|
Name |
Accession |
Description |
Interval |
E-value |
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
32-444 |
1.18e-92 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 290.94 E-value: 1.18e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 32 FGYFILGTVVNkTLMGPIVMKL-VHQEKLEGDFRFKHMQIRVNAEPAAFYRAGHVEHMRTDRRLQRLLQTQRELMSKELW 110
Cdd:COG4178 189 LIYAIIGTLLT-HLIGRPLIRLnFEQQRREADFRFALVRVRENAESIALYRGEAAERRRLRRRFDAVIANWRRLIRRQRN 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 111 LYIGINTFDYLGSILSYVVIAIPIFSGvygDLSPAELSTLVSknAFVciYLISCFTQLIDLSTTLSDVAGYTHRIGQLRE 190
Cdd:COG4178 268 LTFFTTGYGQLAVIFPILVAAPRYFAG---EITLGGLMQAAS--AFG--QVQGALSWFVDNYQSLAEWRATVDRLAGFEE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 191 TLLDMSLKSQDCEILGESEwgldtppgwpaaepaDTAFLLERVSISAPSsDKPLIKDLSLKISEGQSLLITGNTGTGKTS 270
Cdd:COG4178 341 ALEAADALPEAASRIETSE---------------DGALALEDLTLRTPD-GRPLLEDLSLSLKPGERLLITGPSGSGKST 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 271 LLRVLGGLWTSTRGSVQMltdfgPHG--VLFLPQKPFFTDGTLREQVIYPLkevypDSGSADDERILRFLELAGLSNLVA 348
Cdd:COG4178 405 LLRAIAGLWPYGSGRIAR-----PAGarVLFLPQRPYLPLGTLREALLYPA-----TAEAFSDAELREALEAVGLGHLAE 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 349 RtegLDQQVDWNwyDVLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEVESELYR-IGQQL-GMTFISVGHRQSLEKF 426
Cdd:COG4178 475 R---LDEEADWD--QVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQlLREELpGTTVISVGHRSTLAAF 549
|
410
....*....|....*...
gi 10947129 427 HSLVLKLCGGGRWELMRI 444
Cdd:COG4178 550 HDRVLELTGDGSWQLLPA 567
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
228-439 |
7.46e-78 |
|
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: 239.36 E-value: 7.46e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 228 FLLERVSISAPSsDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQMLTDfgpHGVLFLPQKPFFT 307
Cdd:cd03223 1 IELENLSLATPD-GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEG---EDLLFLPQRPYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 308 DGTLREQVIYPlkevypdsgsadderilrflelaglsnlvartegldqqvdwnWYDVLSPGEMQRLSFARLFYLQPKYAV 387
Cdd:cd03223 77 LGTLREQLIYP------------------------------------------WDDVLSGGEQQRLAFARLLLHKPKFVF 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 10947129 388 LDEATSALTEEVESELYRIGQQLGMTFISVGHRQSLEKFHSLVLKLCGGGRW 439
Cdd:cd03223 115 LDEATSALDEESEDRLYQLLKELGITVISVGHRPSLWKFHDRVLDLDGEGGW 166
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
12-441 |
7.42e-74 |
|
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: 244.27 E-value: 7.42e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 12 LVYYTYQCFQSTGWLGPVSIFGYFILGTVVNKTLMGPIVMKLVHQEKLEGDFRFKHMQIRVNAEPAAFYRAGHVEHMRTD 91
Cdd:TIGR00954 226 VILYSFKLLTALGSVGPAGLFAYLFATGVVLTKLRPPIGKLTVEEQALEGEYRYVHSRLIMNSEEIAFYQGNKVEKETVM 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 92 RRLQRLLqtqrELMSKELWLYIGINTFD-----YLGSILSYVVIAIPIFSGV---YGDLSPAELSTLVSKNAFVCIYLIS 163
Cdd:TIGR00954 306 SSFYRLV----EHLNLIIKFRFSYGFLDnivakYTWSAVGLVAVSIPIFDKThpaFLEMSEEELMQEFYNNGRLLLKAAD 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 164 CFTQLIDLSTTLSDVAGYTHRIGQLRETLLDMSL----KSQDCEILGESEWGLDTP--PGWPAAEPADTAFLLERVSISA 237
Cdd:TIGR00954 382 ALGRLMLAGRDMTRLAGFTARVDTLLQVLDDVKSgnfkRPRVEEIESGREGGRNSNlvPGRGIVEYQDNGIKFENIPLVT 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 238 PSSDKpLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWtSTRGSVqmLTDFGPHGVLFLPQKPFFTDGTLREQVIY 317
Cdd:TIGR00954 462 PNGDV-LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELW-PVYGGR--LTKPAKGKLFYVPQRPYMTLGTLRDQIIY 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 318 PL-KEVYPDSGSADDERIlRFLELAGLSNLVARTEGLDQQVDWNwyDVLSPGEMQRLSFARLFYLQPKYAVLDEATSALT 396
Cdd:TIGR00954 538 PDsSEDMKRRGLSDKDLE-QILDNVQLTHILEREGGWSAVQDWM--DVLSGGEKQRIAMARLFYHKPQFAILDECTSAVS 614
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 10947129 397 EEVESELYRIGQQLGMTFISVGHRQSLEKFHSLVLKLCGGGRWEL 441
Cdd:TIGR00954 615 VDVEGYMYRLCREFGITLFSVSHRKSLWKYHEYLLYMDGRGGYQF 659
|
|
| ABC_membrane_2 |
pfam06472 |
ABC transporter transmembrane region 2; This domain covers the transmembrane of a small family ... |
1-135 |
2.55e-46 |
|
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: 161.24 E-value: 2.55e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 1 MASKLIISPFTLVYYTYQCFQSTGWLGPVSIFGYFILGTVVNKTLMGPIVMKLVHQEKLEGDFRFKHMQIRVNAEPAAFY 80
Cdd:pfam06472 134 LYSNLLKPILDIILFTFRLWRLSGWRGPAILFLYVLLSAVILRRLSPPFGKLVAEEQKLEGEFRYLHSRLITNAEEIAFY 213
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 10947129 81 RAGHVEHMRTDRRLQRLLQTQRELMSKELWLYIGINTF-DYLGSILSYVVIAIPIF 135
Cdd:pfam06472 214 RGEKREKKQLQRSFKSLIDHMRRILRRRLWYGFIEDFVlKYTWSILGYVLVALPIF 269
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
89-423 |
4.98e-31 |
|
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: 126.10 E-value: 4.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 89 RTDRRLQRLLQTQRELMSKELWLYIGINTFdylgSILSYVVIaipIFSGVY----GDLSpaeLSTLVsknAFVCI--YLI 162
Cdd:COG2274 359 RWENLLAKYLNARFKLRRLSNLLSTLSGLL----QQLATVAL---LWLGAYlvidGQLT---LGQLI---AFNILsgRFL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 163 SCFTQLIDLSTTLSDVAGYTHRIGQLretlldmslksqdceilgesewgLDTPPGWPAAEPADT------AFLLERVSIS 236
Cdd:COG2274 426 APVAQLIGLLQRFQDAKIALERLDDI-----------------------LDLPPEREEGRSKLSlprlkgDIELENVSFR 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 237 APSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM----LTDFGPH------GVlfLPQKPFF 306
Cdd:COG2274 483 YPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIdgidLRQIDPAslrrqiGV--VLQDVFL 560
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 307 TDGTLREQVIYplkevypDSGSADDERILRFLELAGLSNLVAR-TEGLDQQVDwNWYDVLSPGEMQRLSFARLFYLQPKY 385
Cdd:COG2274 561 FSGTIRENITL-------GDPDATDEEIIEAARLAGLHDFIEAlPMGYDTVVG-EGGSNLSGGQRQRLAIARALLRNPRI 632
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 10947129 386 AVLDEATSALTEEVESELYRIGQQL--GMTFISVGHRQSL 423
Cdd:COG2274 633 LILDEATSALDAETEAIILENLRRLlkGRTVIIIAHRLST 672
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
235-419 |
1.88e-30 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 116.84 E-value: 1.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 235 ISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----QMLTDFGPHG----VLFLPQKPFF 306
Cdd:COG4619 6 LSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIyldgKPLSAMPPPEwrrqVAYVPQEPAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 307 TDGTLREQVIYPLKevyPDSGSADDERILRFLELAGLSNLVartegLDQQVDwnwydVLSPGEMQRLSFARLFYLQPKYA 386
Cdd:COG4619 86 WGGTVRDNLPFPFQ---LRERKFDRERALELLERLGLPPDI-----LDKPVE-----RLSGGERQRLALIRALLLQPDVL 152
|
170 180 190
....*....|....*....|....*....|....*..
gi 10947129 387 VLDEATSAL----TEEVESELYRIGQQLGMTFISVGH 419
Cdd:COG4619 153 LLDEPTSALdpenTRRVEELLREYLAEEGRAVLWVSH 189
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
230-423 |
1.29e-27 |
|
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: 109.60 E-value: 1.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 230 LERVSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM----LTDFGP----HGVLFLP 301
Cdd:cd03245 5 FRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLdgtdIRQLDPadlrRNIGYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 302 QKPFFTDGTLREQVIYplkevypDSGSADDERILRFLELAGLSNLVAR-TEGLDQQVDWNWYDvLSPGEMQRLSFARLFY 380
Cdd:cd03245 85 QDVTLFYGTLRDNITL-------GAPLADDERILRAAELAGVTDFVNKhPNGLDLQIGERGRG-LSGGQRQAVALARALL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 10947129 381 LQPKYAVLDEATSALTEEVESELYRIGQQL--GMTFISVGHRQSL 423
Cdd:cd03245 157 NDPPILLLDEPTSAMDMNSEERLKERLRQLlgDKTLIIITHRPSL 201
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
80-420 |
2.23e-25 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 108.71 E-value: 2.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 80 YRAGHVEHMRTDRRLQRLLQTQRELMSKELWLYIGINTFDYLGSILSYVVIAIPIFSGvygDLSPAELSTLVSknafvci 159
Cdd:COG1132 216 FGREERELERFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSG---SLTVGDLVAFIL------- 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 160 YLISCFTQLIDLSTTLSDV---AGYTHRIgqlrETLLDMSLKSQDceilgesewgldtPPGWPAAEPADTAFLLERVSIS 236
Cdd:COG1132 286 YLLRLFGPLRQLANVLNQLqraLASAERI----FELLDEPPEIPD-------------PPGAVPLPPVRGEIEFENVSFS 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 237 APSsDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM----LTDFGPHG----VLFLPQKPFFTD 308
Cdd:COG1132 349 YPG-DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIdgvdIRDLTLESlrrqIGVVPQDTFLFS 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 309 GTLREQVIYPLKEvypdsgsADDERILRFLELAGLSNLVAR-TEGLDQQVDWNWYDvLSPGEMQRLSFARLFYLQPKYAV 387
Cdd:COG1132 428 GTIRENIRYGRPD-------ATDEEVEEAAKAAQAHEFIEAlPDGYDTVVGERGVN-LSGGQRQRIAIARALLKDPPILI 499
|
330 340 350
....*....|....*....|....*....|....*..
gi 10947129 388 LDEATSAL---TE-EVESELYRIGQqlGMTFISVGHR 420
Cdd:COG1132 500 LDEATSALdteTEaLIQEALERLMK--GRTTIVIAHR 534
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
214-423 |
3.05e-25 |
|
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: 108.14 E-value: 3.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 214 TPPGWPAAEPADTAFLLERVSISAPSSDkPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM----L 289
Cdd:TIGR02857 308 LAGKAPVTAAPASSLEFSGVSVAYPGRR-PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVngvpL 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 290 TDFGPHG----VLFLPQKPFFTDGTLREQVIYPLKEvypdsgsADDERILRFLELAGLSNLV-ARTEGLDQQVDWNWYDv 364
Cdd:TIGR02857 387 ADADADSwrdqIAWVPQHPFLFAGTIAENIRLARPD-------ASDAEIREALERAGLDEFVaALPQGLDTPIGEGGAG- 458
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 10947129 365 LSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEVESELYRIGQQL--GMTFISVGHRQSL 423
Cdd:TIGR02857 459 LSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALaqGRTVLLVTHRLAL 519
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
230-423 |
6.70e-25 |
|
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: 107.15 E-value: 6.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 230 LERVSISAPSsDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----QMLTDFGP----HGVLFLP 301
Cdd:COG4988 339 LEDVSFSYPG-GRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSIlingVDLSDLDPaswrRQIAWVP 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 302 QKPFFTDGTLREQviypLKEVYPDsgsADDERILRFLELAGLSNLVAR-TEGLDQQVD---WNwydvLSPGEMQRLSFAR 377
Cdd:COG4988 418 QNPYLFAGTIREN----LRLGRPD---ASDEELEAALEAAGLDEFVAAlPDGLDTPLGeggRG----LSGGQAQRLALAR 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 10947129 378 LFYLQPKYAVLDEATSALTEEVESELYRIGQQL--GMTFISVGHRQSL 423
Cdd:COG4988 487 ALLRDAPLLLLDEPTAHLDAETEAEILQALRRLakGRTVILITHRLAL 534
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
230-420 |
2.29e-24 |
|
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: 100.23 E-value: 2.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 230 LERVSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM----LTDFGPH------GVLF 299
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVdgkdLTKLSLKelrrkvGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 300 lpQKP---FFTDgTLREQVIYPLkEVYPDSGSADDERILRFLELAGLSNLvartegldqqVDWNWYDvLSPGEMQRLSFA 376
Cdd:cd03225 82 --QNPddqFFGP-TVEEEVAFGL-ENLGLPEEEIEERVEEALELVGLEGL----------RDRSPFT-LSGGQKQRVAIA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 10947129 377 RLFYLQPKYAVLDEATSAL----TEEVESELYRIGQQlGMTFISVGHR 420
Cdd:cd03225 147 GVLAMDPDILLLDEPTAGLdpagRRELLELLKKLKAE-GKTIIIVTHD 193
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
230-423 |
2.32e-24 |
|
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: 98.99 E-value: 2.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 230 LERVSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----QMLTDFGPHG----VLFLP 301
Cdd:cd03228 3 FKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEIlidgVDLRDLDLESlrknIAYVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 302 QKPFFTDGTLREqviyplkevypdsgsadderilrflelaglsNLvartegldqqvdwnwydvLSPGEMQRLSFARLFYL 381
Cdd:cd03228 83 QDPFLFSGTIRE-------------------------------NI------------------LSGGQRQRIAIARALLR 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 10947129 382 QPKYAVLDEATSAL---TE-EVESELYRIGQqlGMTFISVGHRQSL 423
Cdd:cd03228 114 DPPILILDEATSALdpeTEaLILEALRALAK--GKTVIVIAHRLST 157
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
230-436 |
7.35e-24 |
|
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: 97.67 E-value: 7.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 230 LERVSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM---------LTDFGPHgVLFL 300
Cdd:cd03246 3 VENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLdgadisqwdPNELGDH-VGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 301 PQKPFFTDGTLREqviyplkevypdsgsadderilrflelaglsnlvartegldqqvdwnwyDVLSPGEMQRLSFARLFY 380
Cdd:cd03246 82 PQDDELFSGSIAE-------------------------------------------------NILSGGQRQRLGLARALY 112
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 10947129 381 LQPKYAVLDEATSALTEEVESELYRIGQQL---GMTFISVGHRQSLEKFHSLVLKLCGG 436
Cdd:cd03246 113 GNPRILVLDEPNSHLDVEGERALNQAIAALkaaGATRIVIAHRPETLASADRILVLEDG 171
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
241-436 |
4.73e-21 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 89.23 E-value: 4.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 241 DKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQmltdFGPHGVLFLPQKPfftdgtLREQVIYplk 320
Cdd:cd00267 11 GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEIL----IDGKDIAKLPLEE------LRRRIGY--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 321 evypdsgsadderilrflelaglsnlvartegLDQqvdwnwydvLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEVE 400
Cdd:cd00267 78 --------------------------------VPQ---------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASR 116
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 10947129 401 SELYRIGQQL---GMTFISVGHRQSL-EKFHSLVLKLCGG 436
Cdd:cd00267 117 ERLLELLRELaeeGRTVIIVTHDPELaELAADRVIVLKDG 156
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
240-436 |
5.77e-21 |
|
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: 91.13 E-value: 5.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 240 SDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGsvQMLTDFGP----------HGVLFLPQKPFFTDG 309
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKG--QILIDGIDirdisrkslrSMIGVVLQDTFLFSG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 310 TLREQVIYplkevypDSGSADDERILRFLELAGLSNLVAR-TEGLDQQVDWNWyDVLSPGEMQRLSFARLFYLQPKYAVL 388
Cdd:cd03254 92 TIMENIRL-------GRPNATDEEVIEAAKEAGAHDFIMKlPNGYDTVLGENG-GNLSQGERQLLAIARAMLRDPKILIL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 10947129 389 DEATSAL---TEE-VESELYRIGQqlGMTFISVGHRQSLEKFHSLVLKLCGG 436
Cdd:cd03254 164 DEATSNIdteTEKlIQEALEKLMK--GRTSIIIAHRLSTIKNADKILVLDDG 213
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
245-393 |
1.21e-20 |
|
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: 88.09 E-value: 1.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 245 IKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQ-----MLTDFGPH---GVLFLPQKP-FFTDGTLREQV 315
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILldgqdLTDDERKSlrkEIGYVFQDPqLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 10947129 316 IYPLKEVYPDSgSADDERILRFLELAGLSNLVARTEGldqqvdwNWYDVLSPGEMQRLSFARLFYLQPKYAVLDEATS 393
Cdd:pfam00005 81 RLGLLLKGLSK-REKDARAEEALEKLGLGDLADRPVG-------ERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
242-436 |
4.63e-19 |
|
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: 85.23 E-value: 4.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 242 KPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV------------QMLTDFGPHGVLFLPQK----PF 305
Cdd:cd03255 17 VQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVrvdgtdisklseKELAAFRRRHIGFVFQSfnllPD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 306 FtdgTLREQVIYPLkEVYPDSGSADDERILRFLELAGLSNLvartegLDQQVDWnwydvLSPGEMQRLSFARLFYLQPKY 385
Cdd:cd03255 97 L---TALENVELPL-LLAGVPKKERRERAEELLERVGLGDR------LNHYPSE-----LSGGQQQRVAIARALANDPKI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 10947129 386 AVLDEATSAL----TEEVESELYRIGQQLGMTFISVGHRQSLEKFHSLVLKLCGG 436
Cdd:cd03255 162 ILADEPTGNLdsetGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDG 216
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
241-422 |
7.54e-19 |
|
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: 85.37 E-value: 7.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 241 DKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----QMLTDFGPH----GVLFlpQK-PFFTDGTL 311
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEIlldgKDITNLPPHkrpvNTVF--QNyALFPHLTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 312 REQVIYPLKeVYPDSGSADDERILRFLELAGLSNLVARTEgldqqvdwnwyDVLSPGEMQRLSFARLFYLQPKYAVLDEA 391
Cdd:cd03300 90 FENIAFGLR-LKKLPKAEIKERVAEALDLVQLEGYANRKP-----------SQLSGGQQQRVAIARALVNEPKVLLLDEP 157
|
170 180 190
....*....|....*....|....*....|....*
gi 10947129 392 TSALT----EEVESELYRIGQQLGMTFISVGHRQS 422
Cdd:cd03300 158 LGALDlklrKDMQLELKRLQKELGITFVFVTHDQE 192
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
241-395 |
8.89e-19 |
|
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: 84.45 E-value: 8.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 241 DKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV--------QMLTDFGPHgVLFLPQKPFFTDG-TL 311
Cdd:COG4133 14 ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVlwngepirDAREDYRRR-LAYLGHADGLKPElTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 312 REQVIYpLKEVYPDSGSADD-ERILRFLELAGLSNLVARTegldqqvdwnwydvLSPGEMQRLSFARLFYLQPKYAVLDE 390
Cdd:COG4133 93 RENLRF-WAALYGLRADREAiDEALEAVGLAGLADLPVRQ--------------LSAGQKRRVALARLLLSPAPLWLLDE 157
|
....*
gi 10947129 391 ATSAL 395
Cdd:COG4133 158 PFTAL 162
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
123-403 |
1.07e-18 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 88.19 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 123 SILSYVVIAIPIFSGvyGDLSPAELSTLVsknaFVCIYLISCFTQLIDLSTTLSDVAGYTHRIGQLRETlldmslksqdc 202
Cdd:TIGR02868 251 AVLGALWAGGPAVAD--GRLAPVTLAVLV----LLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVLDA----------- 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 203 eilgESEWGLDTPPGWPAAEPADTAFLLERVSISAPSsDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTST 282
Cdd:TIGR02868 314 ----AGPVAEGSAPAAGAVGLGKPTLELRDLSAGYPG-APPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPL 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 283 RGSVqMLTDFGPHG---------VLFLPQKPFFTDGTLREQVIYPLKEvypdsgsADDERILRFLELAGLSNLVART-EG 352
Cdd:TIGR02868 389 QGEV-TLDGVPVSSldqdevrrrVSVCAQDAHLFDTTVRENLRLARPD-------ATDEELWAALERVGLADWLRALpDG 460
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 10947129 353 LDQQVDWNWyDVLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEVESEL 403
Cdd:TIGR02868 461 LDTVLGEGG-ARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADEL 510
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
241-422 |
1.39e-18 |
|
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: 84.11 E-value: 1.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 241 DKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----QMLTDFGPH--GVLFLPQKP-FFTDGTLRE 313
Cdd:cd03259 12 SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEIlidgRDVTGVPPErrNIGMVFQDYaLFPHLTVAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 314 QVIYPLKEVYPDSGSAdDERILRFLELAGLSNLVARtegldqqvdwnWYDVLSPGEMQRLSFARLFYLQPKYAVLDEATS 393
Cdd:cd03259 92 NIAFGLKLRGVPKAEI-RARVRELLELVGLEGLLNR-----------YPHELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190
....*....|....*....|....*....|...
gi 10947129 394 AL----TEEVESELYRIGQQLGMTFISVGHRQS 422
Cdd:cd03259 160 ALdaklREELREELKELQRELGITTIYVTHDQE 192
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
245-419 |
2.86e-18 |
|
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: 83.54 E-value: 2.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 245 IKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM----LTDFGP--HGVLFLPQ-KPFFTDGTLREQVIY 317
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLngkdITNLPPekRDISYVPQnYALFPHMTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 318 PLKEVYPDSgSADDERILRFLELAGLSNLVARTEGldqqvdwnwydVLSPGEMQRLSFARLFYLQPKYAVLDEATSAL-- 395
Cdd:cd03299 95 GLKKRKVDK-KEIERKVLEIAEMLGIDHLLNRKPE-----------TLSGGEQQRVAIARALVVNPKILLLDEPFSALdv 162
|
170 180
....*....|....*....|....*.
gi 10947129 396 --TEEVESELYRIGQQLGMTFISVGH 419
Cdd:cd03299 163 rtKEKLREELKKIRKEFGVTVLHVTH 188
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
240-419 |
4.92e-18 |
|
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: 82.20 E-value: 4.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 240 SDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQML---TDFGPHGVLFLPQKPFF-TD--GTLRE 313
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFgkpLEKERKRIGYVPQRRSIdRDfpISVRD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 314 QV---IYPLKEVYPDSGSADDERILRFLELAGLSNLVARTegLDQqvdwnwydvLSPGEMQRLSFARLFYLQPKYAVLDE 390
Cdd:cd03235 90 VVlmgLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQ--IGE---------LSGGQQQRVLLARALVQDPDLLLLDE 158
|
170 180 190
....*....|....*....|....*....|..
gi 10947129 391 ATSALTEEVESELYRIGQQL---GMTFISVGH 419
Cdd:cd03235 159 PFAGVDPKTQEDIYELLRELrreGMTILVVTH 190
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
230-419 |
8.85e-18 |
|
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: 82.24 E-value: 8.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 230 LERVS--ISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----QMLTDFGPHGVLFLPQK 303
Cdd:cd03258 4 LKNVSkvFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVlvdgTDLTLLSGKELRKARRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 304 --------PFFTDGTLREQVIYPLkEVYPDSGSADDERILRFLELAGLSNlvaRTEGLDQQvdwnwydvLSPGEMQRLSF 375
Cdd:cd03258 84 igmifqhfNLLSSRTVFENVALPL-EIAGVPKAEIEERVLELLELVGLED---KADAYPAQ--------LSGGQKQRVGI 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 10947129 376 ARLFYLQPKYAVLDEATSAL----TEEVESELYRIGQQLGMTFISVGH 419
Cdd:cd03258 152 ARALANNPKVLLCDEATSALdpetTQSILALLRDINRELGLTIVLITH 199
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
241-419 |
1.15e-17 |
|
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: 81.84 E-value: 1.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 241 DKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTST-----------RGSVQMLTDFGPH------GVLFlpQK 303
Cdd:cd03260 12 DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdegevllDGKDIYDLDVDVLelrrrvGMVF--QK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 304 PFFTDGTLREQVIYPLKEVYPDSGSADDERILRFLELAGLSNLVA-RTEGLDqqvdwnwydvLSPGEMQRLSFARLFYLQ 382
Cdd:cd03260 90 PNPFPGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKdRLHALG----------LSGGQQQRLCLARALANE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 10947129 383 PKYAVLDEATSAL----TEEVESELYRIGQQlgMTFISVGH 419
Cdd:cd03260 160 PEVLLLDEPTSALdpisTAKIEELIAELKKE--YTIVIVTH 198
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
230-422 |
1.48e-17 |
|
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: 81.51 E-value: 1.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 230 LERVSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM----LTDFGPHG----VLFLP 301
Cdd:cd03251 3 FKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIdghdVRDYTLASlrrqIGLVS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 302 QKPFFTDGTLREQVIYPLKEvypdsgsADDERILRFLELAGLSNLVART-EGLDQQVDWNWYDvLSPGEMQRLSFARLFY 380
Cdd:cd03251 83 QDVFLFNDTVAENIAYGRPG-------ATREEVEEAARAANAHEFIMELpEGYDTVIGERGVK-LSGGQRQRIAIARALL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 10947129 381 LQPKYAVLDEATSALTEEVESELYRIGQQL--GMTFISVGHRQS 422
Cdd:cd03251 155 KDPPILILDEATSALDTESERLVQAALERLmkNRTTFVIAHRLS 198
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
121-422 |
2.40e-17 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 84.38 E-value: 2.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 121 LGSILSYVVIAIPIFSGVYGDLSPAELSTLvsknafvciylISCFTQLIDLSTTLSDVAGYTHRIGQLRETLldmslksq 200
Cdd:TIGR02203 247 IASLALAVVLFIALFQAQAGSLTAGDFTAF-----------ITAMIALIRPLKSLTNVNAPMQRGLAAAESL-------- 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 201 dCEILgesewglDTPP----GWPAAEPADTAFLLERVSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLG 276
Cdd:TIGR02203 308 -FTLL-------DSPPekdtGTRAIERARGDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIP 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 277 GLWTSTRGSVQM---------LTDFGPHgVLFLPQKPFFTDGTLREQViyplkeVYPDSGSADDERILRFLELAGLSNLV 347
Cdd:TIGR02203 380 RFYEPDSGQILLdghdladytLASLRRQ-VALVSQDVVLFNDTIANNI------AYGRTEQADRAEIERALAAAYAQDFV 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 348 ART-EGLDQQVDWNWyDVLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEE----VESELYRIGQqlGMTFISVGHRQS 422
Cdd:TIGR02203 453 DKLpLGLDTPIGENG-VLLSGGQRQRLAIARALLKDAPILILDEATSALDNEserlVQAALERLMQ--GRTTLVIAHRLS 529
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
231-420 |
1.04e-16 |
|
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: 78.69 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 231 ERVSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM----LTDFGPHgVL-----FLP 301
Cdd:cd03244 6 KNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIdgvdISKIGLH-DLrsrisIIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 302 QKPFFTDGTLREQvIYPLKEvypdsgsADDERILRFLELAGLSNLV-ARTEGLDQQVDWNWyDVLSPGEMQRLSFARLFY 380
Cdd:cd03244 85 QDPVLFSGTIRSN-LDPFGE-------YSDEELWQALERVGLKEFVeSLPGGLDTVVEEGG-ENLSVGQRQLLCLARALL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 10947129 381 LQPKYAVLDEATSAlteeVESELYRIGQQL------GMTFISVGHR 420
Cdd:cd03244 156 RKSKILVLDEATAS----VDPETDALIQKTireafkDCTVLTIAHR 197
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
242-426 |
3.04e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 77.31 E-value: 3.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 242 KPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSvqmltdfgphGVLFLPQKPFFTDGTLREQViyplke 321
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVA----------GCVDVPDNQFGREASLIDAI------ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 322 vyPDSGSADDerILRFLELAGLS---NLVARtegldqqvdwnwYDVLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEE 398
Cdd:COG2401 107 --GRKGDFKD--AVELLNAVGLSdavLWLRR------------FKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
170 180 190
....*....|....*....|....*....|..
gi 10947129 399 VESELYRIGQQL----GMTFISVGHRQSLEKF 426
Cdd:COG2401 171 TAKRVARNLQKLarraGITLVVATHHYDVIDD 202
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
241-419 |
3.22e-16 |
|
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: 77.54 E-value: 3.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 241 DKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM----LTDFGPH---------GVLFlpQKP-FF 306
Cdd:cd03261 12 GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIdgedISGLSEAelyrlrrrmGMLF--QSGaLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 307 TDGTLREQVIYPLKEVYPDSGSADDERILRFLELAGLSnlvartegldQQVDwnwydvLSPGE----MQ-RLSFARLFYL 381
Cdd:cd03261 90 DSLTVFENVAFPLREHTRLSEEEIREIVLEKLEAVGLR----------GAED------LYPAElsggMKkRVALARALAL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 10947129 382 QPKYAVLDEATSAL----TEEVESELYRIGQQLGMTFISVGH 419
Cdd:cd03261 154 DPELLLYDEPTAGLdpiaSGVIDDLIRSLKKELGLTSIMVTH 195
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
233-432 |
3.39e-16 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 80.92 E-value: 3.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 233 VSISAPS-SDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----QMLTDFGPH----GVLFLPQK 303
Cdd:TIGR00958 484 VSFSYPNrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVlldgVPLVQYDHHylhrQVALVGQE 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 304 PFFTDGTLREQVIYPLKevypdsgSADDERILRFLELAGLSNLVAR-TEGLDQQVDWNWyDVLSPGEMQRLSFARLFYLQ 382
Cdd:TIGR00958 564 PVLFSGSVRENIAYGLT-------DTPDEEIMAAAKAANAHDFIMEfPNGYDTEVGEKG-SQLSGGQKQRIAIARALVRK 635
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 10947129 383 PKYAVLDEATSALTEEVESELYRIGQQLGMTFISVGHRQSL-EKFHS-LVLK 432
Cdd:TIGR00958 636 PRVLILDEATSALDAECEQLLQESRSRASRTVLLIAHRLSTvERADQiLVLK 687
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
221-421 |
4.02e-16 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 79.61 E-value: 4.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 221 AEPADTAFLLERVSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----QMLTDFGPHg 296
Cdd:PRK09452 6 KQPSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRImldgQDITHVPAE- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 297 vlflpQKP---------FFTDGTLREQVIYPLK-------EVYPdsgsaddeRILRFLELAGLSNLVARTEgldQQvdwn 360
Cdd:PRK09452 85 -----NRHvntvfqsyaLFPHMTVFENVAFGLRmqktpaaEITP--------RVMEALRMVQLEEFAQRKP---HQ---- 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 10947129 361 wydvLSPGEMQRLSFARLFYLQPKYAVLDEATSALT----EEVESELYRIGQQLGMTFISVGHRQ 421
Cdd:PRK09452 145 ----LSGGQQQRVAIARAVVNKPKVLLLDESLSALDyklrKQMQNELKALQRKLGITFVFVTHDQ 205
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
241-422 |
1.77e-15 |
|
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: 75.60 E-value: 1.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 241 DKPLI-KDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVqmLTDfGPHGVLFLPQkpfftdgTLREQVIYPL 319
Cdd:cd03252 13 DGPVIlDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRV--LVD-GHDLALADPA-------WLRRQVGVVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 320 KEVYPDSGSADD-----------ERILRFLELAGLSNLVART-EGLDQQVDWNWYDvLSPGEMQRLSFARLFYLQPKYAV 387
Cdd:cd03252 83 QENVLFNRSIRDnialadpgmsmERVIEAAKLAGAHDFISELpEGYDTIVGEQGAG-LSGGQRQRIAIARALIHNPRILI 161
|
170 180 190
....*....|....*....|....*....|....*..
gi 10947129 388 LDEATSALTEEVESELYRIGQQL--GMTFISVGHRQS 422
Cdd:cd03252 162 FDEATSALDYESEHAIMRNMHDIcaGRTVIIIAHRLS 198
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
232-419 |
1.89e-15 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 75.23 E-value: 1.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 232 RVSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV------------QMLTDFGpHGVLF 299
Cdd:cd03257 8 SVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIifdgkdllklsrRLRKIRR-KEIQM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 300 LPQKPF------FTdgtLREQVIYPLKEVYPDSGSAD-DERILRFLELAGLSNLVAR---TEgldqqvdwnwydvLSPGE 369
Cdd:cd03257 87 VFQDPMsslnprMT---IGEQIAEPLRIHGKLSKKEArKEAVLLLLVGVGLPEEVLNrypHE-------------LSGGQ 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 10947129 370 MQRLSFARLFYLQPKYAVLDEATSAL---TE-EVESELYRIGQQLGMTFISVGH 419
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALdvsVQaQILDLLKKLQEELGLTLLFITH 204
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
230-419 |
2.89e-15 |
|
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: 74.43 E-value: 2.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 230 LERVSISAPSSDKPL--IKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM----LTDFGPH-GVLF--- 299
Cdd:cd03293 3 VRNVSKTYGGGGGAVtaLEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVdgepVTGPGPDrGYVFqqd 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 300 --LPQKpfftdgTLREQVIYPLKEVYPDSGSAdDERILRFLELAGLSNLVARtegldqqvdwnWYDVLSPGEMQRLSFAR 377
Cdd:cd03293 83 alLPWL------TVLDNVALGLELQGVPKAEA-RERAEELLELVGLSGFENA-----------YPHQLSGGMRQRVALAR 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 10947129 378 LFYLQPKYAVLDEATSAL---T-EEVESELYRIGQQLGMTFISVGH 419
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALdalTrEQLQEELLDIWRETGKTVLLVTH 190
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
241-421 |
4.78e-15 |
|
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: 73.83 E-value: 4.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 241 DKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----QMLTDFGPH----GVLF-----LPQKpfft 307
Cdd:cd03301 12 NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIyiggRDVTDLPPKdrdiAMVFqnyalYPHM---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 308 dgTLREQVIYPLKeVYPDSGSADDERILRFLELAGLSNLvartegLDQQVdwnwyDVLSPGEMQRLSFARLFYLQPKYAV 387
Cdd:cd03301 88 --TVYDNIAFGLK-LRKVPKDEIDERVREVAELLQIEHL------LDRKP-----KQLSGGQRQRVALGRAIVREPKVFL 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 10947129 388 LDEATSALT----EEVESELYRIGQQLGMTFISVGHRQ 421
Cdd:cd03301 154 MDEPLSNLDaklrVQMRAELKRLQQRLGTTTIYVTHDQ 191
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
230-420 |
5.10e-15 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 76.87 E-value: 5.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 230 LERVSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTST---RGSV----QMLTDFGPHG----VL 298
Cdd:COG1123 7 VRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVlldgRDLLELSEALrgrrIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 299 FLPQKPF--FTDGTLREQVIYPLkEVYPDSGSADDERILRFLELAGLSNLVARtegldqqvdwnWYDVLSPGEMQRLSFA 376
Cdd:COG1123 87 MVFQDPMtqLNPVTVGDQIAEAL-ENLGLSRAEARARVLELLEAVGLERRLDR-----------YPHQLSGGQRQRVAIA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 10947129 377 RLFYLQPKYAVLDEATSAL----TEEVESELYRIGQQLGMTFISVGHR 420
Cdd:COG1123 155 MALALDPDLLIADEPTTALdvttQAEILDLLRELQRERGTTVLLITHD 202
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
241-422 |
7.45e-15 |
|
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: 73.80 E-value: 7.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 241 DKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM---------LTDFGPH-GVLflPQK-PFFTDg 309
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIdgqdirevtLDSLRRAiGVV--PQDtVLFND- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 310 TLREQVIYplkevypdsG--SADDERILRFLELAGLSNLVAR-TEGLDQQV-DWNWYdvLSPGEMQRLSFARLFYLQPKY 385
Cdd:cd03253 90 TIGYNIRY---------GrpDATDEEVIEAAKAAQIHDKIMRfPDGYDTIVgERGLK--LSGGEKQRVAIARAILKNPPI 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 10947129 386 AVLDEATSALTEEVESELYRIGQQL--GMTFISVGHRQS 422
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAALRDVskGRTTIVIAHRLS 197
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
225-419 |
7.67e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 74.44 E-value: 7.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 225 DTAFLLERVSISAPssDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----QMLTDFGPHG---- 296
Cdd:PRK10575 9 DTTFALRNVSFRVP--GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEIlldaQPLESWSSKAfark 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 297 VLFLPQKPFFTDG-TLREQVI---YPLKEVYPDSGSADDERILRFLELAGLSNLVARTegldqqvdwnwYDVLSPGEMQR 372
Cdd:PRK10575 87 VAYLPQQLPAAEGmTVRELVAigrYPWHGALGRFGAADREKVEEAISLVGLKPLAHRL-----------VDSLSGGERQR 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 10947129 373 LSFARLFYLQPKYAVLDEATSAL----TEEVESELYRIGQQLGMTFISVGH 419
Cdd:PRK10575 156 AWIAMLVAQDSRCLLLDEPTSALdiahQVDVLALVHRLSQERGLTVIAVLH 206
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
212-416 |
1.05e-14 |
|
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: 76.10 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 212 LDTPPGWPAAEPADTAFLLE--RVSIS---APSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV 286
Cdd:COG1123 243 LGAARGRAAPAAAAAEPLLEvrNLSKRypvRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSI 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 287 QM------------LTDFGPH-GVLFlpQKP---FFTDGTLREQVIYPLKEVYPDSGSADDERILRFLELAGLSNLVArt 350
Cdd:COG1123 323 LFdgkdltklsrrsLRELRRRvQMVF--QDPyssLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPDLA-- 398
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 10947129 351 egldqqvdwNWY-DVLSPGEMQRLSFARLFYLQPKYAVLDEATSAL----TEEVESELYRIGQQLGMT--FIS 416
Cdd:COG1123 399 ---------DRYpHELSGGQRQRVAIARALALEPKLLILDEPTSALdvsvQAQILNLLRDLQRELGLTylFIS 462
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
233-426 |
1.17e-14 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 71.96 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 233 VSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM-------LTDFGPHGVLFLPQKPF 305
Cdd:cd03247 6 VSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLdgvpvsdLEKALSSLISVLNQRPY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 306 FTDGTLREqviyplkevypdsgsadderilrflelaglsNLVARtegldqqvdwnwydvLSPGEMQRLSFARLFYLQPKY 385
Cdd:cd03247 86 LFDTTLRN-------------------------------NLGRR---------------FSGGERQRLALARILLQDAPI 119
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 10947129 386 AVLDEATSALTEEVESELYR-IGQQL-GMTFISVGHR-QSLEKF 426
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSlIFEVLkDKTLIWITHHlTGIEHM 163
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
233-422 |
1.24e-14 |
|
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: 72.96 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 233 VSISAPS-SDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----QMLTDFGPHGVL----FLPQK 303
Cdd:cd03249 6 VSFRYPSrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEIlldgVDIRDLNLRWLRsqigLVSQE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 304 PFFTDGTLREQVIYPLKevypdsgSADDERILRFLELAGLSNLVAR-TEGLDQQVDWNwYDVLSPGEMQRLSFARLFYLQ 382
Cdd:cd03249 86 PVLFDGTIAENIRYGKP-------DATDEEVEEAAKKANIHDFIMSlPDGYDTLVGER-GSQLSGGQKQRIAIARALLRN 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 10947129 383 PKYAVLDEATSALTEEVESELYRIGQQL--GMTFISVGHRQS 422
Cdd:cd03249 158 PKILLLDEATSALDAESEKLVQEALDRAmkGRTTIVIAHRLS 199
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
230-395 |
2.74e-14 |
|
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: 71.52 E-value: 2.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 230 LERVSISAPSSDKpLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQMLTDFGPHGVL-----FLPQKP 304
Cdd:cd03226 2 IENISFSYKKGTE-ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERrksigYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 305 ---FFTDgTLREQVIYPLKEvyPDSGSADDERILRFLELAGLsnlvartegldqqVDWNWYDvLSPGEMQRLSFARLFYL 381
Cdd:cd03226 81 dyqLFTD-SVREELLLGLKE--LDAGNEQAETVLKDLDLYAL-------------KERHPLS-LSGGQKQRLAIAAALLS 143
|
170
....*....|....
gi 10947129 382 QPKYAVLDEATSAL 395
Cdd:cd03226 144 GKDLLIFDEPTSGL 157
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
216-431 |
4.10e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 74.48 E-value: 4.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 216 PGWPAAEPADTAFLLERVSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM----LTD 291
Cdd:PRK11160 327 PTTSTAAADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLngqpIAD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 292 FGP----HGVLFLPQKPFFTDGTLREQviypLKEVYPDsgsADDERILRFLELAGLSNLVARTEGLDQqvdwnWYD---- 363
Cdd:PRK11160 407 YSEaalrQAISVVSQRVHLFSATLRDN----LLLAAPN---ASDEALIEVLQQVGLEKLLEDDKGLNA-----WLGeggr 474
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 10947129 364 VLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEVESELYRIGQQL--GMTFISVGHR-QSLEKFHSLVL 431
Cdd:PRK11160 475 QLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHaqNKTVLMITHRlTGLEQFDRICV 545
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
241-422 |
6.00e-14 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 72.82 E-value: 6.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 241 DKPLIKDLSLKISEGQ--SLLitGNTGTGKTSLLRVLGGLWTSTRGSV----QMLTDFGPH----GVLFlpQK----PFF 306
Cdd:COG3842 17 DVTALDDVSLSIEPGEfvALL--GPSGCGKTTLLRMIAGFETPDSGRIlldgRDVTGLPPEkrnvGMVF--QDyalfPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 307 tdgTLREQVIYPLKeVYPDSGSADDERILRFLELAGLSNLVAR--TEgldqqvdwnwydvLSPGEMQRLSFARLFYLQPK 384
Cdd:COG3842 93 ---TVAENVAFGLR-MRGVPKAEIRARVAELLELVGLEGLADRypHQ-------------LSGGQQQRVALARALAPEPR 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 10947129 385 YAVLDEATSAL----TEEVESELYRIGQQLGMTFISVGHRQS 422
Cdd:COG3842 156 VLLLDEPLSALdaklREEMREELRRLQRELGITFIYVTHDQE 197
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
236-431 |
1.15e-13 |
|
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: 69.42 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 236 SAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQMltdfgPHGVLFLPQKPFFTDGTLREQV 315
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV-----PGSIAYVSQEPWIQNGTIRENI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 316 I--YPLkevypdsgsaDDERILRFLELAGLSNLVARTEGLDQQVdwnwydV------LSPGEMQRLSFARLFYLQPKYAV 387
Cdd:cd03250 87 LfgKPF----------DEERYEKVIKACALEPDLEILPDGDLTE------IgekginLSGGQKQRISLARAVYSDADIYL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 10947129 388 LDEATSALTEEVESELYR--IGQQL--GMTFISVGHR-QSLEKFHSLVL 431
Cdd:cd03250 151 LDDPLSAVDAHVGRHIFEncILGLLlnNKTRILVTHQlQLLPHADQIVV 199
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
241-419 |
1.69e-13 |
|
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: 68.37 E-value: 1.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 241 DKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQML-TDFGPHGVLFLPQKP----FFTDGTLreqv 315
Cdd:cd03229 12 QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDgEDLTDLEDELPPLRRrigmVFQDFAL---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 316 iYPLKEVYpdsgsadderilrflelaglSNLVARtegldqqvdwnwydvLSPGEMQRLSFARLFYLQPKYAVLDEATSAL 395
Cdd:cd03229 88 -FPHLTVL--------------------ENIALG---------------LSGGQQQRVALARALAMDPDVLLLDEPTSAL 131
|
170 180
....*....|....*....|....*...
gi 10947129 396 ----TEEVESELYRIGQQLGMTFISVGH 419
Cdd:cd03229 132 dpitRREVRALLKSLQAQLGITVVLVTH 159
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
230-419 |
2.11e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 70.04 E-value: 2.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 230 LERVSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQMltdFGPH-------------G 296
Cdd:PRK13635 8 VEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITV---GGMVlseetvwdvrrqvG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 297 VLFlpQKP--FFTDGTLREQVIYPLKevypDSGSADDERILRFLELAglsNLVARTEGLDQQVDwnwydVLSPGEMQRLS 374
Cdd:PRK13635 85 MVF--QNPdnQFVGATVQDDVAFGLE----NIGVPREEMVERVDQAL---RQVGMEDFLNREPH-----RLSGGQKQRVA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 10947129 375 FARLFYLQPKYAVLDEATSALT----EEVESELYRIGQQLGMTFISVGH 419
Cdd:PRK13635 151 IAGVLALQPDIIILDEATSMLDprgrREVLETVRQLKEQKGITVLSITH 199
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
243-422 |
8.12e-13 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 67.75 E-value: 8.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 243 PLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----QMLTDFGPH--GVLFLPQK-PFFTDGTLREQV 315
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTIlfggEDATDVPVQerNVGFVFQHyALFRHMTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 316 IYPLKeVYPDSGSAD----DERILRFLELAGLSNLVARtegldqqvdwnWYDVLSPGEMQRLSFARLFYLQPKYAVLDEA 391
Cdd:cd03296 96 AFGLR-VKPRSERPPeaeiRAKVHELLKLVQLDWLADR-----------YPAQLSGGQRQRVALARALAVEPKVLLLDEP 163
|
170 180 190
....*....|....*....|....*....|....*
gi 10947129 392 TSALTEEVESELY----RIGQQLGMTFISVGHRQS 422
Cdd:cd03296 164 FGALDAKVRKELRrwlrRLHDELHVTTVFVTHDQE 198
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
241-419 |
9.45e-13 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 67.81 E-value: 9.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 241 DKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGS--VQMLTDFGPH----------GVLFlPQKPFFTD 308
Cdd:PRK09493 13 PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDliVDGLKVNDPKvderlirqeaGMVF-QQFYLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 309 GTLREQVIYPLKEVYpDSGSADDERILRflELAGLSNLVARTEGLDQQvdwnwydvLSPGEMQRLSFARLFYLQPKYAVL 388
Cdd:PRK09493 92 LTALENVMFGPLRVR-GASKEEAEKQAR--ELLAKVGLAERAHHYPSE--------LSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190
....*....|....*....|....*....|....
gi 10947129 389 DEATSALTEEVESELYRIGQQL---GMTFISVGH 419
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLaeeGMTMVIVTH 194
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
230-419 |
1.08e-12 |
|
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: 66.30 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 230 LERVSISAPssDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQMltdfgphgvlflpqkpfftDG 309
Cdd:cd03214 2 VENLSVGYG--GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILL-------------------DG 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 310 TLREQviYPLKEVypdsgsAddeRILRF----LELAGLSNLVARTegldqqvdwnwYDVLSPGEMQRLSFARLFYLQPKY 385
Cdd:cd03214 61 KDLAS--LSPKEL------A---RKIAYvpqaLELLGLAHLADRP-----------FNELSGGERQRVLLARALAQEPPI 118
|
170 180 190
....*....|....*....|....*....|....*...
gi 10947129 386 AVLDEATSAL----TEEVESELYRIGQQLGMTFISVGH 419
Cdd:cd03214 119 LLLDEPTSHLdiahQIELLELLRRLARERGKTVVMVLH 156
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
233-437 |
1.17e-12 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 67.79 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 233 VSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGL----------------------WTSTRGSVQMLT 290
Cdd:PRK10419 16 GGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLespsqgnvswrgeplaklnraqRKAFRRDIQMVF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 291 DFGPHGVLflPQKpfftdgTLREQVIYPLKEVYPDSGSADDERILRFLELAGLSNLVArtEGLDQQvdwnwydvLSPGEM 370
Cdd:PRK10419 96 QDSISAVN--PRK------TVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVL--DKRPPQ--------LSGGQL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 10947129 371 QRLSFARLFYLQPKYAVLDEATS----ALTEEVESELYRIGQQLGMTFISVGHRQSL-EKFHSLVLKLCGGG 437
Cdd:PRK10419 158 QRVCLARALAVEPKLLILDEAVSnldlVLQAGVIRLLKKLQQQFGTACLFITHDLRLvERFCQRVMVMDNGQ 229
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
246-419 |
1.45e-12 |
|
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: 66.55 E-value: 1.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 246 KDLSLKIS---EGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----------QMLTDFGPH----GVLFlPQKPFFTD 308
Cdd:cd03297 11 PDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIvlngtvlfdsRKKINLPPQqrkiGLVF-QQYALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 309 GTLREQVIYPLKEVypdSGSADDERILRFLELAGLSNLVARteGLDQqvdwnwydvLSPGEMQRLSFARLFYLQPKYAVL 388
Cdd:cd03297 90 LNVRENLAFGLKRK---RNREDRISVDELLDLLGLDHLLNR--YPAQ---------LSGGEKQRVALARALAAQPELLLL 155
|
170 180 190
....*....|....*....|....*....|....*
gi 10947129 389 DEATSAL----TEEVESELYRIGQQLGMTFISVGH 419
Cdd:cd03297 156 DEPFSALdralRLQLLPELKQIKKNLNIPVIFVTH 190
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
241-419 |
1.54e-12 |
|
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: 66.93 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 241 DKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----QMLTDFGPH---------GVLF----Lpqk 303
Cdd:COG1127 17 DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEIlvdgQDITGLSEKelyelrrriGMLFqggaL--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 304 pfFTDGTLREQVIYPLKEVYPDSGSADDERILRFLELAGLSNlvARTegldqqvdwnwydvLSPGE----MQ-RLSFARL 378
Cdd:COG1127 94 --FDSLTVFENVAFPLREHTDLSEAEIRELVLEKLELVGLPG--AAD--------------KMPSElsggMRkRVALARA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 10947129 379 FYLQPKYAVLDEATSAL----TEEVESELYRIGQQLGMTFISVGH 419
Cdd:COG1127 156 LALDPEILLYDEPTAGLdpitSAVIDELIRELRDELGLTSVVVTH 200
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
243-425 |
2.14e-12 |
|
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: 69.00 E-value: 2.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 243 PLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM----LTDFGPHG----VLFLPQKPFFTDGTLREQ 314
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLngfsLKDIDRHTlrqfINYLPQEPYIFSGSILEN 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 315 VIYPLKEvypdsgSADDERILRFLELAGLSNLVAR-TEGLDQQVDWNWYDvLSPGEMQRLSFARLFYLQPKYAVLDEATS 393
Cdd:TIGR01193 568 LLLGAKE------NVSQDEIWAACEIAEIKDDIENmPLGYQTELSEEGSS-ISGGQKQRIALARALLTDSKVLILDESTS 640
|
170 180 190
....*....|....*....|....*....|....*
gi 10947129 394 ALTEEVESELyrIGQQLGM---TFISVGHRQSLEK 425
Cdd:TIGR01193 641 NLDTITEKKI--VNNLLNLqdkTIIFVAHRLSVAK 673
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
229-419 |
3.25e-12 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 65.89 E-value: 3.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 229 LLERVSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----QMLTDFGP----HGVLFL 300
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLlfegEDISTLKPeiyrQQVSYC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 301 PQKPFFTDGTLREQVIYP--LKEVYPdsgsaDDERILRFLELAGLSNlvartEGLDQQVdwnwyDVLSPGEMQRLSFARL 378
Cdd:PRK10247 87 AQTPTLFGDTVYDNLIFPwqIRNQQP-----DPAIFLDDLERFALPD-----TILTKNI-----AELSGGEKQRISLIRN 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 10947129 379 FYLQPKYAVLDEATSALTEE----VESELYRIGQQLGMTFISVGH 419
Cdd:PRK10247 152 LQFMPKVLLLDEITSALDESnkhnVNEIIHRYVREQNIAVLWVTH 196
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
241-419 |
9.86e-12 |
|
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: 64.09 E-value: 9.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 241 DKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----QMLTDFGPH--------GVLFlPQKPFFTD 308
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIiidgLKLTDDKKNinelrqkvGMVF-QQFNLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 309 GTLREQVIYPLKEVYPDSGSADDERILRFLELAGLSnlvarteglDQQvdwNWY-DVLSPGEMQRLSFARLFYLQPKYAV 387
Cdd:cd03262 91 LTVLENITLAPIKVKGMSKAEAEERALELLEKVGLA---------DKA---DAYpAQLSGGQQQRVAIARALAMNPKVML 158
|
170 180 190
....*....|....*....|....*....|....*
gi 10947129 388 LDEATSALTEEVESELYRIGQQL---GMTFISVGH 419
Cdd:cd03262 159 FDEPTSALDPELVGEVLDVMKDLaeeGMTMVVVTH 193
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
238-419 |
1.03e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 65.14 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 238 PSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----QMLT-----DFGPH-GVLFlpQKP--F 305
Cdd:PRK13650 16 EDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIiidgDLLTeenvwDIRHKiGMVF--QNPdnQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 306 FTDGTLREQVIY-------PLKEVypdsgsadDERILRFLELAGLSNLVARTEGLdqqvdwnwydvLSPGEMQRLSFARL 378
Cdd:PRK13650 94 FVGATVEDDVAFglenkgiPHEEM--------KERVNEALELVGMQDFKEREPAR-----------LSGGQKQRVAIAGA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 10947129 379 FYLQPKYAVLDEATSALTEEVESELYR----IGQQLGMTFISVGH 419
Cdd:PRK13650 155 VAMRPKIIILDEATSMLDPEGRLELIKtikgIRDDYQMTVISITH 199
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
245-434 |
1.75e-11 |
|
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: 64.00 E-value: 1.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 245 IKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----QMLTDFGPH-----GVL--FlpQKP-FFTDGTLR 312
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVlfdgEDITGLPPHeiarlGIGrtF--QIPrLFPELTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 313 EQVI---------YPLKEVYPDSGSADDERILRFLELAGLSNLVARTEGLdqqvdwnwydvLSPGEMQRLSFARLFYLQP 383
Cdd:cd03219 94 ENVMvaaqartgsGLLLARARREEREARERAEELLERVGLADLADRPAGE-----------LSYGQQRRLEIARALATDP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 10947129 384 KYAVLDEATSALT-EEVESELYRIGQ--QLGMTFISVGHRQslekfhSLVLKLC 434
Cdd:cd03219 163 KLLLLDEPAAGLNpEETEELAELIRElrERGITVLLVEHDM------DVVMSLA 210
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
242-395 |
1.87e-11 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 64.02 E-value: 1.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 242 KPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM----LTDFGPH------GVlfLPQK-----PFf 306
Cdd:PRK13548 15 RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLngrpLADWSPAelarrrAV--LPQHsslsfPF- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 307 tdgTLREQV---IYPLkevyPDSGSADDERILRFLELAGLSNLVARTegldqqvdwnwYDVLSPGEMQRLSFAR-LFYL- 381
Cdd:PRK13548 92 ---TVEEVVamgRAPH----GLSRAEDDALVAAALAQVDLAHLAGRD-----------YPQLSGGEQQRVQLARvLAQLw 153
|
170
....*....|....*...
gi 10947129 382 ----QPKYAVLDEATSAL 395
Cdd:PRK13548 154 epdgPPRWLLLDEPTSAL 171
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
230-419 |
3.39e-11 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 62.97 E-value: 3.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 230 LERVSISAPSSDKPLiKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV--------------------QML 289
Cdd:cd03256 3 VENLSKTYPNGKKAL-KDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVlidgtdinklkgkalrqlrrQIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 290 TDFGPHG----------VL--FLPQKPFFtdgtlreQVIYPLkevYPDsgsADDERILRFLELAGLSNLV-ARTegldqq 356
Cdd:cd03256 82 MIFQQFNlierlsvlenVLsgRLGRRSTW-------RSLFGL---FPK---EEKQRALAALERVGLLDKAyQRA------ 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 10947129 357 vdwnwyDVLSPGEMQRLSFARLFYLQPKYAVLDEATSAL----TEEVESELYRIGQQLGMTFISVGH 419
Cdd:cd03256 143 ------DQLSGGQQQRVAIARALMQQPKLILADEPVASLdpasSRQVMDLLKRINREEGITVIVSLH 203
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
230-392 |
5.08e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 64.32 E-value: 5.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 230 LERVSISAPssDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQMltdfgPHG--VLFLPQKPFFT 307
Cdd:COG0488 1 LENLSKSFG--GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI-----PKGlrIGYLPQEPPLD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 308 DG-TLREQVIYPLKEVY------------PDSGSADDERIL----RFLELAG----------LSNLVARTEGLDQQVdwn 360
Cdd:COG0488 74 DDlTVLDTVLDGDAELRaleaeleeleakLAEPDEDLERLAelqeEFEALGGweaearaeeiLSGLGFPEEDLDRPV--- 150
|
170 180 190
....*....|....*....|....*....|..
gi 10947129 361 wyDVLSPGEMQRLSFARLFYLQPKYAVLDEAT 392
Cdd:COG0488 151 --SELSGGWRRRVALARALLSEPDLLLLDEPT 180
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
241-422 |
6.50e-11 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 64.46 E-value: 6.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 241 DKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----QMLTDFGPH------GVLflPQKP-FFTDg 309
Cdd:COG5265 370 ERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRIlidgQDIRDVTQAslraaiGIV--PQDTvLFND- 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 310 TLREQVIYPLkevyPDsgsADDERILRFLELAGLSNLVART-EGLDQQVdwnwydvLSPGEMQRLSFARLFYLQPKYAVL 388
Cdd:COG5265 447 TIAYNIAYGR----PD---ASEEEVEAAARAAQIHDFIESLpDGYDTRVger-glkLSGGEKQRVAIARTLLKNPPILIF 518
|
170 180 190
....*....|....*....|....*....|....*...
gi 10947129 389 DEATSAL---TE-EVESELYRIGQqlGMTFISVGHRQS 422
Cdd:COG5265 519 DEATSALdsrTErAIQAALREVAR--GRTTLVIAHRLS 554
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
244-401 |
7.12e-11 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 64.58 E-value: 7.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 244 LIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM----LTDFGPHGVLF----LPQKPFFTDGTLREQv 315
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIdglnIAKIGLHDLRFkitiIPQDPVLFSGSLRMN- 1379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 316 IYPLkevypdsGSADDERILRFLELAGLSNLV-ARTEGLDQQVDWNWYDvLSPGEMQRLSFARLFYLQPKYAVLDEATSA 394
Cdd:TIGR00957 1380 LDPF-------SQYSDEEVWWALELAHLKTFVsALPDKLDHECAEGGEN-LSVGQRQLVCLARALLRKTKILVLDEATAA 1451
|
....*..
gi 10947129 395 LTEEVES 401
Cdd:TIGR00957 1452 VDLETDN 1458
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
247-421 |
1.66e-10 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 62.41 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 247 DLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQMltdfgpHG------------VLFLPQK-PFFTDGTLRE 313
Cdd:PRK10851 20 DISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRF------HGtdvsrlhardrkVGFVFQHyALFRHMTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 314 QVIYPLKeVYP----DSGSADDERILRFLELAGLSNLVARtegldqqvdwnWYDVLSPGEMQRLSFARLFYLQPKYAVLD 389
Cdd:PRK10851 94 NIAFGLT-VLPrrerPNAAAIKAKVTQLLEMVQLAHLADR-----------YPAQLSGGQKQRVALARALAVEPQILLLD 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 10947129 390 EATSALTEEVESELYR----IGQQLGMTFISVGHRQ 421
Cdd:PRK10851 162 EPFGALDAQVRKELRRwlrqLHEELKFTSVFVTHDQ 197
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
219-419 |
1.66e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 61.23 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 219 PAAEPADTAFLLERVSISApsSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGsvQMLTDFGPHGVL 298
Cdd:PRK11247 4 TARLNQGTPLLLNAVSKRY--GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAG--ELLAGTAPLAEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 299 FLPQKPFFTDGTLreqviYPLKEVYPDSG---SAD-DERILRFLELAGLSNLVArtegldqqvdwNWYDVLSPGEMQRLS 374
Cdd:PRK11247 80 REDTRLMFQDARL-----LPWKKVIDNVGlglKGQwRDAALQALAAVGLADRAN-----------EWPAALSGGQKQRVA 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 10947129 375 FARLFYLQPKYAVLDE---ATSALTE-EVESELYRIGQQLGMTFISVGH 419
Cdd:PRK11247 144 LARALIHRPGLLLLDEplgALDALTRiEMQDLIESLWQQHGFTVLLVTH 192
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
231-430 |
1.67e-10 |
|
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: 60.95 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 231 ERVSISAPS-SDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGsvQMLTDFGP---------HGVLFL 300
Cdd:cd03248 15 QNVTFAYPTrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGG--QVLLDGKPisqyehkylHSKVSL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 301 -PQKPFFTDGTLREQVIYPLkevypdsGSADDERILRFLELAGLSNLVARTE-GLDQQVDWNWyDVLSPGEMQRLSFARL 378
Cdd:cd03248 93 vGQEPVLFARSLQDNIAYGL-------QSCSFECVKEAAQKAHAHSFISELAsGYDTEVGEKG-SQLSGGQKQRVAIARA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 10947129 379 FYLQPKYAVLDEATSALteEVESELyRIGQQL-----GMTFISVGHR-QSLEKFHSLV 430
Cdd:cd03248 165 LIRNPQVLILDEATSAL--DAESEQ-QVQQALydwpeRRTVLVIAHRlSTVERADQIL 219
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
126-404 |
2.77e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 62.69 E-value: 2.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 126 SYVVIAIPIFS-----GVY----GDLSPAElstlvsknAFVCIYLISCF-TQLIDLSTTLSDVAGYTHRIGQLRETLLdm 195
Cdd:PLN03232 527 SFILNSIPVVVtlvsfGVFvllgGDLTPAR--------AFTSLSLFAVLrSPLNMLPNLLSQVVNANVSLQRIEELLL-- 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 196 slksQDCEILGESewgldtppgwPAAEPADTAFLLERVSISAPS-SDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLR- 273
Cdd:PLN03232 597 ----SEERILAQN----------PPLQPGAPAISIKNGYFSWDSkTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISa 662
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 274 VLGGLWTSTRGSVQMLTDfgphgVLFLPQKPFFTDGTLREQVIYplkevypdsGSA-DDERILRFLELAGLS---NLVA- 348
Cdd:PLN03232 663 MLGELSHAETSSVVIRGS-----VAYVPQVSWIFNATVRENILF---------GSDfESERYWRAIDVTALQhdlDLLPg 728
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 10947129 349 --RTEGLDQQVDwnwydvLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEVESELY 404
Cdd:PLN03232 729 rdLTEIGERGVN------ISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVF 780
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
236-419 |
2.80e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 60.90 E-value: 2.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 236 SAPSSDKPLIkDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQ----MLTDFGPH----------GVLF-L 300
Cdd:PRK13643 14 NSPFASRALF-DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTvgdiVVSSTSKQkeikpvrkkvGVVFqF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 301 PQKPFFTDGTLREQVIYPlkEVYPDSGSADDERILRFLELAGLSNLVARTEGLDqqvdwnwydvLSPGEMQRLSFARLFY 380
Cdd:PRK13643 93 PESQLFEETVLKDVAFGP--QNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFE----------LSGGQMRRVAIAGILA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 10947129 381 LQPKYAVLDEATSALTEEVESELYRIGQ---QLGMTFISVGH 419
Cdd:PRK13643 161 MEPEVLVLDEPTAGLDPKARIEMMQLFEsihQSGQTVVLVTH 202
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
243-404 |
3.11e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 62.62 E-value: 3.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 243 PLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQmltdfgpHG--VLFLPQKPFFTDGTLREQVIYPLk 320
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIK-------HSgrISFSPQTSWIMPGTIKDNIIFGL- 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 321 evypdsgSADDERILRFLELAGLSNLVARTEGLDQQVDWNWYDVLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEVE 400
Cdd:TIGR01271 512 -------SYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTE 584
|
....
gi 10947129 401 SELY 404
Cdd:TIGR01271 585 KEIF 588
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
244-419 |
4.71e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 59.98 E-value: 4.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 244 LIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV-------QMLTD-------FGPHGVLFLPQK------ 303
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIvvngqtiNLVRDkdgqlkvADKNQLRLLRTRltmvfq 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 304 --PFFTDGTLREQVIYPLKEVYPDSGSADDERILRFLELAGLsnlvarteglDQQVDWNWYDVLSPGEMQRLSFARLFYL 381
Cdd:PRK10619 100 hfNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGI----------DERAQGKYPVHLSGGQQQRVSIARALAM 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 10947129 382 QPKYAVLDEATSALTEEVESELYRIGQQL---GMTFISVGH 419
Cdd:PRK10619 170 EPEVLLFDEPTSALDPELVGEVLRIMQQLaeeGKTMVVVTH 210
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
215-420 |
5.51e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 61.92 E-value: 5.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 215 PPGWPAAepadTAFLLERVSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM----LT 290
Cdd:PLN03232 1226 VSGWPSR----GSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIddcdVA 1301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 291 DFGPHGVL----FLPQKPFFTDGTLREQvIYPLKEvypdsgsADDERILRFLELAGLSNLVARTE-GLDQQVdWNWYDVL 365
Cdd:PLN03232 1302 KFGLTDLRrvlsIIPQSPVLFSGTVRFN-IDPFSE-------HNDADLWEALERAHIKDVIDRNPfGLDAEV-SEGGENF 1372
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 10947129 366 SPGEMQRLSFARLFYLQPKYAVLDEATSALTEEVESELYR-IGQQL-GMTFISVGHR 420
Cdd:PLN03232 1373 SVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRtIREEFkSCTMLVIAHR 1429
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
243-404 |
8.74e-10 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 59.49 E-value: 8.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 243 PLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQmltdfgpHG--VLFLPQKPFFTDGTLREQVIYPLk 320
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK-------HSgrISFSSQFSWIMPGTIKENIIFGV- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 321 evypdsgSADDERILRFLELAGLSNLVARTEGLDQQVDWNWYDVLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEVE 400
Cdd:cd03291 123 -------SYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTE 195
|
....
gi 10947129 401 SELY 404
Cdd:cd03291 196 KEIF 199
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
245-419 |
1.01e-09 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 60.05 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 245 IKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGsvQMLTDfgphGVLFLPqkpfFTDGTLRE------QVIYP 318
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRG--QVLID----GVDIAK----ISDAELREvrrkkiAMVFQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 319 LKEVYPDSGSADDERIlrFLELAGLSNLVARTEGLD--QQVDWNWY-----DVLSPGEMQRLSFARLFYLQPKYAVLDEA 391
Cdd:PRK10070 114 SFALMPHMTVLDNTAF--GMELAGINAEERREKALDalRQVGLENYahsypDELSGGMRQRVGLARALAINPDILLMDEA 191
|
170 180 190
....*....|....*....|....*....|..
gi 10947129 392 TSALT----EEVESELYRIGQQLGMTFISVGH 419
Cdd:PRK10070 192 FSALDplirTEMQDELVKLQAKHQRTIVFISH 223
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
230-395 |
1.07e-09 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 58.44 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 230 LERVSISAPSSDKP--LIKDLSLKISEGQSLLITGNTGTGKTSLL-----RVLGGlwTSTRGSV----------QMLTDF 292
Cdd:cd03234 6 WWDVGLKAKNWNKYarILNDVSLHVESGQVMAILGSSGSGKTTLLdaisgRVEGG--GTTSGQIlfngqprkpdQFQKCV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 293 GphgvlFLPQKPFFTDG-TLREQVIY--PLKEVYPDSGSADDER--ILRFLELAglsnlvarteglDQQVDWNWYDVLSP 367
Cdd:cd03234 84 A-----YVRQDDILLPGlTVRETLTYtaILRLPRKSSDAIRKKRveDVLLRDLA------------LTRIGGNLVKGISG 146
|
170 180
....*....|....*....|....*...
gi 10947129 368 GEMQRLSFARLFYLQPKYAVLDEATSAL 395
Cdd:cd03234 147 GERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
245-413 |
1.18e-09 |
|
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: 58.21 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 245 IKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM----LTDFGPH-----GVLFLPQ-KPFFTDGTLREQ 314
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFdgrdITGLPPHeraraGIGYVPEgRRIFPELTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 315 VIYPLKEVYPDSGSADDERIL-RFLELAglsnlvartEGLDQQVdwnwyDVLSPGEMQRLSFARLFYLQPKYAVLDEATS 393
Cdd:cd03224 96 LLLGAYARRRAKRKARLERVYeLFPRLK---------ERRKQLA-----GTLSGGEQQMLAIARALMSRPKLLLLDEPSE 161
|
170 180
....*....|....*....|....
gi 10947129 394 AL----TEEVESELYRIgQQLGMT 413
Cdd:cd03224 162 GLapkiVEEIFEAIREL-RDEGVT 184
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
223-420 |
2.54e-09 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 57.04 E-value: 2.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 223 PADTAFLLERVSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM---------LTDFg 293
Cdd:cd03369 2 PEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIdgidistipLEDL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 294 PHGVLFLPQKPFFTDGTLREQViyplkEVYpdsGSADDERILRFLELA-GLSNlvartegldqqvdwnwydvLSPGEMQR 372
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNL-----DPF---DEYSDEEIYGALRVSeGGLN-------------------LSQGQRQL 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 10947129 373 LSFARLFYLQPKYAVLDEATSALTEEVESELYRIGQQL--GMTFISVGHR 420
Cdd:cd03369 134 LCLARALLKRPRVLVLDEATASIDYATDALIQKTIREEftNSTILTIAHR 183
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
241-395 |
2.56e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 56.81 E-value: 2.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 241 DKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQmLTDFGPHGVLFLPQ----------KPFFtdgT 310
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIK-LDGGDIDDPDVAEAchylghrnamKPAL---T 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 311 LREQVIYpLKEVYpDSGSADDERILRFLELAGLSNLVARtegldqqvdwnwydVLSPGEMQRLSFARLFYLQPKYAVLDE 390
Cdd:PRK13539 90 VAENLEF-WAAFL-GGEELDIAAALEAVGLAPLAHLPFG--------------YLSAGQKRRVALARLLVSNRPIWILDE 153
|
....*
gi 10947129 391 ATSAL 395
Cdd:PRK13539 154 PTAAL 158
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
215-403 |
2.56e-09 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 59.20 E-value: 2.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 215 PPGwpAAEPADTAFLLE--RVSISAPSSdKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM---- 288
Cdd:PRK13657 322 PPG--AIDLGRVKGAVEfdDVSFSYDNS-RQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIdgtd 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 289 LTDFGPH------GVLFlpQKPFFTDGTLREQviypLKEVYPDsgsADDERILRFLELAGLSNLVARTE-GLDQQVDWNW 361
Cdd:PRK13657 399 IRTVTRAslrrniAVVF--QDAGLFNRSIEDN----IRVGRPD---ATDEEMRAAAERAQAHDFIERKPdGYDTVVGERG 469
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 10947129 362 yDVLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEVESEL 403
Cdd:PRK13657 470 -RQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKV 510
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
219-421 |
3.01e-09 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 58.69 E-value: 3.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 219 PAAEPADTAF-LLERVSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----QMLTDFG 293
Cdd:PRK11607 8 PQAKTRKALTpLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQImldgVDLSHVP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 294 PHgvlflpQKP---------FFTDGTLREQVIYPLKEVYPDSGSADDeRILRFLELAGLSNLVARTEgldQQvdwnwydv 364
Cdd:PRK11607 88 PY------QRPinmmfqsyaLFPHMTVEQNIAFGLKQDKLPKAEIAS-RVNEMLGLVHMQEFAKRKP---HQ-------- 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 10947129 365 LSPGEMQRLSFARLFYLQPKYAVLDEATSALT----EEVESELYRIGQQLGMTFISVGHRQ 421
Cdd:PRK11607 150 LSGGQRQRVALARSLAKRPKLLLLDEPMGALDkklrDRMQLEVVDILERVGVTCVMVTHDQ 210
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
225-419 |
4.11e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 57.31 E-value: 4.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 225 DTAFLLERVSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQMltdfgphgvlflpqkp 304
Cdd:PRK13632 5 SVMIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKI---------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 305 fftDGTL--REQVIYPLKEV-----YPDS---GSADDERIlRFlelaGLSN-LVARTE------GLDQQVDWNWY----- 362
Cdd:PRK13632 69 ---DGITisKENLKEIRKKIgiifqNPDNqfiGATVEDDI-AF----GLENkKVPPKKmkdiidDLAKKVGMEDYldkep 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 10947129 363 DVLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEVESELYRIGQQL----GMTFISVGH 419
Cdd:PRK13632 141 QNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLrktrKKTLISITH 201
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
241-395 |
4.20e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 58.70 E-value: 4.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 241 DKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGlWTSTRGSVQM----LTDFGP----HGVLFLPQKPFFTDGTLR 312
Cdd:PRK11174 362 GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLG-FLPYQGSLKIngieLRELDPeswrKHLSWVGQNPQLPHGTLR 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 313 EQVIyplkevyPDSGSADDERILRFLELAGLSNLVAR-TEGLDQQV-DWNwyDVLSPGEMQRLSFARLFYLQPKYAVLDE 390
Cdd:PRK11174 441 DNVL-------LGNPDASDEQLQQALENAWVSEFLPLlPQGLDTPIgDQA--AGLSVGQAQRLALARALLQPCQLLLLDE 511
|
....*
gi 10947129 391 ATSAL 395
Cdd:PRK11174 512 PTASL 516
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
245-417 |
4.47e-09 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 57.11 E-value: 4.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 245 IKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVqMLTD----FGPHGVLFLPQKPFFTDGTLR---EQVI- 316
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGEL-LIDDhplhFGDYSYRSQRIRMIFQDPSTSlnpRQRIs 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 317 ----YPLKEVYPDSGSADDERILRFLELAGLSNLVArtegldqqvdwNWY-DVLSPGEMQRLSFARLFYLQPKYAVLDEA 391
Cdd:PRK15112 108 qildFPLRLNTDLEPEQREKQIIETLRQVGLLPDHA-----------SYYpHMLAPGQKQRLGLARALILRPKVIIADEA 176
|
170 180 190
....*....|....*....|....*....|
gi 10947129 392 TSALTEEVESELYRIGQQL----GMTFISV 417
Cdd:PRK15112 177 LASLDMSMRSQLINLMLELqekqGISYIYV 206
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
215-394 |
4.85e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 58.98 E-value: 4.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 215 PPGWPAAepadTAFLLERVSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM------ 288
Cdd:PLN03130 1229 PPGWPSS----GSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIdgcdis 1304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 289 ---LTDFgpHGVL-FLPQKPFFTDGTLREQvIYPLKEvypdsgsADDERILRFLELAGLSNLVAR-TEGLDQQVDwNWYD 363
Cdd:PLN03130 1305 kfgLMDL--RKVLgIIPQAPVLFSGTVRFN-LDPFNE-------HNDADLWESLERAHLKDVIRRnSLGLDAEVS-EAGE 1373
|
170 180 190
....*....|....*....|....*....|.
gi 10947129 364 VLSPGEMQRLSFARLFYLQPKYAVLDEATSA 394
Cdd:PLN03130 1374 NFSVGQRQLLSLARALLRRSKILVLDEATAA 1404
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
245-419 |
4.91e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 57.34 E-value: 4.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 245 IKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQ----MLT------DFGPH----GVLF-LPQKPFFTDG 309
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTigerVITagkknkKLKPLrkkvGIVFqFPEHQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 310 TLREQVIYPLkevypDSGSADDERILR---FLELAGLS-NLVARTEgldqqvdwnwYDvLSPGEMQRLSFARLFYLQPKY 385
Cdd:PRK13634 103 VEKDICFGPM-----NFGVSEEDAKQKareMIELVGLPeELLARSP----------FE-LSGGQMRRVAIAGVLAMEPEV 166
|
170 180 190
....*....|....*....|....*....|....*...
gi 10947129 386 AVLDEATSAL----TEEVESELYRIGQQLGMTFISVGH 419
Cdd:PRK13634 167 LVLDEPTAGLdpkgRKEMMEMFYKLHKEKGLTTVLVTH 204
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
247-419 |
4.92e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 57.06 E-value: 4.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 247 DLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----QMLTDFGPH----------GVLF-LPQKPFFTDGTL 311
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVrvddTLITSTSKNkdikqirkkvGLVFqFPESQLFEETVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 312 REQVIYPlkEVYPDSGSADDERILRFLELAGLSnlvarteglDQQVDWNWYDvLSPGEMQRLSFARLFYLQPKYAVLDEA 391
Cdd:PRK13649 105 KDVAFGP--QNFGVSQEEAEALAREKLALVGIS---------ESLFEKNPFE-LSGGQMRRVAIAGILAMEPKILVLDEP 172
|
170 180 190
....*....|....*....|....*....|.
gi 10947129 392 TSALTEEVESELYRIGQQL---GMTFISVGH 419
Cdd:PRK13649 173 TAGLDPKGRKELMTLFKKLhqsGMTIVLVTH 203
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
230-395 |
5.81e-09 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 55.83 E-value: 5.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 230 LERVSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM-------LTDFGPHGVLFLPQ 302
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWngtplaeQRDEPHENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 303 KPFF-TDGTLREQviypLKEVYPDSGSADD--ERILRFLELAGLSNLVARTegldqqvdwnwydvLSPGEMQRLSFARLF 379
Cdd:TIGR01189 81 LPGLkPELSALEN----LHFWAAIHGGAQRtiEDALAAVGLTGFEDLPAAQ--------------LSAGQQRRLALARLW 142
|
170
....*....|....*.
gi 10947129 380 YLQPKYAVLDEATSAL 395
Cdd:TIGR01189 143 LSRRPLWILDEPTTAL 158
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
230-413 |
7.40e-09 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 57.01 E-value: 7.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 230 LERVSISAPSSDKPLI--KDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----QMLTDFGPH-------- 295
Cdd:COG1135 4 LENLSKTFPTKGGPVTalDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVlvdgVDLTALSERelraarrk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 296 -GVLF-----LPQKpfftdgTLREQVIYPLK--EVypdSGSADDERILRFLELAGLSNLVARtegldqqvdwnwY-DVLS 366
Cdd:COG1135 84 iGMIFqhfnlLSSR------TVAENVALPLEiaGV---PKAEIRKRVAELLELVGLSDKADA------------YpSQLS 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 10947129 367 PGEMQRLSFARLFYLQPKyaVL--DEATSAL----TEEVESELYRIGQQLGMT 413
Cdd:COG1135 143 GGQKQRVGIARALANNPK--VLlcDEATSALdpetTRSILDLLKDINRELGLT 193
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
223-419 |
7.88e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 56.73 E-value: 7.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 223 PADTAFLLERVSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLwtstrgsvqMLTDFGPHGVLFLpq 302
Cdd:PRK13640 1 MKDNIVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGL---------LLPDDNPNSKITV-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 303 kpfftDG-TLREQVIYPLKE----VY--PDS---GSADDERILRFLELAGLS---------NLVARTEGLDQQVDWNWYd 363
Cdd:PRK13640 70 -----DGiTLTAKTVWDIREkvgiVFqnPDNqfvGATVGDDVAFGLENRAVPrpemikivrDVLADVGMLDYIDSEPAN- 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 364 vLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEVESELYRIGQQL----GMTFISVGH 419
Cdd:PRK13640 144 -LSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLkkknNLTVISITH 202
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
241-395 |
9.62e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 55.20 E-value: 9.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 241 DKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV---------------QMLTDFGPH-GVlflpqKP 304
Cdd:PRK13538 13 ERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVlwqgepirrqrdeyhQDLLYLGHQpGI-----KT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 305 fftDGTLREQviypLKEVYPDSGSADDERILRFLE---LAGLSNLVARTegldqqvdwnwydvLSPGEMQRLSFARLFYL 381
Cdd:PRK13538 88 ---ELTALEN----LRFYQRLHGPGDDEALWEALAqvgLAGFEDVPVRQ--------------LSAGQQRRVALARLWLT 146
|
170
....*....|....
gi 10947129 382 QPKYAVLDEATSAL 395
Cdd:PRK13538 147 RAPLWILDEPFTAI 160
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
245-421 |
9.84e-09 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 56.62 E-value: 9.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 245 IKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----QMLTDFGPH--GVLFLPQK----PFFtdgTLREQ 314
Cdd:COG3839 19 LKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEIliggRDVTDLPPKdrNIAMVFQSyalyPHM---TVYEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 315 VIYPLK-------EVypdsgsadDERILRFLELAGLSNLVAR--TEgldqqvdwnwydvLSPGEMQRLSFARLFYLQPKY 385
Cdd:COG3839 96 IAFPLKlrkvpkaEI--------DRRVREAAELLGLEDLLDRkpKQ-------------LSGGQRQRVALGRALVREPKV 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 10947129 386 AVLDEATS----ALTEEVESELYRIGQQLGMTFISVGHRQ 421
Cdd:COG3839 155 FLLDEPLSnldaKLRVEMRAEIKRLHRRLGTTTIYVTHDQ 194
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
220-421 |
1.49e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 55.44 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 220 AAEPADTAFLLERVSISApsSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM---LTDFGPH- 295
Cdd:PRK14246 3 AGKSAEDVFNISRLYLYI--NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVdgkVLYFGKDi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 296 ------------GVLFLPQKPFfTDGTLREQVIYPLKEvypdSGSADDERILRFLELAglsnlvARTEGLDQQVdwnwYD 363
Cdd:PRK14246 81 fqidaiklrkevGMVFQQPNPF-PHLSIYDNIAYPLKS----HGIKEKREIKKIVEEC------LRKVGLWKEV----YD 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 10947129 364 -------VLSPGEMQRLSFARLFYLQPKYAVLDEATSAL----TEEVESELYRIGQQLGMTFISVGHRQ 421
Cdd:PRK14246 146 rlnspasQLSGGQQQRLTIARALALKPKVLLMDEPTSMIdivnSQAIEKLITELKNEIAIVIVSHNPQQ 214
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
241-421 |
1.49e-08 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 56.19 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 241 DKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----QMLTDFGP--HGVLFLPQKpfftdgtlreq 314
Cdd:PRK11000 15 DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLfigeKRMNDVPPaeRGVGMVFQS----------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 315 viYPLkevYPDSGSADDeriLRF-LELAGLS--------NLVARTEGLDQQVDWNWYDvLSPGEMQRLSFARLFYLQPKY 385
Cdd:PRK11000 84 --YAL---YPHLSVAEN---MSFgLKLAGAKkeeinqrvNQVAEVLQLAHLLDRKPKA-LSGGQRQRVAIGRTLVAEPSV 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 10947129 386 AVLDEATS----ALTEEVESELYRIGQQLGMTFISVGHRQ 421
Cdd:PRK11000 155 FLLDEPLSnldaALRVQMRIEISRLHKRLGRTMIYVTHDQ 194
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
244-395 |
1.58e-08 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 54.42 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 244 LIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM-------LTDFGPHGVLFLPQKPFFTdGTLreQVI 316
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLnggpldfQRDSIARGLLYLGHAPGIK-TTL--SVL 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 10947129 317 YPLKEVYPDSGSADDERILRFLELAGLSNLVARTegldqqvdwnwydvLSPGEMQRLSFARLFYLQPKYAVLDEATSAL 395
Cdd:cd03231 92 ENLRFWHADHSDEQVEEALARVGLNGFEDRPVAQ--------------LSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
241-395 |
4.41e-08 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 53.44 E-value: 4.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 241 DKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM----LTDFGPHGVLFLPQ-KPFFTDGTLREQV 315
Cdd:cd03269 12 RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFdgkpLDIAARNRIGYLPEeRGLYPKMKVIDQL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 316 IYpLKEVYPDSGSADDERILRFLELAGLSNLvaRTEGLDQqvdwnwydvLSPGEMQRLSFARLFYLQPKYAVLDEATSAL 395
Cdd:cd03269 92 VY-LAQLKGLKKEEARRRIDEWLERLELSEY--ANKRVEE---------LSKGNQQKVQFIAAVIHDPELLILDEPFSGL 159
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
247-423 |
7.17e-08 |
|
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: 52.80 E-value: 7.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 247 DLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----QMLTDFGPHGVLFLPQK--------PFFTDGTLREQ 314
Cdd:cd03292 19 GINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIrvngQDVSDLRGRAIPYLRRKigvvfqdfRLLPDRNVYEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 315 VIYPLkEVYPDSGSADDERILRFLELAGLSNlvaRTEGLDQQvdwnwydvLSPGEMQRLSFARLFYLQPKYAVLDEATSA 394
Cdd:cd03292 99 VAFAL-EVTGVPPREIRKRVPAALELVGLSH---KHRALPAE--------LSGGEQQRVAIARAIVNSPTILIADEPTGN 166
|
170 180 190
....*....|....*....|....*....|..
gi 10947129 395 LTEEVESELYRIGQQL---GMTFISVGHRQSL 423
Cdd:cd03292 167 LDPDTTWEIMNLLKKInkaGTTVVVATHAKEL 198
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
233-425 |
8.54e-08 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 54.25 E-value: 8.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 233 VSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM---------LTDFGPHGVLFLPQK 303
Cdd:PRK11176 347 VTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLdghdlrdytLASLRNQVALVSQNV 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 304 PFFTDgTLREQVIYPLKEVYpdsgsaDDERILRFLELAGLSNLVARTE-GLDQQVDWNWYdVLSPGEMQRLSFARLFYLQ 382
Cdd:PRK11176 427 HLFND-TIANNIAYARTEQY------SREQIEEAARMAYAMDFINKMDnGLDTVIGENGV-LLSGGQRQRIAIARALLRD 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 10947129 383 PKYAVLDEATSALteEVESElyRIGQ------QLGMTFISVGHRQS-LEK 425
Cdd:PRK11176 499 SPILILDEATSAL--DTESE--RAIQaaldelQKNRTSLVIAHRLStIEK 544
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
241-419 |
1.21e-07 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 52.71 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 241 DKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----QMLTDFGP----HGVLFLPQKPFFTDG-TL 311
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVflgdKPISMLSSrqlaRRLALLPQHHLTPEGiTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 312 REQVIY---PLKEVYPDSGSADDERILRFLELAGLSNLVarteglDQQVdwnwyDVLSPGEMQRLSFARLFYLQPKYAVL 388
Cdd:PRK11231 94 RELVAYgrsPWLSLWGRLSAEDNARVNQAMEQTRINHLA------DRRL-----TDLSGGQRQRAFLAMVLAQDTPVVLL 162
|
170 180 190
....*....|....*....|....*....|....
gi 10947129 389 DEATSALTEEVESELYRIGQQL---GMTFISVGH 419
Cdd:PRK11231 163 DEPTTYLDINHQVELMRLMRELntqGKTVVTVLH 196
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
241-422 |
1.56e-07 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 53.81 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 241 DKPLI-KDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVqmltdfgphgvlflpqkpfFTDG---------T 310
Cdd:TIGR03797 464 DGPLIlDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSV-------------------FYDGqdlagldvqA 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 311 LREQVIYPLKEVYPDSGSadderILRflELAGLSNL-------VARTEGLDQQVD---WNWYDV-------LSPGEMQRL 373
Cdd:TIGR03797 525 VRRQLGVVLQNGRLMSGS-----IFE--NIAGGAPLtldeaweAARMAGLAEDIRampMGMHTVisegggtLSGGQRQRL 597
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 10947129 374 SFARLFYLQPKYAVLDEATSAL---TEEVESELYrigQQLGMTFISVGHRQS 422
Cdd:TIGR03797 598 LIARALVRKPRILLFDEATSALdnrTQAIVSESL---ERLKVTRIVIAHRLS 646
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
229-403 |
2.05e-07 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 52.01 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 229 LLERVSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM--LTDFGP---HGVLF---- 299
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLdgKPVEGPgaeRGVVFqneg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 300 -LPQKpfftdgTLREQVIYPLKEvypdSGSADDERILRFLELAGLSNLvartEGLDQQVDWNwydvLSPGEMQRLSFARL 378
Cdd:PRK11248 81 lLPWR------NVQDNVAFGLQL----AGVEKMQRLEIAHQMLKKVGL----EGAEKRYIWQ----LSGGQRQRVGIARA 142
|
170 180
....*....|....*....|....*...
gi 10947129 379 FYLQPKYAVLDE---ATSALTEEVESEL 403
Cdd:PRK11248 143 LAANPQLLLLDEpfgALDAFTREQMQTL 170
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
240-436 |
2.30e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 53.41 E-value: 2.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 240 SDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQMltdfgPHGVLFLPQKPFFTDGTLREQVIY-- 317
Cdd:TIGR00957 649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHM-----KGSVAYVPQQAWIQNDSLRENILFgk 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 318 PLKEVYPDSgSADDERILRFLELAGLSNlvaRTEGLDQQVDwnwydvLSPGEMQRLSFARLFYLQPKYAVLDEATSALTE 397
Cdd:TIGR00957 724 ALNEKYYQQ-VLEACALLPDLEILPSGD---RTEIGEKGVN------LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDA 793
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 10947129 398 EVESELYR-----IGQQLGMTFISVGHRQSLEKFHSLVLKLCGG 436
Cdd:TIGR00957 794 HVGKHIFEhvigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGG 837
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
240-431 |
3.26e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 51.68 E-value: 3.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 240 SDKPL-IKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV---------QMLTDFGPH-GVLFlpQKPfftd 308
Cdd:PRK13648 19 SDASFtLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqaitdDNFEKLRKHiGIVF--QNP---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 309 gtlREQVIyplkevypdsGSadderILRFLELAGLSNLVARTEGLDQQVDWNWYDV------------LSPGEMQRLSFA 376
Cdd:PRK13648 93 ---DNQFV----------GS-----IVKYDVAFGLENHAVPYDEMHRRVSEALKQVdmleradyepnaLSGGQKQRVAIA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 10947129 377 RLFYLQPKYAVLDEATSALTEEVESELYRIGQQL----GMTFISVGH--RQSLEKFHSLVL 431
Cdd:PRK13648 155 GVLALNPSVIILDEATSMLDPDARQNLLDLVRKVksehNITIISITHdlSEAMEADHVIVM 215
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
115-404 |
4.31e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 52.43 E-value: 4.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 115 INTFdYLGSILSYV-VIAIPIFSGVYGDLSPAELSTLVSKNA---FVCIYLISCFTQLIDLSTTLSdvagythrigQLRE 190
Cdd:PLN03130 525 FNSF-ILNSIPVLVtVVSFGVFTLLGGDLTPARAFTSLSLFAvlrFPLFMLPNLITQAVNANVSLK----------RLEE 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 191 TLldmslksqdceiLGESEWGLDTPP---GWPAAEPADTAFLLErvsisaPSSDKPLIKDLSLKISEGQSLLITGNTGTG 267
Cdd:PLN03130 594 LL------------LAEERVLLPNPPlepGLPAISIKNGYFSWD------SKAERPTLSNINLDVPVGSLVAIVGSTGEG 655
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 268 KTSLLR-VLGGLWTSTRGSVQMLTDfgphgVLFLPQKPFFTDGTLREQVIYplkevypdsGSA-DDERILRFLELAGLSN 345
Cdd:PLN03130 656 KTSLISaMLGELPPRSDASVVIRGT-----VAYVPQVSWIFNATVRDNILF---------GSPfDPERYERAIDVTALQH 721
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 10947129 346 LVARTEGLDQQ------VDwnwydvLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEVESELY 404
Cdd:PLN03130 722 DLDLLPGGDLTeigergVN------ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVF 780
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
244-425 |
4.55e-07 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 50.58 E-value: 4.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 244 LIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----QMLT--------DFGPHGVLFLPQ-KPFFTDGT 310
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVifngQPMSklssaakaELRNQKLGFIYQfHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 311 LREQVIYPLKevypDSGSADDERILRFLELAGLSNLVARTEGLDQQvdwnwydvLSPGEMQRLSFARLFYLQPKYAVLDE 390
Cdd:PRK11629 104 ALENVAMPLL----IGKKKPAEINSRALEMLAAVGLEHRANHRPSE--------LSGGERQRVAIARALVNNPRLVLADE 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 10947129 391 ATSALTEEVESELYRIGQQL----GMTFISVGHRQSLEK 425
Cdd:PRK11629 172 PTGNLDARNADSIFQLLGELnrlqGTAFLVVTHDLQLAK 210
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
239-395 |
5.98e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 52.22 E-value: 5.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 239 SSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLwTSTRG----------SVQMLTDFGPHGVlfLPQKPFFTD 308
Cdd:TIGR01271 1229 EAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGeiqidgvswnSVTLQTWRKAFGV--IPQKVFIFS 1305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 309 GTLReqviyplKEVYPDSGSADDErILRFLELAGLSNLVARTEG-LDQQVDWNWYdVLSPGEMQRLSFARLFYLQPKYAV 387
Cdd:TIGR01271 1306 GTFR-------KNLDPYEQWSDEE-IWKVAEEVGLKSVIEQFPDkLDFVLVDGGY-VLSNGHKQLMCLARSILSKAKILL 1376
|
....*...
gi 10947129 388 LDEATSAL 395
Cdd:TIGR01271 1377 LDEPSAHL 1384
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
226-419 |
6.27e-07 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 51.65 E-value: 6.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 226 TAFL-LERVSISAPSSDKPL--IKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----QMLTDFGPHGVL 298
Cdd:PRK10535 2 TALLeLKDIRRSYPSGEEQVevLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYrvagQDVATLDADALA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 299 FLPQKPF---------FTDGTLREQVIYPlkEVYpdSGSADDERILRFLELagLSNLvarteGLDQQVDWNwYDVLSPGE 369
Cdd:PRK10535 82 QLRREHFgfifqryhlLSHLTAAQNVEVP--AVY--AGLERKQRLLRAQEL--LQRL-----GLEDRVEYQ-PSQLSGGQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 10947129 370 MQRLSFARLFYLQPKYAVLDEATSAL----TEEVESELYRIGQQlGMTFISVGH 419
Cdd:PRK10535 150 QQRVSIARALMNGGQVILADEPTGALdshsGEEVMAILHQLRDR-GHTVIIVTH 202
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
230-395 |
6.81e-07 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 49.88 E-value: 6.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 230 LERVSISAPSsdKPLIKDLSLKISEGQSLLItGNTGTGKTSLLRVLGGLWTSTRGSVQML------TDFGPHGVL-FLPQ 302
Cdd:cd03264 3 LENLTKRYGK--KRALDGVSLTLGPGMYGLL-GPNGAGKTTLMRILATLTPPSSGTIRIDgqdvlkQPQKLRRRIgYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 303 KP-FFTDGTLREQVIYP--LKEVyPDSGSadDERILRFLELAGLSNLVARTEGldqqvdwnwydVLSPGEMQRLSFARLF 379
Cdd:cd03264 80 EFgVYPNFTVREFLDYIawLKGI-PSKEV--KARVDEVLELVNLGDRAKKKIG-----------SLSGGMRRRVGIAQAL 145
|
170
....*....|....*.
gi 10947129 380 YLQPKYAVLDEATSAL 395
Cdd:cd03264 146 VGDPSILIVDEPTAGL 161
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
219-422 |
6.96e-07 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 51.64 E-value: 6.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 219 PAAEPADTAFLLER----VSISA---PSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----Q 287
Cdd:PRK10789 298 PVVKDGSEPVPEGRgeldVNIRQftyPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIrfhdI 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 288 MLTDFGPHG----VLFLPQKPF-FTDgtlreQVIYPLKEVYPDSGSADDERILRfleLAGLSNLVAR-TEGLDQQVDWNW 361
Cdd:PRK10789 378 PLTKLQLDSwrsrLAVVSQTPFlFSD-----TVANNIALGRPDATQQEIEHVAR---LASVHDDILRlPQGYDTEVGERG 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 10947129 362 YdVLSPGEMQRLSFARLFYLQPKYAVLDEATSAL---TE-EVESELYRIGQqlGMTFISVGHRQS 422
Cdd:PRK10789 450 V-MLSGGQKQRISIARALLLNAEILILDDALSAVdgrTEhQILHNLRQWGE--GRTVIISAHRLS 511
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
240-422 |
1.05e-06 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 50.87 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 240 SDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQMltDFGP-----HGVL-----FLPQKP----- 304
Cdd:PRK10790 352 DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRL--DGRPlsslsHSVLrqgvaMVQQDPvvlad 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 305 -FFTDGTLREQViyplkevypdsgsaDDERILRFLELAGLSNLV-ARTEGLDQQVDwNWYDVLSPGEMQRLSFARLFYLQ 382
Cdd:PRK10790 430 tFLANVTLGRDI--------------SEEQVWQALETVQLAELArSLPDGLYTPLG-EQGNNLSVGQKQLLALARVLVQT 494
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 10947129 383 PKYAVLDEATSAL---TEE-VESELYRIGQQlgMTFISVGHRQS 422
Cdd:PRK10790 495 PQILILDEATANIdsgTEQaIQQALAAVREH--TTLVVIAHRLS 536
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
245-419 |
1.24e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 49.85 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 245 IKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV---QMLTDFGPHGVLFL----------PQKPFFTdGTL 311
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRIlfdGKPIDYSRKGLMKLresvgmvfqdPDNQLFS-ASV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 312 REQVIY-------PLKEVYpdsgsaddERILRFLELAGLSNLVarteglDQQVDWnwydvLSPGEMQRLSFARLFYLQPK 384
Cdd:PRK13636 101 YQDVSFgavnlklPEDEVR--------KRVDNALKRTGIEHLK------DKPTHC-----LSFGQKKRVAIAGVLVMEPK 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 10947129 385 YAVLDEATSAL----TEEVESELYRIGQQLGMTFISVGH 419
Cdd:PRK13636 162 VLVLDEPTAGLdpmgVSEIMKLLVEMQKELGLTIIIATH 200
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
240-419 |
1.49e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 49.71 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 240 SDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM----LTDFG------PHGVLFLPQKPFFTDG 309
Cdd:PRK13642 18 SDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIdgelLTAENvwnlrrKIGMVFQNPDNQFVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 310 TLREQVIYPLKevypDSGSADDERILRFLE-LAGLSNLVARTEGLDQqvdwnwydvLSPGEMQRLSFARLFYLQPKYAVL 388
Cdd:PRK13642 98 TVEDDVAFGME----NQGIPREEMIKRVDEaLLAVNMLDFKTREPAR---------LSGGQKQRVAVAGIIALRPEIIIL 164
|
170 180 190
....*....|....*....|....*....|....*
gi 10947129 389 DEATSALTEEVESELYRIGQQLG----MTFISVGH 419
Cdd:PRK13642 165 DESTSMLDPTGRQEIMRVIHEIKekyqLTVLSITH 199
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
247-419 |
1.56e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 49.44 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 247 DLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQMLtdfGPH-----------------GVLF-LPQKPFFTD 308
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIA---GYHitpetgnknlkklrkkvSLVFqFPEAQLFEN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 309 GTLREQVIYPLkevypDSGSADDE---RILRFLELAGLSNLVARTEGLDqqvdwnwydvLSPGEMQRLSFARLFYLQPKY 385
Cdd:PRK13641 102 TVLKDVEFGPK-----NFGFSEDEakeKALKWLKKVGLSEDLISKSPFE----------LSGGQMRRVAIAGVMAYEPEI 166
|
170 180 190
....*....|....*....|....*....|....*..
gi 10947129 386 AVLDEATSALTEEVESELYRI---GQQLGMTFISVGH 419
Cdd:PRK13641 167 LCLDEPAAGLDPEGRKEMMQLfkdYQKAGHTVILVTH 203
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
228-419 |
1.60e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 50.32 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 228 FLLERVSISAPSsDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQMLTDFgphGVLFLPQKPFFT 307
Cdd:TIGR03719 5 YTMNRVSKVVPP-KKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGI---KVGYLPQEPQLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 308 DG-TLREQV----------IYPLKEVYPDSGSADDERILRFLELAGLSNLVARTEG--LDQQVD----------WNWyDV 364
Cdd:TIGR03719 81 PTkTVRENVeegvaeikdaLDRFNEISAKYAEPDADFDKLAAEQAELQEIIDAADAwdLDSQLEiamdalrcppWDA-DV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 10947129 365 --LSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEVESELYRIGQQLGMTFISVGH 419
Cdd:TIGR03719 160 tkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTH 216
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
219-392 |
1.63e-06 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 50.45 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 219 PAAEPADTAFLLERVSISAPssDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVqmltDFGPHGVL 298
Cdd:COG0488 307 PPERLGKKVLELEGLSKSYG--DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV----KLGETVKI 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 299 -FLPQKPFFTDGTLReqviyPLKEVYPDSGSADDERILRFLELAGLSNlvartEGLDQQVdwnwyDVLSPGEMQRLSFAR 377
Cdd:COG0488 381 gYFDQHQEELDPDKT-----VLDELRDGAPGGTEQEVRGYLGRFLFSG-----DDAFKPV-----GVLSGGEKARLALAK 445
|
170
....*....|....*
gi 10947129 378 LFYLQPKYAVLDEAT 392
Cdd:COG0488 446 LLLSPPNVLLLDEPT 460
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
244-395 |
1.76e-06 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 49.47 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 244 LIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLwTSTRGSVQM-------------LTDFGphgvlFLPQKPFFTDGT 310
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQIdgvswnsvplqkwRKAFG-----VIPQKVFIFSGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 311 LReqviyplKEVYPdSGSADDERILRFLELAGLSNLVARTEG-LDQQVDWNWYdVLSPGEMQRLSFARLFYLQPKYAVLD 389
Cdd:cd03289 93 FR-------KNLDP-YGKWSDEEIWKVAEEVGLKSVIEQFPGqLDFVLVDGGC-VLSHGHKQLMCLARSVLSKAKILLLD 163
|
....*.
gi 10947129 390 EATSAL 395
Cdd:cd03289 164 EPSAHL 169
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
241-433 |
2.22e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.41 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 241 DKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV-----QMLTDFGPH------GVLflPQKPFFTDG 309
Cdd:PTZ00265 397 DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIiindsHNLKDINLKwwrskiGVV--SQDPLLFSN 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 310 TLREQV---IYPLKEV--------------YPDSGSADDERILRFLELAGLSNLVARTEGLDQQVDWNW----------- 361
Cdd:PTZ00265 475 SIKNNIkysLYSLKDLealsnyynedgndsQENKNKRNSCRAKCAGDLNDMSNTTDSNELIEMRKNYQTikdsevvdvsk 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 362 --------------YDVL--------SPGEMQRLSFARLFYLQPKYAVLDEATSALTEEVESELYRI-----GQQLGMTF 414
Cdd:PTZ00265 555 kvlihdfvsalpdkYETLvgsnasklSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTinnlkGNENRITI 634
|
250
....*....|....*....
gi 10947129 415 IsVGHRQSLEKFHSLVLKL 433
Cdd:PTZ00265 635 I-IAHRLSTIRYANTIFVL 652
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
228-419 |
2.32e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 48.68 E-value: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 228 FLLERVSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLW-----TSTRGSVQML------TDFGP-- 294
Cdd:PRK14267 3 FAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLelneeARVEGEVRLFgrniysPDVDPie 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 295 ----HGVLFLPQKPFfTDGTLREQVIYPLKevypdsgsadderilrflelagLSNLVARTEGLDQQVDWN------WYDV 364
Cdd:PRK14267 83 vrreVGMVFQYPNPF-PHLTIYDNVAIGVK----------------------LNGLVKSKKELDERVEWAlkkaalWDEV 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 10947129 365 ----------LSPGEMQRLSFARLFYLQPKYAVLDEATSAL----TEEVESELYRIGQQLgmTFISVGH 419
Cdd:PRK14267 140 kdrlndypsnLSGGQRQRLVIARALAMKPKILLMDEPTANIdpvgTAKIEELLFELKKEY--TIVLVTH 206
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
239-420 |
2.83e-06 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 48.10 E-value: 2.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 239 SSDKPLIKDLSLKISEGQSLLITGNTGTGKTS-LLRVLGGL--------WTSTRGSVQMLTDFGP---HGVLFLPQKPFF 306
Cdd:cd03290 11 GSGLATLSNINIRIPTGQLTMIVGQVGCGKSSlLLAILGEMqtlegkvhWSNKNESEPSFEATRSrnrYSVAYAAQKPWL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 307 TDGTLREQVIY--PL-----KEVYPDSGSADDERILRFLElaglsnlvaRTEGLDQQVDwnwydvLSPGEMQRLSFARLF 379
Cdd:cd03290 91 LNATVEENITFgsPFnkqryKAVTDACSLQPDIDLLPFGD---------QTEIGERGIN------LSGGQRQRICVARAL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 10947129 380 YLQPKYAVLDEATSALTEEVESELYRIG-----QQLGMTFISVGHR 420
Cdd:cd03290 156 YQNTNIVFLDDPFSALDIHLSDHLMQEGilkflQDDKRTLVLVTHK 201
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
242-399 |
3.03e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 49.78 E-value: 3.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 242 KPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVqmltdFGPHGVLFLPQKPFFTDGTLREQVIYplke 321
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-----WAERSIAYVPQQAWIMNATVRGNILF---- 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 322 vYPDSGSADDERILRFLEL-AGLSNLVA--RTEGLDQQVDwnwydvLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEE 398
Cdd:PTZ00243 744 -FDEEDAARLADAVRVSQLeADLAQLGGglETEIGEKGVN------LSGGQKARVSLARAVYANRDVYLLDDPLSALDAH 816
|
.
gi 10947129 399 V 399
Cdd:PTZ00243 817 V 817
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
241-416 |
3.24e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 48.46 E-value: 3.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 241 DKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV---QMLTDFGPHGVLFL-----------PQKPFF 306
Cdd:PRK13638 13 DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVlwqGKPLDYSKRGLLALrqqvatvfqdpEQQIFY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 307 TDgtLREQVIYPLKEVypdsGSADDERILRFLELAGLSNlvarTEGLDQQVdwnwYDVLSPGEMQRLSFARLFYLQPKYA 386
Cdd:PRK13638 93 TD--IDSDIAFSLRNL----GVPEAEITRRVDEALTLVD----AQHFRHQP----IQCLSHGQKKRVAIAGALVLQARYL 158
|
170 180 190
....*....|....*....|....*....|....
gi 10947129 387 VLDEATSALTEEVESELY----RIGQQLGMTFIS 416
Cdd:PRK13638 159 LLDEPTAGLDPAGRTQMIaiirRIVAQGNHVIIS 192
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
215-416 |
3.36e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 49.32 E-value: 3.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 215 PPGWPAAEPADTAFLL--ERVSISAP---------SSDKPLIKDLSLKISEGQSLLITGNTGTGKTS----LLRVL---G 276
Cdd:PRK15134 261 PSGDPVPLPEPASPLLdvEQLQVAFPirkgilkrtVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLInsqG 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 277 GLWTS-----TRGSVQMLTDFGPHGVLFlpQKPfftDGTLR-----EQVIYPLKEV-YPD-SGSADDERILRFLELAGLs 344
Cdd:PRK15134 341 EIWFDgqplhNLNRRQLLPVRHRIQVVF--QDP---NSSLNprlnvLQIIEEGLRVhQPTlSAAQREQQVIAVMEEVGL- 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 10947129 345 nlvarteglDQQVDWNWYDVLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEVESE---LYRIGQQ---LGMTFIS 416
Cdd:PRK15134 415 ---------DPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQilaLLKSLQQkhqLAYLFIS 483
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
241-394 |
3.56e-06 |
|
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: 47.91 E-value: 3.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 241 DKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM------LTDFGpHGvlFLPqkpfftDGTLREQ 314
Cdd:cd03220 34 EFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVrgrvssLLGLG-GG--FNP------ELTGREN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 315 vIYPLKEVYPDSGSADDERILRFLELAGLsnlvarTEGLDQQVdwnwyDVLSPGEMQRLSFARLFYLQPKYAVLDEATSA 394
Cdd:cd03220 105 -IYLNGRLLGLSRKEIDEKIDEIIEFSEL------GDFIDLPV-----KTYSSGMKARLAFAIATALEPDILLIDEVLAV 172
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
250-440 |
3.72e-06 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 47.85 E-value: 3.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 250 LKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQML------------TDFGPHGVLFLPQKpFFTDGTL--REQV 315
Cdd:PRK10584 31 LVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVgqplhqmdeearAKLRAKHVGFVFQS-FMLIPTLnaLENV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 316 IYP-LKEVYPDSGSADDERILrfLELAGLSNlvaRTEGLDQQvdwnwydvLSPGEMQRLSFARLFYLQPKYAVLDEATSA 394
Cdd:PRK10584 110 ELPaLLRGESSRQSRNGAKAL--LEQLGLGK---RLDHLPAQ--------LSGGEQQRVALARAFNGRPDVLFADEPTGN 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 10947129 395 LT----EEVESELYRIGQQLGMTFISVGHRQSLEKFHSLVLKLCGGGRWE 440
Cdd:PRK10584 177 LDrqtgDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
223-288 |
3.90e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 47.54 E-value: 3.90e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 10947129 223 PADTAFLLERVSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM 288
Cdd:PRK13543 5 LHTAPPLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQI 70
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
230-413 |
4.40e-06 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 48.64 E-value: 4.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 230 LERVSISAPSSDKPLI--KDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----QMLTDFGPH-------- 295
Cdd:PRK11153 4 LKNISKVFPQGGRTIHalNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVlvdgQDLTALSEKelrkarrq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 296 -GVLF-----LPQKpfftdgTLREQVIYPLkEVYPDSGSADDERILRFLELAGLSNLVARtegldqqvdwnwYDV-LSPG 368
Cdd:PRK11153 84 iGMIFqhfnlLSSR------TVFDNVALPL-ELAGTPKAEIKARVTELLELVGLSDKADR------------YPAqLSGG 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 10947129 369 EMQRLSFARLFYLQPKyaVL--DEATSAL----TEEVESELYRIGQQLGMT 413
Cdd:PRK11153 145 QKQRVAIARALASNPK--VLlcDEATSALdpatTRSILELLKDINRELGLT 193
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
241-395 |
5.03e-06 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 48.68 E-value: 5.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 241 DKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVqMLTDFGPHG---------VLFLPQK---PFFTD 308
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTV-LVAGDDVEAlsaraasrrVASVPQDtslSFEFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 309 GtlrEQVI----YPLKEVYPDSGSADDERILRFLELAGLSNLVARTegldqqvdwnwYDVLSPGEMQRLSFARLFYLQPK 384
Cdd:PRK09536 94 V---RQVVemgrTPHRSRFDTWTETDRAAVERAMERTGVAQFADRP-----------VTSLSGGERQRVLLARALAQATP 159
|
170
....*....|.
gi 10947129 385 YAVLDEATSAL 395
Cdd:PRK09536 160 VLLLDEPTASL 170
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
226-419 |
5.39e-06 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 47.84 E-value: 5.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 226 TAFLLERVSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQMLTDFGP---HGVLFLPQ 302
Cdd:PRK11831 4 VANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPamsRSRLYTVR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 303 K---------PFFTDGTLREQVIYPLKEvypdsGSADDERILRF-----LELAGL---SNLVARTegldqqvdwnwydvL 365
Cdd:PRK11831 84 KrmsmlfqsgALFTDMNVFDNVAYPLRE-----HTQLPAPLLHStvmmkLEAVGLrgaAKLMPSE--------------L 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 10947129 366 SPGEMQRLSFARLFYLQPKYAVLDEA-------TSALTEEVESELyriGQQLGMTFISVGH 419
Cdd:PRK11831 145 SGGMARRAALARAIALEPDLIMFDEPfvgqdpiTMGVLVKLISEL---NSALGVTCVVVSH 202
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
244-422 |
6.09e-06 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 47.44 E-value: 6.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 244 LIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQMLTDFGPHGVLFLPQKPFFTDgtLREQV-------- 315
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQQKGLIRQ--LRQHVgfvfqnfn 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 316 IYPLKEVYPD--------SGSADDERILRFLELAGLSNLVARTEGLDQQvdwnwydvLSPGEMQRLSFARLFYLQPKYAV 387
Cdd:PRK11264 96 LFPHRTVLENiiegpvivKGEPKEEATARARELLAKVGLAGKETSYPRR--------LSGGQQQRVAIARALAMRPEVIL 167
|
170 180 190
....*....|....*....|....*....|....*...
gi 10947129 388 LDEATSALTEEVESELYRIGQQLG---MTFISVGHRQS 422
Cdd:PRK11264 168 FDEPTSALDPELVGEVLNTIRQLAqekRTMVIVTHEMS 205
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
246-395 |
6.33e-06 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 48.53 E-value: 6.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 246 KDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLwTSTRGSVQM----LTDFGPHG---------VLFlpQKPFftdGTL- 311
Cdd:COG4172 303 DGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFdgqdLDGLSRRAlrplrrrmqVVF--QDPF---GSLs 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 312 -R---EQVIY-PLKEVYPDSGSAD-DERILRFLELAGLS-NLVAR--TEgldqqvdwnwydvLSPGEMQRLSFARLFYLQ 382
Cdd:COG4172 377 pRmtvGQIIAeGLRVHGPGLSAAErRARVAEALEEVGLDpAARHRypHE-------------FSGGQRQRIAIARALILE 443
|
170
....*....|...
gi 10947129 383 PKYAVLDEATSAL 395
Cdd:COG4172 444 PKLLVLDEPTSAL 456
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
365-420 |
1.08e-05 |
|
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: 45.50 E-value: 1.08e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 365 LSPGEMQRLSFARLFYLQPKYAVLDEATSALT-EEVEsELYRIGQQL---GMTFISVGHR 420
Cdd:cd03216 83 LSVGERQMVEIARALARNARLLILDEPTAALTpAEVE-RLFKVIRRLraqGVAVIFISHR 141
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
229-397 |
1.39e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 45.71 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 229 LLERVSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQML-----TDFGPH--GVLFLP 301
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFErqsikKDLCTYqkQLCFVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 302 QK----PFFtdgTLREQVIYplkEVYPDSGSADDERILRFLElagLSNLVARTEGLdqqvdwnwydvLSPGEMQRLSFAR 377
Cdd:PRK13540 81 HRsginPYL---TLRENCLY---DIHFSPGAVGITELCRLFS---LEHLIDYPCGL-----------LSSGQKRQVALLR 140
|
170 180
....*....|....*....|
gi 10947129 378 LFYLQPKYAVLDEATSALTE 397
Cdd:PRK13540 141 LWMSKAKLWLLDEPLVALDE 160
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
230-427 |
1.91e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 46.13 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 230 LERVSISAPSSdKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM----LTDFGPH-------GVL 298
Cdd:PRK13644 4 LENVSYSYPDG-TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVsgidTGDFSKLqgirklvGIV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 299 FLPQKPFFTDGTLREQVIY-PLKEVYPDsgSADDERILRFLELAGLSNLVARTEgldqqvdwnwyDVLSPGEMQRLSFAR 377
Cdd:PRK13644 83 FQNPETQFVGRTVEEDLAFgPENLCLPP--IEIRKRVDRALAEIGLEKYRHRSP-----------KTLSGGQGQCVALAG 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 10947129 378 LFYLQPKYAVLDEATSALTEEV-ESELYRIGQ--QLGMTFISVGHrqSLEKFH 427
Cdd:PRK13644 150 ILTMEPECLIFDEVTSMLDPDSgIAVLERIKKlhEKGKTIVYITH--NLEELH 200
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
242-419 |
2.45e-05 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 45.75 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 242 KPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----QMLTDFGPHGV-----LFLPQKPFFTDGTLR 312
Cdd:PRK10253 20 YTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVwldgEHIQHYASKEVarrigLLAQNATTPGDITVQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 313 EQVI---YPLKEVYPDSGSADDERILRFLELAGLSNLVarteglDQQVdwnwyDVLSPGEMQRLSFARLFYLQPKYAVLD 389
Cdd:PRK10253 100 ELVArgrYPHQPLFTRWRKEDEEAVTKAMQATGITHLA------DQSV-----DTLSGGQRQRAWIAMVLAQETAIMLLD 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 10947129 390 EATSALT-------EEVESELYRigqQLGMTFISVGH 419
Cdd:PRK10253 169 EPTTWLDishqidlLELLSELNR---EKGYTLAAVLH 202
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
241-401 |
3.41e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.04 E-value: 3.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 241 DKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQML--TDFGphgvlFLPQ---KPFFTDGTLREQV 315
Cdd:PRK15064 331 NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSenANIG-----YYAQdhaYDFENDLTLFDWM 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 316 IYPLKEvypdsgsADDERILRflelAGLSNLVARTEGLDQQVdwnwyDVLSPGEMQRLSFARLFYLQPKYAVLDEATSAL 395
Cdd:PRK15064 406 SQWRQE-------GDDEQAVR----GTLGRLLFSQDDIKKSV-----KVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHM 469
|
....*..
gi 10947129 396 -TEEVES 401
Cdd:PRK15064 470 dMESIES 476
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
246-287 |
4.80e-05 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 44.69 E-value: 4.80e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 10947129 246 KDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQ 287
Cdd:COG1134 43 KDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
242-390 |
6.32e-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: 44.07 E-value: 6.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 242 KPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----QMLTDFGPH-----GVLFLPQKP-FFTDGTL 311
Cdd:cd03218 13 RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKIlldgQDITKLPMHkrarlGIGYLPQEAsIFRKLTV 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 10947129 312 REQVIYPLkEVYPDSGSADDERILRFLELAGLSNLvARTEGLDqqvdwnwydvLSPGEMQRLSFARLFYLQPKYAVLDE 390
Cdd:cd03218 93 EENILAVL-EIRGLSKKEREEKLEELLEEFHITHL-RKSKASS----------LSGGERRRVEIARALATNPKFLLLDE 159
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
230-434 |
7.61e-05 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 44.44 E-value: 7.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 230 LERVSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQMLTDFGPH-------GVLFLPQ 302
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPArarlaraRIGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 303 ----KPFFtdgTLREQVIYpLKEVYPDSGSADDERILRFLELAGLSNLVarteglDQQVdwnwyDVLSPGEMQRLSFARL 378
Cdd:PRK13536 122 fdnlDLEF---TVRENLLV-FGRYFGMSTREIEAVIPSLLEFARLESKA------DARV-----SDLSGGMKRRLTLARA 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 10947129 379 FYLQPKYAVLDEATSALT--------EEVESELYRigqqlGMTFISVGHrqSLEKFHSLVLKLC 434
Cdd:PRK13536 187 LINDPQLLILDEPTTGLDpharhliwERLRSLLAR-----GKTILLTTH--FMEEAERLCDRLC 243
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
302-420 |
1.01e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.02 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 302 QKPFFTDGTLREQVIYPlKEvypDSGSADDERILRFlelAGLSNLVartEGLDQQVDWN---WYDVLSPGEMQRLSFARL 378
Cdd:PTZ00265 1303 QEPMLFNMSIYENIKFG-KE---DATREDVKRACKF---AAIDEFI---ESLPNKYDTNvgpYGKSLSGGQKQRIAIARA 1372
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 10947129 379 FYLQPKYAVLDEATSALTEE----VESELYRIGQQLGMTFISVGHR 420
Cdd:PTZ00265 1373 LLREPKILLLDEATSSLDSNseklIEKTIVDIKDKADKTIITIAHR 1418
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
245-419 |
1.02e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 44.85 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 245 IKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM---LTDFGPHGVL--------FLPQKPFFT---DGT 310
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFngqRIDTLSPGKLqalrrdiqFIFQDPYASldpRQT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 311 LREQVIYPLKEVYPDSGSADDERILRFLELAGLSNLVArtegldqqvdWNWYDVLSPGEMQRLSFARLFYLQPKYAVLDE 390
Cdd:PRK10261 420 VGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHA----------WRYPHEFSGGQRQRICIARALALNPKVIIADE 489
|
170 180 190
....*....|....*....|....*....|...
gi 10947129 391 ATSALTEEVESE----LYRIGQQLGMTFISVGH 419
Cdd:PRK10261 490 AVSALDVSIRGQiinlLLDLQRDFGIAYLFISH 522
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
243-420 |
1.10e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 44.77 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 243 PLI-KDLSLKISEGQSLLITGNTGTGKTSLL-------RVLGG-LWTSTRgsvqmltDFGPHGV-----LF--LPQKPFF 306
Cdd:PTZ00243 1323 PLVlRGVSFRIAPREKVGIVGRTGSGKSTLLltfmrmvEVCGGeIRVNGR-------EIGAYGLrelrrQFsmIPQDPVL 1395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 307 TDGTLREQViYPLKEvypdsgsADDERILRFLELAGLSNLVA-RTEGLDQQV---DWNWydvlSPGEMQRLSFAR-LFYL 381
Cdd:PTZ00243 1396 FDGTVRQNV-DPFLE-------ASSAEVWAALELVGLRERVAsESEGIDSRVlegGSNY----SVGQRQLMCMARaLLKK 1463
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 10947129 382 QPKYAVLDEATSalteEVESELYRIGQQLGM------TFISVGHR 420
Cdd:PTZ00243 1464 GSGFILMDEATA----NIDPALDRQIQATVMsafsayTVITIAHR 1504
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
241-419 |
2.45e-04 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 43.25 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 241 DKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGL--WTSTRGSV------------------------QMLTDFGP 294
Cdd:TIGR03269 12 GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpskvgepcpVCGGTLEP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 295 HGVLFL-PQKPFFTDGTLR--------------EQVIYPLKEVYPDSGSADDERILRFLELAGLSNLVARTEGLDQQvdw 359
Cdd:TIGR03269 92 EEVDFWnLSDKLRRRIRKRiaimlqrtfalygdDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSHRITHIARD--- 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 10947129 360 nwydvLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEE----VESELYRIGQQLGMTFISVGH 419
Cdd:TIGR03269 169 -----LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQtaklVHNALEEAVKASGISMVLTSH 227
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
245-419 |
2.66e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 42.46 E-value: 2.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 245 IKDLSLKISEGQSLLITGNTGTGKTSLLRV---LGGLWTSTR--GSVQMLTD--FGPH----------GVLFlpQKPFFT 307
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIPGFRveGKVTFHGKnlYAPDvdpvevrrriGMVF--QKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 308 DGTLREQVIYPLKeVYPDSGSADdERILRFLELAGLSNLVA---RTEGLDqqvdwnwydvLSPGEMQRLSFARLFYLQPK 384
Cdd:PRK14243 104 PKSIYDNIAYGAR-INGYKGDMD-ELVERSLRQAALWDEVKdklKQSGLS----------LSGGQQQRLCIARAIAVQPE 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 10947129 385 YAVLDEATSAL----TEEVESELYRIGQQlgMTFISVGH 419
Cdd:PRK14243 172 VILMDEPCSALdpisTLRIEELMHELKEQ--YTIIIVTH 208
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
240-417 |
5.00e-04 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 41.09 E-value: 5.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 240 SDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLwTSTRGSVQMLTDFGPHgvlflPQKPFFTdgTLREQVIYpl 319
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANR-TEGNVSVEGDIHYNGI-----PYKEFAE--KYPGEIIY-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 320 kevypdsGSADD--------ERILRFlelaglsnlVARTEGlDQQVdwnwyDVLSPGEMQRLSFARLFYLQPKYAVLDEA 391
Cdd:cd03233 88 -------VSEEDvhfptltvRETLDF---------ALRCKG-NEFV-----RGISGGERKRVSIAEALVSRASVLCWDNS 145
|
170 180 190
....*....|....*....|....*....|.
gi 10947129 392 T----SALTEEVESELYRIGQQLGMT-FISV 417
Cdd:cd03233 146 TrgldSSTALEILKCIRTMADVLKTTtFVSL 176
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
255-423 |
6.86e-04 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 41.01 E-value: 6.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 255 GQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQmltdFGPHGVLFLPQK--PFftdgtLREQV--IYPLKEVYPDSGSAD 330
Cdd:PRK10908 28 GEMAFLTGHSGAGKSTLLKLICGIERPSAGKIW----FSGHDITRLKNRevPF-----LRRQIgmIFQDHHLLMDRTVYD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 331 DERILRFLELAGLSNLVARTEGLDQQVDW-----NWYDVLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEVESELYR 405
Cdd:PRK10908 99 NVAIPLIIAGASGDDIRRRVSAALDKVGLldkakNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILR 178
|
170 180
....*....|....*....|.
gi 10947129 406 IGQQ---LGMTFISVGHRQSL 423
Cdd:PRK10908 179 LFEEfnrVGVTVLMATHDIGL 199
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
365-420 |
6.95e-04 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 41.93 E-value: 6.95e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 365 LSPGEMQRLSFARLFYLQPKYAVLDEATSALTE-EVESeLYRIGQQL---GMTFISVGHR 420
Cdd:COG1129 141 LSVAQQQLVEIARALSRDARVLILDEPTASLTErEVER-LFRIIRRLkaqGVAIIYISHR 199
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
240-422 |
7.82e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 40.91 E-value: 7.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 240 SDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLW-----TSTRGSVqmltDFGPH----------------GVL 298
Cdd:PRK14239 16 NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNdlnpeVTITGSI----VYNGHniysprtdtvdlrkeiGMV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 299 FLPQKPFftDGTLREQVIYPLKEvypdSGSADDERILRFLElaglsnlvartEGLDQQVDWN-----WYDV---LSPGEM 370
Cdd:PRK14239 92 FQQPNPF--PMSIYENVVYGLRL----KGIKDKQVLDEAVE-----------KSLKGASIWDevkdrLHDSalgLSGGQQ 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 10947129 371 QRLSFARLFYLQPKYAVLDEATSAL----TEEVESELYRIGQQLGMTFISVGHRQS 422
Cdd:PRK14239 155 QRVCIARVLATSPKIILLDEPTSALdpisAGKIEETLLGLKDDYTMLLVTRSMQQA 210
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
219-301 |
7.98e-04 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 41.55 E-value: 7.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 219 PAAEPADTAFLLERVSIsAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM----LTDFGP 294
Cdd:COG3845 249 APAEPGEVVLEVENLSV-RDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLdgedITGLSP 327
|
90
....*....|..
gi 10947129 295 -----HGVLFLP 301
Cdd:COG3845 328 rerrrLGVAYIP 339
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
365-416 |
8.41e-04 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 41.55 E-value: 8.41e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 10947129 365 LSPGEMQRLSFARLFYLQPKYAVLDEATSALT-EEVEsELYRIGQQL---GMT--FIS 416
Cdd:COG3845 142 LSVGEQQRVEILKALYRGARILILDEPTAVLTpQEAD-ELFEILRRLaaeGKSiiFIT 198
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
247-416 |
1.28e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.87 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 247 DLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQML---TDFGP------HGVLFLPQKpffTDGTLREQVI- 316
Cdd:PRK10982 16 NVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQgkeIDFKSskealeNGISMVHQE---LNLVLQRSVMd 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 317 ------YPLKEVYPDSGSADDERILRFLELaglsnlvarteglDQQVDWN-WYDVLSPGEMQRLSFARLFYLQPKYAVLD 389
Cdd:PRK10982 93 nmwlgrYPTKGMFVDQDKMYRDTKAIFDEL-------------DIDIDPRaKVATLSVSQMQMIEIAKAFSYNAKIVIMD 159
|
170 180 190
....*....|....*....|....*....|..
gi 10947129 390 EATSALTEEVESELYRIGQQL-----GMTFIS 416
Cdd:PRK10982 160 EPTSSLTEKEVNHLFTIIRKLkergcGIVYIS 191
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
245-419 |
4.36e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 38.95 E-value: 4.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 245 IKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQMLtdfgphGVLFLPQkpffTDGTLREQVIYPLKEvyP 324
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVM------GREVNAE----NEKWVRSKVGLVFQD--P 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10947129 325 D----SGSADDERIL--RFLELAGlSNLVARTEGLDQQVD-WNWYDV----LSPGEMQRLSFARLFYLQPKYAVLDEATS 393
Cdd:PRK13647 89 DdqvfSSTVWDDVAFgpVNMGLDK-DEVERRVEEALKAVRmWDFRDKppyhLSYGQKKRVAIAGVLAMDPDVIVLDEPMA 167
|
170 180 190
....*....|....*....|....*....|
gi 10947129 394 AL----TEEVESELYRIGQQlGMTFISVGH 419
Cdd:PRK13647 168 YLdprgQETLMEILDRLHNQ-GKTVIVATH 196
|
|
| |
