|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
103-746 |
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: 691.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 103 RSLSLRRSSNVQENTNVVEQTSPVEKSTDVNLK------RTDFLMKLLLGDK--KVMILFMTQAFLLVLRTFLSLHVATL 174
Cdd:TIGR00954 39 RAADRRGDKSGKEELTIVGKHSTIEGAKKKAHVngvflgKLDFLLKILIPRVfcKETGLLILIAFLLVSRTYLSVYVATL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 175 DGRLVSSLVKAQYGKFLKILLgQWMVLGIPASFINSLINYVTKLCSVSINRLVTNHLMGKYLSNHrTFYAVAAADSA-SE 253
Cdd:TIGR00954 119 DGQIESSIVRRSPRNFAWILF-KWFLIAPPASFINSAIKYLLKELKLRFRVRLTRYLYSKYLSGF-TFYKVSNLDSRiQN 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 254 VQDNLTKDISKFSNNTSVLLNQLLKPMLDLILCSFKLLMSGSGVMGEGTLVLgliVYISNSMLKLIQPNFTKITMMRSSL 333
Cdd:TIGR00954 197 PDQLLTQDVEKFCDSVVELYSNLTKPILDVILYSFKLLTALGSVGPAGLFAY---LFATGVVLTKLRPPIGKLTVEEQAL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 334 ESWFRSLHSSVHRNNEEIALLRGQSRELTSLDFSFYRLAFFMGREIKARAFYDLASTFVIKYTWGAAGLALCSIPIFFKG 413
Cdd:TIGR00954 274 EGEYRYVHSRLIMNSEEIAFYQGNKVEKETVMSSFYRLVEHLNLIIKFRFSYGFLDNIVAKYTWSAVGLVAVSIPIFDKT 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 414 KVQNGDQpDATDATADFITNRRLLLTASSSVGRFVELKKNIQELRGTSLRLNYLNDLLDKYAVGNIDK-KDEDVLDL--- 489
Cdd:TIGR00954 354 HPAFLEM-SEEELMQEFYNNGRLLLKAADALGRLMLAGRDMTRLAGFTARVDTLLQVLDDVKSGNFKRpRVEEIESGreg 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 490 ------------VEYNENLIKFEHVPLITPANQVLVPELNFELKHGDHLLIIGPNGCGKSSLFRLLGGLWPIRQietgvq 557
Cdd:TIGR00954 433 grnsnlvpgrgiVEYQDNGIKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYG------ 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 558 TKLTVPPrkigqDCAIFYLPQKPYMGNGsTFREQIIYPDTIEDFEERfngdyNMGDEKLISVLELLDLTDLITENLSlvl 637
Cdd:TIGR00954 507 GRLTKPA-----KGKLFYVPQRPYMTLG-TLRDQIIYPDSSEDMKRR-----GLSDKDLEQILDNVQLTHILEREGG--- 572
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 638 agkgtkksdnldeenlteiraaFDLKRNWSEELSIGVQQRLAMARMYYHKPKFAVLDECTSAVSPEMEQKMYENAQNLGI 717
Cdd:TIGR00954 573 ----------------------WSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFGI 630
|
650 660
....*....|....*....|....*....
gi 50285999 718 SVISVCHRTTLWHFHNYLLKFDGKGSYQF 746
Cdd:TIGR00954 631 TLFSVSHRKSLWKYHEYLLYMDGRGGYQF 659
|
|
| ABC_membrane_2 |
pfam06472 |
ABC transporter transmembrane region 2; This domain covers the transmembrane of a small family ... |
140-410 |
1.48e-75 |
|
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: 247.14 E-value: 1.48e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 140 LMKLLLG--DKKVMILFMTQAFLLVLRTFLSLHVATLDGRLVSSLVKAQYGKFlKILLGQWMVLGIPASFINSLINYVTK 217
Cdd:pfam06472 1 LLKILFPrwFSKEAGLLLALAALLVLRTFLSVLVAQLDGQIVKALVAKNGRGF-IRLLLKWALLAVPASFVNSALKYLTQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 218 LCSVSINRLVTNHLMGKYLSNhRTFYAVAAADSA-SEVQDNLTKDISKFSNNTSVLLNQLLKPMLDLILCSFKLlmsgSG 296
Cdd:pfam06472 80 RLALRFRTRLTRHLHDEYLKG-RTYYKMSNLDGRiDNPDQRITQDVEKFCSSLSDLYSNLLKPILDIILFTFRL----WR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 297 VMG-EGTLVLGLIVYISNSMLKLIQPNFTKITMMRSSLESWFRSLHSSVHRNNEEIALLRGQSRELTSLDFSFYRLAFFM 375
Cdd:pfam06472 155 LSGwRGPAILFLYVLLSAVILRRLSPPFGKLVAEEQKLEGEFRYLHSRLITNAEEIAFYRGEKREKKQLQRSFKSLIDHM 234
|
250 260 270
....*....|....*....|....*....|....*
gi 50285999 376 GREIKARAFYDLASTFVIKYTWGAAGLALCSIPIF 410
Cdd:pfam06472 235 RRILRRRLWYGFIEDFVLKYTWSILGYVLVALPIF 269
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
497-744 |
2.14e-71 |
|
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: 232.04 E-value: 2.14e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 497 IKFEHVPLITPANQVLVPELNFELKHGDHLLIIGPNGCGKSSLFRLLGGLWPIRQietGvqtKLTVPPrkigqDCAIFYL 576
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGS---G---RIGMPE-----GEDLLFL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 577 PQKPYMGNGsTFREQIIYPdtiedfeerfngdynmgdeklisvlelldltdlitenlslvlagkgtkksdnldeenltei 656
Cdd:cd03223 70 PQRPYLPLG-TLREQLIYP------------------------------------------------------------- 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 657 raafdlkrnWSEELSIGVQQRLAMARMYYHKPKFAVLDECTSAVSPEMEQKMYENAQNLGISVISVCHRTTLWHFHNYLL 736
Cdd:cd03223 88 ---------WDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGHRPSLWKFHDRVL 158
|
....*...
gi 50285999 737 KFDGKGSY 744
Cdd:cd03223 159 DLDGEGGW 166
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
150-746 |
1.28e-68 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 238.17 E-value: 1.28e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 150 VMILFMT--QAFLLVLRTFLSlhvatldGRLVSSLVKAQYGKFLKiLLGQWMVLGIPASFINSLINYVTKLcsVSIN--R 225
Cdd:COG4178 28 ALLLLLTlaSVGLNVLLNFWN-------RDFYDALQARDAAAFWQ-QLGVFALLAAISILLAVYQTYLRQR--LQIRwrE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 226 LVTNHLMGKYLSNhRTFYAVAAADSASevqDN----LTKDISKFSNNTSVLLNQLLKPMLDLIlcSF-KLLMSGSGVMG- 299
Cdd:COG4178 98 WLTERLLDRWLSN-RAYYRLQLSGGEI---DNpdqrIAEDIRLFTETTLSLSLGLLSSVVTLI--SFiGILWSLSGSLTf 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 300 ---------EGTLVLGLIVY-ISNSML------KLIQPNFtkitmMRSSLESWFRS--LHssVHRNNEEIALLRGQSREL 361
Cdd:COG4178 172 tlggysitiPGYMVWAALIYaIIGTLLthligrPLIRLNF-----EQQRREADFRFalVR--VRENAESIALYRGEAAER 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 362 TSLDFSFYRLAFFMGREIKARAFYDLASTFvikYTWGAAGLA-LCSIPIFFKGKVQNGDqpdatdatadfitnrrlLLTA 440
Cdd:COG4178 245 RRLRRRFDAVIANWRRLIRRQRNLTFFTTG---YGQLAVIFPiLVAAPRYFAGEITLGG-----------------LMQA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 441 SSSVGR-------FVELKKNIQELRGTSLRLNYLNDLLDkyavgNIDKKDEDVLDLVEYNENLIKFEHVPLITPANQVLV 513
Cdd:COG4178 305 ASAFGQvqgalswFVDNYQSLAEWRATVDRLAGFEEALE-----AADALPEAASRIETSEDGALALEDLTLRTPDGRPLL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 514 PELNFELKHGDHLLIIGPNGCGKSSLFRLLGGLWPirqIETGvqtKLTVPPrkiGQDcaIFYLPQKPYMGNGsTFREQII 593
Cdd:COG4178 380 EDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWP---YGSG---RIARPA---GAR--VLFLPQRPYLPLG-TLREALL 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 594 YPDTIEDFEerfngdynmgDEKLISVLELLDLTDLItenlslvlagkgtkksDNLDEEnlteiraafdlkRNWSEELSIG 673
Cdd:COG4178 448 YPATAEAFS----------DAELREALEAVGLGHLA----------------ERLDEE------------ADWDQVLSLG 489
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 50285999 674 VQQRLAMARMYYHKPKFAVLDECTSAVSPEMEQKMYE--NAQNLGISVISVCHRTTLWHFHNYLLKFDGKGSYQF 746
Cdd:COG4178 490 EQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQllREELPGTTVISVGHRSTLAAFHDRVLELTGDGSWQL 564
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
139-725 |
2.68e-18 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 89.45 E-value: 2.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 139 FLMKLLLGDKKVMILFMtqaFLLVLRTFLSLHVATLDGRLVSSLVKAQYGKFLKILLGQWMVLGIPASFINSLINYVTKL 218
Cdd:COG1132 11 RLLRYLRPYRGLLILAL---LLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLLAR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 219 CSVSINRLVTNHLMGKYLSNHRTFYAvaaADSASEVQDNLTKDISKFSNNTSVLLNQLLKPMLdLILCSFKLLMSGSGVM 298
Cdd:COG1132 88 LAQRVVADLRRDLFEHLLRLPLSFFD---RRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVV-TLIGALVVLFVIDWRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 299 GEGTLV-LGLIVYISNSMLKLIQPNFTKITMMRSSLeswFRSLHSSVHrNNEEIALLRGQSRELTSLDFSFYRLAFFMGR 377
Cdd:COG1132 164 ALIVLLvLPLLLLVLRLFGRRLRKLFRRVQEALAEL---NGRLQESLS-GIRVVKAFGREERELERFREANEELRRANLR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 378 EIKARAFYDLASTFVIkyTWGAAGLALCSIPIFFKGKVQNGDqpdatdATAdFITnrrLLLTASSSVGRFVELKKNIQEL 457
Cdd:COG1132 240 AARLSALFFPLMELLG--NLGLALVLLVGGLLVLSGSLTVGD------LVA-FIL---YLLRLFGPLRQLANVLNQLQRA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 458 RGTSLRLNylnDLLDkYAVGNIDKKDEDVLDLVEYNenlIKFEHV----PlitPANQVLvPELNFELKHGDHLLIIGPNG 533
Cdd:COG1132 308 LASAERIF---ELLD-EPPEIPDPPGAVPLPPVRGE---IEFENVsfsyP---GDRPVL-KDISLTIPPGETVALVGPSG 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 534 CGKSSLFRLLGGLW------------PIRQIetgvqtKLTVPPRKIGqdcaifYLPQKPYMGNGsTFREQIIYpdtiedf 601
Cdd:COG1132 377 SGKSTLVNLLLRFYdptsgrilidgvDIRDL------TLESLRRQIG------VVPQDTFLFSG-TIRENIRY------- 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 602 eerfnGDYNMGDEKLISVLELLDLTDLItenlslvlagkgTKKSDNLDeenlTEI--RAAfdlkrnwseELSIGVQQRLA 679
Cdd:COG1132 437 -----GRPDATDEEVEEAAKAAQAHEFI------------EALPDGYD----TVVgeRGV---------NLSGGQRQRIA 486
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 50285999 680 MARMYYHKPKFAVLDECTSAVSPEMEQKMYENAQNL--GISVISVCHR 725
Cdd:COG1132 487 IARALLKDPPILILDEATSALDTETEALIQEALERLmkGRTTIVIAHR 534
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
497-725 |
4.68e-18 |
|
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: 82.43 E-value: 4.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 497 IKFEHVPLITPANQVLVPE-LNFELKHGDHLLIIGPNGCGKSSLFRLLGGLWPIRQ--IETGVQTKLTVPPRKIGQdcAI 573
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKdVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSgeILIDGVDLRDLDLESLRK--NI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 574 FYLPQKPYmgngstfreqiIYPDTIEdfeerfngdynmgdeklisvlelldltdlitenlslvlagkgtkksdnldeENL 653
Cdd:cd03228 79 AYVPQDPF-----------LFSGTIR---------------------------------------------------ENI 96
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50285999 654 teiraafdlkrnwseeLSIGVQQRLAMARMYYHKPKFAVLDECTSAVSPEMEQKMYENAQNL--GISVISVCHR 725
Cdd:cd03228 97 ----------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALakGKTVIVIAHR 154
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
497-724 |
5.62e-18 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 83.33 E-value: 5.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 497 IKFEHVPlITPANQVLVPELNFELKHGDHLLIIGPNGCGKSSLFRLLGGLWPI---------RQIETgvqtkltVPPRKI 567
Cdd:COG4619 1 LELEGLS-FRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPtsgeiyldgKPLSA-------MPPPEW 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 568 GQDCAifYLPQKPYMGNGsTFREQIIYPDTIEdfEERFNgdynmgDEKLISVLELLDLTDlitenlslvlagkgtkksDN 647
Cdd:COG4619 73 RRQVA--YVPQEPALWGG-TVRDNLPFPFQLR--ERKFD------RERALELLERLGLPP------------------DI 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 648 LDeenlteiraafdlkrnWS-EELSIGVQQRLAMARMYYHKPKFAVLDECTSAVSPEMEQK----MYENAQNLGISVISV 722
Cdd:COG4619 124 LD----------------KPvERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRveelLREYLAEEGRAVLWV 187
|
..
gi 50285999 723 CH 724
Cdd:COG4619 188 SH 189
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
436-725 |
1.23e-17 |
|
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: 87.58 E-value: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 436 LLLTASSSVGRFVELKKNIQELRGTSLRLNylnDLLDKyavgNIDKKDEDVLDLVEYNENLIKFEHV----PlitPANQV 511
Cdd:COG2274 420 LSGRFLAPVAQLIGLLQRFQDAKIALERLD---DILDL----PPEREEGRSKLSLPRLKGDIELENVsfryP---GDSPP 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 512 LVPELNFELKHGDHLLIIGPNGCGKSSLFRLLGGLW------------PIRQIETGVqtkLTvppRKIGqdcaifYLPQK 579
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYeptsgrilidgiDLRQIDPAS---LR---RQIG------VVLQD 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 580 PYmgngstfreqiIYPDTIEDfeerfN---GDYNMGDEKLISVLELLDLTDLItENLslvlagkgtkkSDNLDeenlTEI 656
Cdd:COG2274 558 VF-----------LFSGTIRE-----NitlGDPDATDEEIIEAARLAGLHDFI-EAL-----------PMGYD----TVV 605
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50285999 657 raafdlkrnwSEE---LSIGVQQRLAMARMYYHKPKFAVLDECTSAVSPEMEQKMYENAQNL--GISVISVCHR 725
Cdd:COG2274 606 ----------GEGgsnLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLlkGRTVIIIAHR 669
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
497-725 |
1.30e-15 |
|
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: 80.96 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 497 IKFEHVPLITPANQVLVPELNFELKHGDHLLIIGPNGCGKSSLFRLLGGLwpiRQIETGvqtKLTV---PPRKIGQD--- 570
Cdd:COG4988 337 IELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGF---LPPYSG---SILIngvDLSDLDPAswr 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 571 CAIFYLPQKPYmgngstfreqiIYPDTIEDfeerfN---GDYNMGDEKLISVLELLDLTDLITEnlslvlagkgtkKSDN 647
Cdd:COG4988 411 RQIAWVPQNPY-----------LFAGTIRE-----NlrlGRPDASDEELEAALEAAGLDEFVAA------------LPDG 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 648 LDeenlTEI--RAAfdlkrnwseELSIGVQQRLAMARMYYHKPKFAVLDECTSAVSPEMEQKMYENAQNL--GISVISVC 723
Cdd:COG4988 463 LD----TPLgeGGR---------GLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLakGRTVILIT 529
|
..
gi 50285999 724 HR 725
Cdd:COG4988 530 HR 531
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
509-724 |
2.06e-15 |
|
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: 76.03 E-value: 2.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 509 NQVLVPELNFELKHGDHLLIIGPNGCGKSSLFRLLGGLWPIRQietGVQTKLTVPPRKIGQDcaIFYLPQKPYMGNGstf 588
Cdd:cd03235 11 GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTS---GSIRVFGKPLEKERKR--IGYVPQRRSIDRD--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 589 reqiiYPDTIEDF-------EERFNGDYNMGD-EKLISVLELLDLTDLITENLSlvlagkgtkksdnldeenlteiraaf 660
Cdd:cd03235 83 -----FPISVRDVvlmglygHKGLFRRLSKADkAKVDEALERVGLSELADRQIG-------------------------- 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50285999 661 dlkrnwseELSIGVQQRLAMARMYYHKPKFAVLDECTSAVSPEMEQKMYENAQNL---GISVISVCH 724
Cdd:cd03235 132 --------ELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrreGMTILVVTH 190
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
516-698 |
2.23e-15 |
|
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: 74.22 E-value: 2.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 516 LNFELKHGDHLLIIGPNGCGKSSLFRLL-GGLWPIR-QI----ETGVQTKLTVPPRKIGqdcaifYLPQKPYMGNGSTFR 589
Cdd:pfam00005 4 VSLTLNPGEILALVGPNGAGKSTLLKLIaGLLSPTEgTIlldgQDLTDDERKSLRKEIG------YVFQDPQLFPRLTVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 590 EQIIYPDTIEDFEERfngdyNMgDEKLISVLELLDLTDLITENLSLVLAgkgtkksdnldeenlteiraafdlkrnwseE 669
Cdd:pfam00005 78 ENLRLGLLLKGLSKR-----EK-DARAEEALEKLGLGDLADRPVGERPG------------------------------T 121
|
170 180
....*....|....*....|....*....
gi 50285999 670 LSIGVQQRLAMARMYYHKPKFAVLDECTS 698
Cdd:pfam00005 122 LSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
497-725 |
3.28e-14 |
|
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: 73.03 E-value: 3.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 497 IKFEHVPLITPANQVLVPELNFELKHGDHLLIIGPNGCGKSSLFRLLGGLW------------PIRQIetgvqtKLTVPP 564
Cdd:cd03254 3 IEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYdpqkgqilidgiDIRDI------SRKSLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 565 RKIGqdcaifYLPQKPYMGNGsTFREQIIYpdtiedfeerfnGDYNMGDEKLISVLELLDLTDLItenlslvlagkgtKK 644
Cdd:cd03254 77 SMIG------VVLQDTFLFSG-TIMENIRL------------GRPNATDEEVIEAAKEAGAHDFI-------------MK 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 645 SDNLDEENLTEiraafdlkrnWSEELSIGVQQRLAMARMYYHKPKFAVLDECTSAVSPEMEQKMYENAQNL--GISVISV 722
Cdd:cd03254 125 LPNGYDTVLGE----------NGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLmkGRTSIII 194
|
...
gi 50285999 723 CHR 725
Cdd:cd03254 195 AHR 197
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
515-725 |
2.16e-13 |
|
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: 70.19 E-value: 2.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 515 ELNFELKHGDHLLIIGPNGCGKSSLFRLLGGLwpiRQIETGV-----QTKLTVPPRKIGQDCAifYLPQKPymgngstfR 589
Cdd:cd03225 19 DISLTIKKGEFVLIVGPNGSGKSTLLRLLNGL---LGPTSGEvlvdgKDLTKLSLKELRRKVG--LVFQNP--------D 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 590 EQIIYPDTIED--FeerfnGDYNMG------DEKLISVLELLDLTDLitenlslvlagkgtkksdnldeenlteiraafd 661
Cdd:cd03225 86 DQFFGPTVEEEvaF-----GLENLGlpeeeiEERVEEALELVGLEGL--------------------------------- 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50285999 662 lkRNWS-EELSIGVQQRLAMARMYYHKPKFAVLDECTSAVSPEMEQKMYE---NAQNLGISVISVCHR 725
Cdd:cd03225 128 --RDRSpFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLEllkKLKAEGKTIIIVTHD 193
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
497-728 |
3.43e-13 |
|
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: 69.54 E-value: 3.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 497 IKFEHVPLITPANQVL-VPELNFELKHGDHLLIIGPNGCGKSSLFRLLGGLW------------PIRQIetgvqtkltvP 563
Cdd:cd03245 3 IEFRNVSFSYPNQEIPaLDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYkptsgsvlldgtDIRQL----------D 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 564 PRKIGQDcaIFYLPQKPYMGNGsTFREQIIYPDTIEDfeerfngdynmgDEKLISVLELLDLTDLITEN---LSLVLAGK 640
Cdd:cd03245 73 PADLRRN--IGYVPQDVTLFYG-TLRDNITLGAPLAD------------DERILRAAELAGVTDFVNKHpngLDLQIGER 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 641 GtkksdnldeenlteiraafdlkrnwsEELSIGVQQRLAMARMYYHKPKFAVLDECTSAVSPEMEQKMYENAQNL--GIS 718
Cdd:cd03245 138 G--------------------------RGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLlgDKT 191
|
250
....*....|
gi 50285999 719 VISVCHRTTL 728
Cdd:cd03245 192 LIIITHRPSL 201
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
516-712 |
1.27e-12 |
|
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: 67.49 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 516 LNFELKHGDHLLIIGPNGCGKSSLFR-LLGGLWPirqietgVQTKLTVPPRkigqdcaIFYLPQKPYMGNGsTFREQIIy 594
Cdd:cd03250 24 INLEVPKGELVAIVGPVGSGKSSLLSaLLGELEK-------LSGSVSVPGS-------IAYVSQEPWIQNG-TIRENIL- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 595 pdtiedFEERFNgdynmgDEKLISVLEL--LDlTDLitenlslvlagkgtkksDNLDEENLTEIraafdlkrnwSEE--- 669
Cdd:cd03250 88 ------FGKPFD------EERYEKVIKAcaLE-PDL-----------------EILPDGDLTEI----------GEKgin 127
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 50285999 670 LSIGVQQRLAMARMYYHKPKFAVLDECTSAVSPEMEQKMYENA 712
Cdd:cd03250 128 LSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENC 170
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
508-725 |
3.91e-12 |
|
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: 65.32 E-value: 3.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 508 ANQVLVPELNFELKHGDHLLIIGPNGCGKSSLFRLLGGLWPIRQ--IETGVQTKLTVPPRKIGQDCAifYLPQkpymgng 585
Cdd:cd03246 13 AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSgrVRLDGADISQWDPNELGDHVG--YLPQ------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 586 stfreqiiypdtiedfeerfngdynmgDEKLisvlelldLTDLITENLslvlagkgtkksdnldeenlteiraafdlkrn 665
Cdd:cd03246 84 ---------------------------DDEL--------FSGSIAENI-------------------------------- 96
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50285999 666 wseeLSIGVQQRLAMARMYYHKPKFAVLDECTSAVSPEMEQKMYENAQNL---GISVISVCHR 725
Cdd:cd03246 97 ----LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALkaaGATRIVIAHR 155
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
508-728 |
4.82e-12 |
|
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: 69.39 E-value: 4.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 508 ANQVLVPELNFELKHGDHLLIIGPNGCGKSSLFRLLGGLWP------------IRQIetgvqtkltvPPRKIGQdcAIFY 575
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPptagsvrldgadLSQW----------DREELGR--HIGY 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 576 LPQkpymgngstfreQI-IYPDTIEDFEERFnGDYNmgDEKLISVLELLDLTDLItenLSLvlagkgtkkSDNLDeenlT 654
Cdd:COG4618 411 LPQ------------DVeLFDGTIAENIARF-GDAD--PEKVVAAAKLAGVHEMI---LRL---------PDGYD----T 459
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50285999 655 EIRAAfdlkrnwSEELSIGVQQRLAMARMYYHKPKFAVLDECTSAVSPEMEQKMYENAQNL---GISVISVCHRTTL 728
Cdd:COG4618 460 RIGEG-------GARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkarGATVVVITHRPSL 529
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
508-724 |
5.37e-12 |
|
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: 66.00 E-value: 5.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 508 ANQVLVPELNFELKHGDHLLIIGPNGCGKSSLFRLLGGLWPIR--QIETGVQTKLTVPP--RKIG---QDCAIFylpqkP 580
Cdd:cd03259 11 GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDsgEILIDGRDVTGVPPerRNIGmvfQDYALF-----P 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 581 YMgngsTFREQIIYPDTIEDFEErfngdynmgDEKLISVLELLDLTDLitenlslvlagkgtkksdnldeenlteiraAF 660
Cdd:cd03259 86 HL----TVAENIAFGLKLRGVPK---------AEIRARVRELLELVGL------------------------------EG 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50285999 661 DLKRnWSEELSIGVQQRLAMARMYYHKPKFAVLDECTSAVSPEMEQKMYENAQ----NLGISVISVCH 724
Cdd:cd03259 123 LLNR-YPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKelqrELGITTIYVTH 189
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
497-724 |
6.04e-12 |
|
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: 66.20 E-value: 6.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 497 IKFEHVPLITPANQVLVPELNFELKHGDHLLIIGPNGCGKSSLFRLLGGLWP-------IRQIETGVQTKLTVpPRKIGq 569
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKptsgevlVDGKDITKKNLREL-RRKVG- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 570 dcaifYLPQKPymgngstfREQIIYPdTIED---FeerfnGDYNMG------DEKLISVLELLDLTDLitenlslvlagk 640
Cdd:COG1122 79 -----LVFQNP--------DDQLFAP-TVEEdvaF-----GPENLGlpreeiRERVEEALELVGLEHL------------ 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 641 gtkksdnldeenlteiraafdLKRNWSeELSIGVQQRLAMARMYYHKPKFAVLDECTSAVSPEMEQKMYENAQNL---GI 717
Cdd:COG1122 128 ---------------------ADRPPH-ELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLnkeGK 185
|
....*..
gi 50285999 718 SVISVCH 724
Cdd:COG1122 186 TVIIVTH 192
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
509-724 |
1.28e-11 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 65.50 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 509 NQVLVPELNFELKHGDHLLIIGPNGCGKSSLFRLLGGLWPIR--QIETGVQtKLTVPPRKIGqdcaifYLPQKpymgngS 586
Cdd:COG1121 18 GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTsgTVRLFGK-PPRRARRRIG------YVPQR------A 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 587 TFREQiiYPDTIEDF-------EERFNGDYNMGDEKLI-SVLELLDLTDLITENLSlvlagkgtkksdnldeenlteira 658
Cdd:COG1121 85 EVDWD--FPITVRDVvlmgrygRRGLFRRPSRADREAVdEALERVGLEDLADRPIG------------------------ 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50285999 659 afdlkrnwseELSIGVQQRLAMARMYYHKPKFAVLDECTSAVSPEMEQKMYE-----NAQnlGISVISVCH 724
Cdd:COG1121 139 ----------ELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYEllrelRRE--GKTILVVTH 197
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
497-728 |
2.37e-11 |
|
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: 67.31 E-value: 2.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 497 IKFEHVPLITPANQVLVPELNFELKHGDHLLIIGPNGCGKSSLFRLLGGLWPIRQ--IETGVQTKLTVPPRKIGQDCAif 574
Cdd:TIGR02857 322 LEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEgsIAVNGVPLADADADSWRDQIA-- 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 575 YLPQKPYMGNGsTFREQIiypdtiedfeeRFnGDYNMGDEKLISVLELLDLTDLITEnlslVLAGKGTKKSDNldeenlt 654
Cdd:TIGR02857 400 WVPQHPFLFAG-TIAENI-----------RL-ARPDASDAEIREALERAGLDEFVAA----LPQGLDTPIGEG------- 455
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 50285999 655 eiraafdlkrnwSEELSIGVQQRLAMARMYYHKPKFAVLDECTSAVSPEMEQKMYENAQNL--GISVISVCHRTTL 728
Cdd:TIGR02857 456 ------------GAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALaqGRTVLLVTHRLAL 519
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
497-725 |
4.76e-11 |
|
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: 63.79 E-value: 4.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 497 IKFEHVPLITPANQVLVPELNFELKHGDHLLIIGPNGCGKSSLFRLLGGLW------------PIRQIetgvqtKLTVPP 564
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYdvssgsilidgqDIREV------TLDSLR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 565 RKIG---QDCAIFylpqkpymgnGSTFREQIIYpdtiedfeerfnGDYNMGDEKLISVLELLDLTDLIT---ENLSLVLA 638
Cdd:cd03253 75 RAIGvvpQDTVLF----------NDTIGYNIRY------------GRPDATDEEVIEAAKAAQIHDKIMrfpDGYDTIVG 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 639 GKGTKksdnldeenlteiraafdlkrnwseeLSIGVQQRLAMARMYYHKPKFAVLDECTSAVSPEMEQKMYENAQNL--G 716
Cdd:cd03253 133 ERGLK--------------------------LSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVskG 186
|
....*....
gi 50285999 717 ISVISVCHR 725
Cdd:cd03253 187 RTTIVIAHR 195
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
509-699 |
4.91e-11 |
|
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: 62.88 E-value: 4.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 509 NQVLVPELNFELKHGDHLLIIGPNGCGKSSLFRLLGGLwpiRQIETGvqtKLTVPPRKIGQDcaifylpqkpymgnGSTF 588
Cdd:COG4133 14 ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGL---LPPSAG---EVLWNGEPIRDA--------------REDY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 589 REQIIYpdtIedfeerfnGDYNMGDEklisvlellDLTdlITENLSLVLAGKGTKksdnLDEENLTEIRAAFDLKRNWSE 668
Cdd:COG4133 74 RRRLAY---L--------GHADGLKP---------ELT--VRENLRFWAALYGLR----ADREAIDEALEAVGLAGLADL 127
|
170 180 190
....*....|....*....|....*....|....
gi 50285999 669 ---ELSIGVQQRLAMARMYYHKPKFAVLDECTSA 699
Cdd:COG4133 128 pvrQLSAGQKRRVALARLLLSPAPLWLLDEPFTA 161
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
498-725 |
5.51e-11 |
|
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: 61.49 E-value: 5.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 498 KFEHVPLITPANQVLVPeLNFELKHGDHLLIIGPNGCGKSSLFRLLGGLWPIRQ--IETGVQTKLTVPPRKIGQDcaIFY 575
Cdd:cd00267 1 EIENLSFRYGGRTALDN-VSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSgeILIDGKDIAKLPLEELRRR--IGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 576 LPQkpymgngstfreqiiypdtiedfeerfngdynmgdeklisvlelldltdlitenlslvlagkgtkksdnldeenlte 655
Cdd:cd00267 78 VPQ----------------------------------------------------------------------------- 80
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50285999 656 iraafdlkrnwseeLSIGVQQRLAMARMYYHKPKFAVLDECTSAVSPEMEQKMYENAQNL---GISVISVCHR 725
Cdd:cd00267 81 --------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELaeeGRTVIIVTHD 139
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
497-725 |
7.86e-11 |
|
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: 62.89 E-value: 7.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 497 IKFEHVPL-ITPANQVLVPELNFELKHGDHLLIIGPNGCGKSSLFRLLGGLWPI---RQIETGVQTKLTVPP---RKIGq 569
Cdd:cd03252 1 ITFEHVRFrYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPengRVLVDGHDLALADPAwlrRQVG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 570 dcaifYLPQKPYMGNGStFREQIIYPDTiedfeerfngdyNMGDEKLISVLELLDLTDLITEnlslVLAGKGTKKSDNld 649
Cdd:cd03252 80 -----VVLQENVLFNRS-IRDNIALADP------------GMSMERVIEAAKLAGAHDFISE----LPEGYDTIVGEQ-- 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50285999 650 eenlteiraafdlkrnwSEELSIGVQQRLAMARMYYHKPKFAVLDECTSAVSPEMEQKMYENAQNL--GISVISVCHR 725
Cdd:cd03252 136 -----------------GAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDIcaGRTVIIIAHR 196
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
516-724 |
4.30e-10 |
|
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: 59.76 E-value: 4.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 516 LNFELKHGDHLLIIGPNGCGKSSLFRLLGGLWPIR--QIETGVQTKLTVPPRKIGQDCAifYLPQkpymgngstfreqii 593
Cdd:cd03214 18 LSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSsgEILLDGKDLASLSPKELARKIA--YVPQ--------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 594 ypdtiedfeerfngdynmgdeklisVLELLDLTDLITENLSlvlagkgtkksdnldeenlteiraafdlkrnwseELSIG 673
Cdd:cd03214 81 -------------------------ALELLGLAHLADRPFN----------------------------------ELSGG 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 50285999 674 VQQRLAMARMYYHKPKFAVLDECTSAVSP----EMEQKMYENAQNLGISVISVCH 724
Cdd:cd03214 102 ERQRVLLARALAQEPPILLLDEPTSHLDIahqiELLELLRRLARERGKTVVMVLH 156
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
494-725 |
7.12e-10 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 62.82 E-value: 7.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 494 ENLIKFEHVPL---ITPANQVLvPELNFELKHGDHLLIIGPNGCGKSSLFRLLGGLWpirQIETGVQTKLTVPPRKIgqD 570
Cdd:TIGR00958 476 EGLIEFQDVSFsypNRPDVPVL-KGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLY---QPTGGQVLLDGVPLVQY--D 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 571 CAifYL-------PQKPYMGNGStFREQIIYpdtiedfeerfnGDYNMGDEKLISVLELLDLTDLITENLSLVLAGKGTK 643
Cdd:TIGR00958 550 HH--YLhrqvalvGQEPVLFSGS-VRENIAY------------GLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEK 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 644 KSdnldeenlteiraafdlkrnwseELSIGVQQRLAMARMYYHKPKFAVLDECTSAVSPEMEQKMYENAQNLGISVISVC 723
Cdd:TIGR00958 615 GS-----------------------QLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIA 671
|
..
gi 50285999 724 HR 725
Cdd:TIGR00958 672 HR 673
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
515-700 |
7.21e-10 |
|
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: 60.26 E-value: 7.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 515 ELNFELKHGDHLLIIGPNGCGKSSLFRLLGG-LWPIR---QIETGVQTKLTVPPRKigqdcAIFYLPQKPYMGNGSTFRE 590
Cdd:COG4555 19 DVSFTAKDGEITGLLGPNGAGKTTLLRMLAGlLKPDSgsiLIDGEDVRKEPREARR-----QIGVLPDERGLYDRLTVRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 591 QI-----IYPDTIEDFEERFngdynmgdEKLISVLELLDltdlitenlslvlagkgtkksdnldeenlteiraafDLKRN 665
Cdd:COG4555 94 NIryfaeLYGLFDEELKKRI--------EELIELLGLEE------------------------------------FLDRR 129
|
170 180 190
....*....|....*....|....*....|....*
gi 50285999 666 WSeELSIGVQQRLAMARMYYHKPKFAVLDECTSAV 700
Cdd:COG4555 130 VG-ELSTGMKKKVALARALVHDPKVLLLDEPTNGL 163
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
497-724 |
1.19e-09 |
|
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: 59.56 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 497 IKFEHVPLITpANQVLVPELNFELKHGDHLLIIGPNGCGKSSLFRLLGGLWPIR--QIETGVQTKLTVPP--RKIG---Q 569
Cdd:cd03300 1 IELENVSKFY-GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTsgEILLDGKDITNLPPhkRPVNtvfQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 570 DCAIFylpqkPYMgngsTFREQIIYPDTIEDFEErfngdynmgDEKLISVLELLDLTDLitenlslvlAGKGTKKSDnld 649
Cdd:cd03300 80 NYALF-----PHL----TVFENIAFGLRLKKLPK---------AEIKERVAEALDLVQL---------EGYANRKPS--- 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 50285999 650 eenlteiraafdlkrnwseELSIGVQQRLAMARMYYHKPKFAVLDECTSAVSPEMEQKMYEN----AQNLGISVISVCH 724
Cdd:cd03300 130 -------------------QLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLElkrlQKELGITFVFVTH 189
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
497-728 |
1.47e-09 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 58.91 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 497 IKFEHVPLITPANQVLVPELNFELKHGDHLLIIGPNGCGKSSLFRLL-GGLWPIR-QIETGVQ--TKLT---VPP--RKI 567
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLyGEERPTSgQVLVNGQdlSRLKrreIPYlrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 568 G---QDCaifylpqkpymgngstfreqiiypdtiedfeerfngdynmgdeKLISvlellDLTdlITENLSLVLAGKGTKK 644
Cdd:COG2884 82 GvvfQDF-------------------------------------------RLLP-----DRT--VYENVALPLRVTGKSR 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 645 SdnldeENLTEIRAAFDL------KRNWSEELSIGVQQRLAMARMYYHKPKFAVLDECTSAVSPEMEQ---KMYENAQNL 715
Cdd:COG2884 112 K-----EIRRRVREVLDLvglsdkAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWeimELLEEINRR 186
|
250
....*....|...
gi 50285999 716 GISVISVCHRTTL 728
Cdd:COG2884 187 GTTVLIATHDLEL 199
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
507-725 |
1.77e-09 |
|
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: 59.09 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 507 PANQVLvPELNFELKHGDHLLIIGPNGCGKSSLFRLLGGLWPIRQIET---GVQTKLTVPP---RKIGqdcaifYLPQKP 580
Cdd:cd03249 14 PDVPIL-KGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEIlldGVDIRDLNLRwlrSQIG------LVSQEP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 581 YMGNGsTFREQIIYpdtiedfeerfnGDYNMGDEKLISVLELLDLTDLIT---ENLSLVLAGKGTKksdnldeenlteir 657
Cdd:cd03249 87 VLFDG-TIAENIRY------------GKPDATDEEVEEAAKKANIHDFIMslpDGYDTLVGERGSQ-------------- 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 658 aafdlkrnwseeLSIGVQQRLAMARMYYHKPKFAVLDECTSAVSPEMEQKMYENAQNL--GISVISVCHR 725
Cdd:cd03249 140 ------------LSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAmkGRTTIVIAHR 197
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
497-725 |
2.34e-09 |
|
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: 58.27 E-value: 2.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 497 IKFEHVPLITPANQVLV-PELNFELKHGDHLLIIGPNGCGKSS----LFRLL---GGLWPIRQIETGvqtklTVPPRKIG 568
Cdd:cd03244 3 IEFKNVSLRYRPNLPPVlKNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLVelsSGSILIDGVDIS-----KIGLHDLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 569 QDCAIfyLPQKPymgngstfreqIIYPDTIedfeeRFNGD-YNM-GDEKLISVLELLDLTDLITEnlslvLAGKGtkksD 646
Cdd:cd03244 78 SRISI--IPQDP-----------VLFSGTI-----RSNLDpFGEySDEELWQALERVGLKEFVES-----LPGGL----D 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 647 NLDEENlteiraafdlkrnwSEELSIGVQQRLAMARMYYHKPKFAVLDECTSAVSPEMEQKMyenaQNL------GISVI 720
Cdd:cd03244 131 TVVEEG--------------GENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALI----QKTireafkDCTVL 192
|
....*
gi 50285999 721 SVCHR 725
Cdd:cd03244 193 TIAHR 197
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
515-724 |
2.50e-09 |
|
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: 58.08 E-value: 2.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 515 ELNFELKHGDHLL------------IIGPNGCGKSSLFRLLGGLWPIR--QIETGVQT------KLTVPP--RKIG---Q 569
Cdd:cd03297 3 CVDIEKRLPDFTLkidfdlneevtgIFGASGAGKSTLLRCIAGLEKPDggTIVLNGTVlfdsrkKINLPPqqRKIGlvfQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 570 DCAIFylpqkPYMgngsTFREQIIYPdtiedfeerFNGDYNMgdEKLISVLELLDLTdlitenlslvlagkgtkksdNLD 649
Cdd:cd03297 83 QYALF-----PHL----NVRENLAFG---------LKRKRNR--EDRISVDELLDLL--------------------GLD 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 50285999 650 EenlteiraafdLKRNWSEELSIGVQQRLAMARMYYHKPKFAVLDECTSAVSPEMEQK----MYENAQNLGISVISVCH 724
Cdd:cd03297 123 H-----------LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQllpeLKQIKKNLNIPVIFVTH 190
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
494-741 |
2.77e-09 |
|
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: 58.25 E-value: 2.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 494 ENLIKFEHVPLI---TPANQVLvPELNFELKHGDHLLIIGPNGCGKSSLFRLLGGLWPIrqieTGVQTKLTVPPRKIGQD 570
Cdd:cd03248 9 KGIVKFQNVTFAyptRPDTLVL-QDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQP----QGGQVLLDGKPISQYEH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 571 CaifYLPQKPYMgngsTFREQIIYPDTIEDfeerfNGDYNMGDEKLISVLELLDLT---DLITENLSLVLAGKGTKKSdn 647
Cdd:cd03248 84 K---YLHSKVSL----VGQEPVLFARSLQD-----NIAYGLQSCSFECVKEAAQKAhahSFISELASGYDTEVGEKGS-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 648 ldeenlteiraafdlkrnwseELSIGVQQRLAMARMYYHKPKFAVLDECTSAVSPEMEQK----MYENAQNLGISVISvc 723
Cdd:cd03248 150 ---------------------QLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQvqqaLYDWPERRTVLVIA-- 206
|
250
....*....|....*....
gi 50285999 724 HR-TTLWHFHNYLLKFDGK 741
Cdd:cd03248 207 HRlSTVERADQILVLDGGR 225
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
509-724 |
3.22e-09 |
|
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: 58.52 E-value: 3.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 509 NQVLVPELNFELKHGDHLLIIGPNGCGKSSLFRLLGGLW------------PIRQIetgvqtkltvPPRKIGQdcAIFYL 576
Cdd:COG1120 13 GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLkpssgevlldgrDLASL----------SRRELAR--RIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 577 PQKPYMGNGSTFREQII---YPDTiedfeeRFNGDYNMGDEKLI-SVLELLDLTDLITenlslvlagkgtkksdnldeen 652
Cdd:COG1120 81 PQEPPAPFGLTVRELVAlgrYPHL------GLFGRPSAEDREAVeEALERTGLEHLAD---------------------- 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 50285999 653 lteiraafdlkRNWSeELSIGVQQRLAMARMYYHKPKFAVLDECTSAVSP----EMEQKMYENAQNLGISVISVCH 724
Cdd:COG1120 133 -----------RPVD-ELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLahqlEVLELLRRLARERGRTVVMVLH 196
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
497-724 |
4.72e-09 |
|
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: 57.70 E-value: 4.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 497 IKFEHVPLITPANQVLVPELNFELKHGDHLLIIGPNGCGKSSLFRLLGGLW------------PIRQIEtGVQTKltvpp 564
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIeptsgeifidgeDIREQD-PVELR----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 565 RKIG---QDCAIFylpqkPYMgngsTFREQIIYPDTIEDFEErfngdynmgdEKLIS-VLELLDLTDlitenlslvlagk 640
Cdd:cd03295 75 RKIGyviQQIGLF-----PHM----TVEENIALVPKLLKWPK----------EKIRErADELLALVG------------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 641 gtkksdnLDEENlteiraafdLKRNWSEELSIGVQQRLAMARMYYHKPKFAVLDECTSAVSP----EMEQKMYENAQNLG 716
Cdd:cd03295 123 -------LDPAE---------FADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPitrdQLQEEFKRLQQELG 186
|
....*...
gi 50285999 717 ISVISVCH 724
Cdd:cd03295 187 KTIVFVTH 194
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
509-724 |
5.84e-09 |
|
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: 56.88 E-value: 5.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 509 NQVLVPELNFELKHGDHLLIIGPNGCGKSSLFRLLGGLWPIR--QIETGVQTKLTVPP--RKIG---QDCAIFylpqkPY 581
Cdd:cd03301 12 NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTsgRIYIGGRDVTDLPPkdRDIAmvfQNYALY-----PH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 582 MgngsTFREQIIYPDTIEDFEERfngdynMGDEKLISVLELLDLTDLitenlslvlagkgtkksdnLDeenlteiraafd 661
Cdd:cd03301 87 M----TVYDNIAFGLKLRKVPKD------EIDERVREVAELLQIEHL-------------------LD------------ 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50285999 662 lkrNWSEELSIGVQQRLAMARMYYHKPKFAVLDECTSAVSP----EMEQKMYENAQNLGISVISVCH 724
Cdd:cd03301 126 ---RKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAklrvQMRAELKRLQQRLGTTTIYVTH 189
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
497-724 |
7.17e-09 |
|
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: 56.73 E-value: 7.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 497 IKFEHVPLITPANQVLVPEL---NFELKHGDHLLIIGPNGCGKSSLFRLLGGLwpirqiETGVQTKLTVpprkIGQDCAi 573
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALkgvSLSIEKGEFVAIVGPSGSGKSTLLNILGGL------DRPTSGEVRV----DGTDIS- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 574 fylpqkpYMGNG--STFR-EQI--IYPdtiedfeerfngDYNmgdekLISvlellDLTdlITENLSLVLAGKGTKKSDNL 648
Cdd:cd03255 70 -------KLSEKelAAFRrRHIgfVFQ------------SFN-----LLP-----DLT--ALENVELPLLLAGVPKKERR 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 649 D--EENLTEIRAAFDLKRNWSeELSIGVQQRLAMARMYYHKPKFAVLDECTSAVSPE----MEQKMYENAQNLGISVISV 722
Cdd:cd03255 119 EraEELLERVGLGDRLNHYPS-ELSGGQQQRVAIARALANDPKIILADEPTGNLDSEtgkeVMELLRELNKEAGTTIVVV 197
|
..
gi 50285999 723 CH 724
Cdd:cd03255 198 TH 199
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
437-728 |
9.48e-09 |
|
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: 58.98 E-value: 9.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 437 LLTASSSVGRFVELKKNI----QELRGTSLRLNYLNDLldkYAVGN--IDKKDEDVLDLVEYNenlIKFEHVPLITPANQ 510
Cdd:TIGR01193 414 LITFNALLSYFLTPLENIinlqPKLQAARVANNRLNEV---YLVDSefINKKKRTELNNLNGD---IVINDVSYSYGYGS 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 511 VLVPELNFELKHGDHLLIIGPNGCGKSSLFRLLGGLWPIRQIETGVQTKLTVPPRKIGQDCAIFYLPQKPYMGNGSTFRE 590
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILEN 567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 591 QIIypdtiedfeerfNGDYNMGDEKLISVLELLDLTDLItENLSLvlaGKGTKksdnLDEENLTeiraafdlkrnwseeL 670
Cdd:TIGR01193 568 LLL------------GAKENVSQDEIWAACEIAEIKDDI-ENMPL---GYQTE----LSEEGSS---------------I 612
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 50285999 671 SIGVQQRLAMARMYYHKPKFAVLDECTSAVSPEMEQKMYENAQNLG-ISVISVCHRTTL 728
Cdd:TIGR01193 613 SGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQdKTIIFVAHRLSV 671
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
528-724 |
1.20e-08 |
|
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: 56.42 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 528 IIGPNGCGKSSLFRLLGGLW---PIRQIE----------TGVQTKLTVPPRKIGQdcaIFylpQKPYMGNGStfreqiiy 594
Cdd:cd03260 31 LIGPSGCGKSTLLRLLNRLNdliPGAPDEgevlldgkdiYDLDVDVLELRRRVGM---VF---QKPNPFPGS-------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 595 pdtiedfeerfngdynmgdeklisvlelldltdlITENLSLVLAGKGTKKSDNLD---EENLTeiRAAFD---LKRNWSE 668
Cdd:cd03260 97 ----------------------------------IYDNVAYGLRLHGIKLKEELDervEEALR--KAALWdevKDRLHAL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 669 ELSIGVQQRLAMARMYYHKPKFAVLDECTSAVSP----EMEQKMYENAQNlgISVISVCH 724
Cdd:cd03260 141 GLSGGQQQRLCLARALANEPEVLLLDEPTSALDPistaKIEELIAELKKE--YTIVIVTH 198
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
497-710 |
1.31e-08 |
|
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: 55.94 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 497 IKFEHV----PLITPANQVLvPELNFELKHGDHLLIIGPNGCGKSSLFRLLGGLwpIRQIETGVQ---TKLTVPPRKIGq 569
Cdd:cd03293 1 LEVRNVsktyGGGGGAVTAL-EDISLSVEEGEFVALVGPSGCGKSTLLRIIAGL--ERPTSGEVLvdgEPVTGPGPDRG- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 570 dcaifYLPQKPYmgngstfreqiiypdtiedfeerfngdynmgdeklisvleLLD-LTdlITENLSLVLAGKGTKKSDnl 648
Cdd:cd03293 77 -----YVFQQDA----------------------------------------LLPwLT--VLDNVALGLELQGVPKAE-- 107
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 50285999 649 DEENLTEIRAAFDLK---RNWSEELSIGVQQRLAMARMYYHKPKFAVLDECTSAVSPEMEQKMYE 710
Cdd:cd03293 108 ARERAEELLELVGLSgfeNAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQE 172
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
497-725 |
3.92e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 56.78 E-value: 3.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 497 IKFEHVPLITPANQVLVPELNFELKHGDHLLIIGPNGCGKSSLFRLLGGLWPIR---QIEtGVQTKLTVPP--RK----I 567
Cdd:PRK11174 350 IEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQgslKIN-GIELRELDPEswRKhlswV 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 568 GQDcaifylPQKPYmgngSTFREQIIYpdtiedfeerfnGDYNMGDEKLISVLELLDLTDLItenlslvlagkgTKKSDN 647
Cdd:PRK11174 429 GQN------PQLPH----GTLRDNVLL------------GNPDASDEQLQQALENAWVSEFL------------PLLPQG 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 648 LDeenlTEI--RAAfdlkrnwseELSIGVQQRLAMARMYYHKPKFAVLDECTSAVSPEMEQKMYE--NAQNLGISVISVC 723
Cdd:PRK11174 475 LD----TPIgdQAA---------GLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQalNAASRRQTTLMVT 541
|
..
gi 50285999 724 HR 725
Cdd:PRK11174 542 HQ 543
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
513-731 |
4.00e-08 |
|
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: 55.14 E-value: 4.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 513 VPELNFELKHGDHLLIIGPNGCGKSSLFRLLGGLWP-----IR---QIETGvqtkltVPPRKIGQdcaifylpqkpyMGN 584
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRptsgsVLfdgEDITG------LPPHEIAR------------LGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 585 GSTFreQIIYPdtiedFEErfngdynmgdeklISVLelldltdlitENLSL-VLAGKGTKKSDNLDEENLTEIRAA---- 659
Cdd:cd03219 78 GRTF--QIPRL-----FPE-------------LTVL----------ENVMVaAQARTGSGLLLARARREEREARERaeel 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 660 ---FDLKRNWSE---ELSIGVQQRLAMARMYYHKPKFAVLDECTSAVSPEMEQKMYE-----NAQNLGISVI-------- 720
Cdd:cd03219 128 lerVGLADLADRpagELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAElirelRERGITVLLVehdmdvvm 207
|
250
....*....|.
gi 50285999 721 SVCHRTTLWHF 731
Cdd:cd03219 208 SLADRVTVLDQ 218
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
516-710 |
5.42e-08 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 54.68 E-value: 5.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 516 LNFELKHGDHLLIIGPNGCGKSSLFRLLGGLwpiRQIETG--------VQTKLTVPPRKIGqdcaifYLPQKPYMGNGST 587
Cdd:COG1131 19 VSLTVEPGEIFGLLGPNGAGKTTTIRMLLGL---LRPTSGevrvlgedVARDPAEVRRRIG------YVPQEPALYPDLT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 588 FREQI-----IYPDTIEDFEERFNgdynmgdekliSVLELLDLTDLITENLSlvlagkgtkksdnldeenlteiraafdl 662
Cdd:COG1131 90 VRENLrffarLYGLPRKEARERID-----------ELLELFGLTDAADRKVG---------------------------- 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 50285999 663 krnwseELSIGVQQRLAMARMYYHKPKFAVLDECTSAVSPEMEQKMYE 710
Cdd:COG1131 131 ------TLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWE 172
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
511-720 |
7.45e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 53.65 E-value: 7.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 511 VLVPELNFELKHGDHLLIIGPNGCGKSSLFRLLGGLwpirqietgvqtkltVPPRKiGQdcaIFYlpqkpymgNGSTFRE 590
Cdd:PRK13538 15 ILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGL---------------ARPDA-GE---VLW--------QGEPIRR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 591 QiiypdtiedfEERFNGDynmgdeklisvleLL----------DLTDLitENLSLVLAGkgtkkSDNLDEENLTEIRAAF 660
Cdd:PRK13538 68 Q----------RDEYHQD-------------LLylghqpgiktELTAL--ENLRFYQRL-----HGPGDDEALWEALAQV 117
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 661 DLKRnwSEE-----LSIGVQQRLAMARMYYHKPKFAVLDEC-----TSAVSpEMEQKMYENAQNLGISVI 720
Cdd:PRK13538 118 GLAG--FEDvpvrqLSAGQQRRVALARLWLTRAPLWILDEPftaidKQGVA-RLEALLAQHAEQGGMVIL 184
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
496-724 |
1.16e-07 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 53.56 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 496 LIKFEHVPLITPANQVLvPELNFELKHGDHLLIIGPNGCGKSSLFRLLGGLWPIRQ---IETGVQTKLT-VPPRKIGQDC 571
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVL-HNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSgdlIVDGLKVNDPkVDERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 572 aifylpqkpymgnGSTFREQIIYPDtiedfeerfngdynmgdeklisvlelldLTDLitENlslVLAG----KGTKKSD- 646
Cdd:PRK09493 80 -------------GMVFQQFYLFPH----------------------------LTAL--EN---VMFGplrvRGASKEEa 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 647 -NLDEENLTEIRAAfDLKRNWSEELSIGVQQRLAMARMYYHKPKFAVLDECTSAVSPEMEQKMYENAQNL---GISVISV 722
Cdd:PRK09493 114 eKQARELLAKVGLA-ERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLaeeGMTMVIV 192
|
..
gi 50285999 723 CH 724
Cdd:PRK09493 193 TH 194
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
516-724 |
1.21e-07 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 54.95 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 516 LNFELKHGDHLLIIGPNGCGKSSLFRLLGGLwpiRQIETGV-----QTKLTVPPRK-----IGQDCAIFylpqkPYMgng 585
Cdd:PRK09452 33 LDLTINNGEFLTLLGPSGCGKTTVLRLIAGF---ETPDSGRimldgQDITHVPAENrhvntVFQSYALF-----PHM--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 586 sTFREQIIY-------PDtiEDFEERfngdynmgdeklisVLELLDLTDLitenlslvlagkgtkksdnldeENLTEIRA 658
Cdd:PRK09452 102 -TVFENVAFglrmqktPA--AEITPR--------------VMEALRMVQL----------------------EEFAQRKP 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50285999 659 AfdlkrnwseELSIGVQQRLAMARMYYHKPKFAVLDECTSAVSPEMEQKMyenaQN--------LGISVISVCH 724
Cdd:PRK09452 143 H---------QLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQM----QNelkalqrkLGITFVFVTH 203
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
500-724 |
2.20e-07 |
|
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: 52.26 E-value: 2.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 500 EHVPLITPANQVLVPELNFELKHGDHLLIIGPNGCGKSSLFRLLGGLwpirQIETGVQTKLTVPPRKIGQDC-AIFYLPQ 578
Cdd:cd03226 3 ENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGL----IKESSGSILLNGKPIKAKERRkSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 579 KPYmgngstfreQIIYPDTIEDfEERF-NGDYNMGDEKLISVLELLDLtdlitenlslvlagkgtkksdnldeenlteir 657
Cdd:cd03226 79 DVD---------YQLFTDSVRE-ELLLgLKELDAGNEQAETVLKDLDL-------------------------------- 116
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 658 aaFDLKRNWSEELSIGVQQRLAMARMYYHKPKFAVLDECTSAVSPE-MEQ--KMYENAQNLGISVISVCH 724
Cdd:cd03226 117 --YALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKnMERvgELIRELAAQGKAVIVITH 184
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
509-724 |
2.38e-07 |
|
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: 52.15 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 509 NQVLVpELNFELKHGDHLLIIGPNGCGKSSLFRLLGGLWPIRQIETGVQ-TKLTVPPRKIGQdcaifyLPQKPYMgngsT 587
Cdd:cd03262 13 FHVLK-GIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDgLKLTDDKKNINE------LRQKVGM----V 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 588 FreqiiypdtiedfeERFNGDYNMgdekliSVLELldltdlITENLSLVLaGKGTKKSDNLDEENLTEIRAAfDLKRNWS 667
Cdd:cd03262 82 F--------------QQFNLFPHL------TVLEN------ITLAPIKVK-GMSKAEAEERALELLEKVGLA-DKADAYP 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 668 EELSIGVQQRLAMARMYYHKPKFAVLDECTSAVSPEMEQKMYENAQNL---GISVISVCH 724
Cdd:cd03262 134 AQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLaeeGMTMVVVTH 193
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
670-725 |
2.41e-07 |
|
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: 51.28 E-value: 2.41e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 50285999 670 LSIGVQQRLAMARMYYHKPKFAVLDECTSAVSPEMEQKMYENAQNL---GISVISVCHR 725
Cdd:cd03216 83 LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLraqGVAVIFISHR 141
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
516-720 |
2.53e-07 |
|
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: 51.24 E-value: 2.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 516 LNFELKHGDHLLIIGPNGCGKSSLFRLLGGLWP-----IRQIETGVQTKLTVPPRKIGqdcaifYLPQKPYmgngstfre 590
Cdd:cd03230 19 ISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKpdsgeIKVLGKDIKKEPEEVKRRIG------YLPEEPS--------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 591 qiIYPDtiedfeerfngdynmgdeklISVLELLDltdlitenlslvlagkgtkksdnldeenlteiraafdlkrnwseeL 670
Cdd:cd03230 84 --LYEN--------------------LTVRENLK---------------------------------------------L 96
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 50285999 671 SIGVQQRLAMARMYYHKPKFAVLDECTSAVSPEMEQKMYENAQNL---GISVI 720
Cdd:cd03230 97 SGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELkkeGKTIL 149
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
515-695 |
4.10e-07 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 53.53 E-value: 4.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 515 ELNFELKHGDHLLIIGPNGCGKSSLFRLLGGLwpiRQIETGvqtKLTVPPR-KIGqdcaifYLPQKPYMGNGSTFREQII 593
Cdd:COG0488 16 DVSLSINPGDRIGLVGRNGAGKSTLLKILAGE---LEPDSG---EVSIPKGlRIG------YLPQEPPLDDDLTVLDTVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 594 ypdtiedfeerfngdynMGDEKLISVLELLD--LTDLITENLSLVLAGKGTKKSDNLDEENL-TEIRAA--------FDL 662
Cdd:COG0488 84 -----------------DGDAELRALEAELEelEAKLAEPDEDLERLAELQEEFEALGGWEAeARAEEIlsglgfpeEDL 146
|
170 180 190
....*....|....*....|....*....|...
gi 50285999 663 KRNWSeELSIGVQQRLAMARMYYHKPKFAVLDE 695
Cdd:COG0488 147 DRPVS-ELSGGWRRRVALARALLSEPDLLLLDE 178
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
515-724 |
5.14e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 52.04 E-value: 5.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 515 ELNFELKHGDHLLIIGPNGCGKSSLFRLLGGLWPIRQIETGVQTKLTVPP------RKIGQdcaIFYLPQKPYMGNgstf 588
Cdd:PRK13650 25 DVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEEnvwdirHKIGM---VFQNPDNQFVGA---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 589 reqiiypdTIEDfeerfngDYNMGDEKliSVLELLDLTDLITENLSLVlagkgtkksdnldeenlteirAAFDLKRNWSE 668
Cdd:PRK13650 98 --------TVED-------DVAFGLEN--KGIPHEEMKERVNEALELV---------------------GMQDFKEREPA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 669 ELSIGVQQRLAMARMYYHKPKFAVLDECTSAVSPEMEQKMYENAQNL----GISVISVCH 724
Cdd:PRK13650 140 RLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIrddyQMTVISITH 199
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
494-724 |
8.20e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 51.55 E-value: 8.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 494 ENLIKFEHVPLITP-ANQVLVPELNFELKHGDHLLIIGPNGCGKSSLFRLLGGLWPIRQ--IETG--VQTKLTV--PPRK 566
Cdd:PRK13635 3 EEIIRVEHISFRYPdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAgtITVGgmVLSEETVwdVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 567 IGQdcaIFYLPQKPYMgnGSTFREQIIYpdtiedfeerfnGDYNMG---DEKLISVLELLDLTDLitenlslvlagkgtk 643
Cdd:PRK13635 83 VGM---VFQNPDNQFV--GATVQDDVAF------------GLENIGvprEEMVERVDQALRQVGM--------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 644 kSDNLDEEnlteiraafdlkrnwSEELSIGVQQRLAMARMYYHKPKFAVLDECTSAVSPEMEQKMYENAQNL----GISV 719
Cdd:PRK13635 131 -EDFLNRE---------------PHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLkeqkGITV 194
|
....*
gi 50285999 720 ISVCH 724
Cdd:PRK13635 195 LSITH 199
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
516-724 |
1.01e-06 |
|
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: 50.11 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 516 LNFELKHGDHLLIIGPNGCGKSSLFRLL-GGLWPirqiETGvqtKLTVPPRKIGQD--------CAIFYLPQKPymgngs 586
Cdd:TIGR01166 11 LNFAAERGEVLALLGANGAGKSTLLLHLnGLLRP----QSG---AVLIDGEPLDYSrkgllerrQRVGLVFQDP------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 587 tfREQIIYPDTIEDFEerFnGDYNMGdeklisvLELLDLTDLITENLSLVlagkgtkksdnldeenlteirAAFDLKRNW 666
Cdd:TIGR01166 78 --DDQLFAADVDQDVA--F-GPLNLG-------LSEAEVERRVREALTAV---------------------GASGLRERP 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50285999 667 SEELSIGVQQRLAMARMYYHKPKFAVLDECTSAVSPEMEQKMYENAQNL---GISVISVCH 724
Cdd:TIGR01166 125 THCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAGREQMLAILRRLraeGMTVVISTH 185
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
497-578 |
1.23e-06 |
|
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: 48.60 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 497 IKFEHVpLITPANQVLVPELNFELKHGDHLLIIGPNGCGKSSLFRLLGGlwpirqietgvQTKLTVPPRKIGQDCAIFYL 576
Cdd:cd03221 1 IELENL-SKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAG-----------ELEPDEGIVTWGSTVKIGYF 68
|
..
gi 50285999 577 PQ 578
Cdd:cd03221 69 EQ 70
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
497-724 |
1.43e-06 |
|
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: 49.49 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 497 IKFEHVPLITPANQVLVpELNFELKHGDHLLIIGPNGCGKSSLFRLLGGL-WPIR-QIE---TGVQTKLTVPP---RKIG 568
Cdd:cd03229 1 LELKNVSKRYGQKTVLN-DVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLeEPDSgSILidgEDLTDLEDELPplrRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 569 ---QDCAIFylpqkPYMgngstfreqiiypdtiedfeerfngdynmgdekliSVLelldltdlitENLSLVLAGkgtkks 645
Cdd:cd03229 80 mvfQDFALF-----PHL-----------------------------------TVL----------ENIALGLSG------ 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 646 dnldeenlteiraafdlkrnwseelsiGVQQRLAMARMYYHKPKFAVLDECTSAVSP----EMEQKMYENAQNLGISVIS 721
Cdd:cd03229 104 ---------------------------GQQQRVALARALAMDPDVLLLDEPTSALDPitrrEVRALLKSLQAQLGITVVL 156
|
...
gi 50285999 722 VCH 724
Cdd:cd03229 157 VTH 159
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
493-724 |
1.57e-06 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 50.10 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 493 NENLIKFEHVPLITPANQVLvPELNFELKHGDHLLIIGPNGCGKSSLFRLLGGLW-PIR-QIETGVQTKLTVPPRKIGQD 570
Cdd:PRK10247 4 NSPLLQLQNVGYLAGDAKIL-NNISFSLRAGEFKLITGPSGCGKSTLLKIVASLIsPTSgTLLFEGEDISTLKPEIYRQQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 571 CAifYLPQKPYMgNGSTFREQIIYPDTIEDfeerfngdyNMGDEKLIsvlelldLTDLITENLSLVLAGKGTkksdnlde 650
Cdd:PRK10247 83 VS--YCAQTPTL-FGDTVYDNLIFPWQIRN---------QQPDPAIF-------LDDLERFALPDTILTKNI-------- 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50285999 651 enlteiraafdlkrnwsEELSIGVQQRLAMARMYYHKPKFAVLDECTSAVSPEMEQKMYE----NAQNLGISVISVCH 724
Cdd:PRK10247 136 -----------------AELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEiihrYVREQNIAVLWVTH 196
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
515-726 |
1.68e-06 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 49.96 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 515 ELNFELKHGDHLLIIGPNGCGKSSLFRLLGGlwpiRQIETGVQTKLTVPPRKIGQDCAIfylpqkpymgngstfreqiiy 594
Cdd:COG2401 48 DLNLEIEPGEIVLIVGASGSGKSTLLRLLAG----ALKGTPVAGCVDVPDNQFGREASL--------------------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 595 pdtIEDFeerfngdYNMGDEKLisVLELLDLTDLitenlslvlagkgtkkSDnldeenlteiraAFDLKRNWSeELSIGV 674
Cdd:COG2401 103 ---IDAI-------GRKGDFKD--AVELLNAVGL----------------SD------------AVLWLRRFK-ELSTGQ 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 50285999 675 QQRLAMARMYYHKPKFAVLDECTSAVSPEMEQ----KMYENAQNLGISVISVCHRT 726
Cdd:COG2401 142 KFRFRLALLLAERPKLLVIDEFCSHLDRQTAKrvarNLQKLARRAGITLVVATHHY 197
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
512-728 |
2.03e-06 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 49.89 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 512 LVPELNFELKHGDHLLIIGPNGCGKSSLFRLLGGLWPiRQIETGV--QTKLTVPPRKIGQDCAIFYLPQKPymgngSTFR 589
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVP-RDAGNIIidDEDISLLPLHARARRGIGYLPQEA-----SIFR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 590 EQIIYpdtiedfeerfngdynmgdEKLISVLELLDltDLITENlslvlagKGTKKSDNLDEENLTEIRaafdlkRNWSEE 669
Cdd:PRK10895 92 RLSVY-------------------DNLMAVLQIRD--DLSAEQ-------REDRANELMEEFHIEHLR------DSMGQS 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50285999 670 LSIGVQQRLAMARMYYHKPKFAVLDECTSAVSPEME---QKMYENAQNLGISVISVCH--RTTL 728
Cdd:PRK10895 138 LSGGERRRVEIARALAANPKFILLDEPFAGVDPISVidiKRIIEHLRDSGLGVLITDHnvRETL 201
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
508-724 |
2.13e-06 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 50.01 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 508 ANQVLVpELNFELKHGDHLLIIGPNGCGKSSLFRLLGGLWPIRQIE---TGVQTKLTVPPrkigQDCAIFYLPQKPYMgn 584
Cdd:PRK11124 14 AHQALF-DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTlniAGNHFDFSKTP----SDKAIRELRRNVGM-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 585 gsTFREQIIYPDtiedfeerfngdynmgdeklISVLElldltDLItENLSLVLaGKGTKKSDNLDEENLTEIRAAfDLKR 664
Cdd:PRK11124 87 --VFQQYNLWPH--------------------LTVQQ-----NLI-EAPCRVL-GLSKDQALARAEKLLERLRLK-PYAD 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50285999 665 NWSEELSIGVQQRLAMARMYYHKPKFAVLDECTSAVSPEMEQ---KMYENAQNLGISVISVCH 724
Cdd:PRK11124 137 RFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAqivSIIRELAETGITQVIVTH 199
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
497-703 |
2.15e-06 |
|
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: 49.33 E-value: 2.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 497 IKFEHVPLITPANQVLVPELNFELKHGDHLLIIGPNGCGKSSLFRLLGGlwpirqIETgvQTKLTVppRKIGQDCAIFYL 576
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYK------EEL--PTSGTI--RVNGQDVSDLRG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 577 PQKPYMgngstfREQI--IYpdtiEDFeerfngdynmgdeKLisvleLLDLTdlITEN--LSLVLAGKGTKksdnldeEN 652
Cdd:cd03292 71 RAIPYL------RRKIgvVF----QDF-------------RL-----LPDRN--VYENvaFALEVTGVPPR-------EI 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 50285999 653 LTEIRAAFDL------KRNWSEELSIGVQQRLAMARMYYHKPKFAVLDECTSAVSPE 703
Cdd:cd03292 114 RKRVPAALELvglshkHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPD 170
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
494-725 |
2.17e-06 |
|
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: 51.06 E-value: 2.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 494 ENLIKFEHVPLITPANQV-LVPELNFELKHGDHLLIIGPNGCGKSSLFRLLGGLWPIR-----QIETGVQTKLTVPPRKI 567
Cdd:COG1123 2 TPLLEVRDLSVRYPGGDVpAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgrisgEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 568 GQDCAifYLPQKPYMG-NGSTFREQIIYpdtiedfeerfngdynmgdeklisVLELLDLTDlitenlslvlagkgtKKSD 646
Cdd:COG1123 82 GRRIG--MVFQDPMTQlNPVTVGDQIAE------------------------ALENLGLSR---------------AEAR 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 647 NLDEENLTEIRAAFDLKRNWSeELSIGVQQRLAMARMYYHKPKFAVLDECTSA----VSPEMEQKMYENAQNLGISVISV 722
Cdd:COG1123 121 ARVLELLEAVGLERRLDRYPH-QLSGGQRQRVAIAMALALDPDLLIADEPTTAldvtTQAEILDLLRELQRERGTTVLLI 199
|
...
gi 50285999 723 CHR 725
Cdd:COG1123 200 THD 202
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
510-724 |
2.37e-06 |
|
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: 49.43 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 510 QVLVPELNFELKHGDHLLIIGPNGCGKSSLFRLLGGLWPI---------RQIETGVQTKLTVPPRKIGqdcaifYLPQKP 580
Cdd:cd03257 18 VKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPtsgsiifdgKDLLKLSRRLRKIRRKEIQ------MVFQDP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 581 YmgnGS-----TFREQIiypdtiedfEERFNGDYNMGDEKLISVLELLDLTDLitenlslvlagkgtkksdNLDEEnlte 655
Cdd:cd03257 92 M---SSlnprmTIGEQI---------AEPLRIHGKLSKKEARKEAVLLLLVGV------------------GLPEE---- 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50285999 656 iraafDLKRnWSEELSIGVQQRLAMARMYYHKPKFAVLDECTSAVSP----EMEQKMYENAQNLGISVISVCH 724
Cdd:cd03257 138 -----VLNR-YPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVsvqaQILDLLKKLQEELGLTLLFITH 204
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
497-724 |
2.55e-06 |
|
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: 49.49 E-value: 2.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 497 IKFEHVPLITPANQVLVPELNFELKHGDHLLIIGPNGCGKSSLFRLLGGLWPIR--QIETGVQTKLTVPPRKIGQdcaif 574
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTsgSVLIDGTDINKLKGKALRQ----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 575 ylpqkpymgngstFREQIiypDTIedFEerfngDYNMGDEklISVLelldltdlitENlslVLAGKGTKKS------DNL 648
Cdd:cd03256 76 -------------LRRQI---GMI--FQ-----QFNLIER--LSVL----------EN---VLSGRLGRRStwrslfGLF 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 649 DEEnltEIRAAFDL-----------KRnwSEELSIGVQQRLAMARMYYHKPKFAVLDECTSAVSPEMEQK----MYENAQ 713
Cdd:cd03256 118 PKE---EKQRALAAlervglldkayQR--ADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQvmdlLKRINR 192
|
250
....*....|.
gi 50285999 714 NLGISVISVCH 724
Cdd:cd03256 193 EEGITVIVSLH 203
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
516-699 |
2.55e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 49.10 E-value: 2.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 516 LNFELKHGDHLLIIGPNGCGKSSLFRLLGGLWPIRQIETGVQTKLTVPPRKIGQdcaIFYLPQKPYMGNGSTFREQIiyp 595
Cdd:PRK13539 21 LSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEA---CHYLGHRNAMKPALTVAENL--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 596 dtieDFEERFNGDynmGDEKLISVLELLDLTDlitenlslvlagkgtkksdnldeenLTEIRAAfdlkrnwseELSIGVQ 675
Cdd:PRK13539 95 ----EFWAAFLGG---EELDIAAALEAVGLAP-------------------------LAHLPFG---------YLSAGQK 133
|
170 180
....*....|....*....|....*
gi 50285999 676 QRLAMAR-MYYHKPKFaVLDECTSA 699
Cdd:PRK13539 134 RRVALARlLVSNRPIW-ILDEPTAA 157
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
497-725 |
3.00e-06 |
|
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: 49.15 E-value: 3.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 497 IKFEHVPLITPANQVLV-PELNFELKHGDHLLIIGPNGCGKSSLFRLLGGLWPIR--QIE---TGVQT-KLTVPPRKIGq 569
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVlRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDsgRILidgHDVRDyTLASLRRQIG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 570 dcaifYLPQKPYMGNGsTFREQIIYpdtiedfeerfnGDYNMGDEKLISVLELLDLTDLIT---ENLSLVLAGKGTKksd 646
Cdd:cd03251 80 -----LVSQDVFLFND-TVAENIAY------------GRPGATREEVEEAARAANAHEFIMelpEGYDTVIGERGVK--- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 647 nldeenlteiraafdlkrnwseeLSIGVQQRLAMARMYYHKPKFAVLDECTSAVSPEMEQKMYENAQNL--GISVISVCH 724
Cdd:cd03251 139 -----------------------LSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLmkNRTTFVIAH 195
|
.
gi 50285999 725 R 725
Cdd:cd03251 196 R 196
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
516-722 |
3.54e-06 |
|
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: 48.97 E-value: 3.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 516 LNFELKHGDHLLIIGPNGCGKSSLFRLLGGLWPIR--QIETGVQ--TKLtvPPRKI---GqdcaIFYLPQkpymgngstf 588
Cdd:cd03224 19 VSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRsgSIRFDGRdiTGL--PPHERaraG----IGYVPE---------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 589 rEQIIYPdtiedfeerfngdynmgdeklisvlellDLTdlITENlsLVLAGKGTKKSDNldEENLTEIRAAF-DLKRNWS 667
Cdd:cd03224 83 -GRRIFP----------------------------ELT--VEEN--LLLGAYARRRAKR--KARLERVYELFpRLKERRK 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50285999 668 ---EELSIGVQQRLAMARMYYHKPKFAVLDECTSAVSPEMEQKMYENAQNL---GISVISV 722
Cdd:cd03224 128 qlaGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELrdeGVTILLV 188
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
515-724 |
3.85e-06 |
|
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: 48.87 E-value: 3.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 515 ELNFELKHGDHLLIIGPNGCGKSSLFRLLGGLW-PIR-QIETGVQTKLTVPP--RKIG---QDCAIFylpqkPYMgngsT 587
Cdd:cd03299 17 NVSLEVERGDYFVILGPTGSGKSVLLETIAGFIkPDSgKILLNGKDITNLPPekRDISyvpQNYALF-----PHM----T 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 588 FREQIIY--PDTIEDFEERfngdynmgDEKLISVLELLDLTDLitenlslvlagkgtkksdnldeenlteiraafdLKRN 665
Cdd:cd03299 88 VYKNIAYglKKRKVDKKEI--------ERKVLEIAEMLGIDHL---------------------------------LNRK 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50285999 666 wSEELSIGVQQRLAMARMYYHKPKFAVLDECTSAVSPEMEQK-MYENA---QNLGISVISVCH 724
Cdd:cd03299 127 -PETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKlREELKkirKEFGVTVLHVTH 188
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
494-548 |
4.34e-06 |
|
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: 48.93 E-value: 4.34e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 50285999 494 ENLIKFEHVPLITPANQVLVPeLNFELKHGDHLLIIGPNGCGKSSLFRLLGG-LWP 548
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDD-ISWTVKPGEHWAILGPNGAGKSTLLSLITGdLPP 55
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
516-546 |
4.95e-06 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 48.92 E-value: 4.95e-06
10 20 30
....*....|....*....|....*....|.
gi 50285999 516 LNFELKHGDHLLIIGPNGCGKSSLFRLLGGL 546
Cdd:COG1134 45 VSFEVERGESVGIIGRNGAGKSTLLKLIAGI 75
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
496-734 |
5.61e-06 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 48.33 E-value: 5.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 496 LIKFEHVPLITPANQVLVPELNFELKHGDHLLIIGPNGCGKSSLFRLLGGlwpIRQIETGvqtkltvpprKI---GQDCA 572
Cdd:PRK10908 1 MIRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICG---IERPSAG----------KIwfsGHDIT 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 573 IFYLPQKPYMgngstfREQI--IYPDtiedfeerfngdYNMgdeklisvleLLDLTDLITENLSLVLAGKGT-----KKS 645
Cdd:PRK10908 68 RLKNREVPFL------RRQIgmIFQD------------HHL----------LMDRTVYDNVAIPLIIAGASGddirrRVS 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 646 DNLDEENLteiraaFDLKRNWSEELSIGVQQRLAMARMYYHKPKFAVLDECTSAVSPEMEQ---KMYENAQNLGISVISV 722
Cdd:PRK10908 120 AALDKVGL------LDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEgilRLFEEFNRVGVTVLMA 193
|
250
....*....|..
gi 50285999 723 CHRTTLWHFHNY 734
Cdd:PRK10908 194 THDIGLISRRSY 205
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
516-720 |
6.76e-06 |
|
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: 47.98 E-value: 6.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 516 LNFELKHGDHLLIIGPNGCGKSSLFRLLGGLwpIRQiETGVQT-------KLTVPPRKIGQ--DCAIFYlpqkPYMgngs 586
Cdd:cd03268 19 ISLHVKKGEIYGFLGPNGAGKTTTMKIILGL--IKP-DSGEITfdgksyqKNIEALRRIGAliEAPGFY----PNL---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 587 TFREQIIYPDTIedfeerfngdYNMGDEKLISVLELLDLTDlitenlslvLAGKGTKKsdnldeenlteiraafdlkrnw 666
Cdd:cd03268 88 TARENLRLLARL----------LGIRKKRIDEVLDVVGLKD---------SAKKKVKG---------------------- 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 50285999 667 seeLSIGVQQRLAMARMYYHKPKFAVLDECTSAVSPEMEQKMYENAQNL---GISVI 720
Cdd:cd03268 127 ---FSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLrdqGITVL 180
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
511-700 |
9.47e-06 |
|
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: 47.49 E-value: 9.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 511 VLVPELNFELKHGDHLLIIGPNGCGKSSLFRLLGGLWPirqIETGvqtKLTVPPRKIGQDC-----AIFYLPQKPymgng 585
Cdd:cd03231 14 ALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSP---PLAG---RVLLNGGPLDFQRdsiarGLLYLGHAP----- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 586 stfreqiiypdtiedfeerfngdynmGDEKLISVLelldltdlitENLSLVLAGKGTKK-SDNLDEENLT--EIRAAfdl 662
Cdd:cd03231 83 --------------------------GIKTTLSVL----------ENLRFWHADHSDEQvEEALARVGLNgfEDRPV--- 123
|
170 180 190
....*....|....*....|....*....|....*...
gi 50285999 663 krnwsEELSIGVQQRLAMARMYYHKPKFAVLDECTSAV 700
Cdd:cd03231 124 -----AQLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
509-724 |
1.01e-05 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 48.56 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 509 NQVLVPELNFELKHGDHLLIIGPNGCGKSSLFRLLGGLwpirQIETGVQ--------TKLTVPPRKIG---QDCAIFylp 577
Cdd:PRK11432 18 SNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGL----EKPTEGQifidgedvTHRSIQQRDICmvfQSYALF--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 578 qkPYMGNGstfrEQIIYpdtiedfeerfnGDYNMG---DEKLISVLELLDLTDlitenlslvLAGKGTKKSDnldeenlt 654
Cdd:PRK11432 91 --PHMSLG----ENVGY------------GLKMLGvpkEERKQRVKEALELVD---------LAGFEDRYVD-------- 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50285999 655 eiraafdlkrnwseELSIGVQQRLAMARMYYHKPKFAVLDECTSAVSP----EMEQKMYENAQNLGISVISVCH 724
Cdd:PRK11432 136 --------------QISGGQQQRVALARALILKPKVLLFDEPLSNLDAnlrrSMREKIRELQQQFNITSLYVTH 195
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
516-724 |
1.28e-05 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 47.50 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 516 LNFELKHGDHLLIIGPNGCGKSSLFRLLGGLwpIRQ-----------IETGVQTKLTVPPRKIG---QDCAIFylpqkpy 581
Cdd:cd03261 19 VDLDVRRGEILAIIGPSGSGKSTLLRLIVGL--LRPdsgevlidgedISGLSEAELYRLRRRMGmlfQSGALF------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 582 mgNGSTFREQIIYPdtiedFEERFNgdynmGDEKLIsvlelldlTDLITENLSLVlagkgtkksdnldeenltEIRAAFD 661
Cdd:cd03261 90 --DSLTVFENVAFP-----LREHTR-----LSEEEI--------REIVLEKLEAV------------------GLRGAED 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50285999 662 LkrnWSEELSIGVQQRLAMARMYYHKPKFAVLDECTSAVSP----EMEQKMYENAQNLGISVISVCH 724
Cdd:cd03261 132 L---YPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPiasgVIDDLIRSLKKELGLTSIMVTH 195
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
495-724 |
1.33e-05 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 47.42 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 495 NLIKFEHVPLITPANQVLvPELNFELKHGDHLLIIGPNGCGKSSLFRLLGGLwpirqIETGVQTKLTVPPRKIGqdcaif 574
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVL-SDVSLELKPGKILTLLGPNGAGKSTLVRVVLGL-----VAPDEGVIKRNGKLRIG------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 575 YLPQKPYMgngstfreQIIYPDTIEDFeerfngdynmgdeklisvlelldltdlitenlslVLAGKGTKKSDNLDEenLT 654
Cdd:PRK09544 71 YVPQKLYL--------DTTLPLTVNRF----------------------------------LRLRPGTKKEDILPA--LK 106
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50285999 655 EIRAAfDLKRNWSEELSIGVQQRLAMARMYYHKPKFAVLDECTSAVSPEMEQKMYENAQN----LGISVISVCH 724
Cdd:PRK09544 107 RVQAG-HLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQlrreLDCAVLMVSH 179
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
516-548 |
1.40e-05 |
|
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: 47.14 E-value: 1.40e-05
10 20 30
....*....|....*....|....*....|...
gi 50285999 516 LNFELKHGDHLLIIGPNGCGKSSLFRLLGGLWP 548
Cdd:cd03220 41 VSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYP 73
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
513-741 |
2.62e-05 |
|
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: 46.38 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 513 VPELNFELKHGDHLLIIGPNGCGKSSLFRLLGGLWPIRQ--IETGVQ--TKLTVPPR-KIGqdcaIFYLPQKPymgngST 587
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSgkILLDGQdiTKLPMHKRaRLG----IGYLPQEA-----SI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 588 FREQiiypdTIEdfeerfngdynmgdEKLISVLELLDLTDLITEnlslvlagkgtKKSDNLDEE-NLTEIRaafdlkRNW 666
Cdd:cd03218 87 FRKL-----TVE--------------ENILAVLEIRGLSKKERE-----------EKLEELLEEfHITHLR------KSK 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 667 SEELSIGVQQRLAMARMYYHKPKFAVLDECTSAVSP----EMeQKMYENAQNLGISV----------ISVCHRTtlwhfh 732
Cdd:cd03218 131 ASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPiavqDI-QKIIKILKDRGIGVlitdhnvretLSITDRA------ 203
|
....*....
gi 50285999 733 nYLLkFDGK 741
Cdd:cd03218 204 -YII-YEGK 210
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
509-545 |
3.09e-05 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 47.37 E-value: 3.09e-05
10 20 30
....*....|....*....|....*....|....*..
gi 50285999 509 NQVLVPELNFELKHGDHLLIIGPNGCGKSSLFRLLGG 545
Cdd:COG0488 327 DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAG 363
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
516-727 |
3.49e-05 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 47.51 E-value: 3.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 516 LNFELKHGDHLLIIGPNGCGKSSLFRLLGGLWpirQIETGVQTKLTVPPRKIGQDC---AIFYLPQKPYMGNGsTFREQI 592
Cdd:PRK11160 359 LSLQIKAGEKVALLGRTGCGKSTLLQLLTRAW---DPQQGEILLNGQPIADYSEAAlrqAISVVSQRVHLFSA-TLRDNL 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 593 IYpdtiedfeerfnGDYNMGDEKLISVLELLDLTDLITENLSLvlagkgtkksdnldeenlteiraafdlkRNWSEE--- 669
Cdd:PRK11160 435 LL------------AAPNASDEALIEVLQQVGLEKLLEDDKGL----------------------------NAWLGEggr 474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50285999 670 -LSIGVQQRLAMARMYYHKPKFAVLDECTSAVSPEMEQKM----YENAQNLgiSVISVCHRTT 727
Cdd:PRK11160 475 qLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQIlellAEHAQNK--TVLMITHRLT 535
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
516-731 |
4.87e-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: 45.80 E-value: 4.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 516 LNFELKHGDHLLIIGPNGCGKSSLFRLLGGLWPI---------RQIeTGvqtkltVPPRKIGQdcaifylpqkpyMGNGS 586
Cdd:COG0411 23 VSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPtsgrilfdgRDI-TG------LPPHRIAR------------LGIAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 587 TFreQIIYPdtiedFEErfngdynMgdekliSVLELLDLTDLITENLSLVLAGKGTKKSDNLDEENLTEIRAA---FDL- 662
Cdd:COG0411 84 TF--QNPRL-----FPE-------L------TVLENVLVAAHARLGRGLLAALLRLPRARREEREARERAEELlerVGLa 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 663 -KRNW-SEELSIGVQQRLAMARMYYHKPKFAVLDECTSAVSPEMEQKMYEN----AQNLGISVI----------SVCHRT 726
Cdd:COG0411 144 dRADEpAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELirrlRDERGITILliehdmdlvmGLADRI 223
|
....*
gi 50285999 727 TLWHF 731
Cdd:COG0411 224 VVLDF 228
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
508-545 |
5.18e-05 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 45.88 E-value: 5.18e-05
10 20 30
....*....|....*....|....*....|....*...
gi 50285999 508 ANQVLVPELNFELKHGDHLLIIGPNGCGKSSLFRLLGG 545
Cdd:COG4559 12 GGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTG 49
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
493-724 |
5.42e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 45.95 E-value: 5.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 493 NENLIKFEHVPLITPANQV-LVPELNFELKHGDHLLIIGPNGCGKSSLFRLLGG-LWPirqiETGVQTKLTVPPRKIGQd 570
Cdd:PRK13640 2 KDNIVEFKHVSFTYPDSKKpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlLLP----DDNPNSKITVDGITLTA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 571 caifylpqkpymgngstfreqiiypDTIEDFEERFNGDYNMGDEKLISVlelldltdLITENLSLVLAGKGTKKSDNLD- 649
Cdd:PRK13640 77 -------------------------KTVWDIREKVGIVFQNPDNQFVGA--------TVGDDVAFGLENRAVPRPEMIKi 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 650 -EENLTEIrAAFDLKRNWSEELSIGVQQRLAMARMYYHKPKFAVLDECTSAVSPEMEQKMYENAQNL----GISVISVCH 724
Cdd:PRK13640 124 vRDVLADV-GMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLkkknNLTVISITH 202
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
475-699 |
6.33e-05 |
|
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: 46.43 E-value: 6.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 475 AVGNIDKKDEDVLDLVEYNENLIKFEHV----PLITPANQVLVPELNFELKHGDHLLIIGPNGCGKSSLFRLLGGLwpir 550
Cdd:COG1123 239 AVPRLGAARGRAAPAAAAAEPLLEVRNLskryPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGL---- 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 551 qietgvqtkltVPPRKiGQdcaIFYLPQKPYMGNGSTFRE-----QIIY--PD-------TIED-FEE--RFNGDYNmGD 613
Cdd:COG1123 315 -----------LRPTS-GS---ILFDGKDLTKLSRRSLRElrrrvQMVFqdPYsslnprmTVGDiIAEplRLHGLLS-RA 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 614 EKLISVLELLDLTDLITENLSlvlagkgtkksdnldeenlteiRAAFdlkrnwseELSIGVQQRLAMARMYYHKPKFAVL 693
Cdd:COG1123 379 ERRERVAELLERVGLPPDLAD----------------------RYPH--------ELSGGQRQRVAIARALALEPKLLIL 428
|
....*.
gi 50285999 694 DECTSA 699
Cdd:COG1123 429 DEPTSA 434
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
496-724 |
7.29e-05 |
|
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: 45.26 E-value: 7.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 496 LIKFEHVPLITPANQVLVPEL---NFELKHGDHLLIIGPNGCGKSSLFRLLGGLwpirqiET---------GVQTKLTVP 563
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALkdvSLSVPKGEIFGIIGRSGAGKSTLIRCINGL------ERptsgsvlvdGTDLTLLSG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 564 P------RKIGQdcaIFylpQKPYMGNGSTFREQIIYPDTI--EDFEERfngdynmgDEKlisVLELLDLTDLitenlsl 635
Cdd:cd03258 75 KelrkarRRIGM---IF---QHFNLLSSRTVFENVALPLEIagVPKAEI--------EER---VLELLELVGL------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 636 vlagkgtkksdnldeenlteiraaFDLKRNWSEELSIGVQQRLAMARMYYHKPKFAVLDECTSAVSPEMEQK----MYEN 711
Cdd:cd03258 131 ------------------------EDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSilalLRDI 186
|
250
....*....|...
gi 50285999 712 AQNLGISVISVCH 724
Cdd:cd03258 187 NRELGLTIVLITH 199
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
516-724 |
1.32e-04 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 45.02 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 516 LNFELKHGDHLLIIGPNGCGKSSLFRLLGGLWPIRQIE--TGVQTKLTVPPRKigqdcaifylpqkpyMGNGSTFREQII 593
Cdd:PRK11000 22 INLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDlfIGEKRMNDVPPAE---------------RGVGMVFQSYAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 594 YPDtiedfeerfngdynmgdeklisvlelLDLTDliteNLSLVLAGKGTKKSDnLDE--ENLTEI-RAAFDLKRNwSEEL 670
Cdd:PRK11000 87 YPH--------------------------LSVAE----NMSFGLKLAGAKKEE-INQrvNQVAEVlQLAHLLDRK-PKAL 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 50285999 671 SIGVQQRLAMARMYYHKPKFAVLDECTS----AVSPEMEQKMYENAQNLGISVISVCH 724
Cdd:PRK11000 135 SGGQRQRVAIGRTLVAEPSVFLLDEPLSnldaALRVQMRIEISRLHKRLGRTMIYVTH 192
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
528-697 |
1.97e-04 |
|
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: 44.93 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 528 IIGPNGCGKSSLFRLLGGL--------WPirqietgvqtkltVPPRKIGqdcaifYLPQKPYMGNGSTFREQII-----Y 594
Cdd:TIGR03719 36 VLGLNGAGKSTLLRIMAGVdkdfngeaRP-------------QPGIKVG------YLPQEPQLDPTKTVRENVEegvaeI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 595 PDTIEDFEERFNgdyNMGDEKlisvlelLDLTDLITENlslvlaGKGTKKSDNLDEENL-TEIRAAFDLKR--NWS---E 668
Cdd:TIGR03719 97 KDALDRFNEISA---KYAEPD-------ADFDKLAAEQ------AELQEIIDAADAWDLdSQLEIAMDALRcpPWDadvT 160
|
170 180
....*....|....*....|....*....
gi 50285999 669 ELSIGVQQRLAMARMYYHKPKFAVLDECT 697
Cdd:TIGR03719 161 KLSGGERRRVALCRLLLSKPDMLLLDEPT 189
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
508-594 |
2.27e-04 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 43.85 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 508 ANQVLVPELNFELKHGDHLLIIGPNGCGKSSLFRLLGglwpirQIETGVQTKLTVPPRKIGQDCA------IFYLPQKPY 581
Cdd:PRK11231 13 GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFA------RLLTPQSGTVFLGDKPISMLSSrqlarrLALLPQHHL 86
|
90
....*....|...
gi 50285999 582 MGNGSTFREQIIY 594
Cdd:PRK11231 87 TPEGITVRELVAY 99
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
415-700 |
2.58e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 44.97 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 415 VQNGDqpdaTDATADFITNRRLLLTASSSVgrfVELKKNIqeLRGTSLRLNYLNDLldkYAVGNIDKKDEDVLDLVEYNE 494
Cdd:PLN03232 1157 LRNGN----AENQAGFASTMGLLLSYTLNI---TTLLSGV--LRQASKAENSLNSV---ERVGNYIDLPSEATAIIENNR 1224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 495 --------NLIKFEHVPL-ITPANQVLVPELNFELKHGDHLLIIGPNGCGKSSlfrLLGGLWPIRQIETGvqtKLTVPpr 565
Cdd:PLN03232 1225 pvsgwpsrGSIKFEDVHLrYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSS---MLNALFRIVELEKG---RIMID-- 1296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 566 kiGQDCAIFYL----------PQKPYMGNGSTfreqiiypdtiedfeeRFNGD--YNMGDEKLISVLELLDLTDLITENl 633
Cdd:PLN03232 1297 --DCDVAKFGLtdlrrvlsiiPQSPVLFSGTV----------------RFNIDpfSEHNDADLWEALERAHIKDVIDRN- 1357
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50285999 634 slvlagkgtkkSDNLDEENLteiraafdlkrNWSEELSIGVQQRLAMARMYYHKPKFAVLDECTSAV 700
Cdd:PLN03232 1358 -----------PFGLDAEVS-----------EGGENFSVGQRQLLSLARALLRRSKILVLDEATASV 1402
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
516-546 |
4.07e-04 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 43.04 E-value: 4.07e-04
10 20 30
....*....|....*....|....*....|.
gi 50285999 516 LNFELKHGDHLLIIGPNGCGKSSLFRLLGGL 546
Cdd:COG1127 24 VSLDVPRGEILAIIGGSGSGKSVLLKLIIGL 54
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
517-724 |
4.65e-04 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 42.84 E-value: 4.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 517 NFELKHGDHLLIIGPNGCGKSSLFRLLGG-LWPIR-QIETGVQTKLTVPPRKIGQDCAIfyLPQKPYMGNGSTFREQI-- 592
Cdd:PRK13548 22 SLTLRPGEVVAILGPNGAGKSTLLRALSGeLSPDSgEVRLNGRPLADWSPAELARRRAV--LPQHSSLSFPFTVEEVVam 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 593 -IYPDTIEDFEerfngdynmgDEKLI-SVLELLDLTDlitenlslvLAGkgtkksdnldeenlteiraafdlkRNWSeEL 670
Cdd:PRK13548 100 gRAPHGLSRAE----------DDALVaAALAQVDLAH---------LAG------------------------RDYP-QL 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50285999 671 SIGVQQRLAMAR------MYYHKPKFAVLDECTSAVSPEMEQKMYENAQNL----GISVISVCH 724
Cdd:PRK13548 136 SGGEQQRVQLARvlaqlwEPDGPPRWLLLDEPTSALDLAHQHHVLRLARQLaherGLAVIVVLH 199
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
497-700 |
8.86e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 43.19 E-value: 8.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 497 IKFEHVPL-ITPANQVLVPELNFELKHGDHLLIIGPNGCGKSSLfrlLGGLWPIRQIETGVQTKLTVPPRKIG-QDC--A 572
Cdd:PLN03130 1238 IKFEDVVLrYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSM---LNALFRIVELERGRILIDGCDISKFGlMDLrkV 1314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 573 IFYLPQKPYMGNGSTfreqiiypdtiedfeeRFNGD-YN-MGDEKLISVLELLDLTDLITENlslvlagkgtkkSDNLDE 650
Cdd:PLN03130 1315 LGIIPQAPVLFSGTV----------------RFNLDpFNeHNDADLWESLERAHLKDVIRRN------------SLGLDA 1366
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 50285999 651 EnLTEIraafdlkrnwSEELSIGVQQRLAMARMYYHKPKFAVLDECTSAV 700
Cdd:PLN03130 1367 E-VSEA----------GENFSVGQRQLLSLARALLRRSKILVLDEATAAV 1405
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
508-562 |
9.00e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 43.02 E-value: 9.00e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 50285999 508 ANQVLVPELNFELKHGDHLLIIGPNGCGKSSLFRL-LGGLWPIR-QIETGvqTKLTV 562
Cdd:PRK11147 330 DGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLmLGQLQADSgRIHCG--TKLEV 384
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
511-545 |
1.04e-03 |
|
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: 42.61 E-value: 1.04e-03
10 20 30
....*....|....*....|....*....|....*
gi 50285999 511 VLVPELNFELKHGDHLLIIGPNGCGKSSLFRLLGG 545
Cdd:TIGR03719 336 LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITG 370
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
493-724 |
1.92e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 41.13 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 493 NENLIKFEHVPL-ITPANQVLVPELNFELKHGDHLLIIGPNGCGKSSLFRLLGGLWPIRQ----IETGVQTKLTVPP--R 565
Cdd:PRK13632 4 KSVMIKVENVSFsYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSgeikIDGITISKENLKEirK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 566 KIGqdcAIFYLPQKPYMGNgstfreqiiypdTIEDfeerfngDYNMGDE-KLISVLELLDltdlITENLSLVLagkGTKk 644
Cdd:PRK13632 84 KIG---IIFQNPDNQFIGA------------TVED-------DIAFGLEnKKVPPKKMKD----IIDDLAKKV---GME- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 645 sDNLDEEnlteiraafdlkrnwSEELSIGVQQRLAMARMYYHKPKFAVLDECTSAVSP----EMEQKMYENAQNLGISVI 720
Cdd:PRK13632 134 -DYLDKE---------------PQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPkgkrEIKKIMVDLRKTRKKTLI 197
|
....
gi 50285999 721 SVCH 724
Cdd:PRK13632 198 SITH 201
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
511-546 |
2.37e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 41.64 E-value: 2.37e-03
10 20 30
....*....|....*....|....*....|....*.
gi 50285999 511 VLVPELNFELKHGDHLLIIGPNGCGKSSLFRLLGGL 546
Cdd:PRK11819 338 LLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQ 373
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
516-548 |
2.93e-03 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 40.21 E-value: 2.93e-03
10 20 30
....*....|....*....|....*....|...
gi 50285999 516 LNFELKHGDHLLIIGPNGCGKSSLFRLLGGLWP 548
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP 47
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
629-715 |
3.37e-03 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 40.14 E-value: 3.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 629 ITENLSLVLAGKGTKKSDNLDEENLTEIRAAfdlkRNWSE----------ELSIGVQQRLAMARMYYHKPKFAVLDECTS 698
Cdd:PRK14239 102 IYENVVYGLRLKGIKDKQVLDEAVEKSLKGA----SIWDEvkdrlhdsalGLSGGQQQRVCIARVLATSPKIILLDEPTS 177
|
90
....*....|....*..
gi 50285999 699 AVSPEMEQKMYENAQNL 715
Cdd:PRK14239 178 ALDPISAGKIEETLLGL 194
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
509-546 |
4.55e-03 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 39.97 E-value: 4.55e-03
10 20 30
....*....|....*....|....*....|....*...
gi 50285999 509 NQVLVPELNFELKHGDHLLIIGPNGCGKSSLFRLLGGL 546
Cdd:PRK10253 19 KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRL 56
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
516-546 |
5.23e-03 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 39.45 E-value: 5.23e-03
10 20 30
....*....|....*....|....*....|.
gi 50285999 516 LNFELKHGDHLLIIGPNGCGKSSLFRLLGGL 546
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGL 60
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
516-549 |
7.09e-03 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 39.30 E-value: 7.09e-03
10 20 30
....*....|....*....|....*....|....
gi 50285999 516 LNFELKHGDHLLIIGPNGCGKSSLFRLLGGLWPI 549
Cdd:COG1101 25 LNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPP 58
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
508-546 |
7.53e-03 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 38.82 E-value: 7.53e-03
10 20 30
....*....|....*....|....*....|....*....
gi 50285999 508 ANQVLvPELNFELKHGDHLLIIGPNGCGKSSLFRLLGGL 546
Cdd:COG1126 13 DLEVL-KGISLDVEKGEVVVIIGPSGSGKSTLLRCINLL 50
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
497-547 |
8.20e-03 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 39.57 E-value: 8.20e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 50285999 497 IKFEHVPLITPANQVLVPELNFELKHGDHLLIIGPNGCGKSSLFRLLGGLW 547
Cdd:PRK10522 323 LELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLY 373
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
516-710 |
9.69e-03 |
|
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: 38.64 E-value: 9.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 516 LNFELKHGDHLLIIGPNGCGKSSLFRLLGGLWP-------IRQIEtgVQTKLTVPPRKIGqdcaifYLPQKpymgngstf 588
Cdd:cd03263 21 LSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRptsgtayINGYS--IRTDRKAARQSLG------YCPQF--------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50285999 589 reQIIYPD-TIED---FEERFNG----DYNMGDEKLISVLELLDltdlitenlslvlagkgtkksdnldeenlteiraaf 660
Cdd:cd03263 84 --DALFDElTVREhlrFYARLKGlpksEIKEEVELLLRVLGLTD------------------------------------ 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 50285999 661 dlKRNW-SEELSIGVQQRL--AMARMYYhkPKFAVLDECTSAVSPEMEQKMYE 710
Cdd:cd03263 126 --KANKrARTLSGGMKRKLslAIALIGG--PSVLLLDEPTSGLDPASRRAIWD 174
|
|
| |
