDMRRNGKTDE----DLMQYLDIVQLTYLEHRengldaiedWIDVLSGGEKQRIAMARLFYHSPQF 590
Cdd:PRK11124 92 nLWPHltvqqnlIEAPCRVLGLSKDqalaRAEKLLERLRLKPYADR---------FPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190
....*....|....*....|....*....|....*..
gi 1678143030 591 AILDECTSAVSVDVEGKMYSYCRE---AGITLFTVSH 624
Cdd:PRK11124 163 LLFDEPTAALDPEITAQIVSIIRElaeTGITQVIVTH 199
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
449-632 |
7.26e-10 |
|
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: 58.48 E-value: 7.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 449 PNGDVLVKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELWPTWGGKVT----------KPQRGKLFYIPQRPYMTLGSL 518
Cdd:cd03247 12 EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITldgvpvsdleKALSSLISVLNQRPYLFDTTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 519 RDQIiyphtredMRRngktdedlmqyldivqltylehrengldaiedwidvLSGGEKQRIAMARLFYHSPQFAILDECTS 598
Cdd:cd03247 92 RNNL--------GRR------------------------------------FSGGERQRLALARILLQDAPIVLLDEPTV 127
|
170 180 190
....*....|....*....|....*....|....*
gi 1678143030 599 AVSVDVEGKMYSycreagiTLFTVSHRKSL-WVHH 632
Cdd:cd03247 128 GLDPITERQLLS-------LIFEVLKDKTLiWITH 155
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
217-605 |
7.53e-10 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 62.04 E-value: 7.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 217 DIFIYVYRLTVNLGGKTpsILMIY---------LLFAGVLLTRMRRPTGRL---TVEEQKLEGEFRYVNSRLITNSEEVA 284
Cdd:TIGR02203 130 DAFIVLVRETLTVIGLF--IVLLYyswqltlivVVMLPVLSILMRRVSKRLrriSKEIQNSMGQVTTVAEETLQGYRVVK 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 285 FYQGNAREkltllasysklrshLRKFlefrvgmGIVDNIVGKYFASIVGFYAVSIPFFtpnhpllsgenqgqRLQAYYTY 364
Cdd:TIGR02203 208 LFGGQAYE--------------TRRF-------DAVSNRNRRLAMKMTSAGSISSPIT--------------QLIASLAL 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 365 GrMLIKLAeaigrLVLAGREMTRLAGFTARMTEL------IKVLNDLNkGTYERTMVN-----NVVNGNSDFGPGKGAME 433
Cdd:TIGR02203 253 A-VVLFIA-----LFQAQAGSLTAGDFTAFITAMialirpLKSLTNVN-APMQRGLAAaeslfTLLDSPPEKDTGTRAIE 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 434 FVDNIIKFENVPLVTPNGDV-LVKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELWptwggkvtKPQRGKLFY--IPQR 510
Cdd:TIGR02203 326 RARGDVEFRNVTFRYPGRDRpALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFY--------EPDSGQILLdgHDLA 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 511 PYmTLGSLRDQI--------IYPHTREDMRRNGKTDE-DLMQYLDIVQLTYLEHRENGL-DAIEDWIDV----LSGGEKQ 576
Cdd:TIGR02203 398 DY-TLASLRRQValvsqdvvLFNDTIANNIAYGRTEQaDRAEIERALAAAYAQDFVDKLpLGLDTPIGEngvlLSGGQRQ 476
|
410 420
....*....|....*....|....*....
gi 1678143030 577 RIAMARLFYHSPQFAILDECTSAVSVDVE 605
Cdd:TIGR02203 477 RLAIARALLKDAPILILDEATSALDNESE 505
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
451-595 |
9.12e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 60.12 E-value: 9.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 451 GDVL-VKDLTFEVKSGTNVLVCGPNGCGKSSLFR-ILGELWP-----TWGGK-VTKPQRGKLFYIPQ----RPYMTLGsl 518
Cdd:COG4152 12 GDKTaVDDVSFTVPKGEIFGLLGPNGAGKTTTIRiILGILAPdsgevLWDGEpLDPEDRRRIGYLPEerglYPKMKVG-- 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1678143030 519 rDQIIYPHTREDMRRNgKTDEDLMQYLDIVQltyLEHRENglDAIEDwidvLSGGEKQRIAMARLFYHSPQFAILDE 595
Cdd:COG4152 90 -EQLVYLARLKGLSKA-EAKRRADEWLERLG---LGDRAN--KKVEE----LSKGNQQKVQLIAALLHDPELLILDE 155
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
455-582 |
1.35e-09 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 60.09 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 455 VKDLTFEVKSGT-NVLVcGPNGCGKSSLFRIL--------GELWptWGGK-VTK--PQRgklfyipqrpymtlgslRD-- 520
Cdd:COG3839 19 LKDIDLDIEDGEfLVLL-GPSGCGKSTLLRMIagledptsGEIL--IGGRdVTDlpPKD-----------------RNia 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 521 ---Q--IIYPHT--REDMR---RNGKTDED-----LMQYLDIVQLTYLEHR---EngldaiedwidvLSGGEKQRIAMAR 582
Cdd:COG3839 79 mvfQsyALYPHMtvYENIAfplKLRKVPKAeidrrVREAAELLGLEDLLDRkpkQ------------LSGGQRQRVALGR 146
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
447-603 |
1.70e-09 |
|
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: 60.72 E-value: 1.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 447 VTPNGDVLVKDLTFEVKSGTNVLVCGPNGCGKSSLFRIL--------GELWPTWGGKVTkpqrgklfYIPQRPY------ 512
Cdd:TIGR03719 13 VVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMagvdkdfnGEARPQPGIKVG--------YLPQEPQldptkt 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 513 ------MTLGSLRDQI--------IYPHTREDMRRNGKTDEDLMQYLDIVQLTYLEHR-ENGLDAI----EDW-IDVLSG 572
Cdd:TIGR03719 85 vrenveEGVAEIKDALdrfneisaKYAEPDADFDKLAAEQAELQEIIDAADAWDLDSQlEIAMDALrcppWDAdVTKLSG 164
|
170 180 190
....*....|....*....|....*....|....
gi 1678143030 573 GEKQRIAMARLFYHSPQFAILDECTS---AVSVD 603
Cdd:TIGR03719 165 GERRRVALCRLLLSKPDMLLLDEPTNhldAESVA 198
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
435-624 |
2.14e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 59.04 E-value: 2.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 435 VDNIIKFENVPLVTPNGDV-LVKDLTFEVKSGTNVLVCGPNGCGKSSLFRIL-GELWPTWGGKVTKPQRGklfyipqrpy 512
Cdd:PRK13640 2 KDNIVEFKHVSFTYPDSKKpALNDISFSIPRGSWTALIGHNGSGKSTISKLInGLLLPDDNPNSKITVDG---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 513 MTLGS-----LRDQIIYPHTREDMRRNGKTDEDLMQY-LDIVQLTYLEHRENGLDAIE-----DWIDV----LSGGEKQR 577
Cdd:PRK13640 72 ITLTAktvwdIREKVGIVFQNPDNQFVGATVGDDVAFgLENRAVPRPEMIKIVRDVLAdvgmlDYIDSepanLSGGQKQR 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1678143030 578 IAMARLFYHSPQFAILDECTSAvsVDVEGK------MYSYCREAGITLFTVSH 624
Cdd:PRK13640 152 VAIAGILAVEPKIIILDESTSM--LDPAGKeqilklIRKLKKKNNLTVISITH 202
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
450-624 |
2.82e-09 |
|
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: 57.76 E-value: 2.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 450 NGDVLVKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELWPTWGGKVT----------KPQRGKLFYIPQRPymtlgSLR 519
Cdd:cd03265 11 GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATvaghdvvrepREVRRRIGIVFQDL-----SVD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 520 DQI-----IYPHTREDMRRNGKTDEDLMQYLDIVQLtylehrengLDAIEDWIDVLSGGEKQRIAMARLFYHSPQFAILD 594
Cdd:cd03265 86 DELtgwenLYIHARLYGVPGAERRERIDELLDFVGL---------LEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLD 156
|
170 180 190
....*....|....*....|....*....|....
gi 1678143030 595 ECTSAVSVDVEGKMYSYCR----EAGITLFTVSH 624
Cdd:cd03265 157 EPTIGLDPQTRAHVWEYIEklkeEFGMTILLTTH 190
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
395-600 |
5.31e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 59.66 E-value: 5.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 395 MTELIKVLNDLNKgTYERTMVNNVVNGNSDfgpGKGamefVDNI--IKFENVPL-VTPNGDV-LVKDLTFEVKSGTNVLV 470
Cdd:PTZ00265 345 ITEYMKSLEATNS-LYEIINRKPLVENNDD---GKK----LKDIkkIQFKNVRFhYDTRKDVeIYKDLNFTLTEGKTYAF 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 471 CGPNGCGKSSLFRILGELW-PTWGGKVT-----------KPQRGKLFYIPQRPYMTLGSLRDQIIYP------------- 525
Cdd:PTZ00265 417 VGESGCGKSTILKLIERLYdPTEGDIIIndshnlkdinlKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsny 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 526 ------------HTREDMRRNGKTD-EDLMQYLDIVQLTYLEHRENGLD-----------AIEDWIDVL----------- 570
Cdd:PTZ00265 497 ynedgndsqenkNKRNSCRAKCAGDlNDMSNTTDSNELIEMRKNYQTIKdsevvdvskkvLIHDFVSALpdkyetlvgsn 576
|
250 260 270
....*....|....*....|....*....|....
gi 1678143030 571 ----SGGEKQRIAMARLFYHSPQFAILDECTSAV 600
Cdd:PTZ00265 577 asklSGGQKQRISIARAIIRNPKILILDEATSSL 610
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
438-624 |
6.39e-09 |
|
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: 56.82 E-value: 6.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 438 IIKFENVPLV---TPNGDVLVKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGEL-WPTWG-------------GKVTKPQ 500
Cdd:cd03258 1 MIELKNVSKVfgdTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLeRPTSGsvlvdgtdltllsGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 501 RGKLFYIPQRpYMTLGSL--RDQIIYP--HTREDMRRNGKTDEDLMQYLDivqltyLEHREngldaiEDWIDVLSGGEKQ 576
Cdd:cd03258 81 RRRIGMIFQH-FNLLSSRtvFENVALPleIAGVPKAEIEERVLELLELVG------LEDKA------DAYPAQLSGGQKQ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1678143030 577 RIAMARLFYHSPQFAILDECTSAV----SVDVEGKMYSYCREAGITLFTVSH 624
Cdd:cd03258 148 RVGIARALANNPKVLLCDEATSALdpetTQSILALLRDINRELGLTIVLITH 199
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
450-624 |
8.86e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 57.20 E-value: 8.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 450 NGDVLVKDLTFEVKSGTNVLVCGPNGCGKSSLFRIL--------GELwPTWGGKVTKPQRGKLF-YIPQRPYM--TLGSL 518
Cdd:PRK15056 18 NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALmgfvrlasGKI-SILGQPTRQALQKNLVaYVPQSEEVdwSFPVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 519 RDQII----YPHTREdMRRNGKTDEDLM-QYLDIVQLTYLEHREngldaiedwIDVLSGGEKQRIAMARLFYHSPQFAIL 593
Cdd:PRK15056 97 VEDVVmmgrYGHMGW-LRRAKKRDRQIVtAALARVDMVEFRHRQ---------IGELSGGQKKRVFLARAIAQQGQVILL 166
|
170 180 190
....*....|....*....|....*....|....
gi 1678143030 594 DECTSAVSVDVEGKMYSYCRE---AGITLFTVSH 624
Cdd:PRK15056 167 DEPFTGVDVKTEARIISLLRElrdEGKTMLVSTH 200
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
439-607 |
1.44e-08 |
|
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: 55.59 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 439 IKFENVPLVTPNGDVL-VKDLTFEVKSGTNVLVCGPNGCGKSSLFRIL-GELWPTWG-----GKVTKPQRGKLF----YI 507
Cdd:cd03263 1 LQIRNLTKTYKKGTKPaVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLtGELRPTSGtayinGYSIRTDRKAARqslgYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 508 PQR----PYMTlgsLRDQIIYpHTREDMRRNGKTDEDLMQYLDIVQLTYLEHREngldaiedwIDVLSGGEKQR--IAMA 581
Cdd:cd03263 81 PQFdalfDELT---VREHLRF-YARLKGLPKSEIKEEVELLLRVLGLTDKANKR---------ARTLSGGMKRKlsLAIA 147
|
170 180
....*....|....*....|....*.
gi 1678143030 582 rlFYHSPQFAILDECTSavSVDVEGK 607
Cdd:cd03263 148 --LIGGPSVLLLDEPTS--GLDPASR 169
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
439-608 |
1.95e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 55.77 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 439 IKFENVPLVTPNGDVLV-KDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELWptwggkvtKPQRGKLF-YIPQRPYMTLG 516
Cdd:PRK13632 8 IKVENVSFSYPNSENNAlKNVSFEINEGEYVAILGHNGSGKSTISKILTGLL--------KPQSGEIKiDGITISKENLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 517 SLRDQIIYPHTREDMRRNGKTDEDlmqylDIVqlTYLEHRE---NGLDAI----------EDWID----VLSGGEKQRIA 579
Cdd:PRK13632 80 EIRKKIGIIFQNPDNQFIGATVED-----DIA--FGLENKKvppKKMKDIiddlakkvgmEDYLDkepqNLSGGQKQRVA 152
|
170 180
....*....|....*....|....*....
gi 1678143030 580 MARLFYHSPQFAILDECTSAvsVDVEGKM 608
Cdd:PRK13632 153 IASVLALNPEIIIFDESTSM--LDPKGKR 179
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
437-598 |
1.98e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 56.18 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 437 NIIKFENVPLVTPNGDVL-VKDLTFEVKSGTNVLVCGPNGCGKSSLFRIL-GELWP-----TWGGKVTKPQ-----RGKL 504
Cdd:PRK13635 4 EIIRVEHISFRYPDAATYaLKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLnGLLLPeagtiTVGGMVLSEEtvwdvRRQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 505 FYIPQRP-YMTLGS-LRDQIIY-------PhtREDMRrngktdEDLMQYLDIVQLTYLEHRENGLdaiedwidvLSGGEK 575
Cdd:PRK13635 84 GMVFQNPdNQFVGAtVQDDVAFglenigvP--REEMV------ERVDQALRQVGMEDFLNREPHR---------LSGGQK 146
|
170 180
....*....|....*....|...
gi 1678143030 576 QRIAMARLFYHSPQFAILDECTS 598
Cdd:PRK13635 147 QRVAIAGVLALQPDIIILDEATS 169
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
432-625 |
2.15e-08 |
|
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: 55.07 E-value: 2.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 432 MEFVDNIIK-FENVPLVTpngdVLVKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELWPTWGGKVT--------KPQ-- 500
Cdd:cd03266 1 MITADALTKrFRDVKKTV----QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATvdgfdvvkEPAea 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 501 RGKLFYIP--QRPYMTLgSLRDQIIYPHTREDMRRNGKTD--EDLMQYLDIVQltYLEHRENGLdaiedwidvlSGGEKQ 576
Cdd:cd03266 77 RRRLGFVSdsTGLYDRL-TARENLEYFAGLYGLKGDELTArlEELADRLGMEE--LLDRRVGGF----------STGMRQ 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1678143030 577 RIAMARLFYHSPQFAILDECTSAVSVDVEGKMYSYC---REAGITLFTVSHR 625
Cdd:cd03266 144 KVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIrqlRALGKCILFSTHI 195
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
455-595 |
2.83e-08 |
|
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: 54.75 E-value: 2.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 455 VKDLTFEVKSGTNVLVCGPNGCGKSSLFR-ILGeLWPTWGGKVT-------------KPQRGkLFYIPQR----PYMT-- 514
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKtIMG-LLPPRSGSIRfdgrditglppheRARAG-IGYVPEGrrifPELTve 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 515 ----LGSLRdqiiyphtredmRRNGKTDEDLMQYLDIV-QLTYLEHRENGldaiedwidVLSGGEKQRIAMARLFYHSPQ 589
Cdd:cd03224 94 enllLGAYA------------RRRAKRKARLERVYELFpRLKERRKQLAG---------TLSGGEQQMLAIARALMSRPK 152
|
....*.
gi 1678143030 590 FAILDE 595
Cdd:cd03224 153 LLLLDE 158
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
455-624 |
3.53e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 56.79 E-value: 3.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 455 VKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELWPTWGGKVT--------------KPQRGKLFYIPQRPYMTLGSlRD 520
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIfngqridtlspgklQALRRDIQFIFQDPYASLDP-RQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 521 QIIYPhTREDMRRNGKTDEDLMQyldiVQLTYLEHREnGLDAIEDW--IDVLSGGEKQRIAMARLFYHSPQFAILDECTS 598
Cdd:PRK10261 419 TVGDS-IMEPLRVHGLLPGKAAA----ARVAWLLERV-GLLPEHAWryPHEFSGGQRQRICIARALALNPKVIIADEAVS 492
|
170 180 190
....*....|....*....|....*....|
gi 1678143030 599 AVSVDVEGK----MYSYCREAGITLFTVSH 624
Cdd:PRK10261 493 ALDVSIRGQiinlLLDLQRDFGIAYLFISH 522
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
435-624 |
4.59e-08 |
|
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: 53.80 E-value: 4.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 435 VDNIIK-FENVplvtpngdVLVKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELWPTWGGKV---------TKPQRGKL 504
Cdd:cd03301 3 LENVTKrFGNV--------TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIyiggrdvtdLPPKDRDI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 505 FYIPQR----PYMTlgsLRDQIIYPHTREDMRRNgKTDEDLMQYLDIVQLTYLEHREngldaiedwIDVLSGGEKQRIAM 580
Cdd:cd03301 75 AMVFQNyalyPHMT---VYDNIAFGLKLRKVPKD-EIDERVREVAELLQIEHLLDRK---------PKQLSGGQRQRVAL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1678143030 581 ARLFYHSPQFAILDECTSAVSVDVEGKMYSYC----REAGITLFTVSH 624
Cdd:cd03301 142 GRAIVREPKVFLMDEPLSNLDAKLRVQMRAELkrlqQRLGTTTIYVTH 189
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
436-605 |
5.16e-08 |
|
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: 56.10 E-value: 5.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 436 DNIIKFENVplVTPNGD-VLVKDLTFEVKSGTNVLVCGPNGCGKSSLFRIL-GELWPTwGGKVTKPQRGKLFYIPQrpym 513
Cdd:TIGR03719 320 DKVIEAENL--TKAFGDkLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMItGQEQPD-SGTIEIGETVKLAYVDQ---- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 514 tlgslrdqiiyphTREDMRRNGKTDEDLMQYLDIVQL--------TYLEhREN--GLDAiEDWIDVLSGGEKQRIAMARL 583
Cdd:TIGR03719 393 -------------SRDALDPNKTVWEEISGGLDIIKLgkreipsrAYVG-RFNfkGSDQ-QKKVGQLSGGERNRVHLAKT 457
|
170 180
....*....|....*....|..
gi 1678143030 584 FYHSPQFAILDECTSavSVDVE 605
Cdd:TIGR03719 458 LKSGGNVLLLDEPTN--DLDVE 477
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
455-624 |
5.53e-08 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 54.26 E-value: 5.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 455 VKDLTFEVKSGTNVLVCGPNGCGKSSLFRIL-GELWPTWG-----GKVTKPQRGKL-----FYIPQR--------PYMTL 515
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILsGLLQPTSGevrvaGLVPWKRRKKFlrrigVVFGQKtqlwwdlpVIDSF 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 516 GSLRDqiIYphtREDMRRNGKTDEDLMQYLDIVQLTYLEHREngldaiedwidvLSGGEKQRIAMARLFYHSPQFAILDE 595
Cdd:cd03267 117 YLLAA--IY---DLPPARFKKRLDELSELLDLEELLDTPVRQ------------LSLGQRMRAEIAAALLHEPEILFLDE 179
|
170 180 190
....*....|....*....|....*....|...
gi 1678143030 596 CTSAVSVDVEGKMYS----YCREAGITLFTVSH 624
Cdd:cd03267 180 PTIGLDVVAQENIRNflkeYNRERGTTVLLTSH 212
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
450-624 |
6.90e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 54.28 E-value: 6.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 450 NGDVLVKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELWPTWGGKVT--------------------KPQRGKLFYIPQ 509
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKvdgkvlyfgkdifqidaiklRKEVGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 510 rPYMTLgSLRDQIIYP---HTREDMRRNGKTDEDLMQYLDIVQLTYlehrenglDAIEDWIDVLSGGEKQRIAMARLFYH 586
Cdd:PRK14246 101 -PFPHL-SIYDNIAYPlksHGIKEKREIKKIVEECLRKVGLWKEVY--------DRLNSPASQLSGGQQQRLTIARALAL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1678143030 587 SPQFAILDECTSAVSV----DVEGKMYSYCREagITLFTVSH 624
Cdd:PRK14246 171 KPKVLLMDEPTSMIDIvnsqAIEKLITELKNE--IAIVIVSH 210
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
457-624 |
7.21e-08 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 54.73 E-value: 7.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 457 DLTFEVKSGTNVLVCGPNGCGKSSLFRIL--------------GELWPTWGGKV-TKPQRGKLFYIPQR----PYMtlgS 517
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIagltrpdegeivlnGRTLFDSRKGIfLPPEKRRIGYVFQEarlfPHL---S 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 518 LRDQIIYPHTREDMRRNGKTDEDLMQYLDIVQLtyLEHRENGLdaiedwidvlSGGEKQRIAMARLFYHSPQFAILDECT 597
Cdd:TIGR02142 92 VRGNLRYGMKRARPSERRISFERVIELLGIGHL--LGRLPGRL----------SGGEKQRVAIGRALLSSPRLLLMDEPL 159
|
170 180 190
....*....|....*....|....*....|.
gi 1678143030 598 SAVSVDVEGKMYSYCR----EAGITLFTVSH 624
Cdd:TIGR02142 160 AALDDPRKYEILPYLErlhaEFGIPILYVSH 190
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
455-602 |
9.81e-08 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 55.08 E-value: 9.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 455 VKDLTFEVKSGTNVLVCGPNGCGKSSL-------------FRILGELWPTWGGKVTKPQRGKLFYIPQRPYmtlGSL--R 519
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLglallrlipsegeIRFDGQDLDGLSRRALRPLRRRMQVVFQDPF---GSLspR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 520 ---DQIIyphtREDMR--RNGKTDEDLMQYldIVQLtyLEhrENGLDAieDWID----VLSGGEKQRIAMARLFYHSPQF 590
Cdd:COG4172 379 mtvGQII----AEGLRvhGPGLSAAERRAR--VAEA--LE--EVGLDP--AARHryphEFSGGQRQRIAIARALILEPKL 446
|
170
....*....|....
gi 1678143030 591 AILDECTSA--VSV 602
Cdd:COG4172 447 LVLDEPTSAldVSV 460
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
427-625 |
1.92e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 54.60 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 427 PGKGAMEFVDNIIKFEnvPLVTPngdvLVKDLTFEVKSGTNVLVCGPNGCGKSS----LFRIL----GELWPTwGGKVTK 498
Cdd:PLN03232 1230 PSRGSIKFEDVHLRYR--PGLPP----VLHGLSFFVSPSEKVGVVGRTGAGKSSmlnaLFRIVelekGRIMID-DCDVAK 1302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 499 ----PQRGKLFYIPQRPYMTLGSLRDQIiYPHTREDmrrngktDEDLMQYLDIVQLTYLEHREN-GLDA-IEDWIDVLSG 572
Cdd:PLN03232 1303 fgltDLRRVLSIIPQSPVLFSGTVRFNI-DPFSEHN-------DADLWEALERAHIKDVIDRNPfGLDAeVSEGGENFSV 1374
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1678143030 573 GEKQRIAMARLFYHSPQFAILDECTSAVSVDVEGKMYSYCREA--GITLFTVSHR 625
Cdd:PLN03232 1375 GQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEfkSCTMLVIAHR 1429
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
451-605 |
2.26e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.19 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 451 GDVLVKDLTFEVKSGTNVLVCGPNGCGKSSLFRI-LGELWPTwGGKV---TKPQ-------RGKLfyIPQRPYMTlgSLR 519
Cdd:PRK11147 331 GKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLmLGQLQAD-SGRIhcgTKLEvayfdqhRAEL--DPEKTVMD--NLA 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 520 DqiiyphTREDMRRNGKtDEDLMQYLDivqlTYLEHRENGLDAIEdwidVLSGGEKQRIAMARLFYHSPQFAILDECTSa 599
Cdd:PRK11147 406 E------GKQEVMVNGR-PRHVLGYLQ----DFLFHPKRAMTPVK----ALSGGERNRLLLARLFLKPSNLLILDEPTN- 469
|
....*.
gi 1678143030 600 vSVDVE 605
Cdd:PRK11147 470 -DLDVE 474
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
448-602 |
2.26e-07 |
|
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: 53.13 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 448 TPNGDV-LVKDLTFEVKSGTNVLVCGPNGCGKS----SLFRILGELWPTwGGKVT--------------KPQRGK-LFYI 507
Cdd:COG0444 13 TRRGVVkAVDGVSFDVRRGETLGLVGESGSGKStlarAILGLLPPPGIT-SGEILfdgedllklsekelRKIRGReIQMI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 508 PQRPY------MTLGslrDQIIYPhtredMRRNGKTDED-----LMQYLDIVqltylehrenGLDAIEDWIDV----LSG 572
Cdd:COG0444 92 FQDPMtslnpvMTVG---DQIAEP-----LRIHGGLSKAearerAIELLERV----------GLPDPERRLDRypheLSG 153
|
170 180 190
....*....|....*....|....*....|..
gi 1678143030 573 GEKQRIAMARLFYHSPQFAILDECTSA--VSV 602
Cdd:COG0444 154 GMRQRVMIARALALEPKLLIADEPTTAldVTI 185
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
432-634 |
2.34e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 52.83 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 432 MEFVDNIIKFENVPLvTPNGD--VLVKDLTFEVKSGTNVLVCGPNGCGKSSLFR-ILGelwptwggkVTKPQRGKLFYip 508
Cdd:PRK13648 1 MEDKNSIIVFKNVSF-QYQSDasFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKlMIG---------IEKVKSGEIFY-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 509 qrpymtlgslRDQIIYPHTREDMRRN-------------GKTDE-DLMQYLDIVQLTYLEHRENGLDAIEDwIDV----- 569
Cdd:PRK13648 69 ----------NNQAITDDNFEKLRKHigivfqnpdnqfvGSIVKyDVAFGLENHAVPYDEMHRRVSEALKQ-VDMlerad 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678143030 570 -----LSGGEKQRIAMARLFYHSPQFAILDECTSAVSVDVEGKMYSYCR----EAGITLFTVSHRKSLWVHHDF 634
Cdd:PRK13648 138 yepnaLSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRkvksEHNITIISITHDLSEAMEADH 211
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
438-628 |
2.79e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 53.71 E-value: 2.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 438 IIKFENVPLVTPNGDVLVKDLTFEVKSGTNVLVCGPNGCGKSSLFR-ILGELWPTwGGKVTKPQRGKLFYIPQRPYMTLG 516
Cdd:PLN03073 508 IISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKlISGELQPS-SGTVFRSAKVRMAVFSQHHVDGLD 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 517 SLRDQIIYphtredMRR--NGKTDEDLMQYLDIVQLTylehrenGLDAIEDwIDVLSGGEKQRIAMARLFYHSPQFAILD 594
Cdd:PLN03073 587 LSSNPLLY------MMRcfPGVPEQKLRAHLGSFGVT-------GNLALQP-MYTLSGGQKSRVAFAKITFKKPHILLLD 652
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1678143030 595 ECTSAVSVD-VEGKMysycreAGITLF-----TVSHRKSL 628
Cdd:PLN03073 653 EPSNHLDLDaVEALI------QGLVLFqggvlMVSHDEHL 686
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
454-598 |
3.29e-07 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 51.01 E-value: 3.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 454 LVKDLTFEVKSGTNVLVCGPNGCGKSSLFRILgelwptwGGKVTKPQ-RGKLFY--IPQRPYmtlgSLRDQIIYphtred 530
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNAL-------AGRRTGLGvSGEVLIngRPLDKR----SFRKIIGY------ 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678143030 531 mrrngkTDEDlmqylDIVqLTYLEHRENGLDAIEdwIDVLSGGEKQRIAMARLFYHSPQFAILDECTS 598
Cdd:cd03213 87 ------VPQD-----DIL-HPTLTVRETLMFAAK--LRGLSGGERKRVSIALELVSNPSLLFLDEPTS 140
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
438-624 |
3.54e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 52.00 E-value: 3.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 438 IIKFENVPLVTPNGDVLVKDLTFEVKSGTNVLVCGPNGCGKSSLF-RILGELWPTWG-----GKVTKPQRGKLFYIPQRP 511
Cdd:PRK13639 1 ILETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFlHFNGILKPTSGevlikGEPIKYDKKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 512 YMTLGSLRDQIIYPHTREDMR---RNGKTDED-----LMQYLDIVQLTYLEHRENgldaiedwiDVLSGGEKQRIAMARL 583
Cdd:PRK13639 81 GIVFQNPDDQLFAPTVEEDVAfgpLNLGLSKEevekrVKEALKAVGMEGFENKPP---------HHLSGGQKKRVAIAGI 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1678143030 584 FYHSPQFAILDECTSAvsVDVEG-----KMYSYCREAGITLFTVSH 624
Cdd:PRK13639 152 LAMKPEIIVLDEPTSG--LDPMGasqimKLLYDLNKEGITIIISTH 195
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
455-602 |
3.77e-07 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 52.43 E-value: 3.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 455 VKDLTFEVKSGTNVLVCGPNGCGKSSLFR-ILGELWPTwGGKVT--------------KPQRGKLFYIPQRPY------M 513
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRlLLRLEEPT-SGEILfdgqditglsgrelRPLRRRMQMVFQDPYaslnprM 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 514 TLGslrdQIIyphtREDMRRNG-KTDEDLMQY----LDIVqltylehrenGLDAieDWID----VLSGGEKQRIAMARLF 584
Cdd:COG4608 113 TVG----DII----AEPLRIHGlASKAERRERvaelLELV----------GLRP--EHADryphEFSGGQRQRIGIARAL 172
|
170 180
....*....|....*....|
gi 1678143030 585 YHSPQFAILDECTSA--VSV 602
Cdd:COG4608 173 ALNPKLIVCDEPVSAldVSI 192
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
472-600 |
3.80e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 51.70 E-value: 3.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 472 GPNGCGKSSLFRIL---GELWP--TWGGKVTkpQRGKLFYIPQRPYMtlgSLRDQI-------------IYPHTREDMRR 533
Cdd:PRK14239 38 GPSGSGKSTLLRSInrmNDLNPevTITGSIV--YNGHNIYSPRTDTV---DLRKEIgmvfqqpnpfpmsIYENVVYGLRL 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1678143030 534 NGKTDEdlmQYLDivqltylEHRENGLDAIEDWIDV----------LSGGEKQRIAMARLFYHSPQFAILDECTSAV 600
Cdd:PRK14239 113 KGIKDK---QVLD-------EAVEKSLKGASIWDEVkdrlhdsalgLSGGQQQRVCIARVLATSPKIILLDEPTSAL 179
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
438-624 |
4.99e-07 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 51.25 E-value: 4.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 438 IIKFENVPLVTPNGDVLvKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELWPTWGG-------KVTKP----------- 499
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVL-HNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGdlivdglKVNDPkvderlirqea 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 500 ----QRGKLFyipqrPYMTlgSLRDQIIYP-HTREDMRRNGKTdedlmQYLDIVQLTYLEHRENGLDAiedwidVLSGGE 574
Cdd:PRK09493 80 gmvfQQFYLF-----PHLT--ALENVMFGPlRVRGASKEEAEK-----QARELLAKVGLAERAHHYPS------ELSGGQ 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1678143030 575 KQRIAMARLFYHSPQFAILDECTSAVSVDVEGKMYSYCR---EAGITLFTVSH 624
Cdd:PRK09493 142 QQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQdlaEEGMTMVIVTH 194
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
470-603 |
5.08e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.81 E-value: 5.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 470 VCGPNGCGKSSLFRIL--------GELWPTWGGKVtkpqrGklfYIPQRPYMT------------LGSLRDQI-----IY 524
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMagvdkefeGEARPAPGIKV-----G---YLPQEPQLDpektvrenveegVAEVKAALdrfneIY 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 525 PHTREDMRRNGKT-DE--DLMQYLDIVQLTYLEHR-ENGLDAI----EDW-IDVLSGGEKQRIAMARLFYHSPQFAILDE 595
Cdd:PRK11819 110 AAYAEPDADFDALaAEqgELQEIIDAADAWDLDSQlEIAMDALrcppWDAkVTKLSGGERRRVALCRLLLEKPDMLLLDE 189
|
170
....*....|.
gi 1678143030 596 CTS---AVSVD 603
Cdd:PRK11819 190 PTNhldAESVA 200
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
451-595 |
5.20e-07 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 52.34 E-value: 5.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 451 GDVLV-KDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELwptwgGKVTkpqRGKLFYIPQR----PYMTLG---SLRDQI 522
Cdd:PRK11000 14 GDVVIsKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGL-----EDIT---SGDLFIGEKRmndvPPAERGvgmVFQSYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 523 IYPH--TREDMR------RNGKTDED--LMQYLDIVQLTYLEHRENgldaiedwiDVLSGGEKQRIAMARLFYHSPQFAI 592
Cdd:PRK11000 86 LYPHlsVAENMSfglklaGAKKEEINqrVNQVAEVLQLAHLLDRKP---------KALSGGQRQRVAIGRTLVAEPSVFL 156
|
...
gi 1678143030 593 LDE 595
Cdd:PRK11000 157 LDE 159
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
427-598 |
5.40e-07 |
|
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: 52.99 E-value: 5.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 427 PGKGAMEFVDNIIKFenvplvTPNGDVLVKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELWPTWG---------GKVT 497
Cdd:TIGR01271 1213 PSGGQMDVQGLTAKY------TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGeiqidgvswNSVT 1286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 498 KPQRGKLF-YIPQRPYMTLGSLRDQiIYPHTRedmrrngKTDEDLMQYLDIVQL-TYLEHRENGLD-AIEDWIDVLSGGE 574
Cdd:TIGR01271 1287 LQTWRKAFgVIPQKVFIFSGTFRKN-LDPYEQ-------WSDEEIWKVAEEVGLkSVIEQFPDKLDfVLVDGGYVLSNGH 1358
|
170 180
....*....|....*....|....
gi 1678143030 575 KQRIAMARLFYHSPQFAILDECTS 598
Cdd:TIGR01271 1359 KQLMCLARSILSKAKILLLDEPSA 1382
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
357-636 |
6.43e-07 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 52.41 E-value: 6.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 357 RLQAYYTYGRMLIKLAEAIGRLVLAGREMtrLAGFTARMT-------ELIKVLNDLNKGTYERT-----MVNNVVNGNSD 424
Cdd:PRK10790 241 RMQTLRLDGFLLRPLLSLFSALILCGLLM--LFGFSASGTievgvlyAFISYLGRLNEPLIELTtqqsmLQQAVVAGERV 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 425 F----GP----GKGAMEFVDNIIKFENVPLVTPNGDVLVKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELWPtwggkv 496
Cdd:PRK10790 319 FelmdGPrqqyGNDDRPLQSGRIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYP------ 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 497 tkPQRGKLfYIPQRPYMTL--GSLR--------DQIIYPHTREDMRRNGK--TDEDLMQYLDIVQLTYLEHR-ENGLDA- 562
Cdd:PRK10790 393 --LTEGEI-RLDGRPLSSLshSVLRqgvamvqqDPVVLADTFLANVTLGRdiSEEQVWQALETVQLAELARSlPDGLYTp 469
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1678143030 563 IEDWIDVLSGGEKQRIAMARLFYHSPQFAILDECTSAVSVDVE---GKMYSYCREAgITLFTVSHRKSLWVHHDFFL 636
Cdd:PRK10790 470 LGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEqaiQQALAAVREH-TTLVVIAHRLSTIVEADTIL 545
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
453-646 |
7.12e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 52.86 E-value: 7.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 453 VLVKDLTFEVKSGTNVLVCGPNGCGKSSLFRIL--------GELWPtwggkvtkpQRgKLFYIPQRPYMTLGSLRDQIIY 524
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLlsqfeiseGRVWA---------ER-SIAYVPQQAWIMNATVRGNILF 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 525 phtredmrrngKTDEDLMQYLDIVQLTYLEHRENGLDA-IEDWIDV----LSGGEKQRIAMARLFYHSPQFAILDECTSA 599
Cdd:PTZ00243 744 -----------FDEEDAARLADAVRVSQLEADLAQLGGgLETEIGEkgvnLSGGQKARVSLARAVYANRDVYLLDDPLSA 812
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1678143030 600 VSVDVEGKMYSYC---REAGITLFTVSHRKSLWVHHDFFLQFdGRGNYEF 646
Cdd:PTZ00243 813 LDAHVGERVVEECflgALAGKTRVLATHQVHVVPRADYVVAL-GDGRVEF 861
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
450-624 |
7.31e-07 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 51.76 E-value: 7.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 450 NGDVLVKDLTFEVKSGTNVLVCGPNGCGKSSLFRIL-GELWPTWGGKVTKPQrgKLFYIP--QRPYMTLgsLRDQIIYPH 526
Cdd:PRK11607 30 DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLaGFEQPTAGQIMLDGV--DLSHVPpyQRPINMM--FQSYALFPH 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 527 T----------REDMRRNGKTDEDLMQYLDIVQLTYLEHRENgldaiedwiDVLSGGEKQRIAMARLFYHSPQFAILDEC 596
Cdd:PRK11607 106 MtveqniafglKQDKLPKAEIASRVNEMLGLVHMQEFAKRKP---------HQLSGGQRQRVALARSLAKRPKLLLLDEP 176
|
170 180 190
....*....|....*....|....*....|..
gi 1678143030 597 TSAVSVDVEGKM----YSYCREAGITLFTVSH 624
Cdd:PRK11607 177 MGALDKKLRDRMqlevVDILERVGVTCVMVTH 208
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
453-605 |
8.45e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 52.01 E-value: 8.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 453 VLVKDLTFEVKSGTNVLVCGPNGCGKSS----LFRIL---GELW----P--TWGGKVTKPQRGKLFYIPQRPYMTLGSLR 519
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLInsqGEIWfdgqPlhNLNRRQLLPVRHRIQVVFQDPNSSLNPRL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 520 D--QIIyphtREDMRRNGKTDEDLMQYLDIVQLTylehRENGLDAI--EDWIDVLSGGEKQRIAMARLFYHSPQFAILDE 595
Cdd:PRK15134 380 NvlQII----EEGLRVHQPTLSAAQREQQVIAVM----EEVGLDPEtrHRYPAEFSGGQRQRIAIARALILKPSLIILDE 451
|
170
....*....|
gi 1678143030 596 CTSAVSVDVE 605
Cdd:PRK15134 452 PTSSLDKTVQ 461
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
455-624 |
1.68e-06 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 50.72 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 455 VKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELwptwggkvTKPQRGKLF-------YIP--QRPYMTLgsLRDQIIYP 525
Cdd:PRK09452 30 ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGF--------ETPDSGRIMldgqditHVPaeNRHVNTV--FQSYALFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 526 H--TRED------MRR--NGKTDEDLMQYLDIVQLTYLEHREngldaiedwIDVLSGGEKQRIAMARLFYHSPQFAILDE 595
Cdd:PRK09452 100 HmtVFENvafglrMQKtpAAEITPRVMEALRMVQLEEFAQRK---------PHQLSGGQQQRVAIARAVVNKPKVLLLDE 170
|
170 180 190
....*....|....*....|....*....|...
gi 1678143030 596 CTSAVSVDVEGKMYSYC----REAGITLFTVSH 624
Cdd:PRK09452 171 SLSALDYKLRKQMQNELkalqRKLGITFVFVTH 203
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
436-624 |
2.71e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 49.46 E-value: 2.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 436 DNIIKFENVPLVTPNGDVLVKDLTFEVKSGTNVLVCGPNGCGKSSLFRIL-GELWPT-----WGGKVTKPQRGKLFYIPQ 509
Cdd:PRK13636 3 DYILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLnGILKPSsgrilFDGKPIDYSRKGLMKLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 510 RPYMTLGSLRDQIIYPHTREDMR---RNGKTDEDLMQYL--DIVQLTYLEHRENgldaieDWIDVLSGGEKQRIAMARLF 584
Cdd:PRK13636 83 SVGMVFQDPDNQLFSASVYQDVSfgaVNLKLPEDEVRKRvdNALKRTGIEHLKD------KPTHCLSFGQKKRVAIAGVL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1678143030 585 YHSPQFAILDECTSAVS-VDVEGKM---YSYCREAGITLFTVSH 624
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDpMGVSEIMkllVEMQKELGLTIIIATH 200
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
451-604 |
2.90e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 49.58 E-value: 2.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 451 GDVLVKDL---TFEVKSGTNVLVCGPNGCGKSSLFRILGelwptwggKVTKPQRGKLFYIPQR----PYMTLGSLRD--Q 521
Cdd:PRK11308 24 PERLVKALdgvSFTLERGKTLAVVGESGCGKSTLARLLT--------MIETPTGGELYYQGQDllkaDPEAQKLLRQkiQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 522 IIY--PHTREDMRRngKTDEDLMQYLDI-VQLTYLEHRENGLDAIED----------WIDVLSGGEKQRIAMARLFYHSP 588
Cdd:PRK11308 96 IVFqnPYGSLNPRK--KVGQILEEPLLInTSLSAAERREKALAMMAKvglrpehydrYPHMFSGGQRQRIAIARALMLDP 173
|
170
....*....|....*.
gi 1678143030 589 QFAILDECTSAVSVDV 604
Cdd:PRK11308 174 DVVVADEPVSALDVSV 189
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
450-627 |
3.17e-06 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 48.98 E-value: 3.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 450 NGDVLVKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELWPTWGGKV---------TKPQRGKLFYIPQrpymtlgsLRD 520
Cdd:PRK11264 14 HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgditidtARSLSQQKGLIRQ--------LRQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 521 QI--------IYPHtREDMrrngktdEDLMQYLDIVQLTYLEHREN---------GLDAIED-WIDVLSGGEKQRIAMAR 582
Cdd:PRK11264 86 HVgfvfqnfnLFPH-RTVL-------ENIIEGPVIVKGEPKEEATArarellakvGLAGKETsYPRRLSGGQQQRVAIAR 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1678143030 583 LFYHSPQFAILDECTSAVSVDVEGKMYSYCR---EAGITLFTVSHRKS 627
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDPELVGEVLNTIRqlaQEKRTMVIVTHEMS 205
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
454-638 |
3.98e-06 |
|
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: 48.75 E-value: 3.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 454 LVKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELWPTWGGKVT-----------KPQRGKLFYIPQRPYMTLGSLRDQI 522
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVidgidisklplHTLRSRLSIILQDPILFSGSIRFNL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 523 iyphtreDMRRNGkTDEDLMQYLDIVQL-TYLEHRENGLDA-IEDWIDVLSGGEKQRIAMARLFYHSPQFAILDECTSAV 600
Cdd:cd03288 116 -------DPECKC-TDDRLWEALEIAQLkNMVKSLPGGLDAvVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASI 187
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1678143030 601 SVDVEGKMYSYCRE--AGITLFTVSHRKSLWVHHDFFLQF 638
Cdd:cd03288 188 DMATENILQKVVMTafADRTVVTIAHRVSTILDADLVLVL 227
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
457-624 |
4.48e-06 |
|
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: 47.87 E-value: 4.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 457 DLTFEvkSGTNVLVCGPNGCGKSSLFR-ILGELWPTWGGKVTKPQRGKLFYIPQRPYMTLgsLRDQIIYPH----TREDM 531
Cdd:cd03298 18 DLTFA--QGEITAIVGPSGSGKSTLLNlIAGFETPQSGRVLINGVDVTAAPPADRPVSML--FQENNLFAHltveQNVGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 532 RRNG--KTDEDLMQYLDIVQltylehRENGLDAIEDWI-DVLSGGEKQRIAMARLFYHSPQFAILDECTSAVSVDVEGKM 608
Cdd:cd03298 94 GLSPglKLTAEDRQAIEVAL------ARVGLAGLEKRLpGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEM 167
|
170 180
....*....|....*....|
gi 1678143030 609 YSY----CREAGITLFTVSH 624
Cdd:cd03298 168 LDLvldlHAETKMTVLMVTH 187
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
455-608 |
5.09e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 48.57 E-value: 5.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 455 VKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELWPTWGGKV--------------TKPQRGKLFYIPQRPYMTlGSLRD 520
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIiidgdllteenvwdIRHKIGMVFQNPDNQFVG-ATVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 521 QIIY-------PHtrEDMRrngktdEDLMQYLDIVQLTYLEHRENGLdaiedwidvLSGGEKQRIAMARLFYHSPQFAIL 593
Cdd:PRK13650 102 DVAFglenkgiPH--EEMK------ERVNEALELVGMQDFKEREPAR---------LSGGQKQRVAIAGAVAMRPKIIIL 164
|
170
....*....|....*
gi 1678143030 594 DECTSAvsVDVEGKM 608
Cdd:PRK13650 165 DEATSM--LDPEGRL 177
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
430-595 |
6.53e-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: 48.31 E-value: 6.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 430 GAMEFVDNIIKFenvplvTPNGDVLVKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELWPTWG---------GKVTKPQ 500
Cdd:cd03289 1 GQMTVKDLTAKY------TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGdiqidgvswNSVPLQK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 501 RGKLF-YIPQRPYMTLGSLRdqiiyphtrEDMRRNGK-TDEDLMQYLDIVQL-TYLEHRENGLD-AIEDWIDVLSGGEKQ 576
Cdd:cd03289 75 WRKAFgVIPQKVFIFSGTFR---------KNLDPYGKwSDEEIWKVAEEVGLkSVIEQFPGQLDfVLVDGGCVLSHGHKQ 145
|
170
....*....|....*....
gi 1678143030 577 RIAMARLFYHSPQFAILDE 595
Cdd:cd03289 146 LMCLARSVLSKAKILLLDE 164
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
459-624 |
7.79e-06 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 47.65 E-value: 7.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 459 TFEVKSGTNVLVCGPNGCGKSSLFR-ILGELWPTwggkvtkpqRGKLF-------YIP--QRPYMTLgsLRDQIIYPH-T 527
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNlIAGFLTPA---------SGSLTlngqdhtTTPpsRRPVSML--FQENNLFSHlT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 528 RED---------MRRNGKTDEDLMQYLDIVqltylehrengldAIEDWIDVL----SGGEKQRIAMARLFYHSPQFAILD 594
Cdd:PRK10771 88 VAQniglglnpgLKLNAAQREKLHAIARQM-------------GIEDLLARLpgqlSGGQRQRVALARCLVREQPILLLD 154
|
170 180 190
....*....|....*....|....*....|....
gi 1678143030 595 ECTSAVSVDVEGKMYSY----CREAGITLFTVSH 624
Cdd:PRK10771 155 EPFSALDPALRQEMLTLvsqvCQERQLTLLMVSH 188
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
439-625 |
9.08e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 49.35 E-value: 9.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 439 IKFENVPL-VTPNGDVLVKDLTFEVKSGTNVLVCGPNGCGKSS----LFRIL----GELWPTwGGKVTK----PQRGKLF 505
Cdd:PLN03130 1238 IKFEDVVLrYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSmlnaLFRIVelerGRILID-GCDISKfglmDLRKVLG 1316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 506 YIPQRPYMTLGSLR---DQIiyphtredmrrNGKTDEDLMQYLDIVQLTYLEHREN-GLDAiedwiDVLSGGE------K 575
Cdd:PLN03130 1317 IIPQAPVLFSGTVRfnlDPF-----------NEHNDADLWESLERAHLKDVIRRNSlGLDA-----EVSEAGEnfsvgqR 1380
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1678143030 576 QRIAMARLFYHSPQFAILDECTSAVSVDVEGKMYSYCREA--GITLFTVSHR 625
Cdd:PLN03130 1381 QLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEfkSCTMLIIAHR 1432
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
434-595 |
9.18e-06 |
|
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: 47.54 E-value: 9.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 434 FVDNIIKFENVPLVtpngdvlVKDLTFEVKSGTNVLVCGPNGCGKSSLFR-ILGELWPTwGGKV--------TKP--QRG 502
Cdd:cd03218 2 RAENLSKRYGKRKV-------VNGVSLSVKQGEIVGLLGPNGAGKTTTFYmIVGLVKPD-SGKIlldgqditKLPmhKRA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 503 KL--FYIPQRPYMTLG-SLRDQII---YPHTREDMRRNGKTDEdlmqYLDIVQLTYLEHReNGLDaiedwidvLSGGEKQ 576
Cdd:cd03218 74 RLgiGYLPQEASIFRKlTVEENILavlEIRGLSKKEREEKLEE----LLEEFHITHLRKS-KASS--------LSGGERR 140
|
170
....*....|....*....
gi 1678143030 577 RIAMARLFYHSPQFAILDE 595
Cdd:cd03218 141 RVEIARALATNPKFLLLDE 159
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
432-581 |
9.25e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 48.65 E-value: 9.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 432 MEFVDNIIKFEN-VPLVTPNGDVLVK---------DLTFEVKSGT----NVL-VCGPNGCGKSSLFRIL-GELWPTWGGK 495
Cdd:PRK13409 317 MRIRPEPIEFEErPPRDESERETLVEypdltkklgDFSLEVEGGEiyegEVIgIVGPNGIGKTTFAKLLaGVLKPDEGEV 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 496 VTKPqrgKLFYIPQRpymtlgsLRDQiiYPHTREDMRRNGKTD-------EDLMQYLDIVQLtyLEHRengldaiedwID 568
Cdd:PRK13409 397 DPEL---KISYKPQY-------IKPD--YDGTVEDLLRSITDDlgssyykSEIIKPLQLERL--LDKN----------VK 452
|
170
....*....|...
gi 1678143030 569 VLSGGEKQRIAMA 581
Cdd:PRK13409 453 DLSGGELQRVAIA 465
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
454-624 |
1.01e-05 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 47.70 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 454 LVKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELWPTWGGKVT---KP-------QRGK-LFYIPQRPYMTLG-SLRDQ 521
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFlgdKPismlssrQLARrLALLPQHHLTPEGiTVREL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 522 IIY---PHTREDMRRNGKTDEDLMQYLDIVQLTYLEHRengldAIEDwidvLSGGEKQRIAMARLFYHSPQFAILDECTS 598
Cdd:PRK11231 97 VAYgrsPWLSLWGRLSAEDNARVNQAMEQTRINHLADR-----RLTD----LSGGQRQRAFLAMVLAQDTPVVLLDEPTT 167
|
170 180
....*....|....*....|....*....
gi 1678143030 599 AVSVDVEGKMYSYCRE---AGITLFTVSH 624
Cdd:PRK11231 168 YLDINHQVELMRLMRElntQGKTVVTVLH 196
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
451-595 |
1.08e-05 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 47.28 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 451 GDVLV-KDLTFEVKSGTNVLVCGPNGCGKSSLFR-ILGeLWPTWGGKVT---------KP----QRGkLFYIPQR----P 511
Cdd:COG0410 14 GGIHVlHGVSLEVEEGEIVALLGRNGAGKTTLLKaISG-LLPPRSGSIRfdgeditglPPhriaRLG-IGYVPEGrrifP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 512 YMT------LGSlrdqiiypHTREDMRRNGKTDEDLMQYLDIvqltyLEHREN---GLdaiedwidvLSGGEKQRIAMAR 582
Cdd:COG0410 92 SLTveenllLGA--------YARRDRAEVRADLERVYELFPR-----LKERRRqraGT---------LSGGEQQMLAIGR 149
|
170
....*....|...
gi 1678143030 583 LFYHSPQFAILDE 595
Cdd:COG0410 150 ALMSRPKLLLLDE 162
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
504-625 |
1.15e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.87 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 504 LFYI-PQRPYMTLGSLRDQIIYPH---TREDMRRNGK---TDEdlmqyldivqltYLEHRENGLDA-IEDWIDVLSGGEK 575
Cdd:PTZ00265 1297 LFSIvSQEPMLFNMSIYENIKFGKedaTREDVKRACKfaaIDE------------FIESLPNKYDTnVGPYGKSLSGGQK 1364
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1678143030 576 QRIAMARLFYHSPQFAILDECTSAVSVD----VEGKMYSYCREAGITLFTVSHR 625
Cdd:PTZ00265 1365 QRIAIARALLREPKILLLDEATSSLDSNseklIEKTIVDIKDKADKTIITIAHR 1418
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
457-640 |
1.44e-05 |
|
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: 47.02 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 457 DLTFEVKSGT----NVLV-CGPNGCGKSSLFRIL-GELWPTwGGKVTKPqRGKLFYIPQrpYMtlgslrdQIIYPHTRED 530
Cdd:cd03237 12 EFTLEVEGGSisesEVIGiLGPNGIGKTTFIKMLaGVLKPD-EGDIEIE-LDTVSYKPQ--YI-------KADYEGTVRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 531 MRRnGKTDE---------DLMQYLDIVQLtylehrengldaIEDWIDVLSGGEKQRIAMARLFYHSPQFAILDEcTSAvS 601
Cdd:cd03237 81 LLS-SITKDfythpyfktEIAKPLQIEQI------------LDREVPELSGGELQRVAIAACLSKDADIYLLDE-PSA-Y 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1678143030 602 VDVEGKMYSycrEAGITLFTVSHRKSLWV-HHDFFLQ---------FDG 640
Cdd:cd03237 146 LDVEQRLMA---SKVIRRFAENNEKTAFVvEHDIIMIdyladrlivFEG 191
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
455-595 |
1.44e-05 |
|
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: 46.96 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 455 VKDLTFEVKSGTNVLVCGPNGCGKSSLFRIL-GELWPTwGGKVT---------KP------------QRGKLF------- 505
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLItGFYRPT-SGRILfdgrditglPPhriarlgiartfQNPRLFpeltvle 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 506 --YIPQRPYMTLGSLRDQIIYPHTREDMRRNgktDEDLMQYLDIVqltylehrenGLDAIEDWI-DVLSGGEKQRIAMAR 582
Cdd:COG0411 99 nvLVAAHARLGRGLLAALLRLPRARREEREA---RERAEELLERV----------GLADRADEPaGNLSYGQQRRLEIAR 165
|
170
....*....|...
gi 1678143030 583 LFYHSPQFAILDE 595
Cdd:COG0411 166 ALATEPKLLLLDE 178
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
450-641 |
1.71e-05 |
|
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: 45.98 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 450 NGDVLVKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGelwptwGGKVTKPQRGKLFY---------IPQRPYMTLGsLRD 520
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIM------GHPKYEVTEGEILFkgeditdlpPEERARLGIF-LAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 521 QiiYPhtredMRRNGKTDEDLMQYLDivqltylehrengldaiedwiDVLSGGEKQRIAMARLFYHSPQFAILDECTSAV 600
Cdd:cd03217 84 Q--YP-----PEIPGVKNADFLRYVN---------------------EGFSGGEKKRNEILQLLLLEPDLAILDEPDSGL 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1678143030 601 SVD---VEGKMYSYCREAGITLFTVSHRKSL--WVHHDF-FLQFDGR 641
Cdd:cd03217 136 DIDalrLVAEVINKLREEGKSVLIITHYQRLldYIKPDRvHVLYDGR 182
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
454-600 |
1.97e-05 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 46.92 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 454 LVKDLTFEVKSGTNVLVCGPNGCGKSSLFRIL-GELWPT-----WGGKVTKPQRGKLFYIPQRPYMTLGSLRDQIIYPHT 527
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLsGLLRPQkgavlWQGKPLDYSKRGLLALRQQVATVFQDPEQQIFYTDI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 528 RED----MRRNGKTDEDLMQYLD----IVQLTYLEHREngldaiedwIDVLSGGEKQRIAMARLFYHSPQFAILDECTSA 599
Cdd:PRK13638 96 DSDiafsLRNLGVPEAEITRRVDealtLVDAQHFRHQP---------IQCLSHGQKKRVAIAGALVLQARYLLLDEPTAG 166
|
.
gi 1678143030 600 V 600
Cdd:PRK13638 167 L 167
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
438-628 |
2.54e-05 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 46.02 E-value: 2.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 438 IIKFENVPLVTPNGDVLVKDLTFEVKSGTNVLVCGPNGCGKSSLFRIL--------GELWPTwGGKVTKPQRGKLFYIPQ 509
Cdd:PRK10908 1 MIRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLIcgierpsaGKIWFS-GHDITRLKNREVPFLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 510 RPYMTLGS---LRDQIIYPHTREDMRRNGKTDEDLMQY----LDIVQLtylehrengLDAIEDWIDVLSGGEKQRIAMAR 582
Cdd:PRK10908 80 QIGMIFQDhhlLMDRTVYDNVAIPLIIAGASGDDIRRRvsaaLDKVGL---------LDKAKNFPIQLSGGEQQRVGIAR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1678143030 583 LFYHSPQFAILDECT----SAVSVDVEgKMYSYCREAGITLFTVSHRKSL 628
Cdd:PRK10908 151 AVVNKPAVLLADEPTgnldDALSEGIL-RLFEEFNRVGVTVLMATHDIGL 199
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
458-598 |
2.58e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 46.62 E-value: 2.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 458 LTFEVKSGTNVLVCGPNGCGKSSLFRILGELWPTWGGKVT----KPQRGKLFYIPQRPYMTLGSLRDQIIYPHTRED--- 530
Cdd:PRK13642 26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKidgeLLTAENVWNLRRKIGMVFQNPDNQFVGATVEDDvaf 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1678143030 531 -MRRNGKTDEDLMQYLDIVQLTYlehreNGLDAIEDWIDVLSGGEKQRIAMARLFYHSPQFAILDECTS 598
Cdd:PRK13642 106 gMENQGIPREEMIKRVDEALLAV-----NMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTS 169
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
455-609 |
2.66e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 47.31 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 455 VKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELWPTWGGKVTkpQRGKLFYI--PQRpymtlgSLRDQIIYphTREDMR 532
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVT--LDGHEVVTrsPQD------GLANGIVY--ISEDRK 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 533 RNGKT-DEDLMQYLDIVQLTYLEHRENGLD------AIEDWIDV--------------LSGGEKQRIAMARLFYHSPQFA 591
Cdd:PRK10762 338 RDGLVlGMSVKENMSLTALRYFSRAGGSLKhadeqqAVSDFIRLfniktpsmeqaiglLSGGNQQKVAIARGLMTRPKVL 417
|
170
....*....|....*...
gi 1678143030 592 ILDECTSAVSVDVEGKMY 609
Cdd:PRK10762 418 ILDEPTRGVDVGAKKEIY 435
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
439-595 |
2.72e-05 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 46.76 E-value: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 439 IKFENVPLVTPNGDVLVKDLTFEVKSGTNVLVCGPNGCGKSSLFRIL--------GELWptWGGKVT---KPqrgklfyi 507
Cdd:PRK11650 4 LKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVagleritsGEIW--IGGRVVnelEP-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 508 pqrpymtlgSLRDqI--------IYPH--TREDM------RRNGKT--DEDLMQYLDIVQL-TYLEH--REngldaiedw 566
Cdd:PRK11650 74 ---------ADRD-IamvfqnyaLYPHmsVRENMayglkiRGMPKAeiEERVAEAARILELePLLDRkpRE--------- 134
|
170 180
....*....|....*....|....*....
gi 1678143030 567 idvLSGGEKQRIAMARLFYHSPQFAILDE 595
Cdd:PRK11650 135 ---LSGGQRQRVAMGRAIVREPAVFLFDE 160
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
472-595 |
3.17e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 46.41 E-value: 3.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 472 GPNGCGKSSLFRILGELwptwggkvTKPQRGK-------LFYIPQRPYMTLGSLR------DQIIYPHTRedMRRN---G 535
Cdd:PRK11144 31 GRSGAGKTSLINAISGL--------TRPQKGRivlngrvLFDAEKGICLPPEKRRigyvfqDARLFPHYK--VRGNlryG 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 536 KTDEDLMQYLDIVQLTYLEHRENGLDAiedwidVLSGGEKQRIAMARLFYHSPQFAILDE 595
Cdd:PRK11144 101 MAKSMVAQFDKIVALLGIEPLLDRYPG------SLSGGEKQRVAIGRALLTAPELLLMDE 154
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
418-627 |
3.22e-05 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 47.01 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 418 VVNGNSDFGPGKGAMEFvdNIIKFeNVPlvTPNGDVLvKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELWPTWGGKV- 496
Cdd:PRK10789 300 VKDGSEPVPEGRGELDV--NIRQF-TYP--QTDHPAL-ENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIr 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 497 ------TKPQ----RGKLFYIPQRPYMTLGSLRDQIIyphtredMRRNGKTDEDLMQ-------YLDIVQLT--YL-EHR 556
Cdd:PRK10789 374 fhdiplTKLQldswRSRLAVVSQTPFLFSDTVANNIA-------LGRPDATQQEIEHvarlasvHDDILRLPqgYDtEVG 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1678143030 557 ENGLdaiedwidVLSGGEKQRIAMARLFYHSPQFAILDECTSAVSVDVEGKMYSYCRE--AGITLFTVSHRKS 627
Cdd:PRK10789 447 ERGV--------MLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQwgEGRTVIISAHRLS 511
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
454-626 |
3.31e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 45.33 E-value: 3.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 454 LVKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELWptwggkvtKPQRGKLFYIPQRPYMTLGSLRDQI--------IYP 525
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLL--------NPEKGEILFERQSIKKDLCTYQKQLcfvghrsgINP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 526 H--TREDMRRNGKTDEDLMQYLDIVQLTYLEHrengldaiedWID----VLSGGEKQRIAMARLFYHSPQFAILDEctSA 599
Cdd:PRK13540 88 YltLRENCLYDIHFSPGAVGITELCRLFSLEH----------LIDypcgLLSSGQKRQVALLRLWMSKAKLWLLDE--PL 155
|
170 180 190
....*....|....*....|....*....|...
gi 1678143030 600 VSVD------VEGKMYSYCREAGITLFTvSHRK 626
Cdd:PRK13540 156 VALDelslltIITKIQEHRAKGGAVLLT-SHQD 187
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
462-598 |
4.24e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 46.73 E-value: 4.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 462 VKSGTNVLVCGPNGCGKSSLFRIL-GELWP---------TW--------------------GGKVT---KPQrgklfYIP 508
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILsGELIPnlgdyeeepSWdevlkrfrgtelqnyfkklyNGEIKvvhKPQ-----YVD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 509 QRPYMTLGSLRDQIiyphTREDMRrnGKTDEdlmqYLDIVQLTYLEHREngldaiedwIDVLSGGEKQRIAMARLFYHSP 588
Cdd:PRK13409 171 LIPKVFKGKVRELL----KKVDER--GKLDE----VVERLGLENILDRD---------ISELSGGELQRVAIAAALLRDA 231
|
170
....*....|
gi 1678143030 589 QFAILDECTS 598
Cdd:PRK13409 232 DFYFFDEPTS 241
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
454-598 |
5.26e-05 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 46.19 E-value: 5.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 454 LVKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELWPTW----------GGKVTKPQRGKLFYIPQRPYMTLGSL--RDQ 521
Cdd:TIGR00955 40 LLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgsgsvllnGMPIDAKEMRAISAYVQQDDLFIPTLtvREH 119
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678143030 522 IIY-PHTRedMRRNGKTDEDLMQYLDIVQLTYLEHRENGLDAIEDWIDVLSGGEKQRIAMARLFYHSPQFAILDECTS 598
Cdd:TIGR00955 120 LMFqAHLR--MPRRVTKKEKRERVDEVLQALGLRKCANTRIGVPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTS 195
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
455-600 |
6.49e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 45.16 E-value: 6.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 455 VKDLTFEVKSGTNVLVCGPNGCGKSSLFRI---LGELWPTW--GGKVTkpQRGKLFYIP---------------QRPYMT 514
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIPGFrvEGKVT--FHGKNLYAPdvdpvevrrrigmvfQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 515 LGSLRDQIIYphtreDMRRNG-KTDEDLMQYLDIVQLTYLEH-----RENGLDaiedwidvLSGGEKQRIAMARLFYHSP 588
Cdd:PRK14243 104 PKSIYDNIAY-----GARINGyKGDMDELVERSLRQAALWDEvkdklKQSGLS--------LSGGQQQRLCIARAIAVQP 170
|
170
....*....|..
gi 1678143030 589 QFAILDECTSAV 600
Cdd:PRK14243 171 EVILMDEPCSAL 182
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
455-574 |
6.82e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 44.96 E-value: 6.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 455 VKDLTFEVKSGTnvLVCGPNGCGKSSLFRILGELwptwggkvtkpQRGKLFYIPqrpymtlgSLRD--QIIYPHTREDMR 532
Cdd:COG4938 12 FKEAELELKPLT--LLIGPNGSGKSTLIQALLLL-----------LQSNFIYLP--------AERSgpARLYPSLVRELS 70
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1678143030 533 RNGKTDEDLMQYLDIVQLTYLEHRENG--LDAIEDWIDVLSGGE 574
Cdd:COG4938 71 DLGSRGEYTADFLAELENLEILDDKSKelLEQVEEWLEKIFPGK 114
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
455-614 |
7.21e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 45.85 E-value: 7.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 455 VKDLTFEVKSGTNVLVCGPNGCGKS----SLFRILgelwPTwgGKVTKPQ---------------------RG-KLFYIP 508
Cdd:PRK15134 25 VNDVSLQIEAGETLALVGESGSGKSvtalSILRLL----PS--PPVVYPSgdirfhgesllhaseqtlrgvRGnKIAMIF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 509 QRPYMTLGSLrdqiiypHTRED-----------MRRNGKTDEdLMQYLDIVQLTYLEHRENgldaieDWIDVLSGGEKQR 577
Cdd:PRK15134 99 QEPMVSLNPL-------HTLEKqlyevlslhrgMRREAARGE-ILNCLDRVGIRQAAKRLT------DYPHQLSGGERQR 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 1678143030 578 --IAMARLfyHSPQFAILDECTSAVSVDVEGKMYSYCRE 614
Cdd:PRK15134 165 vmIAMALL--TRPELLIADEPTTALDVSVQAQILQLLRE 201
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
455-634 |
1.05e-04 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 45.02 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 455 VKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELW-PTWG--------------GKVTKPQRGKLFYIPQR----PYMTl 515
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIePTRGqvlidgvdiakisdAELREVRRKKIAMVFQSfalmPHMT- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 516 gslrdqiIYPHTREDMRRNG-KTDEDLMQYLDIVQLTYLEHRENGldaiedWIDVLSGGEKQRIAMARLFYHSPQFAILD 594
Cdd:PRK10070 123 -------VLDNTAFGMELAGiNAEERREKALDALRQVGLENYAHS------YPDELSGGMRQRVGLARALAINPDILLMD 189
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1678143030 595 ECTSAVSVDVEGKMysycREAGITLFTVSHRKSLWVHHDF 634
Cdd:PRK10070 190 EAFSALDPLIRTEM----QDELVKLQAKHQRTIVFISHDL 225
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
455-503 |
1.10e-04 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 44.30 E-value: 1.10e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1678143030 455 VKDLTFEVKSGTNVLVCGPNGCGKSSLFRILgelwptwgGKVTKPQRGK 503
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLI--------AGILEPTSGR 82
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
432-581 |
1.17e-04 |
|
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: 45.16 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 432 MEFVDNIIKFEN-VPLVTPNGDVLVK---------DLTFEVKSGT----NVL-VCGPNGCGKSSLFRIL-GELWPTwGGK 495
Cdd:COG1245 318 VRIRDEPIEFEVhAPRREKEEETLVEypdltksygGFSLEVEGGEiregEVLgIVGPNGIGKTTFAKILaGVLKPD-EGE 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 496 VTKPQrgKLFYIPQRPymtlgslrdQIIYPHTREDMRRNGKTD--EDLMQYLDIV---QLTYLEHREngldaiedwIDVL 570
Cdd:COG1245 397 VDEDL--KISYKPQYI---------SPDYDGTVEEFLRSANTDdfGSSYYKTEIIkplGLEKLLDKN---------VKDL 456
|
170
....*....|.
gi 1678143030 571 SGGEKQRIAMA 581
Cdd:COG1245 457 SGGELQRVAIA 467
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
435-595 |
1.53e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 43.96 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 435 VDNIIKFENVPLVTPNGDVLVKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELWPTWGGKVT-----------KPQRGK 503
Cdd:PRK13647 1 MDNIIEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKvmgrevnaeneKWVRSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 504 LFYIPQRPymtlgslRDQIIYPHTRED-------MRRNGK-TDEDLMQYLDIVQLTYLEHRENgldaiedwiDVLSGGEK 575
Cdd:PRK13647 81 VGLVFQDP-------DDQVFSSTVWDDvafgpvnMGLDKDeVERRVEEALKAVRMWDFRDKPP---------YHLSYGQK 144
|
170 180
....*....|....*....|
gi 1678143030 576 QRIAMARLFYHSPQFAILDE 595
Cdd:PRK13647 145 KRVAIAGVLAMDPDVIVLDE 164
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
455-497 |
2.79e-04 |
|
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: 42.90 E-value: 2.79e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1678143030 455 VKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELWPTWGGKVT 497
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
454-637 |
3.13e-04 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 43.03 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 454 LVKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELwptwggkvTKPQRGKLFYIPQRPYMT--------------LGSLR 519
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFL--------EKPSEGSIVVNGQTINLVrdkdgqlkvadknqLRLLR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 520 DQIIYPHTREDMRRNGKTDEDLMQY-LDIVQLTYLEHREN--------GLD--AIEDWIDVLSGGEKQRIAMARLFYHSP 588
Cdd:PRK10619 92 TRLTMVFQHFNLWSHMTVLENVMEApIQVLGLSKQEARERavkylakvGIDerAQGKYPVHLSGGQQQRVSIARALAMEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1678143030 589 QFAILDECTSAVSVDVEGKMYSYCR---EAGITLFTVSHRKSLWVH---HDFFLQ 637
Cdd:PRK10619 172 EVLLFDEPTSALDPELVGEVLRIMQqlaEEGKTMVVVTHEMGFARHvssHVIFLH 226
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
436-485 |
3.27e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 43.57 E-value: 3.27e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1678143030 436 DNIIKFENvpLVTPNGD-VLVKDLTFEVKSGTNVLVCGPNGCGKSSLFRIL 485
Cdd:PRK11819 322 DKVIEAEN--LSKSFGDrLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMI 370
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
570-628 |
6.16e-04 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 41.69 E-value: 6.16e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1678143030 570 LSGGEKQRIAMARLFYHSPQFAILDECTSAVSVDVEGK----MYSYCREAGITLFTVSHRKSL 628
Cdd:PRK10584 147 LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKiadlLFSLNREHGTTLILVTHDLQL 209
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
439-624 |
6.98e-04 |
|
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: 42.48 E-value: 6.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 439 IKFENVpLVTPNGDVLVKDLTFEVKSGTNVLVCGPNGCGKSSLFRIL--------------------------------G 486
Cdd:TIGR03269 1 IEVKNL-TKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgmdqyeptsgriiyhvalcekcgyverpskvG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 487 ELWPTWGG--------------KVTKPQRGKLFYIPQRPYMTLGslrDQIIYPHTREDMRRNG-KTDEDLMQYLDIVQLT 551
Cdd:TIGR03269 80 EPCPVCGGtlepeevdfwnlsdKLRRRIRKRIAIMLQRTFALYG---DDTVLDNVLEALEEIGyEGKEAVGRAVDLIEMV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1678143030 552 YLEHRengldaIEDWIDVLSGGEKQRIAMARLFYHSPQFAILDECTSAVSVDVEGKMYSYCREA----GITLFTVSH 624
Cdd:TIGR03269 157 QLSHR------ITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvkasGISMVLTSH 227
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
439-624 |
8.64e-04 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 41.61 E-value: 8.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 439 IKFENVPLVTPNgdVLVKDLTFEVKSGTNVLVCGPNGCGKS-SLFRILGELWP----TWG-----GKVTKPQ--RGKLF- 505
Cdd:PRK10418 5 IELRNIALQAAQ--PLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILPAgvrqTAGrvlldGKPVAPCalRGRKIa 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 506 YIPQRPYMTLGSLRDqiIYPHTREDMRRNGKTDED--LMQYLDIVQLTYlEHRENGLDAIEdwidvLSGGEKQR--IAMA 581
Cdd:PRK10418 83 TIMQNPRSAFNPLHT--MHTHARETCLALGKPADDatLTAALEAVGLEN-AARVLKLYPFE-----MSGGMLQRmmIALA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1678143030 582 rLFYHSPqFAILDECTSAVSVDVEGK----MYSYCREAGITLFTVSH 624
Cdd:PRK10418 155 -LLCEAP-FIIADEPTTDLDVVAQARildlLESIVQKRALGMLLVTH 199
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
457-624 |
9.26e-04 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 41.45 E-value: 9.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 457 DLTFEVKSGTNVLVCGPNGCGKSSLFRIL-GELwptwggkvtKPQRGKLFYIpqrpyMTLGSLRDqiIYPHTREDMRRNG 535
Cdd:PRK11701 24 DVSFDLYPGEVLGIVGESGSGKTTLLNALsARL---------APDAGEVHYR-----MRDGQLRD--LYALSEAERRRLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 536 KTD-----------------------EDLM-----QYLDIVQ--LTYLEHRENGLDAIEDWIDVLSGGEKQRIAMARLFY 585
Cdd:PRK11701 88 RTEwgfvhqhprdglrmqvsaggnigERLMavgarHYGDIRAtaGDWLERVEIDAARIDDLPTTFSGGMQQRLQIARNLV 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1678143030 586 HSPQFAILDECTSAVSVDVEGK----MYSYCREAGITLFTVSH 624
Cdd:PRK11701 168 THPRLVFMDEPTGGLDVSVQARlldlLRGLVRELGLAVVIVTH 210
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
437-620 |
1.06e-03 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 40.71 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 437 NIIKFENVPLVTPNGDV---LVKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELWPTWG---GKVTKPqrGKLFYIPQR 510
Cdd:cd03233 2 STLSWRNISFTTGKGRSkipILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYN--GIPYKEFAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 511 PYmtlgslRDQIIYphtredmrrNGKTDEDlMQYLDIVQLTYLEHRENGldaiEDWIDVLSGGEKQRIAMARLFYHSPQF 590
Cdd:cd03233 80 KY------PGEIIY---------VSEEDVH-FPTLTVRETLDFALRCKG----NEFVRGISGGERKRVSIAEALVSRASV 139
|
170 180 190
....*....|....*....|....*....|....
gi 1678143030 591 AILDECT----SAVSVDVEGKMYSYCREAGITLF 620
Cdd:cd03233 140 LCWDNSTrgldSSTALEILKCIRTMADVLKTTTF 173
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
455-485 |
4.93e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 39.60 E-value: 4.93e-03
10 20 30
....*....|....*....|....*....|.
gi 1678143030 455 VKDLTFEVKSGTNVLVcGPNGCGKSSLFRIL 485
Cdd:COG3593 14 IKDLSIELSDDLTVLV-GENNSGKSSILEAL 43
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
439-599 |
6.60e-03 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 39.40 E-value: 6.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 439 IKFENVPLVTPNGD---VLVKDLTFEVKSGTNVLVCGPNGCGKSSLFRILGELwptwggkvTKPQRGKLF----YIPQRP 511
Cdd:PRK11153 2 IELKNISKVFPQGGrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLL--------ERPTSGRVLvdgqDLTALS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678143030 512 YMTLGSLRDQI--IYPH-------TRED-----MRRNGKTDEDLMQ----YLDIVQLTylEHRengldaiedwiDV---- 569
Cdd:PRK11153 74 EKELRKARRQIgmIFQHfnllssrTVFDnvalpLELAGTPKAEIKArvteLLELVGLS--DKA-----------DRypaq 140
|
170 180 190
....*....|....*....|....*....|
gi 1678143030 570 LSGGEKQRIAMARLFYHSPQFAILDECTSA 599
Cdd:PRK11153 141 LSGGQKQRVAIARALASNPKVLLCDEATSA 170
|
|
| |
