|
Name |
Accession |
Description |
Interval |
E-value |
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
124-335 |
3.14e-80 |
|
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: 241.67 E-value: 3.14e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 124 FLLEQVSISAPSsDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQMLTDfgpHGVLFLPQKPFFT 203
Cdd:cd03223 1 IELENLSLATPD-GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEG---EDLLFLPQRPYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 204 DGTLREQVIYPlkevypdsgsadderilrflelaglsnlvartegldqqvdwnWYDVLSPGEMQRLSFARLFYLQPKYAV 283
Cdd:cd03223 77 LGTLREQLIYP------------------------------------------WDDVLSGGEQQRLAFARLLLHKPKFVF 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1297598371 284 LDEATSALTEEVENELYRIGQQLGMTFISVGHRQSLEKFHSFVLKLCGGGRW 335
Cdd:cd03223 115 LDEATSALDEESEDRLYQLLKELGITVISVGHRPSLWKFHDRVLDLDGEGGW 166
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
12-340 |
1.46e-75 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 242.79 E-value: 1.46e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 12 NTFDYLGSILSYVVIAIPIFSGvygDLSPAELSTLVSknAFVciYLISCFTQLIDLSTTLSDVAGYTHRIGQLQETLLDM 91
Cdd:COG4178 273 TGYGQLAVIFPILVAAPRYFAG---EITLGGLMQAAS--AFG--QVQGALSWFVDNYQSLAEWRATVDRLAGFEEALEAA 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 92 SLKSQDCEILGESEwgldkasgwpaaepaDTAFLLEQVSISAPSsDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVL 171
Cdd:COG4178 346 DALPEAASRIETSE---------------DGALALEDLTLRTPD-GRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAI 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 172 GGLWTSTRGSVQMltdfgPHG--VLFLPQKPFFTDGTLREQVIYPLkevypDSGSADDERILRFLELAGLSNLVARtegL 249
Cdd:COG4178 410 AGLWPYGSGRIAR-----PAGarVLFLPQRPYLPLGTLREALLYPA-----TAEAFSDAELREALEAVGLGHLAER---L 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 250 DQQVDWNwyDVLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEVENELYR-IGQQL-GMTFISVGHRQSLEKFHSFVL 327
Cdd:COG4178 477 DEEADWD--QVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQlLREELpGTTVISVGHRSTLAAFHDRVL 554
|
330
....*....|...
gi 1297598371 328 KLCGGGRWELMRI 340
Cdd:COG4178 555 ELTGDGSWQLLPA 567
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
16-337 |
2.29e-60 |
|
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: 204.60 E-value: 2.29e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 16 YLGSILSYVVIAIPIFSGV---YGDLSPAELSTLVSKNAFVCIYLISCFTQLIDLSTTLSDVAGYTHRIGQLQETLLDMS 92
Cdd:TIGR00954 335 YTWSAVGLVAVSIPIFDKThpaFLEMSEEELMQEFYNNGRLLLKAADALGRLMLAGRDMTRLAGFTARVDTLLQVLDDVK 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 93 L----KSQDCEILGESEWG--LDKASGWPAAEPADTAFLLEQVSISAPSSDKpLIKDLSLKISEGQSLLITGNTGTGKTS 166
Cdd:TIGR00954 415 SgnfkRPRVEEIESGREGGrnSNLVPGRGIVEYQDNGIKFENIPLVTPNGDV-LIESLSFEVPSGNNLLICGPNGCGKSS 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 167 LLRVLGGLWtSTRGSVqmLTDFGPHGVLFLPQKPFFTDGTLREQVIYPL-KEVYPDSGSADDERIlRFLELAGLSNLVAR 245
Cdd:TIGR00954 494 LFRILGELW-PVYGGR--LTKPAKGKLFYVPQRPYMTLGTLRDQIIYPDsSEDMKRRGLSDKDLE-QILDNVQLTHILER 569
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 246 TEGLDQQVDWNwyDVLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEVENELYRIGQQLGMTFISVGHRQSLEKFHSF 325
Cdd:TIGR00954 570 EGGWSAVQDWM--DVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFGITLFSVSHRKSLWKYHEY 647
|
330
....*....|..
gi 1297598371 326 VLKLCGGGRWEL 337
Cdd:TIGR00954 648 LLYMDGRGGYQF 659
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
126-315 |
4.20e-31 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 116.45 E-value: 4.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 126 LEQVSISApsSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----QMLTDFGPHG----VLFLP 197
Cdd:COG4619 3 LEGLSFRV--GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIyldgKPLSAMPPPEwrrqVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 198 QKPFFTDGTLREQVIYPLKevyPDSGSADDERILRFLELAGLSNLVartegLDQQVDwnwydVLSPGEMQRLSFARLFYL 277
Cdd:COG4619 81 QEPALWGGTVRDNLPFPFQ---LRERKFDRERALELLERLGLPPDI-----LDKPVE-----RLSGGERQRLALIRALLL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1297598371 278 QPKYAVLDEATSAL----TEEVENELYRIGQQLGMTFISVGH 315
Cdd:COG4619 148 QPDVLLLDEPTSALdpenTRRVEELLREYLAEEGRAVLWVSH 189
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
12-319 |
1.49e-29 |
|
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: 119.17 E-value: 1.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 12 NTFDYLGSILSYVVIAIPIFSGVY----GDLSpaeLSTLVsknAFVCI--YLISCFTQLIDLSTTLSDVAGYTHRIGQLQ 85
Cdd:COG2274 379 NLLSTLSGLLQQLATVALLWLGAYlvidGQLT---LGQLI---AFNILsgRFLAPVAQLIGLLQRFQDAKIALERLDDIL 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 86 ETLLDmslksqdcEILGESEWGLDKASGwpaaepadtAFLLEQVSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKT 165
Cdd:COG2274 453 DLPPE--------REEGRSKLSLPRLKG---------DIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKS 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 166 SLLRVLGGLWTSTRGSVQM----LTDFGPH------GVlfLPQKPFFTDGTLREQVIYplkevypDSGSADDERILRFLE 235
Cdd:COG2274 516 TLLKLLLGLYEPTSGRILIdgidLRQIDPAslrrqiGV--VLQDVFLFSGTIRENITL-------GDPDATDEEIIEAAR 586
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 236 LAGLSNLVAR-TEGLDQQVDwNWYDVLSPGEMQRLSFARLFYLQPKYAVLDEATSAL---TEE-VENELYRIGQqlGMTF 310
Cdd:COG2274 587 LAGLHDFIEAlPMGYDTVVG-EGGSNLSGGQRQRLAIARALLRNPRILILDEATSALdaeTEAiILENLRRLLK--GRTV 663
|
....*....
gi 1297598371 311 ISVGHRQSL 319
Cdd:COG2274 664 IIIAHRLST 672
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
126-319 |
8.95e-29 |
|
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: 110.76 E-value: 8.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 126 LEQVSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM----LTDFGP----HGVLFLP 197
Cdd:cd03245 5 FRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLdgtdIRQLDPadlrRNIGYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 198 QKPFFTDGTLREQVIYplkevypDSGSADDERILRFLELAGLSNLVAR-TEGLDQQVDWNWYDvLSPGEMQRLSFARLFY 276
Cdd:cd03245 85 QDVTLFYGTLRDNITL-------GAPLADDERILRAAELAGVTDFVNKhPNGLDLQIGERGRG-LSGGQRQAVALARALL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1297598371 277 LQPKYAVLDEATSALTEEVENELYRIGQQL--GMTFISVGHRQSL 319
Cdd:cd03245 157 NDPPILLLDEPTSAMDMNSEERLKERLRQLlgDKTLIIITHRPSL 201
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
115-319 |
2.78e-26 |
|
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: 109.30 E-value: 2.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 115 PAAEPADTAFLLEQVSISAPSSDkPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM----LTDFGP 190
Cdd:TIGR02857 313 PVTAAPASSLEFSGVSVAYPGRR-PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVngvpLADADA 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 191 HG----VLFLPQKPFFTDGTLREQVIYPLKEvypdsgsADDERILRFLELAGLSNLV-ARTEGLDQQVDWNWYDvLSPGE 265
Cdd:TIGR02857 392 DSwrdqIAWVPQHPFLFAGTIAENIRLARPD-------ASDAEIREALERAGLDEFVaALPQGLDTPIGEGGAG-LSGGQ 463
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1297598371 266 MQRLSFARLFYLQPKYAVLDEATSALTEEVENELYRIGQQL--GMTFISVGHRQSL 319
Cdd:TIGR02857 464 AQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALaqGRTVLLVTHRLAL 519
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
126-319 |
2.81e-26 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 109.08 E-value: 2.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 126 LEQVSISAPSsDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----QMLTDFGPH----GVLFLP 197
Cdd:COG4988 339 LEDVSFSYPG-GRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSIlingVDLSDLDPAswrrQIAWVP 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 198 QKPFFTDGTLREQviypLKEVYPDsgsADDERILRFLELAGLSNLVAR-TEGLDQQVD---WNwydvLSPGEMQRLSFAR 273
Cdd:COG4988 418 QNPYLFAGTIREN----LRLGRPD---ASDEELEAALEAAGLDEFVAAlPDGLDTPLGeggRG----LSGGQAQRLALAR 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1297598371 274 LFYLQPKYAVLDEATSALTEEVENELYRIGQQL--GMTFISVGHRQSL 319
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 ... |
126-316 |
3.32e-25 |
|
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: 101.00 E-value: 3.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 126 LEQVSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM----LTDFGPH------GVLF 195
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVdgkdLTKLSLKelrrkvGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 196 lpQKP---FFTDgTLREQVIYPLkEVYPDSGSADDERILRFLELAGLSNLvartegldqqVDWNWYDvLSPGEMQRLSFA 272
Cdd:cd03225 82 --QNPddqFFGP-TVEEEVAFGL-ENLGLPEEEIEERVEEALELVGLEGL----------RDRSPFT-LSGGQKQRVAIA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1297598371 273 RLFYLQPKYAVLDEATSAL----TEEVENELYRIGQQlGMTFISVGHR 316
Cdd:cd03225 147 GVLAMDPDILLLDEPTAGLdpagRRELLELLKKLKAE-GKTIIIVTHD 193
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
126-319 |
4.56e-25 |
|
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: 99.38 E-value: 4.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 126 LEQVSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----QMLTDFGPHG----VLFLP 197
Cdd:cd03228 3 FKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEIlidgVDLRDLDLESlrknIAYVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 198 QKPFFTDGTLREqviyplkevypdsgsadderilrflelaglsNLvartegldqqvdwnwydvLSPGEMQRLSFARLFYL 277
Cdd:cd03228 83 QDPFLFSGTIRE-------------------------------NI------------------LSGGQRQRIAIARALLR 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1297598371 278 QPKYAVLDEATSAL---TE-EVENELYRIGQqlGMTFISVGHRQSL 319
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 ... |
126-319 |
2.15e-23 |
|
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: 94.98 E-value: 2.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 126 LEQVSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM---------LTDFGPHgVLFL 196
Cdd:cd03246 3 VENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLdgadisqwdPNELGDH-VGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 197 PQKPFFTDGTLREqviyplkevypdsgsadderilrflelaglsnlvartegldqqvdwnwyDVLSPGEMQRLSFARLFY 276
Cdd:cd03246 82 PQDDELFSGSIAE-------------------------------------------------NILSGGQRQRLGLARALY 112
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1297598371 277 LQPKYAVLDEATSALTEEVENELYRIGQQL---GMTFISVGHRQSL 319
Cdd:cd03246 113 GNPRILVLDEPNSHLDVEGERALNQAIAALkaaGATRIVIAHRPET 158
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
13-316 |
7.50e-23 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 99.47 E-value: 7.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 13 TFDYLGSILSYVVIAIPIFSGVY----GDLSPAELSTLVSknafvciYLISCFTQLIDLSTTLSDV---AGYTHRIGQLQ 85
Cdd:COG1132 246 LFFPLMELLGNLGLALVLLVGGLlvlsGSLTVGDLVAFIL-------YLLRLFGPLRQLANVLNQLqraLASAERIFELL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 86 ETLLDMSlksqdceilgesewglDKASGwPAAEPADTAFLLEQVSISAPSsDKPLIKDLSLKISEGQSLLITGNTGTGKT 165
Cdd:COG1132 319 DEPPEIP----------------DPPGA-VPLPPVRGEIEFENVSFSYPG-DRPVLKDISLTIPPGETVALVGPSGSGKS 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 166 SLLRVLGGLWTSTRGSVQM----LTDFGPHG----VLFLPQKPFFTDGTLREQVIYPLKEvypdsgsADDERILRFLELA 237
Cdd:COG1132 381 TLVNLLLRFYDPTSGRILIdgvdIRDLTLESlrrqIGVVPQDTFLFSGTIRENIRYGRPD-------ATDEEVEEAAKAA 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 238 GLSNLVAR-TEGLDQQVDWNWYDvLSPGEMQRLSFARLFYLQPKYAVLDEATSAL---TE-EVENELYRIGQqlGMTFIS 312
Cdd:COG1132 454 QAHEFIEAlPDGYDTVVGERGVN-LSGGQRQRIAIARALLKDPPILILDEATSALdteTEaLIQEALERLMK--GRTTIV 530
|
....
gi 1297598371 313 VGHR 316
Cdd:COG1132 531 IAHR 534
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
137-332 |
1.78e-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: 1.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 137 DKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQmltdFGPHGVLFLPQKPfftdgtLREQVIYplk 216
Cdd:cd00267 11 GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEIL----IDGKDIAKLPLEE------LRRRIGY--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 217 evypdsgsadderilrflelaglsnlvartegLDQqvdwnwydvLSPGEMQRLSFARLFYLQPKYAVLDEATSAL----T 292
Cdd:cd00267 78 --------------------------------VPQ---------LSGGQRQRVALARALLLNPDLLLLDEPTSGLdpasR 116
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1297598371 293 EEVENELYRIGQQlGMTFISVGHRQSL-EKFHSFVLKLCGG 332
Cdd:cd00267 117 ERLLELLRELAEE-GRTVIIVTHDPELaELAADRVIVLKDG 156
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
141-289 |
7.34e-21 |
|
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: 87.32 E-value: 7.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 141 IKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQ-----MLTDFGPH---GVLFLPQKP-FFTDGTLREQV 211
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILldgqdLTDDERKSlrkEIGYVFQDPqLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1297598371 212 IYPLKEVYPDSgSADDERILRFLELAGLSNLVARTEGldqqvdwNWYDVLSPGEMQRLSFARLFYLQPKYAVLDEATS 289
Cdd:pfam00005 81 RLGLLLKGLSK-REKDARAEEALEKLGLGDLADRPVG-------ERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
136-318 |
8.10e-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: 89.59 E-value: 8.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 136 SDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGsvQMLTDFGP----------HGVLFLPQKPFFTDG 205
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKG--QILIDGIDirdisrkslrSMIGVVLQDTFLFSG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 206 TLREQVIYplkevypDSGSADDERILRFLELAGLSNLVAR-TEGLDQQVDWNWyDVLSPGEMQRLSFARLFYLQPKYAVL 284
Cdd:cd03254 92 TIMENIRL-------GRPNATDEEVIEAAKEAGAHDFIMKlPNGYDTVLGENG-GNLSQGERQLLAIARAMLRDPKILIL 163
|
170 180 190
....*....|....*....|....*....|....*...
gi 1297598371 285 DEATSAL---TEE-VENELYRIGQqlGMTFISVGHRQS 318
Cdd:cd03254 164 DEATSNIdteTEKlIQEALEKLMK--GRTSIIIAHRLS 199
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
138-332 |
6.73e-20 |
|
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: 86.77 E-value: 6.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 138 KPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV------------QMLTDFGPHGVLFLPQK----PF 201
Cdd:cd03255 17 VQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVrvdgtdisklseKELAAFRRRHIGFVFQSfnllPD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 202 FtdgTLREQVIYPLkEVYPDSGSADDERILRFLELAGLSNLvartegLDQQVDWnwydvLSPGEMQRLSFARLFYLQPKY 281
Cdd:cd03255 97 L---TALENVELPL-LLAGVPKKERRERAEELLERVGLGDR------LNHYPSE-----LSGGQQQRVAIARALANDPKI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1297598371 282 AVLDEATSAL----TEEVENELYRIGQQLGMTFISVGHRQSLEKFHSFVLKLCGG 332
Cdd:cd03255 162 ILADEPTGNLdsetGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDG 216
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
137-318 |
2.70e-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: 2.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 137 DKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----QMLTDFGPH----GVLFlpQK-PFFTDGTL 207
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEIlldgKDITNLPPHkrpvNTVF--QNyALFPHLTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 208 REQVIYPLKeVYPDSGSADDERILRFLELAGLSNLVARTEgldqqvdwnwyDVLSPGEMQRLSFARLFYLQPKYAVLDEA 287
Cdd:cd03300 90 FENIAFGLR-LKKLPKAEIKERVAEALDLVQLEGYANRKP-----------SQLSGGQQQRVAIARALVNEPKVLLLDEP 157
|
170 180 190
....*....|....*....|....*....|....*
gi 1297598371 288 TSALT----EEVENELYRIGQQLGMTFISVGHRQS 318
Cdd:cd03300 158 LGALDlklrKDMQLELKRLQKELGITFVFVTHDQE 192
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
137-291 |
5.25e-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: 83.68 E-value: 5.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 137 DKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV--------QMLTDFGPHgVLFLPQKPFFTDG-TL 207
Cdd:COG4133 14 ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVlwngepirDAREDYRRR-LAYLGHADGLKPElTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 208 REQVIYpLKEVYPDSGSADD-ERILRFLELAGLSNLVARTegldqqvdwnwydvLSPGEMQRLSFARLFYLQPKYAVLDE 286
Cdd:COG4133 93 RENLRF-WAALYGLRADREAiDEALEAVGLAGLADLPVRQ--------------LSAGQKRRVALARLLLSPAPLWLLDE 157
|
....*
gi 1297598371 287 ATSAL 291
Cdd:COG4133 158 PFTAL 162
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
126-318 |
5.89e-19 |
|
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: 83.72 E-value: 5.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 126 LEQVSISAPSsdKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----QMLTDFGPH--GVLFLPQK 199
Cdd:cd03259 3 LKGLSKTYGS--VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEIlidgRDVTGVPPErrNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 200 P-FFTDGTLREQVIYPLKEVYPDSGSAdDERILRFLELAGLSNLVARtegldqqvdwnWYDVLSPGEMQRLSFARLFYLQ 278
Cdd:cd03259 81 YaLFPHLTVAENIAFGLKLRGVPKAEI-RARVRELLELVGLEGLLNR-----------YPHELSGGQQQRVALARALARE 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1297598371 279 PKYAVLDEATSAL----TEEVENELYRIGQQLGMTFISVGHRQS 318
Cdd:cd03259 149 PSLLLLDEPLSALdaklREELREELKELQRELGITTIYVTHDQE 192
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
126-315 |
6.58e-19 |
|
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: 83.74 E-value: 6.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 126 LEQVSISApsSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQML---TDFGPHGVLFLPQKPFF 202
Cdd:cd03235 2 VEDLTVSY--GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFgkpLEKERKRIGYVPQRRSI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 203 -TD--GTLREQV---IYPLKEVYPDSGSADDERILRFLELAGLSNLVARTegLDQqvdwnwydvLSPGEMQRLSFARLFY 276
Cdd:cd03235 80 dRDfpISVRDVVlmgLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQ--IGE---------LSGGQQQRVLLARALV 148
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1297598371 277 LQPKYAVLDEATSALTEEVENELYRIGQQL---GMTFISVGH 315
Cdd:cd03235 149 QDPDLLLLDEPFAGVDPKTQEDIYELLRELrreGMTILVVTH 190
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
141-315 |
1.35e-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: 1.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 141 IKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM----LTDFGP--HGVLFLPQ-KPFFTDGTLREQVIY 213
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLngkdITNLPPekRDISYVPQnYALFPHMTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 214 PLKEVYPDSgSADDERILRFLELAGLSNLVARTEGldqqvdwnwydVLSPGEMQRLSFARLFYLQPKYAVLDEATSAL-- 291
Cdd:cd03299 95 GLKKRKVDK-KEIERKVLEIAEMLGIDHLLNRKPE-----------TLSGGEQQRVAIARALVVNPKILLLDEPFSALdv 162
|
170 180
....*....|....*....|....*.
gi 1297598371 292 --TEEVENELYRIGQQLGMTFISVGH 315
Cdd:cd03299 163 rtKEKLREELKKIRKEFGVTVLHVTH 188
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
126-315 |
3.45e-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: 3.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 126 LEQVS--ISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----QMLTDFGPHGVLFLPQK 199
Cdd:cd03258 4 LKNVSkvFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVlvdgTDLTLLSGKELRKARRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 200 --------PFFTDGTLREQVIYPLkEVYPDSGSADDERILRFLELAGLSNlvaRTEGLDQQvdwnwydvLSPGEMQRLSF 271
Cdd:cd03258 84 igmifqhfNLLSSRTVFENVALPL-EIAGVPKAEIEERVLELLELVGLED---KADAYPAQ--------LSGGQKQRVGI 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1297598371 272 ARLFYLQPKYAVLDEATSAL----TEEVENELYRIGQQLGMTFISVGH 315
Cdd:cd03258 152 ARALANNPKVLLCDEATSALdpetTQSILALLRDINRELGLTIVLITH 199
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
19-299 |
5.36e-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: 84.72 E-value: 5.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 19 SILSYVVIAIPIFSGvyGDLSPAELSTLVsknaFVCIYLISCFTQLIDLSTTLSDVAGYTHRIGQLQETLLDMSLKSQdc 98
Cdd:TIGR02868 251 AVLGALWAGGPAVAD--GRLAPVTLAVLV----LLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVLDAAGPVAEGSA-- 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 99 eilgesewgldkasgwPAAEPA---DTAFLLEQVSISAPSsDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLW 175
Cdd:TIGR02868 323 ----------------PAAGAVglgKPTLELRDLSAGYPG-APPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLL 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 176 TSTRGSVqMLTDFGPHG---------VLFLPQKPFFTDGTLREQVIYPLKEvypdsgsADDERILRFLELAGLSNLVART 246
Cdd:TIGR02868 386 DPLQGEV-TLDGVPVSSldqdevrrrVSVCAQDAHLFDTTVRENLRLARPD-------ATDEELWAALERVGLADWLRAL 457
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1297598371 247 -EGLDQQVDWNWyDVLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEVENEL 299
Cdd:TIGR02868 458 pDGLDTVLGEGG-ARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADEL 510
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
126-318 |
5.87e-18 |
|
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: 5.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 126 LEQVSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM----LTDFGPHG----VLFLP 197
Cdd:cd03251 3 FKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIdghdVRDYTLASlrrqIGLVS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 198 QKPFFTDGTLREQVIYPLKEvypdsgsADDERILRFLELAGLSNLVART-EGLDQQVDWNWYDvLSPGEMQRLSFARLFY 276
Cdd:cd03251 83 QDVFLFNDTVAENIAYGRPG-------ATREEVEEAARAANAHEFIMELpEGYDTVIGERGVK-LSGGQRQRIAIARALL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1297598371 277 LQPKYAVLDEATSALTEEVENELYRIGQQL--GMTFISVGHRQS 318
Cdd:cd03251 155 KDPPILILDEATSALDTESERLVQAALERLmkNRTTFVIAHRLS 198
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
137-315 |
5.91e-18 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 81.46 E-value: 5.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 137 DKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTST-----------RGSVQMLTDFGPH------GVLFlpQK 199
Cdd:cd03260 12 DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdegevllDGKDIYDLDVDVLelrrrvGMVF--QK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 200 PFFTDGTLREQVIYPLKEVYPDSGSADDERILRFLELAGLSNLVA-RTEGLDqqvdwnwydvLSPGEMQRLSFARLFYLQ 278
Cdd:cd03260 90 PNPFPGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKdRLHALG----------LSGGQQQRLCLARALANE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1297598371 279 PKYAVLDEATSAL----TEEVENELYRIGQQlgMTFISVGH 315
Cdd:cd03260 160 PEVLLLDEPTSALdpisTAKIEELIAELKKE--YTIVIVTH 198
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
17-318 |
6.19e-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: 81.69 E-value: 6.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 17 LGSILSYVVIAIPIFSGVYGDLSPAELSTLvsknafvciylISCFTQLIDLSTTLSDVAGYTHRIGQLQETLldmslksq 96
Cdd:TIGR02203 247 IASLALAVVLFIALFQAQAGSLTAGDFTAF-----------ITAMIALIRPLKSLTNVNAPMQRGLAAAESL-------- 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 97 dCEILGESEwglDKASGWPAAEPADTAFLLEQVSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWT 176
Cdd:TIGR02203 308 -FTLLDSPP---EKDTGTRAIERARGDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 177 STRGSVQM---------LTDFGPHgVLFLPQKPFFTDGTLREQViyplkeVYPDSGSADDERILRFLELAGLSNLVART- 246
Cdd:TIGR02203 384 PDSGQILLdghdladytLASLRRQ-VALVSQDVVLFNDTIANNI------AYGRTEQADRAEIERALAAAYAQDFVDKLp 456
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1297598371 247 EGLDQQVDWNWyDVLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEVENELYRIGQQL--GMTFISVGHRQS 318
Cdd:TIGR02203 457 LGLDTPIGENG-VLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLmqGRTTLVIAHRLS 529
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
137-315 |
6.35e-17 |
|
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: 78.70 E-value: 6.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 137 DKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM----LTDFGPH---------GVLFlpQKP-FF 202
Cdd:cd03261 12 GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIdgedISGLSEAelyrlrrrmGMLF--QSGaLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 203 TDGTLREQVIYPLKEVYPDSGSADDERILRFLELAGLSnlvartegldQQVDwnwydvLSPGE----MQ-RLSFARLFYL 277
Cdd:cd03261 90 DSLTVFENVAFPLREHTRLSEEEIREIVLEKLEAVGLR----------GAED------LYPAElsggMKkRVALARALAL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1297598371 278 QPKYAVLDEATSAL----TEEVENELYRIGQQLGMTFISVGH 315
Cdd:cd03261 154 DPELLLYDEPTAGLdpiaSGVIDDLIRSLKKELGLTSIMVTH 195
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
117-317 |
7.55e-17 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 80.38 E-value: 7.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 117 AEPADTAFLLEQVSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----QMLTDFGPHg 192
Cdd:PRK09452 6 KQPSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRImldgQDITHVPAE- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 193 vlflpQKP---------FFTDGTLREQVIYPLK-------EVYPdsgsaddeRILRFLELAGLSNLVARTEgldQQvdwn 256
Cdd:PRK09452 85 -----NRHvntvfqsyaLFPHMTVFENVAFGLRmqktpaaEITP--------RVMEALRMVQLEEFAQRKP---HQ---- 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1297598371 257 wydvLSPGEMQRLSFARLFYLQPKYAVLDEATSALT----EEVENELYRIGQQLGMTFISVGHRQ 317
Cdd:PRK09452 145 ----LSGGQQQRVAIARAVVNKPKVLLLDESLSALDyklrKQMQNELKALQRKLGITFVFVTHDQ 205
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
127-316 |
1.14e-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: 77.53 E-value: 1.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 127 EQVSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM----LTDFGPHgVL-----FLP 197
Cdd:cd03244 6 KNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIdgvdISKIGLH-DLrsrisIIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 198 QKPFFTDGTLREQvIYPLKEvypdsgsADDERILRFLELAGLSNLV-ARTEGLDQQVDWNWyDVLSPGEMQRLSFARLFY 276
Cdd:cd03244 85 QDPVLFSGTIRSN-LDPFGE-------YSDEELWQALERVGLKEFVeSLPGGLDTVVEEGG-ENLSVGQRQLLCLARALL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1297598371 277 LQPKYAVLDEATSALTEEVENELyrigQQL------GMTFISVGHR 316
Cdd:cd03244 156 RKSKILVLDEATASVDPETDALI----QKTireafkDCTVLTIAHR 197
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
138-322 |
1.34e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 77.69 E-value: 1.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 138 KPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSvqmltdfgphGVLFLPQKPFFTDGTLREQViyplke 217
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVA----------GCVDVPDNQFGREASLIDAI------ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 218 vyPDSGSADDerILRFLELAGLS---NLVARtegldqqvdwnwYDVLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEE 294
Cdd:COG2401 107 --GRKGDFKD--AVELLNAVGLSdavLWLRR------------FKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
170 180 190
....*....|....*....|....*....|..
gi 1297598371 295 VENELYRIGQQL----GMTFISVGHRQSLEKF 322
Cdd:COG2401 171 TAKRVARNLQKLarraGITLVVATHHYDVIDD 202
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
129-315 |
1.68e-16 |
|
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: 77.55 E-value: 1.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 129 VSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV------------QMLTDFGpHGVLFL 196
Cdd:cd03257 9 VSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIifdgkdllklsrRLRKIRR-KEIQMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 197 PQKPF------FTdgtLREQVIYPLKEVYPDSGSAD-DERILRFLELAGLSNLVAR---TEgldqqvdwnwydvLSPGEM 266
Cdd:cd03257 88 FQDPMsslnprMT---IGEQIAEPLRIHGKLSKKEArKEAVLLLLVGVGLPEEVLNrypHE-------------LSGGQR 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1297598371 267 QRLSFARLFYLQPKYAVLDEATSAL---TE-EVENELYRIGQQLGMTFISVGH 315
Cdd:cd03257 152 QRVAIARALALNPKLLIADEPTSALdvsVQaQILDLLKKLQEELGLTLLFITH 204
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
129-319 |
1.96e-16 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 80.15 E-value: 1.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 129 VSISAPS-SDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----QMLTDFGPH----GVLFLPQK 199
Cdd:TIGR00958 484 VSFSYPNrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVlldgVPLVQYDHHylhrQVALVGQE 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 200 PFFTDGTLREQVIYPLKevypdsgSADDERILRFLELAGLSNLVAR-TEGLDQQVDWNWyDVLSPGEMQRLSFARLFYLQ 278
Cdd:TIGR00958 564 PVLFSGSVRENIAYGLT-------DTPDEEIMAAAKAANAHDFIMEfPNGYDTEVGEKG-SQLSGGQKQRIAIARALVRK 635
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1297598371 279 PKYAVLDEATSALTEEVENELYRIGQQLGMTFISVGHRQSL 319
Cdd:TIGR00958 636 PRVLILDEATSALDAECEQLLQESRSRASRTVLLIAHRLST 676
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
108-312 |
4.69e-16 |
|
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: 78.79 E-value: 4.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 108 LDKASGWPAAEPADTAFLLE--QVSIS---APSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV 182
Cdd:COG1123 243 LGAARGRAAPAAAAAEPLLEvrNLSKRypvRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSI 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 183 QM------------LTDFGPH-GVLFlpQKP---FFTDGTLREQVIYPLKEVYPDSGSADDERILRFLELAGLSNLVArt 246
Cdd:COG1123 323 LFdgkdltklsrrsLRELRRRvQMVF--QDPyssLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPDLA-- 398
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1297598371 247 egldqqvdwNWY-DVLSPGEMQRLSFARLFYLQPKYAVLDEATSAL----TEEVENELYRIGQQLGMT--FIS 312
Cdd:COG1123 399 ---------DRYpHELSGGQRQRVAIARALALEPKLLILDEPTSALdvsvQAQILNLLRDLQRELGLTylFIS 462
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
126-315 |
5.42e-16 |
|
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: 75.97 E-value: 5.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 126 LEQVSISAPSSDKPL--IKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM----LTDFGPH-GVLF--- 195
Cdd:cd03293 3 VRNVSKTYGGGGGAVtaLEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVdgepVTGPGPDrGYVFqqd 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 196 --LPQKpfftdgTLREQVIYPLKEVYPDSGSAdDERILRFLELAGLSNLVARtegldqqvdwnWYDVLSPGEMQRLSFAR 273
Cdd:cd03293 83 alLPWL------TVLDNVALGLELQGVPKAEA-RERAEELLELVGLSGFENA-----------YPHQLSGGMRQRVALAR 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1297598371 274 LFYLQPKYAVLDEATSAL---T-EEVENELYRIGQQLGMTFISVGH 315
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALdalTrEQLQEELLDIWRETGKTVLLVTH 190
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
137-318 |
1.81e-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: 74.83 E-value: 1.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 137 DKPLI-KDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVqmLTDfGPHGVLFLPQkpfftdgTLREQVIYPL 215
Cdd:cd03252 13 DGPVIlDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRV--LVD-GHDLALADPA-------WLRRQVGVVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 216 KEVYPDSGSADD-----------ERILRFLELAGLSNLVART-EGLDQQVDWNWYDvLSPGEMQRLSFARLFYLQPKYAV 283
Cdd:cd03252 83 QENVLFNRSIRDnialadpgmsmERVIEAAKLAGAHDFISELpEGYDTIVGEQGAG-LSGGQRQRIAIARALIHNPRILI 161
|
170 180 190
....*....|....*....|....*....|....*..
gi 1297598371 284 LDEATSALTEEVENELYRIGQQL--GMTFISVGHRQS 318
Cdd:cd03252 162 FDEATSALDYESEHAIMRNMHDIcaGRTVIIIAHRLS 198
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
126-316 |
1.91e-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: 1.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 126 LEQVSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTST---RGSV----QMLTDFGPHG----VL 194
Cdd:COG1123 7 VRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVlldgRDLLELSEALrgrrIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 195 FLPQKPF--FTDGTLREQVIYPLkEVYPDSGSADDERILRFLELAGLSNLVARtegldqqvdwnwY-DVLSPGEMQRLSF 271
Cdd:COG1123 87 MVFQDPMtqLNPVTVGDQIAEAL-ENLGLSRAEARARVLELLEAVGLERRLDR------------YpHQLSGGQRQRVAI 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1297598371 272 ARLFYLQPKYAVLDEATSAL----TEEVENELYRIGQQLGMTFISVGHR 316
Cdd:COG1123 154 AMALALDPDLLIADEPTTALdvttQAEILDLLRELQRERGTTVLLITHD 202
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
137-317 |
2.55e-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: 2.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 137 DKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----QMLTDFGPH----GVLF-----LPQKpfft 203
Cdd:cd03301 12 NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIyiggRDVTDLPPKdrdiAMVFqnyalYPHM---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 204 dgTLREQVIYPLKeVYPDSGSADDERILRFLELAGLSNLvartegLDQQVdwnwyDVLSPGEMQRLSFARLFYLQPKYAV 283
Cdd:cd03301 88 --TVYDNIAFGLK-LRKVPKDEIDERVREVAELLQIEHL------LDRKP-----KQLSGGQRQRVALGRAIVREPKVFL 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 1297598371 284 LDEATSALT----EEVENELYRIGQQLGMTFISVGHRQ 317
Cdd:cd03301 154 MDEPLSNLDaklrVQMRAELKRLQQRLGTTTIYVTHDQ 191
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
126-322 |
3.16e-15 |
|
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: 72.73 E-value: 3.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 126 LEQVSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM-------LTDFGPHGVLFLPQ 198
Cdd:cd03247 3 INNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLdgvpvsdLEKALSSLISVLNQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 199 KPFFTDGTLREqviyplkevypdsgsadderilrflelaglsNLVARtegldqqvdwnwydvLSPGEMQRLSFARLFYLQ 278
Cdd:cd03247 83 RPYLFDTTLRN-------------------------------NLGRR---------------FSGGERQRLALARILLQD 116
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1297598371 279 PKYAVLDEATSALTEEVENELYR-IGQQL-GMTFISVGHR-QSLEKF 322
Cdd:cd03247 117 APIVLLDEPTVGLDPITERQLLSlIFEVLkDKTLIWITHHlTGIEHM 163
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
137-318 |
3.97e-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: 3.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 137 DKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM---------LTDFGPH-GVLflPQK-PFFTDg 205
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIdgqdirevtLDSLRRAiGVV--PQDtVLFND- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 206 TLREQVIYplkevypdsG--SADDERILRFLELAGLSNLVAR-TEGLDQQV-DWNWYdvLSPGEMQRLSFARLFYLQPKY 281
Cdd:cd03253 90 TIGYNIRY---------GrpDATDEEVIEAAKAAQIHDKIMRfPDGYDTIVgERGLK--LSGGEKQRVAIARAILKNPPI 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 1297598371 282 AVLDEATSALTEEVENELYRIGQQL--GMTFISVGHRQS 318
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAALRDVskGRTTIVIAHRLS 197
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
121-315 |
4.13e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 74.05 E-value: 4.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 121 DTAFLLEQVSISAPssDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----QMLTDFGPHG---- 192
Cdd:PRK10575 9 DTTFALRNVSFRVP--GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEIlldaQPLESWSSKAfark 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 193 VLFLPQKPFFTDG-TLREQVI---YPLKEVYPDSGSADDERILRFLELAGLSNLVARTegldqqvdwnwYDVLSPGEMQR 268
Cdd:PRK10575 87 VAYLPQQLPAAEGmTVRELVAigrYPWHGALGRFGAADREKVEEAISLVGLKPLAHRL-----------VDSLSGGERQR 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1297598371 269 LSFARLFYLQPKYAVLDEATSAL----TEEVENELYRIGQQLGMTFISVGH 315
Cdd:PRK10575 156 AWIAMLVAQDSRCLLLDEPTSALdiahQVDVLALVHRLSQERGLTVIAVLH 206
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
126-318 |
7.44e-15 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 72.96 E-value: 7.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 126 LEQVSISAPS-SDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----QMLTDFGPHGVL----FL 196
Cdd:cd03249 3 FKNVSFRYPSrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEIlldgVDIRDLNLRWLRsqigLV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 197 PQKPFFTDGTLREQVIYPLKevypdsgSADDERILRFLELAGLSNLVAR-TEGLDQQVDWNwYDVLSPGEMQRLSFARLF 275
Cdd:cd03249 83 SQEPVLFDGTIAENIRYGKP-------DATDEEVEEAAKKANIHDFIMSlPDGYDTLVGER-GSQLSGGQKQRIAIARAL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1297598371 276 YLQPKYAVLDEATSALTEEVENELYRIGQQL--GMTFISVGHRQS 318
Cdd:cd03249 155 LRNPKILLLDEATSALDAESEKLVQEALDRAmkGRTTIVIAHRLS 199
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
137-318 |
2.23e-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: 73.21 E-value: 2.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 137 DKPLIKDLSLKISEGQ--SLLitGNTGTGKTSLLRVLGGLWTSTRGSV----QMLTDFGPH----GVLFlpQK----PFF 202
Cdd:COG3842 17 DVTALDDVSLSIEPGEfvALL--GPSGCGKTTLLRMIAGFETPDSGRIlldgRDVTGLPPEkrnvGMVF--QDyalfPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 203 tdgTLREQVIYPLKeVYPDSGSADDERILRFLELAGLSNLVAR--TEgldqqvdwnwydvLSPGEMQRLSFARLFYLQPK 280
Cdd:COG3842 93 ---TVAENVAFGLR-MRGVPKAEIRARVAELLELVGLEGLADRypHQ-------------LSGGQQQRVALARALAPEPR 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1297598371 281 YAVLDEATSAL----TEEVENELYRIGQQLGMTFISVGHRQS 318
Cdd:COG3842 156 VLLLDEPLSALdaklREEMREELRRLQRELGITFIYVTHDQE 197
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
140-291 |
3.00e-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: 70.75 E-value: 3.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 140 LIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQMLTDFGPHGVL-----FLPQKP---FFTDgTLREQV 211
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERrksigYVMQDVdyqLFTD-SVREEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 212 IYPLKEvyPDSGSADDERILRFLELAGLsnlvartegldqqVDWNWYDvLSPGEMQRLSFARLFYLQPKYAVLDEATSAL 291
Cdd:cd03226 94 LLGLKE--LDAGNEQAETVLKDLDLYAL-------------KERHPLS-LSGGQKQRLAIAAALLSGKDLLIFDEPTSGL 157
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
109-322 |
4.20e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 72.94 E-value: 4.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 109 DKASGWPAAEPAdtaFLLEQVSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM---- 184
Cdd:PRK11160 327 PTTSTAAADQVS---LTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLngqp 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 185 LTDFGP----HGVLFLPQKPFFTDGTLREQviypLKEVYPDsgsADDERILRFLELAGLSNLVARTEGLDQqvdwnWYD- 259
Cdd:PRK11160 404 IADYSEaalrQAISVVSQRVHLFSATLRDN----LLLAAPN---ASDEALIEVLQQVGLEKLLEDDKGLNA-----WLGe 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1297598371 260 ---VLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEVENELYRIGQQL--GMTFISVGHR-QSLEKF 322
Cdd:PRK11160 472 ggrQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHaqNKTVLMITHRlTGLEQF 540
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
132-316 |
9.26e-14 |
|
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: 69.04 E-value: 9.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 132 SAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQMltdfgPHGVLFLPQKPFFTDGTLREQV 211
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV-----PGSIAYVSQEPWIQNGTIRENI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 212 I--YPLkevypdsgsaDDERILRFLELAGLSNLVARTEGLDQQVdwnwydV------LSPGEMQRLSFARLFYLQPKYAV 283
Cdd:cd03250 87 LfgKPF----------DEERYEKVIKACALEPDLEILPDGDLTE------IgekginLSGGQKQRISLARAVYSDADIYL 150
|
170 180 190
....*....|....*....|....*....|....*..
gi 1297598371 284 LDEATSALTEEVENELYR--IGQQL--GMTFISVGHR 316
Cdd:cd03250 151 LDDPLSAVDAHVGRHIFEncILGLLlnNKTRILVTHQ 187
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
126-315 |
9.87e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 70.43 E-value: 9.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 126 LEQVSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQMltdFGPH-------------G 192
Cdd:PRK13635 8 VEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITV---GGMVlseetvwdvrrqvG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 193 VLFlpQKP--FFTDGTLREQVIYPLKevypDSGSADDERILRFLELAglsNLVARTEGLDQQVDwnwydVLSPGEMQRLS 270
Cdd:PRK13635 85 MVF--QNPdnQFVGATVQDDVAFGLE----NIGVPREEMVERVDQAL---RQVGMEDFLNREPH-----RLSGGQKQRVA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1297598371 271 FARLFYLQPKYAVLDEATSALT----EEVENELYRIGQQLGMTFISVGH 315
Cdd:PRK13635 151 IAGVLALQPDIIILDEATSMLDprgrREVLETVRQLKEQKGITVLSITH 199
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
137-315 |
2.63e-13 |
|
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: 68.47 E-value: 2.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 137 DKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----QMLTDFGPH---------GVLF----Lpqk 199
Cdd:COG1127 17 DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEIlvdgQDITGLSEKelyelrrriGMLFqggaL--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 200 pfFTDGTLREQVIYPLKEVYPDSGSADDERILRFLELAGLSNlvARTegldqqvdwnwydvLSPGE----MQ-RLSFARL 274
Cdd:COG1127 94 --FDSLTVFENVAFPLREHTDLSEAEIRELVLEKLELVGLPG--AAD--------------KMPSElsggMRkRVALARA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1297598371 275 FYLQPKYAVLDEATSAL----TEEVENELYRIGQQLGMTFISVGH 315
Cdd:COG1127 156 LALDPEILLYDEPTAGLdpitSAVIDELIRELRDELGLTSVVVTH 200
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
142-315 |
2.89e-13 |
|
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: 68.09 E-value: 2.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 142 KDLSLKIS---EGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----------QMLTDFGPH----GVLFlPQKPFFTD 204
Cdd:cd03297 11 PDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIvlngtvlfdsRKKINLPPQqrkiGLVF-QQYALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 205 GTLREQVIYPLKEVypdSGSADDERILRFLELAGLSNLVARteGLDQqvdwnwydvLSPGEMQRLSFARLFYLQPKYAVL 284
Cdd:cd03297 90 LNVRENLAFGLKRK---RNREDRISVDELLDLLGLDHLLNR--YPAQ---------LSGGEKQRVALARALAAQPELLLL 155
|
170 180 190
....*....|....*....|....*....|....*
gi 1297598371 285 DEATSAL----TEEVENELYRIGQQLGMTFISVGH 315
Cdd:cd03297 156 DEPFSALdralRLQLLPELKQIKKNLNIPVIFVTH 190
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
139-318 |
3.40e-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: 68.13 E-value: 3.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 139 PLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----QMLTDFGPH--GVLFLPQK-PFFTDGTLREQV 211
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTIlfggEDATDVPVQerNVGFVFQHyALFRHMTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 212 IYPLKeVYPDSGSAD----DERILRFLELAGLSNLVARtegldqqvdwnWYDVLSPGEMQRLSFARLFYLQPKYAVLDEA 287
Cdd:cd03296 96 AFGLR-VKPRSERPPeaeiRAKVHELLKLVQLDWLADR-----------YPAQLSGGQRQRVALARALAVEPKVLLLDEP 163
|
170 180 190
....*....|....*....|....*....|....*
gi 1297598371 288 TSALTEEVENEL----YRIGQQLGMTFISVGHRQS 318
Cdd:cd03296 164 FGALDAKVRKELrrwlRRLHDELHVTTVFVTHDQE 198
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
137-315 |
3.45e-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: 66.83 E-value: 3.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 137 DKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQML-TDFGPHGVLFLPQKP----FFTDGTLreqv 211
Cdd:cd03229 12 QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDgEDLTDLEDELPPLRRrigmVFQDFAL---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 212 iYPLKEVYpdsgsadderilrflelaglSNLVARtegldqqvdwnwydvLSPGEMQRLSFARLFYLQPKYAVLDEATSAL 291
Cdd:cd03229 88 -FPHLTVL--------------------ENIALG---------------LSGGQQQRVALARALAMDPDVLLLDEPTSAL 131
|
170 180
....*....|....*....|....*...
gi 1297598371 292 ----TEEVENELYRIGQQLGMTFISVGH 315
Cdd:cd03229 132 dpitRREVRALLKSLQAQLGITVVLVTH 159
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
137-315 |
3.70e-13 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 68.20 E-value: 3.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 137 DKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGS--VQMLTDFGPH----------GVLFlPQKPFFTD 204
Cdd:PRK09493 13 PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDliVDGLKVNDPKvderlirqeaGMVF-QQFYLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 205 GTLREQVIYPLKEVYpDSGSADDERILRflELAGLSNLVARTEGLDQQvdwnwydvLSPGEMQRLSFARLFYLQPKYAVL 284
Cdd:PRK09493 92 LTALENVMFGPLRVR-GASKEEAEKQAR--ELLAKVGLAERAHHYPSE--------LSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190
....*....|....*....|....*....|....
gi 1297598371 285 DEATSALTEEVENELYRIGQQL---GMTFISVGH 315
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLaeeGMTMVIVTH 194
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
126-315 |
6.95e-13 |
|
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: 65.92 E-value: 6.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 126 LEQVSISAPssDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQMltdfgphgvlflpqkpfftDG 205
Cdd:cd03214 2 VENLSVGYG--GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILL-------------------DG 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 206 TLREQviYPLKEVypdsgsAddeRILRF----LELAGLSNLVARTegldqqvdwnwYDVLSPGEMQRLSFARLFYLQPKY 281
Cdd:cd03214 61 KDLAS--LSPKEL------A---RKIAYvpqaLELLGLAHLADRP-----------FNELSGGERQRVLLARALAQEPPI 118
|
170 180 190
....*....|....*....|....*....|....*...
gi 1297598371 282 AVLDEATSAL----TEEVENELYRIGQQLGMTFISVGH 315
Cdd:cd03214 119 LLLDEPTSHLdiahQIELLELLRRLARERGKTVVMVLH 156
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
139-321 |
9.15e-13 |
|
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: 9.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 139 PLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM----LTDFGPHG----VLFLPQKPFFTDGTLREQ 210
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLngfsLKDIDRHTlrqfINYLPQEPYIFSGSILEN 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 211 VIYPLKEvypdsgSADDERILRFLELAGLSNLVAR-TEGLDQQVDWNWYDvLSPGEMQRLSFARLFYLQPKYAVLDEATS 289
Cdd:TIGR01193 568 LLLGAKE------NVSQDEIWAACEIAEIKDDIENmPLGYQTELSEEGSS-ISGGQKQRIALARALLTDSKVLILDESTS 640
|
170 180 190
....*....|....*....|....*....|....*.
gi 1297598371 290 AL---TEE-VENELYRIGQQlgmTFISVGHRQSLEK 321
Cdd:TIGR01193 641 NLdtiTEKkIVNNLLNLQDK---TIIFVAHRLSVAK 673
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
125-315 |
1.02e-12 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 66.66 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 125 LLEQVSISApsSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----QMLTDFGPHG----VLFL 196
Cdd:PRK10247 9 QLQNVGYLA--GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLlfegEDISTLKPEIyrqqVSYC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 197 PQKPFFTDGTLREQVIYP--LKEVYPdsgsaDDERILRFLELAGLSNlvartEGLDQQVdwnwyDVLSPGEMQRLSFARL 274
Cdd:PRK10247 87 AQTPTLFGDTVYDNLIFPwqIRNQQP-----DPAIFLDDLERFALPD-----TILTKNI-----AELSGGEKQRISLIRN 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1297598371 275 FYLQPKYAVLDEATSALTEE----VENELYRIGQQLGMTFISVGH 315
Cdd:PRK10247 152 LQFMPKVLLLDEITSALDESnkhnVNEIIHRYVREQNIAVLWVTH 196
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
137-315 |
1.24e-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: 66.01 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 137 DKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----QMLTDFGPH--------GVLFlPQKPFFTD 204
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIiidgLKLTDDKKNinelrqkvGMVF-QQFNLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 205 GTLREQVIYPLKEVYPDSGSADDERILRFLELAGLSnlvarteglDQQvdwNWY-DVLSPGEMQRLSFARLFYLQPKYAV 283
Cdd:cd03262 91 LTVLENITLAPIKVKGMSKAEAEERALELLEKVGLA---------DKA---DAYpAQLSGGQQQRVAIARALAMNPKVML 158
|
170 180 190
....*....|....*....|....*....|....*
gi 1297598371 284 LDEATSALTEEVENELYRIGQQL---GMTFISVGH 315
Cdd:cd03262 159 FDEPTSALDPELVGEVLDVMKDLaeeGMTMVVVTH 193
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
129-333 |
2.20e-12 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 66.25 E-value: 2.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 129 VSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGL----------------------WTSTRGSVQMLT 186
Cdd:PRK10419 16 GGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLespsqgnvswrgeplaklnraqRKAFRRDIQMVF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 187 DFGPHGVLflPQKpfftdgTLREQVIYPLKEVYPDSGSADDERILRFLELAGLSNLVArtEGLDQQvdwnwydvLSPGEM 266
Cdd:PRK10419 96 QDSISAVN--PRK------TVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVL--DKRPPQ--------LSGGQL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1297598371 267 QRLSFARLFYLQPKYAVLDEATS----ALTEEVENELYRIGQQLGMTFISVGHRQSL-EKFHSFVLKLCGGG 333
Cdd:PRK10419 158 QRVCLARALAVEPKLLILDEAVSnldlVLQAGVIRLLKKLQQQFGTACLFITHDLRLvERFCQRVMVMDNGQ 229
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
141-330 |
2.87e-12 |
|
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: 65.54 E-value: 2.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 141 IKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----QMLTDFGPH-----GVL--FlpQKP-FFTDGTLR 208
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVlfdgEDITGLPPHeiarlGIGrtF--QIPrLFPELTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 209 EQVI---------YPLKEVYPDSGSADDERILRFLELAGLSNLVARTEGLdqqvdwnwydvLSPGEMQRLSFARLFYLQP 279
Cdd:cd03219 94 ENVMvaaqartgsGLLLARARREEREARERAEELLERVGLADLADRPAGE-----------LSYGQQRRLEIARALATDP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1297598371 280 KYAVLDEATSALT-EEVENELYRIGQ--QLGMTFISVGHRQslekfhSFVLKLC 330
Cdd:cd03219 163 KLLLLDEPAAGLNpEETEELAELIRElrERGITVLLVEHDM------DVVMSLA 210
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
140-297 |
7.86e-12 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 66.51 E-value: 7.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 140 LIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM----LTDFGPHGVLF----LPQKPFFTDGTLREQv 211
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIdglnIAKIGLHDLRFkitiIPQDPVLFSGSLRMN- 1379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 212 IYPLkevypdsGSADDERILRFLELAGLSNLV-ARTEGLDQQVDWNWYDvLSPGEMQRLSFARLFYLQPKYAVLDEATSA 290
Cdd:TIGR00957 1380 LDPF-------SQYSDEEVWWALELAHLKTFVsALPDKLDHECAEGGEN-LSVGQRQLVCLARALLRKTKILVLDEATAA 1451
|
....*..
gi 1297598371 291 LTEEVEN 297
Cdd:TIGR00957 1452 VDLETDN 1458
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
134-315 |
1.12e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 64.37 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 134 PSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----QMLT-----DFGPH-GVLFlpQKP--F 201
Cdd:PRK13650 16 EDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIiidgDLLTeenvwDIRHKiGMVF--QNPdnQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 202 FTDGTLREQVIY-------PLKEVypdsgsadDERILRFLELAGLSNLVARTEGLdqqvdwnwydvLSPGEMQRLSFARL 274
Cdd:PRK13650 94 FVGATVEDDVAFglenkgiPHEEM--------KERVNEALELVGMQDFKEREPAR-----------LSGGQKQRVAIAGA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1297598371 275 FYLQPKYAVLDEATSALTEEVENELYR----IGQQLGMTFISVGH 315
Cdd:PRK13650 155 VAMRPKIIILDEATSMLDPEGRLELIKtikgIRDDYQMTVISITH 199
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
138-291 |
1.25e-11 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 64.02 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 138 KPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM----LTDFGPH------GVlfLPQK-----PFf 202
Cdd:PRK13548 15 RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLngrpLADWSPAelarrrAV--LPQHsslsfPF- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 203 tdgTLREQV---IYPLkevyPDSGSADDERILRFLELAGLSNLVARTegldqqvdwnwYDVLSPGEMQRLSFAR-LFYL- 277
Cdd:PRK13548 92 ---TVEEVVamgRAPH----GLSRAEDDALVAAALAQVDLAHLAGRD-----------YPQLSGGEQQRVQLARvLAQLw 153
|
170
....*....|....*...
gi 1297598371 278 ----QPKYAVLDEATSAL 291
Cdd:PRK13548 154 epdgPPRWLLLDEPTSAL 171
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
126-315 |
1.55e-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: 63.36 E-value: 1.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 126 LEQVSISAPSSDKPLiKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV--------------------QML 185
Cdd:cd03256 3 VENLSKTYPNGKKAL-KDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVlidgtdinklkgkalrqlrrQIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 186 TDFGPHG----------VL--FLPQKPFFtdgtlreQVIYPLkevYPDsgsADDERILRFLELAGLSNLV-ARTegldqq 252
Cdd:cd03256 82 MIFQQFNlierlsvlenVLsgRLGRRSTW-------RSLFGL---FPK---EEKQRALAALERVGLLDKAyQRA------ 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1297598371 253 vdwnwyDVLSPGEMQRLSFARLFYLQPKYAVLDEATSAL----TEEVENELYRIGQQLGMTFISVGH 315
Cdd:cd03256 143 ------DQLSGGQQQRVAIARALMQQPKLILADEPVASLdpasSRQVMDLLKRINREEGITVIVSLH 203
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
126-288 |
2.09e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 64.70 E-value: 2.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 126 LEQVSISAPssDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQMltdfgPHG--VLFLPQKPFFT 203
Cdd:COG0488 1 LENLSKSFG--GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI-----PKGlrIGYLPQEPPLD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 204 DG-TLREQVIYPLKEVY------------PDSGSADDERIL----RFLELAG----------LSNLVARTEGLDQQVdwn 256
Cdd:COG0488 74 DDlTVLDTVLDGDAELRaleaeleeleakLAEPDEDLERLAelqeEFEALGGweaearaeeiLSGLGFPEEDLDRPV--- 150
|
170 180 190
....*....|....*....|....*....|..
gi 1297598371 257 wyDVLSPGEMQRLSFARLFYLQPKYAVLDEAT 288
Cdd:COG0488 151 --SELSGGWRRRVALARALLSEPDLLLLDEPT 180
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
137-318 |
5.12e-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: 63.69 E-value: 5.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 137 DKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----QMLTDFGPH------GVLflPQKP-FFTDg 205
Cdd:COG5265 370 ERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRIlidgQDIRDVTQAslraaiGIV--PQDTvLFND- 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 206 TLREQVIYPLkevyPDsgsADDERILRFLELAGLSNLVART-EGLDQQVdwnwydvLSPGEMQRLSFARLFYLQPKYAVL 284
Cdd:COG5265 447 TIAYNIAYGR----PD---ASEEEVEAAARAAQIHDFIESLpDGYDTRVger-glkLSGGEKQRVAIARTLLKNPPILIF 518
|
170 180 190
....*....|....*....|....*....|....*...
gi 1297598371 285 DEATSAL---TE-EVENELYRIGQqlGMTFISVGHRQS 318
Cdd:COG5265 519 DEATSALdsrTErAIQAALREVAR--GRTTLVIAHRLS 554
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
22-300 |
6.78e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 63.84 E-value: 6.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 22 SYVVIAIPIFS-----GVY----GDLSPAElstlvsknAFVCIYLISCF-TQLIDLSTTLSDVAGYTHRIGQLQETLLdm 91
Cdd:PLN03232 527 SFILNSIPVVVtlvsfGVFvllgGDLTPAR--------AFTSLSLFAVLrSPLNMLPNLLSQVVNANVSLQRIEELLL-- 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 92 slksQDCEILGESewgldkasgwPAAEPADTAFLLEQVSISAPS-SDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLR- 169
Cdd:PLN03232 597 ----SEERILAQN----------PPLQPGAPAISIKNGYFSWDSkTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISa 662
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 170 VLGGLWTSTRGSVQMLTDfgphgVLFLPQKPFFTDGTLREQVIYplkevypdsGSA-DDERILRFLELAGLS---NLVA- 244
Cdd:PLN03232 663 MLGELSHAETSSVVIRGS-----VAYVPQVSWIFNATVRENILF---------GSDfESERYWRAIDVTALQhdlDLLPg 728
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1297598371 245 --RTEGLDQQVDwnwydvLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEVENELY 300
Cdd:PLN03232 729 rdLTEIGERGVN------ISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVF 780
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
143-317 |
6.93e-11 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 62.79 E-value: 6.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 143 DLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQMltdfgpHG------------VLFLPQK-PFFTDGTLRE 209
Cdd:PRK10851 20 DISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRF------HGtdvsrlhardrkVGFVFQHyALFRHMTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 210 QVIYPLKeVYP----DSGSADDERILRFLELAGLSNLVARtegldqqvdwnWYDVLSPGEMQRLSFARLFYLQPKYAVLD 285
Cdd:PRK10851 94 NIAFGLT-VLPrrerPNAAAIKAKVTQLLEMVQLAHLADR-----------YPAQLSGGQKQRVALARALAVEPQILLLD 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 1297598371 286 EATSALTEEVENELYR----IGQQLGMTFISVGHRQ 317
Cdd:PRK10851 162 EPFGALDAQVRKELRRwlrqLHEELKFTSVFVTHDQ 197
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
139-300 |
1.45e-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: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 139 PLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQmltdfgpHG--VLFLPQKPFFTDGTLREQVIYPLk 216
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIK-------HSgrISFSPQTSWIMPGTIKDNIIFGL- 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 217 evypdsgSADDERILRFLELAGLSNLVARTEGLDQQVDWNWYDVLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEVE 296
Cdd:TIGR01271 512 -------SYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTE 584
|
....
gi 1297598371 297 NELY 300
Cdd:TIGR01271 585 KEIF 588
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
115-315 |
1.80e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 60.46 E-value: 1.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 115 PAAEPADTAFLLEqvSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGsvQMLTDFGPHGVL 194
Cdd:PRK11247 4 TARLNQGTPLLLN--AVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAG--ELLAGTAPLAEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 195 FLPQKPFFTDGTLreqviYPLKEVYPDSG---SAD-DERILRFLELAGLSNLVArtegldqqvdwNWYDVLSPGEMQRLS 270
Cdd:PRK11247 80 REDTRLMFQDARL-----LPWKKVIDNVGlglKGQwRDAALQALAAVGLADRAN-----------EWPAALSGGQKQRVA 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1297598371 271 FARLFYLQPKYAVLDE---ATSALTE-EVENELYRIGQQLGMTFISVGH 315
Cdd:PRK11247 144 LARALIHRPGLLLLDEplgALDALTRiEMQDLIESLWQQHGFTVLLVTH 192
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
140-315 |
3.03e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 59.98 E-value: 3.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 140 LIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV-------QMLTD-------FGPHGVLFLPQK------ 199
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIvvngqtiNLVRDkdgqlkvADKNQLRLLRTRltmvfq 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 200 --PFFTDGTLREQVIYPLKEVYPDSGSADDERILRFLELAGLsnlvarteglDQQVDWNWYDVLSPGEMQRLSFARLFYL 277
Cdd:PRK10619 100 hfNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGI----------DERAQGKYPVHLSGGQQQRVSIARALAM 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1297598371 278 QPKYAVLDEATSALTEEVENELYRIGQQL---GMTFISVGH 315
Cdd:PRK10619 170 EPEVLLFDEPTSALDPELVGEVLRIMQQLaeeGKTMVVVTH 210
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
132-315 |
3.08e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 60.13 E-value: 3.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 132 SAPSSDKPLIkDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQ----MLTDFGPH----------GVLF-L 196
Cdd:PRK13643 14 NSPFASRALF-DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTvgdiVVSSTSKQkeikpvrkkvGVVFqF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 197 PQKPFFTDGTLREQVIYPlkEVYPDSGSADDERILRFLELAGLSNLVARTEGLDqqvdwnwydvLSPGEMQRLSFARLFY 276
Cdd:PRK13643 93 PESQLFEETVLKDVAFGP--QNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFE----------LSGGQMRRVAIAGILA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1297598371 277 LQPKYAVLDEATSALTEEVENELYRIGQ---QLGMTFISVGH 315
Cdd:PRK13643 161 MEPEVLVLDEPTAGLDPKARIEMMQLFEsihQSGQTVVLVTH 202
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
127-296 |
4.06e-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: 59.02 E-value: 4.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 127 EQVSISAPS-SDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGsvQMLTDFGP---------HGVLFL 196
Cdd:cd03248 15 QNVTFAYPTrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGG--QVLLDGKPisqyehkylHSKVSL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 197 -PQKPFFTDGTLREQVIYPLkevypdsGSADDERILRFLELAGLSNLVARTE-GLDQQVDWNWyDVLSPGEMQRLSFARL 274
Cdd:cd03248 93 vGQEPVLFARSLQDNIAYGL-------QSCSFECVKEAAQKAHAHSFISELAsGYDTEVGEKG-SQLSGGQKQRVAIARA 164
|
170 180
....*....|....*....|..
gi 1297598371 275 FYLQPKYAVLDEATSALTEEVE 296
Cdd:cd03248 165 LIRNPQVLILDEATSALDAESE 186
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
141-315 |
5.29e-10 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 60.05 E-value: 5.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 141 IKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGsvQMLTDfgphGVLFLPqkpfFTDGTLRE------QVIYP 214
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRG--QVLID----GVDIAK----ISDAELREvrrkkiAMVFQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 215 LKEVYPDSGSADDERIlrFLELAGLSNLVARTEGLD--QQVDWNWY-----DVLSPGEMQRLSFARLFYLQPKYAVLDEA 287
Cdd:PRK10070 114 SFALMPHMTVLDNTAF--GMELAGINAEERREKALDalRQVGLENYahsypDELSGGMRQRVGLARALAINPDILLMDEA 191
|
170 180 190
....*....|....*....|....*....|..
gi 1297598371 288 TSALT----EEVENELYRIGQQLGMTFISVGH 315
Cdd:PRK10070 192 FSALDplirTEMQDELVKLQAKHQRTIVFISH 223
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
141-309 |
5.74e-10 |
|
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: 58.60 E-value: 5.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 141 IKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM----LTDFGPH-----GVLFLPQ-KPFFTDGTLREQ 210
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFdgrdITGLPPHeraraGIGYVPEgRRIFPELTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 211 VIYPLKEVYPDSGSADDERIL-RFLELAglsnlvartEGLDQQVdwnwyDVLSPGEMQRLSFARLFYLQPKYAVLDEATS 289
Cdd:cd03224 96 LLLGAYARRRAKRKARLERVYeLFPRLK---------ERRKQLA-----GTLSGGEQQMLAIARALMSRPKLLLLDEPSE 161
|
170 180
....*....|....*....|....
gi 1297598371 290 AL----TEEVENELYRIgQQLGMT 309
Cdd:cd03224 162 GLapkiVEEIFEAIREL-RDEGVT 184
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
112-316 |
7.22e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 60.37 E-value: 7.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 112 SGWPAAepadTAFLLEQVSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM----LTD 187
Cdd:PLN03232 1227 SGWPSR----GSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIddcdVAK 1302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 188 FGPHGVL----FLPQKPFFTDGTLREQvIYPLKEvypdsgsADDERILRFLELAGLSNLVARTE-GLDQQVdWNWYDVLS 262
Cdd:PLN03232 1303 FGLTDLRrvlsIIPQSPVLFSGTVRFN-IDPFSE-------HNDADLWEALERAHIKDVIDRNPfGLDAEV-SEGGENFS 1373
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1297598371 263 PGEMQRLSFARLFYLQPKYAVLDEATSALTEEVENELYR-IGQQL-GMTFISVGHR 316
Cdd:PLN03232 1374 VGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRtIREEFkSCTMLVIAHR 1429
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
139-300 |
7.76e-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: 59.10 E-value: 7.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 139 PLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQmltdfgpHG--VLFLPQKPFFTDGTLREQVIYPLk 216
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK-------HSgrISFSSQFSWIMPGTIKENIIFGV- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 217 evypdsgSADDERILRFLELAGLSNLVARTEGLDQQVDWNWYDVLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEVE 296
Cdd:cd03291 123 -------SYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTE 195
|
....
gi 1297598371 297 NELY 300
Cdd:cd03291 196 KEIF 199
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
127-299 |
1.20e-09 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 59.59 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 127 EQVSISAPSSdKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM----LTDFGPH------GVLFl 196
Cdd:PRK13657 338 DDVSFSYDNS-RQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIdgtdIRTVTRAslrrniAVVF- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 197 pQKPFFTDGTLREQviypLKEVYPDsgsADDERILRFLELAGLSNLVARTE-GLDQQVDWNWyDVLSPGEMQRLSFARLF 275
Cdd:PRK13657 416 -QDAGLFNRSIEDN----IRVGRPD---ATDEEMRAAAERAQAHDFIERKPdGYDTVVGERG-RQLSGGERQRLAIARAL 486
|
170 180
....*....|....*....|....
gi 1297598371 276 YLQPKYAVLDEATSALTEEVENEL 299
Cdd:PRK13657 487 LKDPPILILDEATSALDVETEAKV 510
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
115-317 |
1.41e-09 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 58.69 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 115 PAAEPADTAF-LLEQVSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----QMLTDFG 189
Cdd:PRK11607 8 PQAKTRKALTpLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQImldgVDLSHVP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 190 PHgvlflpQKP---------FFTDGTLREQVIYPLKEVYPDSGSADDeRILRFLELAGLSNLVARTEgldQQvdwnwydv 260
Cdd:PRK11607 88 PY------QRPinmmfqsyaLFPHMTVEQNIAFGLKQDKLPKAEIAS-RVNEMLGLVHMQEFAKRKP---HQ-------- 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1297598371 261 LSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEVEN----ELYRIGQQLGMTFISVGHRQ 317
Cdd:PRK11607 150 LSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDrmqlEVVDILERVGVTCVMVTHDQ 210
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
121-315 |
1.61e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 57.69 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 121 DTAFLLEQVSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQMltdfgphgvlflpqkp 200
Cdd:PRK13632 5 SVMIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKI---------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 201 fftDGTL--REQVIYPLKEV-----YPDS---GSADDERIlRFlelaGLSN-LVARTE------GLDQQVDWNWY----- 258
Cdd:PRK13632 69 ---DGITisKENLKEIRKKIgiifqNPDNqfiGATVEDDI-AF----GLENkKVPPKKmkdiidDLAKKVGMEDYldkep 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1297598371 259 DVLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEVENELYRIGQQL----GMTFISVGH 315
Cdd:PRK13632 141 QNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLrktrKKTLISITH 201
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
134-291 |
1.64e-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: 57.28 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 134 PSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLL-----RVLGGlwTSTRGSV----------QMLTDFGphgvlFLPQ 198
Cdd:cd03234 16 WNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLdaisgRVEGG--GTTSGQIlfngqprkpdQFQKCVA-----YVRQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 199 KPFFTDG-TLREQVIY--PLKEVYPDSGSADDER--ILRFLELAglsnlvarteglDQQVDWNWYDVLSPGEMQRLSFAR 273
Cdd:cd03234 89 DDILLPGlTVRETLTYtaILRLPRKSSDAIRKKRveDVLLRDLA------------LTRIGGNLVKGISGGERRRVSIAV 156
|
170
....*....|....*...
gi 1297598371 274 LFYLQPKYAVLDEATSAL 291
Cdd:cd03234 157 QLLWDPKVLILDEPTSGL 174
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
137-291 |
1.94e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 56.81 E-value: 1.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 137 DKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQmLTDFGPHGVLFLPQ----------KPFFtdgT 206
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIK-LDGGDIDDPDVAEAchylghrnamKPAL---T 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 207 LREQVIYpLKEVYpDSGSADDERILRFLELAGLSNLVARtegldqqvdwnwydVLSPGEMQRLSFARLFYLQPKYAVLDE 286
Cdd:PRK13539 90 VAENLEF-WAAFL-GGEELDIAAALEAVGLAPLAHLPFG--------------YLSAGQKRRVALARLLVSNRPIWILDE 153
|
....*
gi 1297598371 287 ATSAL 291
Cdd:PRK13539 154 PTAAL 158
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
141-315 |
2.14e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 57.72 E-value: 2.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 141 IKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQ----MLT------DFGPH----GVLF-LPQKPFFTDG 205
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTigerVITagkknkKLKPLrkkvGIVFqFPEHQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 206 TLREQVIYPLkevypDSGSADDERILR---FLELAGLS-NLVARTEgldqqvdwnwYDvLSPGEMQRLSFARLFYLQPKY 281
Cdd:PRK13634 103 VEKDICFGPM-----NFGVSEEDAKQKareMIELVGLPeELLARSP----------FE-LSGGQMRRVAIAGVLAMEPEV 166
|
170 180 190
....*....|....*....|....*....|....*...
gi 1297598371 282 AVLDEATSALTEEVENEL----YRIGQQLGMTFISVGH 315
Cdd:PRK13634 167 LVLDEPTAGLDPKGRKEMmemfYKLHKEKGLTTVLVTH 204
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
119-315 |
2.17e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 57.50 E-value: 2.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 119 PADTAFLLEQVSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLwtstrgsvqMLTDFGPHGVLFLpq 198
Cdd:PRK13640 1 MKDNIVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGL---------LLPDDNPNSKITV-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 199 kpfftDG-TLREQVIYPLKE----VY--PDS---GSADDERILRFLELAGLS---------NLVARTEGLDQQVDWNWYd 259
Cdd:PRK13640 70 -----DGiTLTAKTVWDIREkvgiVFqnPDNqfvGATVGDDVAFGLENRAVPrpemikivrDVLADVGMLDYIDSEPAN- 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 260 vLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEVENELYRIGQQL----GMTFISVGH 315
Cdd:PRK13640 144 -LSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLkkknNLTVISITH 202
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
137-291 |
2.91e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 58.32 E-value: 2.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 137 DKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGlWTSTRGSVQM----LTDFGP----HGVLFLPQKPFFTDGTLR 208
Cdd:PRK11174 362 GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLG-FLPYQGSLKIngieLRELDPeswrKHLSWVGQNPQLPHGTLR 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 209 EQVIyplkevyPDSGSADDERILRFLELAGLSNLVAR-TEGLDQQV-DWNwyDVLSPGEMQRLSFARLFYLQPKYAVLDE 286
Cdd:PRK11174 441 DNVL-------LGNPDASDEQLQQALENAWVSEFLPLlPQGLDTPIgDQA--AGLSVGQAQRLALARALLQPCQLLLLDE 511
|
....*
gi 1297598371 287 ATSAL 291
Cdd:PRK11174 512 PTASL 516
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
126-309 |
3.76e-09 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 57.40 E-value: 3.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 126 LEQVSISAPSSDKPLI--KDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----QMLTDFGPH-------- 191
Cdd:COG1135 4 LENLSKTFPTKGGPVTalDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVlvdgVDLTALSERelraarrk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 192 -GVLF-----LPQKpfftdgTLREQVIYPLK--EVypdSGSADDERILRFLELAGLSNLVARtegldqqvdwnwY-DVLS 262
Cdd:COG1135 84 iGMIFqhfnlLSSR------TVAENVALPLEiaGV---PKAEIRKRVAELLELVGLSDKADA------------YpSQLS 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1297598371 263 PGEMQRLSFARLFYLQPKyaVL--DEATSAL----TEEVENELYRIGQQLGMT 309
Cdd:COG1135 143 GGQKQRVGIARALANNPK--VLlcDEATSALdpetTRSILDLLKDINRELGLT 193
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
119-316 |
3.85e-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: 55.88 E-value: 3.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 119 PADTAFLLEQVSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM---------LTDFg 189
Cdd:cd03369 2 PEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIdgidistipLEDL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 190 PHGVLFLPQKPFFTDGTLREQViyplkEVYpdsGSADDERILRFLELA-GLSNlvartegldqqvdwnwydvLSPGEMQR 268
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNL-----DPF---DEYSDEEIYGALRVSeGGLN-------------------LSQGQRQL 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1297598371 269 LSFARLFYLQPKYAVLDEATSALTEEVENELYRIGQQL--GMTFISVGHR 316
Cdd:cd03369 134 LCLARALLKRPRVLVLDEATASIDYATDALIQKTIREEftNSTILTIAHR 183
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
143-315 |
3.87e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 56.68 E-value: 3.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 143 DLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----QMLTDFGPH----------GVLF-LPQKPFFTDGTL 207
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVrvddTLITSTSKNkdikqirkkvGLVFqFPESQLFEETVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 208 REQVIYPlkEVYPDSGSADDERILRFLELAGLSnlvarteglDQQVDWNWYDvLSPGEMQRLSFARLFYLQPKYAVLDEA 287
Cdd:PRK13649 105 KDVAFGP--QNFGVSQEEAEALAREKLALVGIS---------ESLFEKNPFE-LSGGQMRRVAIAGILAMEPKILVLDEP 172
|
170 180 190
....*....|....*....|....*....|.
gi 1297598371 288 TSALTEEVENELYRIGQQL---GMTFISVGH 315
Cdd:PRK13649 173 TAGLDPKGRKELMTLFKKLhqsGMTIVLVTH 203
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
126-291 |
4.70e-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: 55.44 E-value: 4.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 126 LEQVSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM-------LTDFGPHGVLFLPQ 198
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWngtplaeQRDEPHENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 199 KPFF-TDGTLREQviypLKEVYPDSGSADD--ERILRFLELAGLSNLVARTegldqqvdwnwydvLSPGEMQRLSFARLF 275
Cdd:TIGR01189 81 LPGLkPELSALEN----LHFWAAIHGGAQRtiEDALAAVGLTGFEDLPAAQ--------------LSAGQQRRLALARLW 142
|
170
....*....|....*.
gi 1297598371 276 YLQPKYAVLDEATSAL 291
Cdd:TIGR01189 143 LSRRPLWILDEPTTAL 158
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
137-291 |
7.53e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 54.81 E-value: 7.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 137 DKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV---------------QMLTDFGPH-GVlflpqKP 200
Cdd:PRK13538 13 ERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVlwqgepirrqrdeyhQDLLYLGHQpGI-----KT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 201 fftDGTLREQviypLKEVYPDSGSADDERILRFLE---LAGLSNLVARTegldqqvdwnwydvLSPGEMQRLSFARLFYL 277
Cdd:PRK13538 88 ---ELTALEN----LRFYQRLHGPGDDEALWEALAqvgLAGFEDVPVRQ--------------LSAGQQRRVALARLWLT 146
|
170
....*....|....
gi 1297598371 278 QPKYAVLDEATSAL 291
Cdd:PRK13538 147 RAPLWILDEPFTAI 160
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
141-313 |
7.96e-09 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 55.95 E-value: 7.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 141 IKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVqMLTD----FGPHGVLFLPQKPFFTDGTLR---EQVI- 212
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGEL-LIDDhplhFGDYSYRSQRIRMIFQDPSTSlnpRQRIs 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 213 ----YPLKEVYPDSGSADDERILRFLELAGLSNLVArtegldqqvdwNWY-DVLSPGEMQRLSFARLFYLQPKYAVLDEA 287
Cdd:PRK15112 108 qildFPLRLNTDLEPEQREKQIIETLRQVGLLPDHA-----------SYYpHMLAPGQKQRLGLARALILRPKVIIADEA 176
|
170 180 190
....*....|....*....|....*....|
gi 1297598371 288 TSALTEEVENELYRIGQQL----GMTFISV 313
Cdd:PRK15112 177 LASLDMSMRSQLINLMLELqekqGISYIYV 206
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
126-291 |
1.30e-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: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 126 LEQVSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM-------LTDFGPHGVLFLPQ 198
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLnggpldfQRDSIARGLLYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 199 KPFFTdGTLreQVIYPLKEVYPDSGSADDERILRFLELAGLSNLVARTegldqqvdwnwydvLSPGEMQRLSFARLFYLQ 278
Cdd:cd03231 81 APGIK-TTL--SVLENLRFWHADHSDEQVEEALARVGLNGFEDRPVAQ--------------LSAGQQRRVALARLLLSG 143
|
170
....*....|...
gi 1297598371 279 PKYAVLDEATSAL 291
Cdd:cd03231 144 RPLWILDEPTTAL 156
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
141-317 |
1.71e-08 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 55.46 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 141 IKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----QMLTDFGPH--GVLFLPQK----PFFtdgTLREQ 210
Cdd:COG3839 19 LKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEIliggRDVTDLPPKdrNIAMVFQSyalyPHM---TVYEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 211 VIYPLK-------EVypdsgsadDERILRFLELAGLSNLVAR--TEgldqqvdwnwydvLSPGEMQRLSFARLFYLQPKY 281
Cdd:COG3839 96 IAFPLKlrkvpkaEI--------DRRVREAAELLGLEDLLDRkpKQ-------------LSGGQRQRVALGRALVREPKV 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1297598371 282 AVLDEATS----ALTEEVENELYRIGQQLGMTFISVGHRQ 317
Cdd:COG3839 155 FLLDEPLSnldaKLRVEMRAEIKRLHRRLGTTTIYVTHDQ 194
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
143-319 |
1.80e-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: 53.95 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 143 DLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----QMLTDFGPHGVLFLPQK--------PFFTDGTLREQ 210
Cdd:cd03292 19 GINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIrvngQDVSDLRGRAIPYLRRKigvvfqdfRLLPDRNVYEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 211 VIYPLkEVYPDSGSADDERILRFLELAGLSNlvaRTEGLDQQvdwnwydvLSPGEMQRLSFARLFYLQPKYAVLDEATSA 290
Cdd:cd03292 99 VAFAL-EVTGVPPREIRKRVPAALELVGLSH---KHRALPAE--------LSGGEQQRVAIARAIVNSPTILIADEPTGN 166
|
170 180 190
....*....|....*....|....*....|..
gi 1297598371 291 LTEEVENELYRIGQQL---GMTFISVGHRQSL 319
Cdd:cd03292 167 LDPDTTWEIMNLLKKInkaGTTVVVATHAKEL 198
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
137-317 |
2.41e-08 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 55.04 E-value: 2.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 137 DKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----QMLTDFGP--HGVLFLPQKpfftdgtlreq 210
Cdd:PRK11000 15 DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLfigeKRMNDVPPaeRGVGMVFQS----------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 211 viYPLkevYPDSGSADDeriLRF-LELAGLS--------NLVARTEGLDQQVDWNWYDvLSPGEMQRLSFARLFYLQPKY 281
Cdd:PRK11000 84 --YAL---YPHLSVAEN---MSFgLKLAGAKkeeinqrvNQVAEVLQLAHLLDRKPKA-LSGGQRQRVAIGRTLVAEPSV 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1297598371 282 AVLDEATS----ALTEEVENELYRIGQQLGMTFISVGHRQ 317
Cdd:PRK11000 155 FLLDEPLSnldaALRVQMRIEISRLHKRLGRTMIYVTHDQ 194
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
137-291 |
2.44e-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: 2.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 137 DKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM----LTDFGPHGVLFLPQ-KPFFTDGTLREQV 211
Cdd:cd03269 12 RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFdgkpLDIAARNRIGYLPEeRGLYPKMKVIDQL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 212 IYpLKEVYPDSGSADDERILRFLELAGLSNLvaRTEGLDQqvdwnwydvLSPGEMQRLSFARLFYLQPKYAVLDEATSAL 291
Cdd:cd03269 92 VY-LAQLKGLKKEEARRRIDEWLERLELSEY--ANKRVEE---------LSKGNQQKVQFIAAVIHDPELLILDEPFSGL 159
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
141-320 |
2.69e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 54.28 E-value: 2.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 141 IKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM----LTDFGPH--------GVLFlpQKPFFTdgtLR 208
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIdgvdITDKKVKlsdirkkvGLVF--QYPEYQ---LF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 209 EQVIYPLKEVYPDS-GSADDE---RILRFLELAGLSnlvartegLDQQVDWNWYDvLSPGEMQRLSFARLFYLQPKYAVL 284
Cdd:PRK13637 98 EETIEKDIAFGPINlGLSEEEienRVKRAMNIVGLD--------YEDYKDKSPFE-LSGGQKRRVAIAGVVAMEPKILIL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1297598371 285 DEATSALT----EEVENELYRIGQQLGMTFISVGHrqSLE 320
Cdd:PRK13637 169 DEPTAGLDpkgrDEILNKIKELHKEYNMTIILVSH--SME 206
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
136-317 |
3.16e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 53.90 E-value: 3.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 136 SDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM---LTDFGPH-------------GVLFLPQK 199
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVdgkVLYFGKDifqidaiklrkevGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 200 PFfTDGTLREQVIYPLKEvypdSGSADDERILRFLELAglsnlvARTEGLDQQVdwnwYD-------VLSPGEMQRLSFA 272
Cdd:PRK14246 101 PF-PHLSIYDNIAYPLKS----HGIKEKREIKKIVEEC------LRKVGLWKEV----YDrlnspasQLSGGQQQRLTIA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1297598371 273 RLFYLQPKYAVLDEATSAL----TEEVENELYRIGQQLGMTFISVGHRQ 317
Cdd:PRK14246 166 RALALKPKVLLMDEPTSMIdivnSQAIEKLITELKNEIAIVIVSHNPQQ 214
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
109-321 |
3.62e-08 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 54.64 E-value: 3.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 109 DKASGWPAAEPADTAFLLEQVSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM---- 184
Cdd:PRK11176 327 EKDEGKRVIERAKGDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLdghd 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 185 -----LTDFGPHGVLFLPQKPFFTDgTLREQVIYPLKEVYpdsgsaDDERILRFLELAGLSNLVARTE-GLDQQVDWNWY 258
Cdd:PRK11176 407 lrdytLASLRNQVALVSQNVHLFND-TIANNIAYARTEQY------SREQIEEAARMAYAMDFINKMDnGLDTVIGENGV 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1297598371 259 dVLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEVE-------NELyrigqQLGMTFISVGHRQS-LEK 321
Cdd:PRK11176 480 -LLSGGQRQRIAIARALLRDSPILILDEATSALDTESEraiqaalDEL-----QKNRTSLVIAHRLStIEK 544
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
136-332 |
4.58e-08 |
|
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: 54.95 E-value: 4.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 136 SDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQMltdfgPHGVLFLPQKPFFTDGTLREQVIY-- 213
Cdd:TIGR00957 649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHM-----KGSVAYVPQQAWIQNDSLRENILFgk 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 214 PLKEVYPDSgSADDERILRFLELAGLSNlvaRTEGLDQQVDwnwydvLSPGEMQRLSFARLFYLQPKYAVLDEATSALTE 293
Cdd:TIGR00957 724 ALNEKYYQQ-VLEACALLPDLEILPSGD---RTEIGEKGVN------LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDA 793
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1297598371 294 EV-----ENELYRIGQQLGMTFISVGHRQSLEKFHSFVLKLCGG 332
Cdd:TIGR00957 794 HVgkhifEHVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGG 837
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
133-321 |
6.49e-08 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 53.56 E-value: 6.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 133 APSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----QMLTDFGPHG---------VLFlpQK 199
Cdd:PRK15079 29 QPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVawlgKDLLGMKDDEwravrsdiqMIF--QD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 200 PFFTDG---TLREQVIYPLKEVYPDSGSAD-DERILRFLELAGL-SNLVARtegldqqvdwnWYDVLSPGEMQRLSFARL 274
Cdd:PRK15079 107 PLASLNprmTIGEIIAEPLRTYHPKLSRQEvKDRVKAMMLKVGLlPNLINR-----------YPHEFSGGQCQRIGIARA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1297598371 275 FYLQPKYAVLDEATSAL----TEEVENELYRIGQQLGMTFISVGHRQSLEK 321
Cdd:PRK15079 176 LILEPKLIICDEPVSALdvsiQAQVVNLLQQLQREMGLSLIFIAHDLAVVK 226
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
125-299 |
1.53e-07 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 51.62 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 125 LLEQVSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM--LTDFGP---HGVLF---- 195
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLdgKPVEGPgaeRGVVFqneg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 196 -LPQKpfftdgTLREQVIYPLKEvypdSGSADDERILRFLELAGLSNLvartEGLDQQVDWNwydvLSPGEMQRLSFARL 274
Cdd:PRK11248 81 lLPWR------NVQDNVAFGLQL----AGVEKMQRLEIAHQMLKKVGL----EGAEKRYIWQ----LSGGQRQRVGIARA 142
|
170 180
....*....|....*....|....*...
gi 1297598371 275 FYLQPKYAVLDE---ATSALTEEVENEL 299
Cdd:PRK11248 143 LAANPQLLLLDEpfgALDAFTREQMQTL 170
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
137-315 |
1.62e-07 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 51.55 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 137 DKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----QMLTDFGP----HGVLFLPQKPFFTDG-TL 207
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVflgdKPISMLSSrqlaRRLALLPQHHLTPEGiTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 208 REQVIY---PLKEVYPDSGSADDERILRFLELAGLSNLVarteglDQQVdwnwyDVLSPGEMQRLSFARLFYLQPKYAVL 284
Cdd:PRK11231 94 RELVAYgrsPWLSLWGRLSAEDNARVNQAMEQTRINHLA------DRRL-----TDLSGGQRQRAFLAMVLAQDTPVVLL 162
|
170 180 190
....*....|....*....|....*....|....
gi 1297598371 285 DEATSALTEEVENELYRIGQQL---GMTFISVGH 315
Cdd:PRK11231 163 DEPTTYLDINHQVELMRLMRELntqGKTVVTVLH 196
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
113-290 |
2.04e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 52.82 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 113 GWPAAepadTAFLLEQVSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM-------- 184
Cdd:PLN03130 1231 GWPSS----GSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIdgcdiskf 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 185 -LTDFgpHGVL-FLPQKPFFTDGTLREQvIYPLKEvypdsgsADDERILRFLELAGLSNLVAR-TEGLDQQVDwNWYDVL 261
Cdd:PLN03130 1307 gLMDL--RKVLgIIPQAPVLFSGTVRFN-LDPFNE-------HNDADLWESLERAHLKDVIRRnSLGLDAEVS-EAGENF 1375
|
170 180
....*....|....*....|....*....
gi 1297598371 262 SPGEMQRLSFARLFYLQPKYAVLDEATSA 290
Cdd:PLN03130 1376 SVGQRQLLSLARALLRRSKILVLDEATAA 1404
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
128-318 |
2.18e-07 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 52.41 E-value: 2.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 128 QVSISA---PSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----QMLTDFGPHG----VLFL 196
Cdd:PRK10789 315 DVNIRQftyPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIrfhdIPLTKLQLDSwrsrLAVV 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 197 PQKPF-FTDgtlreQVIYPLKEVYPDSGSADDERILRfleLAGLSNLVAR-TEGLDQQVDWNWYdVLSPGEMQRLSFARL 274
Cdd:PRK10789 395 SQTPFlFSD-----TVANNIALGRPDATQQEIEHVAR---LASVHDDILRlPQGYDTEVGERGV-MLSGGQKQRISIARA 465
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1297598371 275 FYLQPKYAVLDEATSALTEEVENE----LYRIGQqlGMTFISVGHRQS 318
Cdd:PRK10789 466 LLLNAEILILDDALSAVDGRTEHQilhnLRQWGE--GRTVIISAHRLS 511
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
140-321 |
2.29e-07 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 50.97 E-value: 2.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 140 LIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----QMLT--------DFGPHGVLFLPQ-KPFFTDGT 206
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVifngQPMSklssaakaELRNQKLGFIYQfHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 207 LREQVIYPLKevypDSGSADDERILRFLELAGLSNLVARTEGLDQQvdwnwydvLSPGEMQRLSFARLFYLQPKYAVLDE 286
Cdd:PRK11629 104 ALENVAMPLL----IGKKKPAEINSRALEMLAAVGLEHRANHRPSE--------LSGGERQRVAIARALVNNPRLVLADE 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 1297598371 287 ATSALTEEVENELYRIGQQL----GMTFISVGHRQSLEK 321
Cdd:PRK11629 172 PTGNLDARNADSIFQLLGELnrlqGTAFLVVTHDLQLAK 210
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
122-315 |
2.56e-07 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 52.42 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 122 TAFL-LEQVSISAPSSDKPL--IKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----QMLTDFGPHGVL 194
Cdd:PRK10535 2 TALLeLKDIRRSYPSGEEQVevLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYrvagQDVATLDADALA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 195 FLPQKPF---------FTDGTLREQVIYPlkEVYpdSGSADDERILRFLELagLSNLvarteGLDQQVDWNwYDVLSPGE 265
Cdd:PRK10535 82 QLRREHFgfifqryhlLSHLTAAQNVEVP--AVY--AGLERKQRLLRAQEL--LQRL-----GLEDRVEYQ-PSQLSGGQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1297598371 266 MQRLSFARLFYLQPKYAVLDEATSAL----TEEVENELYRIGQQlGMTFISVGH 315
Cdd:PRK10535 150 QQRVSIARALMNGGQVILADEPTGALdshsGEEVMAILHQLRDR-GHTVIIVTH 202
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
135-291 |
3.37e-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: 3.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 135 SSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLwTSTRG----------SVQMLTDFGPHGVlfLPQKPFFTD 204
Cdd:TIGR01271 1229 EAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGeiqidgvswnSVTLQTWRKAFGV--IPQKVFIFS 1305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 205 GTLReqviyplKEVYPDSGSADDErILRFLELAGLSNLVARTEG-LDQQVDWNWYdVLSPGEMQRLSFARLFYLQPKYAV 283
Cdd:TIGR01271 1306 GTFR-------KNLDPYEQWSDEE-IWKVAEEVGLKSVIEQFPDkLDFVLVDGGY-VLSNGHKQLMCLARSILSKAKILL 1376
|
....*...
gi 1297598371 284 LDEATSAL 291
Cdd:TIGR01271 1377 LDEPSAHL 1384
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
137-318 |
3.85e-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: 51.88 E-value: 3.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 137 DKPLI-KDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVqmltdfgphgvlflpqkpfFTDG---------T 206
Cdd:TIGR03797 464 DGPLIlDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSV-------------------FYDGqdlagldvqA 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 207 LREQVIYPLKEVYPDSGSadderILRflELAGLSNL-------VARTEGLDQQVD---WNWYDV-------LSPGEMQRL 269
Cdd:TIGR03797 525 VRRQLGVVLQNGRLMSGS-----IFE--NIAGGAPLtldeaweAARMAGLAEDIRampMGMHTVisegggtLSGGQRQRL 597
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1297598371 270 SFARLFYLQPKYAVLDEATSAL---TEE-VENELyrigQQLGMTFISVGHRQS 318
Cdd:TIGR03797 598 LIARALVRKPRILLFDEATSALdnrTQAiVSESL----ERLKVTRIVIAHRLS 646
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
126-318 |
4.10e-07 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 51.64 E-value: 4.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 126 LEQVSIsAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQMltDFGP-----HGVL-----F 195
Cdd:PRK10790 343 IDNVSF-AYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRL--DGRPlsslsHSVLrqgvaM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 196 LPQKP------FFTDGTLREQViyplkevypdsgsaDDERILRFLELAGLSNLV-ARTEGLDQQVDwNWYDVLSPGEMQR 268
Cdd:PRK10790 420 VQQDPvvladtFLANVTLGRDI--------------SEEQVWQALETVQLAELArSLPDGLYTPLG-EQGNNLSVGQKQL 484
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1297598371 269 LSFARLFYLQPKYAVLDEATSAL---TEE-VENELYRIGQQlgMTFISVGHRQS 318
Cdd:PRK10790 485 LALARVLVQTPQILILDEATANIdsgTEQaIQQALAAVREH--TTLVVIAHRLS 536
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
141-315 |
7.92e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 49.85 E-value: 7.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 141 IKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV---QMLTDFGPHGVLFL----------PQKPFFTdGTL 207
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRIlfdGKPIDYSRKGLMKLresvgmvfqdPDNQLFS-ASV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 208 REQVIY-------PLKEVYpdsgsaddERILRFLELAGLSNLVarteglDQQVDWnwydvLSPGEMQRLSFARLFYLQPK 280
Cdd:PRK13636 101 YQDVSFgavnlklPEDEVR--------KRVDNALKRTGIEHLK------DKPTHC-----LSFGQKKRVAIAGVLVMEPK 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 1297598371 281 YAVLDEATSAL----TEEVENELYRIGQQLGMTFISVGH 315
Cdd:PRK13636 162 VLVLDEPTAGLdpmgVSEIMKLLVEMQKELGLTIIIATH 200
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
141-291 |
8.46e-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: 49.11 E-value: 8.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 141 IKDLSLKISEGQSLLItGNTGTGKTSLLRVLGGLWTSTRGSVQML------TDFGPHGVL-FLPQKP-FFTDGTLREQVI 212
Cdd:cd03264 16 LDGVSLTLGPGMYGLL-GPNGAGKTTLMRILATLTPPSSGTIRIDgqdvlkQPQKLRRRIgYLPQEFgVYPNFTVREFLD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 213 YP--LKEVyPDSGSadDERILRFLELAGLSNLVARTEGldqqvdwnwydVLSPGEMQRLSFARLFYLQPKYAVLDEATSA 290
Cdd:cd03264 95 YIawLKGI-PSKEV--KARVDEVLELVNLGDRAKKKIG-----------SLSGGMRRRVGIAQALVGDPSILIVDEPTAG 160
|
.
gi 1297598371 291 L 291
Cdd:cd03264 161 L 161
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
124-315 |
9.32e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 49.46 E-value: 9.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 124 FLLEQVSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLW-----TSTRGSVQML------TDFGP-- 190
Cdd:PRK14267 3 FAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLelneeARVEGEVRLFgrniysPDVDPie 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 191 ----HGVLFLPQKPFfTDGTLREQVIYPLKevypdsgsadderilrflelagLSNLVARTEGLDQQVDWN------WYDV 260
Cdd:PRK14267 83 vrreVGMVFQYPNPF-PHLTIYDNVAIGVK----------------------LNGLVKSKKELDERVEWAlkkaalWDEV 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1297598371 261 ----------LSPGEMQRLSFARLFYLQPKYAVLDEATSAL----TEEVENELYRIGQQLgmTFISVGH 315
Cdd:PRK14267 140 kdrlndypsnLSGGQRQRLVIARALAMKPKILLMDEPTANIdpvgTAKIEELLFELKKEY--TIVLVTH 206
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
143-315 |
9.47e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 49.83 E-value: 9.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 143 DLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQMLtdfGPH-----------------GVLF-LPQKPFFTD 204
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIA---GYHitpetgnknlkklrkkvSLVFqFPEAQLFEN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 205 GTLREQVIYPLkevypDSGSADDE---RILRFLELAGLSNLVARTEGLDqqvdwnwydvLSPGEMQRLSFARLFYLQPKY 281
Cdd:PRK13641 102 TVLKDVEFGPK-----NFGFSEDEakeKALKWLKKVGLSEDLISKSPFE----------LSGGQMRRVAIAGVMAYEPEI 166
|
170 180 190
....*....|....*....|....*....|....*..
gi 1297598371 282 AVLDEATSALTEEVENELYRI---GQQLGMTFISVGH 315
Cdd:PRK13641 167 LCLDEPAAGLDPEGRKEMMQLfkdYQKAGHTVILVTH 203
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
115-288 |
9.99e-07 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 50.06 E-value: 9.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 115 PAAEPADTAFLLEQVSISAPssDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVqmltDFGPHGVL 194
Cdd:COG0488 307 PPERLGKKVLELEGLSKSYG--DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV----KLGETVKI 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 195 -FLPQKPFFTDGTLReqviyPLKEVYPDSGSADDERILRFLELAGLSNlvartEGLDQQVdwnwyDVLSPGEMQRLSFAR 273
Cdd:COG0488 381 gYFDQHQEELDPDKT-----VLDELRDGAPGGTEQEVRGYLGRFLFSG-----DDAFKPV-----GVLSGGEKARLALAK 445
|
170
....*....|....*
gi 1297598371 274 LFYLQPKYAVLDEAT 288
Cdd:COG0488 446 LLLSPPNVLLLDEPT 460
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
136-315 |
1.01e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 49.36 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 136 SDKPL-IKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV---------QMLTDFGPH-GVLFlpQKPfftd 204
Cdd:PRK13648 19 SDASFtLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqaitdDNFEKLRKHiGIVF--QNP---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 205 gtlREQVIyplkevypdsGSadderILRFLELAGLSNLVARTEGLDQQVDWNWYDV------------LSPGEMQRLSFA 272
Cdd:PRK13648 93 ---DNQFV----------GS-----IVKYDVAFGLENHAVPYDEMHRRVSEALKQVdmleradyepnaLSGGQKQRVAIA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1297598371 273 RLFYLQPKYAVLDEATSALTEEVENELYRIGQQL----GMTFISVGH 315
Cdd:PRK13648 155 GVLALNPSVIILDEATSMLDPDARQNLLDLVRKVksehNITIISITH 201
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
137-327 |
1.35e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.41 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 137 DKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV-----QMLTDFGPH------GVLflPQKPFFTDG 205
Cdd:PTZ00265 397 DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIiindsHNLKDINLKwwrskiGVV--SQDPLLFSN 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 206 TLREQV---IYPLKEV--------------YPDSGSADDERILRFLELAGLSNLVARTEGLDQQVDWNW----------- 257
Cdd:PTZ00265 475 SIKNNIkysLYSLKDLealsnyynedgndsQENKNKRNSCRAKCAGDLNDMSNTTDSNELIEMRKNYQTikdsevvdvsk 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 258 --------------YDVL--------SPGEMQRLSFARLFYLQPKYAVLDEATSALTEEVENELYRI-----GQQLGMTF 310
Cdd:PTZ00265 555 kvlihdfvsalpdkYETLvgsnasklSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTinnlkGNENRITI 634
|
250
....*....|....*....
gi 1297598371 311 IsVGHRQSLEKFHS--FVL 327
Cdd:PTZ00265 635 I-IAHRLSTIRYANtiFVL 652
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
138-295 |
1.56e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 50.16 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 138 KPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVqmltdFGPHGVLFLPQKPFFTDGTLREQVIYplke 217
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-----WAERSIAYVPQQAWIMNATVRGNILF---- 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 218 vYPDSGSADDERILRFLEL-AGLSNLVA--RTEGLDQQVDwnwydvLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEE 294
Cdd:PTZ00243 744 -FDEEDAARLADAVRVSQLeADLAQLGGglETEIGEKGVN------LSGGQKARVSLARAVYANRDVYLLDDPLSALDAH 816
|
.
gi 1297598371 295 V 295
Cdd:PTZ00243 817 V 817
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
140-291 |
1.65e-06 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 48.70 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 140 LIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLwTSTRGSVQM-------------LTDFGphgvlFLPQKPFFTDGT 206
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQIdgvswnsvplqkwRKAFG-----VIPQKVFIFSGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 207 LReqviyplKEVYPdSGSADDERILRFLELAGLSNLVARTEG-LDQQVDWNWYdVLSPGEMQRLSFARLFYLQPKYAVLD 285
Cdd:cd03289 93 FR-------KNLDP-YGKWSDEEIWKVAEEVGLKSVIEQFPGqLDFVLVDGGC-VLSHGHKQLMCLARSVLSKAKILLLD 163
|
....*.
gi 1297598371 286 EATSAL 291
Cdd:cd03289 164 EPSAHL 169
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
135-316 |
1.71e-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: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 135 SSDKPLIKDLSLKISEGQSLLITGNTGTGKTS-LLRVLGGL--------WTSTRGSVQMLTDFGP---HGVLFLPQKPFF 202
Cdd:cd03290 11 GSGLATLSNINIRIPTGQLTMIVGQVGCGKSSlLLAILGEMqtlegkvhWSNKNESEPSFEATRSrnrYSVAYAAQKPWL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 203 TDGTLREQVIY--PL-----KEVYPDSGSADDERILRFLElaglsnlvaRTEGLDQQVDwnwydvLSPGEMQRLSFARLF 275
Cdd:cd03290 91 LNATVEENITFgsPFnkqryKAVTDACSLQPDIDLLPFGD---------QTEIGERGIN------LSGGQRQRICVARAL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1297598371 276 YLQPKYAVLDEATSALTEEVENELYRIG-----QQLGMTFISVGHR 316
Cdd:cd03290 156 YQNTNIVFLDDPFSALDIHLSDHLMQEGilkflQDDKRTLVLVTHK 201
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
142-312 |
2.12e-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: 49.30 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 142 KDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLwTSTRGSVQM----LTDFGPHG---------VLFlpQKPFftdGTL- 207
Cdd:COG4172 303 DGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFdgqdLDGLSRRAlrplrrrmqVVF--QDPF---GSLs 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 208 -R---EQVIY-PLKEVYPDSGSAD-DERILRFLELAGLS-NLVAR--TEgldqqvdwnwydvLSPGEMQRLSFARLFYLQ 278
Cdd:COG4172 377 pRmtvGQIIAeGLRVHGPGLSAAErRARVAEALEEVGLDpAARHRypHE-------------FSGGQRQRIAIARALILE 443
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1297598371 279 PKYAVLDEATSALTEEVENE----LYRIGQQLGMT--FIS 312
Cdd:COG4172 444 PKLLVLDEPTSALDVSVQAQildlLRDLQREHGLAylFIS 483
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
119-184 |
2.16e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 47.92 E-value: 2.16e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1297598371 119 PADTAFLLEQVSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM 184
Cdd:PRK13543 5 LHTAPPLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQI 70
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
137-290 |
2.21e-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: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 137 DKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM------LTDFGpHGvlFLPqkpfftDGTLREQ 210
Cdd:cd03220 34 EFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVrgrvssLLGLG-GG--FNP------ELTGREN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 211 vIYPLKEVYPDSGSADDERILRFLELAGLsnlvarTEGLDQQVdwnwyDVLSPGEMQRLSFARLFYLQPKYAVLDEATSA 290
Cdd:cd03220 105 -IYLNGRLLGLSRKEIDEKIDEIIEFSEL------GDFIDLPV-----KTYSSGMKARLAFAIATALEPDILLIDEVLAV 172
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
137-291 |
2.70e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 48.08 E-value: 2.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 137 DKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV---QMLTDFGPHGVLFL-----------PQKPFF 202
Cdd:PRK13638 13 DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVlwqGKPLDYSKRGLLALrqqvatvfqdpEQQIFY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 203 TDgtLREQVIYPLKEVypdsGSADDERILRFLELAGLSNlvarTEGLDQQVdwnwYDVLSPGEMQRLSFARLFYLQPKYA 282
Cdd:PRK13638 93 TD--IDSDIAFSLRNL----GVPEAEITRRVDEALTLVD----AQHFRHQP----IQCLSHGQKKRVAIAGALVLQARYL 158
|
....*....
gi 1297598371 283 VLDEATSAL 291
Cdd:PRK13638 159 LLDEPTAGL 167
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
137-291 |
3.12e-06 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 48.68 E-value: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 137 DKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVqMLTDFGPHG---------VLFLPQK---PFFTD 204
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTV-LVAGDDVEAlsaraasrrVASVPQDtslSFEFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 205 GtlrEQVI----YPLKEVYPDSGSADDERILRFLELAGLSNLVARTegldqqvdwnwYDVLSPGEMQRLSFARLFYLQPK 280
Cdd:PRK09536 94 V---RQVVemgrTPHRSRFDTWTETDRAAVERAMERTGVAQFADRP-----------VTSLSGGERQRVLLARALAQATP 159
|
170
....*....|.
gi 1297598371 281 YAVLDEATSAL 291
Cdd:PRK09536 160 VLLLDEPTASL 170
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
146-336 |
3.39e-06 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 47.47 E-value: 3.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 146 LKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQML------------TDFGPHGVLFLPQKpFFTDGTL--REQV 211
Cdd:PRK10584 31 LVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVgqplhqmdeearAKLRAKHVGFVFQS-FMLIPTLnaLENV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 212 IYP-LKEVYPDSGSADDERILrfLELAGLSNlvaRTEGLDQQvdwnwydvLSPGEMQRLSFARLFYLQPKYAVLDEATSA 290
Cdd:PRK10584 110 ELPaLLRGESSRQSRNGAKAL--LEQLGLGK---RLDHLPAQ--------LSGGEQQRVALARAFNGRPDVLFADEPTGN 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1297598371 291 LT----EEVENELYRIGQQLGMTFISVGHRQSLEKFHSFVLKLCGGGRWE 336
Cdd:PRK10584 177 LDrqtgDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
11-300 |
3.39e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 48.97 E-value: 3.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 11 INTFdYLGSILSYV-VIAIPIFSGVYGDLSPAELSTLVSKNA---FVCIYLISCFTQLIDLSTTLSdvagythrigQLQE 86
Cdd:PLN03130 525 FNSF-ILNSIPVLVtVVSFGVFTLLGGDLTPARAFTSLSLFAvlrFPLFMLPNLITQAVNANVSLK----------RLEE 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 87 TLLdmslksQDCEILGESewgldkasgwPAAEPADTAFLLEQVSIS-APSSDKPLIKDLSLKISEGQSLLITGNTGTGKT 165
Cdd:PLN03130 594 LLL------AEERVLLPN----------PPLEPGLPAISIKNGYFSwDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKT 657
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 166 SLLR-VLGGLWTSTRGSVQMLTDfgphgVLFLPQKPFFTDGTLREQVIYplkevypdsGSA-DDERILRFLELAGLSNLV 243
Cdd:PLN03130 658 SLISaMLGELPPRSDASVVIRGT-----VAYVPQVSWIFNATVRDNILF---------GSPfDPERYERAIDVTALQHDL 723
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1297598371 244 ARTEGLDQQ------VDwnwydvLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEVENELY 300
Cdd:PLN03130 724 DLLPGGDLTeigergVN------ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVF 780
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
140-318 |
3.52e-06 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 47.82 E-value: 3.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 140 LIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQMLTDFGPHGVLFLPQKPFFTDgtLREQV-------- 211
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQQKGLIRQ--LRQHVgfvfqnfn 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 212 IYPLKEVYPD--------SGSADDERILRFLELAGLSNLVARTEGLDQQvdwnwydvLSPGEMQRLSFARLFYLQPKYAV 283
Cdd:PRK11264 96 LFPHRTVLENiiegpvivKGEPKEEATARARELLAKVGLAGKETSYPRR--------LSGGQQQRVAIARALAMRPEVIL 167
|
170 180 190
....*....|....*....|....*....|....*...
gi 1297598371 284 LDEATSALTEEVENELYRIGQQLG---MTFISVGHRQS 318
Cdd:PRK11264 168 FDEPTSALDPELVGEVLNTIRQLAqekRTMVIVTHEMS 205
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
126-318 |
4.22e-06 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 47.60 E-value: 4.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 126 LEQVSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM----LTDFGPHGVL----FLP 197
Cdd:cd03288 22 IHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIdgidISKLPLHTLRsrlsIIL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 198 QKPFFTDGTLREQViyplkevYPDSGSADDeRILRFLELAGLSNLV-ARTEGLDQQVDWNWYDvLSPGEMQRLSFARLFY 276
Cdd:cd03288 102 QDPILFSGSIRFNL-------DPECKCTDD-RLWEALEIAQLKNMVkSLPGGLDAVVTEGGEN-FSVGQRQLFCLARAFV 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1297598371 277 LQPKYAVLDEATSALTEEVENelyrIGQQLGM------TFISVGHRQS 318
Cdd:cd03288 173 RKSSILIMDEATASIDMATEN----ILQKVVMtafadrTVVTIAHRVS 216
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
122-315 |
5.13e-06 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 47.45 E-value: 5.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 122 TAFLLEQVSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQMLTDFGP---HGVLFLPQ 198
Cdd:PRK11831 4 VANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPamsRSRLYTVR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 199 K---------PFFTDGTLREQVIYPLKEvypdsGSADDERILRF-----LELAGL---SNLVARTegldqqvdwnwydvL 261
Cdd:PRK11831 84 KrmsmlfqsgALFTDMNVFDNVAYPLRE-----HTQLPAPLLHStvmmkLEAVGLrgaAKLMPSE--------------L 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1297598371 262 SPGEMQRLSFARLFYLQPKYAVLDEA-------TSALTEEVENELyriGQQLGMTFISVGH 315
Cdd:PRK11831 145 SGGMARRAALARAIALEPDLIMFDEPfvgqdpiTMGVLVKLISEL---NSALGVTCVVVSH 202
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
126-309 |
5.42e-06 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 47.49 E-value: 5.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 126 LEQVSISAPSSDKPLI--KDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----QMLTDFGPH-------- 191
Cdd:PRK11153 4 LKNISKVFPQGGRTIHalNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVlvdgQDLTALSEKelrkarrq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 192 -GVLF-----LPQKpfftdgTLREQVIYPLkEVYPDSGSADDERILRFLELAGLSNLVARtegldqqvdwnwYDV-LSPG 264
Cdd:PRK11153 84 iGMIFqhfnlLSSR------TVFDNVALPL-ELAGTPKAEIKARVTELLELVGLSDKADR------------YPAqLSGG 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1297598371 265 EMQRLSFARLFYLQPKyaVL--DEATSAL----TEEVENELYRIGQQLGMT 309
Cdd:PRK11153 145 QKQRVAIARALASNPK--VLlcDEATSALdpatTRSILELLKDINRELGLT 193
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
112-312 |
6.24e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 47.78 E-value: 6.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 112 SGWPAAEPADTAFLL--EQVSISAP---------SSDKPLIKDLSLKISEGQSLLITGNTGTGKTS----LLRVL---GG 173
Cdd:PRK15134 262 SGDPVPLPEPASPLLdvEQLQVAFPirkgilkrtVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLInsqGE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 174 LWTS-----TRGSVQMLTDFGPHGVLFlpQKPfftDGTLR-----EQVIYPLKEV-YPD-SGSADDERILRFLELAGLsn 241
Cdd:PRK15134 342 IWFDgqplhNLNRRQLLPVRHRIQVVF--QDP---NSSLNprlnvLQIIEEGLRVhQPTlSAAQREQQVIAVMEEVGL-- 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1297598371 242 lvarteglDQQVDWNWYDVLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEVENE---LYRIGQQ---LGMTFIS 312
Cdd:PRK15134 415 --------DPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQilaLLKSLQQkhqLAYLFIS 483
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
142-316 |
6.56e-06 |
|
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: 6.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 142 KDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQMltdfgphgvlflpqkpfftDGtlreqviyplKEVYPD 221
Cdd:cd03216 17 DGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILV-------------------DG----------KEVSFA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 222 SgSADDERilrflelAGLSnLVartegldQQvdwnwydvLSPGEMQRLSFARLFYLQPKYAVLDEATSALT-EEVENELY 300
Cdd:cd03216 68 S-PRDARR-------AGIA-MV-------YQ--------LSVGERQMVEIARALARNARLLILDEPTAALTpAEVERLFK 123
|
170
....*....|....*...
gi 1297598371 301 RIGQ--QLGMTFISVGHR 316
Cdd:cd03216 124 VIRRlrAQGVAVIFISHR 141
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
125-293 |
9.36e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 45.71 E-value: 9.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 125 LLEQVSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQML-----TDFGPH--GVLFLP 197
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFErqsikKDLCTYqkQLCFVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 198 QK----PFFtdgTLREQVIYplkEVYPDSGSADDERILRFLElagLSNLVARTEGLdqqvdwnwydvLSPGEMQRLSFAR 273
Cdd:PRK13540 81 HRsginPYL---TLRENCLY---DIHFSPGAVGITELCRLFS---LEHLIDYPCGL-----------LSSGQKRQVALLR 140
|
170 180
....*....|....*....|
gi 1297598371 274 LFYLQPKYAVLDEATSALTE 293
Cdd:PRK13540 141 LWMSKAKLWLLDEPLVALDE 160
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
137-315 |
1.12e-05 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 46.85 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 137 DKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQMLTDFgphGVLFLPQKPFFTDG-TLREQV---- 211
Cdd:TIGR03719 17 KKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGI---KVGYLPQEPQLDPTkTVRENVeegv 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 212 ------IYPLKEVYPDSGSADDERILRFLELAGLSNLVARTEG--LDQQVD----------WNWyDV--LSPGEMQRLSF 271
Cdd:TIGR03719 94 aeikdaLDRFNEISAKYAEPDADFDKLAAEQAELQEIIDAADAwdLDSQLEiamdalrcppWDA-DVtkLSGGERRRVAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1297598371 272 ARLFYLQPKYAVLDEATSALTEEVENELYRIGQQLGMTFISVGH 315
Cdd:TIGR03719 173 CRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTH 216
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
138-315 |
1.48e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 45.85 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 138 KPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVqmltdfgphgvlflpqkpfFTDG--TLREQVIYPL 215
Cdd:PRK13633 23 KLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKV-------------------YVDGldTSDEENLWDI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 216 KE----VY--PDSG--SADDERILRFlelaGLSNLVARTEGLDQQVDW-----NWYD-------VLSPGEMQRLSFARLF 275
Cdd:PRK13633 84 RNkagmVFqnPDNQivATIVEEDVAF----GPENLGIPPEEIRERVDEslkkvGMYEyrrhaphLLSGGQKQRVAIAGIL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1297598371 276 YLQPKYAVLDEATSALT----EEVENELYRIGQQLGMTFISVGH 315
Cdd:PRK13633 160 AMRPECIIFDEPTAMLDpsgrREVVNTIKELNKKYGITIILITH 203
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
126-332 |
2.09e-05 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 44.83 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 126 LEQVSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGL--WTSTRGSV----QMLTDFGPH-----GVL 194
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEIlfkgEDITDLPPEerarlGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 195 FLPQKPFFTDG-TLREqviyplkevypdsgsadderILRFLElaglsnlvartEGLdqqvdwnwydvlSPGEMQRLSFAR 273
Cdd:cd03217 81 LAFQYPPEIPGvKNAD--------------------FLRYVN-----------EGF------------SGGEKKRNEILQ 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1297598371 274 LFYLQPKYAVLDEATSAL----TEEVENELYRIGQQlGMTFISVGHRQSLEKFHS--FVLKLCGG 332
Cdd:cd03217 118 LLLLEPDLAILDEPDSGLdidaLRLVAEVINKLREE-GKSVLIITHYQRLLDYIKpdRVHVLYDG 181
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
126-323 |
2.69e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 44.98 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 126 LEQVSISAPSSdKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM----LTDFGPH-------GVL 194
Cdd:PRK13644 4 LENVSYSYPDG-TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVsgidTGDFSKLqgirklvGIV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 195 FLPQKPFFTDGTLREQVIY-PLKEVYPDsgSADDERILRFLELAGLSNLVARTEgldqqvdwnwyDVLSPGEMQRLSFAR 273
Cdd:PRK13644 83 FQNPETQFVGRTVEEDLAFgPENLCLPP--IEIRKRVDRALAEIGLEKYRHRSP-----------KTLSGGQGQCVALAG 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1297598371 274 LFYLQPKYAVLDEATSALTEEV-ENELYRIGQ--QLGMTFISVGHrqSLEKFH 323
Cdd:PRK13644 150 ILTMEPECLIFDEVTSMLDPDSgIAVLERIKKlhEKGKTIVYITH--NLEELH 200
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
142-183 |
2.78e-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: 2.78e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1297598371 142 KDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQ 183
Cdd:COG1134 43 KDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
141-315 |
3.01e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 45.62 E-value: 3.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 141 IKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM---LTDFGPHGVL--------FLPQKPFFT---DGT 206
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFngqRIDTLSPGKLqalrrdiqFIFQDPYASldpRQT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 207 LREQVIYPLKEVYPDSGSADDERILRFLELAGLSNLVArtegldqqvdWNWYDVLSPGEMQRLSFARLFYLQPKYAVLDE 286
Cdd:PRK10261 420 VGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHA----------WRYPHEFSGGQRQRICIARALALNPKVIIADE 489
|
170 180 190
....*....|....*....|....*....|...
gi 1297598371 287 ATSALTEEVE----NELYRIGQQLGMTFISVGH 315
Cdd:PRK10261 490 AVSALDVSIRgqiiNLLLDLQRDFGIAYLFISH 522
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
138-315 |
3.48e-05 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 44.59 E-value: 3.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 138 KPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----QMLTDFGPHGV-----LFLPQKPFFTDGTLR 208
Cdd:PRK10253 20 YTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVwldgEHIQHYASKEVarrigLLAQNATTPGDITVQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 209 EQVI---YPLKEVYPDSGSADDERILRFLELAGLSNLVarteglDQQVdwnwyDVLSPGEMQRLSFARLFYLQPKYAVLD 285
Cdd:PRK10253 100 ELVArgrYPHQPLFTRWRKEDEEAVTKAMQATGITHLA------DQSV-----DTLSGGQRQRAWIAMVLAQETAIMLLD 168
|
170 180 190
....*....|....*....|....*....|....
gi 1297598371 286 EATSALTEEVENELYRIGQQL----GMTFISVGH 315
Cdd:PRK10253 169 EPTTWLDISHQIDLLELLSELnrekGYTLAAVLH 202
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
138-286 |
3.65e-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: 44.46 E-value: 3.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 138 KPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----QMLTDFGPH-----GVLFLPQKP-FFTDGTL 207
Cdd:cd03218 13 RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKIlldgQDITKLPMHkrarlGIGYLPQEAsIFRKLTV 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1297598371 208 REQVIYPLkEVYPDSGSADDERILRFLELAGLSNLvARTEGLDqqvdwnwydvLSPGEMQRLSFARLFYLQPKYAVLDE 286
Cdd:cd03218 93 EENILAVL-EIRGLSKKEREEKLEELLEEFHITHL-RKSKASS----------LSGGERRRVEIARALATNPKFLLLDE 159
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
141-315 |
5.43e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 44.39 E-value: 5.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 141 IKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQmLTDFGPH---------------GVLF-LPQKPFFTD 204
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVT-VDDITIThktkdkyirpvrkriGMVFqFPESQLFED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 205 GTLREQVIYP------LKEVypdsgsadDERILRFLELAGLSNLVARTEGLDqqvdwnwydvLSPGEMQRLSFARLFYLQ 278
Cdd:PRK13646 102 TVEREIIFGPknfkmnLDEV--------KNYAHRLLMDLGFSRDVMSQSPFQ----------MSGGQMRKIAIVSILAMN 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1297598371 279 PKYAVLDEATSALTEEVENELYRIGQQL----GMTFISVGH 315
Cdd:PRK13646 164 PDIIVLDEPTAGLDPQSKRQVMRLLKSLqtdeNKTIILVSH 204
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
145-312 |
5.73e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 44.19 E-value: 5.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 145 SLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSV----QMLTDFGPHGVLFLPQK-------PFftdGTL--REQV 211
Cdd:PRK11308 35 SFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELyyqgQDLLKADPEAQKLLRQKiqivfqnPY---GSLnpRKKV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 212 IYPLKEvyP------DSGSADDERILRFLELAGLsnlvaRTEgldqqvdwnWYD----VLSPGEMQRLSFARLFYLQPKY 281
Cdd:PRK11308 112 GQILEE--PllintsLSAAERREKALAMMAKVGL-----RPE---------HYDryphMFSGGQRQRIAIARALMLDPDV 175
|
170 180 190
....*....|....*....|....*....|....*..
gi 1297598371 282 AVLDEATSAL----TEEVENELYRIGQQLGMT--FIS 312
Cdd:PRK11308 176 VVADEPVSALdvsvQAQVLNLMMDLQQELGLSyvFIS 212
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
198-316 |
6.22e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.02 E-value: 6.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 198 QKPFFTDGTLREQVIYPlKEvypDSGSADDERILRFlelAGLSNLVartEGLDQQVDWN---WYDVLSPGEMQRLSFARL 274
Cdd:PTZ00265 1303 QEPMLFNMSIYENIKFG-KE---DATREDVKRACKF---AAIDEFI---ESLPNKYDTNvgpYGKSLSGGQKQRIAIARA 1372
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1297598371 275 FYLQPKYAVLDEATSALTEE----VENELYRIGQQLGMTFISVGHR 316
Cdd:PTZ00265 1373 LLREPKILLLDEATSSLDSNseklIEKTIVDIKDKADKTIITIAHR 1418
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
137-294 |
6.28e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.50 E-value: 6.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 137 DKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQML--TDFGphgvlFLPQ---KPFFTDGTLREQV 211
Cdd:PRK15064 331 NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSenANIG-----YYAQdhaYDFENDLTLFDWM 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 212 IYPLKEvypdsgsADDERILRflelAGLSNLVARTEGLDQQVdwnwyDVLSPGEMQRLSFARLFYLQPKYAVLDEATSAL 291
Cdd:PRK15064 406 SQWRQE-------GDDEQAVR----GTLGRLLFSQDDIKKSV-----KVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHM 469
|
...
gi 1297598371 292 TEE 294
Cdd:PRK15064 470 DME 472
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
139-316 |
6.32e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 44.77 E-value: 6.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 139 PLI-KDLSLKISEGQSLLITGNTGTGKTSLL-------RVLGG-LWTSTRgsvqmltDFGPHGV-----LF--LPQKPFF 202
Cdd:PTZ00243 1323 PLVlRGVSFRIAPREKVGIVGRTGSGKSTLLltfmrmvEVCGGeIRVNGR-------EIGAYGLrelrrQFsmIPQDPVL 1395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 203 TDGTLREQViYPLKEvypdsgsADDERILRFLELAGLSNLVA-RTEGLDQQV---DWNWydvlSPGEMQRLSFAR-LFYL 277
Cdd:PTZ00243 1396 FDGTVRQNV-DPFLE-------ASSAEVWAALELVGLRERVAsESEGIDSRVlegGSNY----SVGQRQLMCMARaLLKK 1463
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1297598371 278 QPKYAVLDEATSalteEVENELYRIGQQLGM------TFISVGHR 316
Cdd:PTZ00243 1464 GSGFILMDEATA----NIDPALDRQIQATVMsafsayTVITIAHR 1504
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
126-291 |
6.62e-05 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 44.05 E-value: 6.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 126 LEQVSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQMLTDFGPH-------GVLFLPQ 198
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPArarlaraRIGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 199 ----KPFFtdgTLREQVIYpLKEVYPDSGSADDERILRFLELAGLSNLVarteglDQQVdwnwyDVLSPGEMQRLSFARL 274
Cdd:PRK13536 122 fdnlDLEF---TVRENLLV-FGRYFGMSTREIEAVIPSLLEFARLESKA------DARV-----SDLSGGMKRRLTLARA 186
|
170
....*....|....*..
gi 1297598371 275 FYLQPKYAVLDEATSAL 291
Cdd:PRK13536 187 LINDPQLLILDEPTTGL 203
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
137-315 |
1.03e-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: 44.02 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 137 DKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGL--WTSTRGSV------------------------QMLTDFGP 190
Cdd:TIGR03269 12 GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpskvgepcpVCGGTLEP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 191 HGVLFL-PQKPFFTDGTLR--------------EQVIYPLKEVYPDSGSADDERILRFLELAGLSNLVARTEGLDQQvdw 255
Cdd:TIGR03269 92 EEVDFWnLSDKLRRRIRKRiaimlqrtfalygdDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSHRITHIARD--- 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1297598371 256 nwydvLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEE----VENELYRIGQQLGMTFISVGH 315
Cdd:TIGR03269 169 -----LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQtaklVHNALEEAVKASGISMVLTSH 227
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
141-315 |
1.85e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 42.46 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 141 IKDLSLKISEGQSLLITGNTGTGKTSLLRV---LGGLWTSTR--GSVQMLTD--FGPH----------GVLFlpQKPFFT 203
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIPGFRveGKVTFHGKnlYAPDvdpvevrrriGMVF--QKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 204 DGTLREQVIYPLKeVYPDSGSADdERILRFLELAGLSNLVA---RTEGLDqqvdwnwydvLSPGEMQRLSFARLFYLQPK 280
Cdd:PRK14243 104 PKSIYDNIAYGAR-INGYKGDMD-ELVERSLRQAALWDEVKdklKQSGLS----------LSGGQQQRLCIARAIAVQPE 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 1297598371 281 YAVLDEATSAL----TEEVENELYRIGQQlgMTFISVGH 315
Cdd:PRK14243 172 VILMDEPCSALdpisTLRIEELMHELKEQ--YTIIIVTH 208
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
126-319 |
2.33e-04 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 41.78 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 126 LEQVSiSAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQmltdFGPHGVLFLPQK--PFft 203
Cdd:PRK10908 4 FEHVS-KAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIW----FSGHDITRLKNRevPF-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 204 dgtLREQV--IYPLKEVYPDSGSADDERILRFLELAGLSNLVARTEGLDQQVDW-----NWYDVLSPGEMQRLSFARLFY 276
Cdd:PRK10908 77 ---LRRQIgmIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLldkakNFPIQLSGGEQQRVGIARAVV 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1297598371 277 LQPKYAVLDEATSALTEEVENELYRIGQQ---LGMTFISVGHRQSL 319
Cdd:PRK10908 154 NKPAVLLADEPTGNLDDALSEGILRLFEEfnrVGVTVLMATHDIGL 199
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
261-316 |
2.58e-04 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 42.70 E-value: 2.58e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 261 LSPGEMQRLSFARLFYLQPKYAVLDEATSALTE-EVENeLYRIGQQL---GMTFISVGHR 316
Cdd:COG1129 141 LSVAQQQLVEIARALSRDARVLILDEPTASLTErEVER-LFRIIRRLkaqGVAIIYISHR 199
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
136-313 |
3.37e-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: 3.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 136 SDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLwTSTRGSVQMLTDFGPHgvlflPQKPFFTdgTLREQVIYpl 215
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANR-TEGNVSVEGDIHYNGI-----PYKEFAE--KYPGEIIY-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 216 kevypdsGSADD--------ERILRFlelaglsnlVARTEGlDQQVdwnwyDVLSPGEMQRLSFARLFYLQPKYAVLDEA 287
Cdd:cd03233 88 -------VSEEDvhfptltvRETLDF---------ALRCKG-NEFV-----RGISGGERKRVSIAEALVSRASVLCWDNS 145
|
170 180 190
....*....|....*....|....*....|.
gi 1297598371 288 T----SALTEEVENELYRIGQQLGMT-FISV 313
Cdd:cd03233 146 TrgldSSTALEILKCIRTMADVLKTTtFVSL 176
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
143-312 |
3.40e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 42.41 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 143 DLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQML---TDFGP------HGVLFLPQKpffTDGTLREQVI- 212
Cdd:PRK10982 16 NVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQgkeIDFKSskealeNGISMVHQE---LNLVLQRSVMd 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 213 ------YPLKEVYPDSGSADDERILRFLELaglsnlvarteglDQQVDWN-WYDVLSPGEMQRLSFARLFYLQPKYAVLD 285
Cdd:PRK10982 93 nmwlgrYPTKGMFVDQDKMYRDTKAIFDEL-------------DIDIDPRaKVATLSVSQMQMIEIAKAFSYNAKIVIMD 159
|
170 180 190
....*....|....*....|....*....|..
gi 1297598371 286 EATSALTEEVENELYRIGQQL-----GMTFIS 312
Cdd:PRK10982 160 EPTSSLTEKEVNHLFTIIRKLkergcGIVYIS 191
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
261-312 |
4.86e-04 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 41.94 E-value: 4.86e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1297598371 261 LSPGEMQRLSFARLFYLQPKYAVLDEATSALT-EEVEnELYRIGQQL---GMT--FIS 312
Cdd:COG3845 142 LSVGEQQRVEILKALYRGARILILDEPTAVLTpQEAD-ELFEILRRLaaeGKSiiFIT 198
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
115-197 |
4.99e-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: 4.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 115 PAAEPADTAFLLEQVSIsAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQM----LTDFGP 190
Cdd:COG3845 249 APAEPGEVVLEVENLSV-RDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLdgedITGLSP 327
|
90
....*....|..
gi 1297598371 191 -----HGVLFLP 197
Cdd:COG3845 328 rerrrLGVAYIP 339
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
136-318 |
6.30e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 40.91 E-value: 6.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 136 SDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLW-----TSTRGSVqmltDFGPH----------------GVL 194
Cdd:PRK14239 16 NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNdlnpeVTITGSI----VYNGHniysprtdtvdlrkeiGMV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 195 FLPQKPFftDGTLREQVIYPLKEvypdSGSADDERILRFLElaglsnlvartEGLDQQVDWN-----WYDV---LSPGEM 266
Cdd:PRK14239 92 FQQPNPF--PMSIYENVVYGLRL----KGIKDKQVLDEAVE-----------KSLKGASIWDevkdrLHDSalgLSGGQQ 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1297598371 267 QRLSFARLFYLQPKYAVLDEATSAL----TEEVENELYRIGQQLGMTFISVGHRQS 318
Cdd:PRK14239 155 QRVCIARVLATSPKIILLDEPTSALdpisAGKIEETLLGLKDDYTMLLVTRSMQQA 210
|
|
| DnaC |
COG1484 |
DNA replication protein DnaC [Replication, recombination and repair]; |
126-172 |
2.94e-03 |
|
DNA replication protein DnaC [Replication, recombination and repair];
Pssm-ID: 441093 [Multi-domain] Cd Length: 242 Bit Score: 38.61 E-value: 2.94e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1297598371 126 LEQVSISA-PSSDKPLIKDL-SLK-ISEGQSLLITGNTGTGKTSLLRVLG 172
Cdd:COG1484 71 LEDFDFDAqPGLDRRQILELaTLDfIERGENLILLGPPGTGKTHLAIALG 120
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
141-185 |
3.61e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 38.56 E-value: 3.61e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1297598371 141 IKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQML 185
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVM 65
|
|
| IS21_help_AAA |
NF038214 |
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ... |
133-167 |
8.11e-03 |
|
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was built to hit full-length AAA+ ATPases of IS21 family IS (insertion sequence) elements.
Pssm-ID: 439516 Cd Length: 232 Bit Score: 37.07 E-value: 8.11e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1297598371 133 APSSDKPLIKDL-SLK-ISEGQSLLITGNTGTGKTSL 167
Cdd:NF038214 70 APGLDKAQIRELaTLDfIERAENVLLLGPPGTGKTHL 106
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
147-272 |
9.00e-03 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 37.84 E-value: 9.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297598371 147 KISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQMLTDfgphgVLFLPQ--KPFFtDGTLREQviypLKEVYPD--S 222
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK-----ISYKPQyiSPDY-DGTVEEF----LRSANTDdfG 431
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1297598371 223 GSADDERILRFLelaGLSNLvartegLDQQVDwnwydVLSPGEMQRLSFA 272
Cdd:COG1245 432 SSYYKTEIIKPL---GLEKL------LDKNVK-----DLSGGELQRVAIA 467
|
|
|