|
Name |
Accession |
Description |
Interval |
E-value |
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
124-335 |
1.56e-78 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 237.44 E-value: 1.56e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 124 FLLERVSVCAPSsHKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQMLTDfgpHGVLFLPQKPFFT 203
Cdd:cd03223 1 IELENLSLATPD-GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEG---EDLLFLPQRPYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 204 DGTLREQVIYPlkeiypdsgstdderilrflelaglsslvtrtegldqqvdwnWYDVLSPGEMQRLSFARLFYLQPKYAV 283
Cdd:cd03223 77 LGTLREQLIYP------------------------------------------WDDVLSGGEQQRLAFARLLLHKPKFVF 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1239915452 284 LDEATSALTEEVESELYRIGQQLGMTFISVGHRHSLEKFHSLVLKLYGEGRW 335
Cdd:cd03223 115 LDEATSALDEESEDRLYQLLKELGITVISVGHRPSLWKFHDRVLDLDGEGGW 166
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-340 |
7.87e-76 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 243.56 E-value: 7.87e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 1 MLNLLLFSVGVNtfdYLGSILSYVVIAIPIFSGvygDLSPTELSTLVSknAFV-----CIYLISCFTRLIDLSSTLSdva 75
Cdd:COG4178 265 QRNLTFFTTGYG---QLAVIFPILVAAPRYFAG---EITLGGLMQAAS--AFGqvqgaLSWFVDNYQSLAEWRATVD--- 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 76 gythRIGELQETLLDMSLKLRGGEILDESEwnmdrapgwpaaepaDTAFLLERVSVCAPSsHKPLIKDLSLKISEGQSLL 155
Cdd:COG4178 334 ----RLAGFEEALEAADALPEAASRIETSE---------------DGALALEDLTLRTPD-GRPLLEDLSLSLKPGERLL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 156 ITGNTGTGKSSLLRVLGGLWASTQGSVQMltdfgPHG--VLFLPQKPFFTDGTLREQVIYPLkeiypDSGSTDDERILRF 233
Cdd:COG4178 394 ITGPSGSGKSTLLRAIAGLWPYGSGRIAR-----PAGarVLFLPQRPYLPLGTLREALLYPA-----TAEAFSDAELREA 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 234 LELAGLSSLVTRtegLDQQVDWNwyDVLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEVESELYR-IGQQL-GMTFI 311
Cdd:COG4178 464 LEAVGLGHLAER---LDEEADWD--QVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQlLREELpGTTVI 538
|
330 340
....*....|....*....|....*....
gi 1239915452 312 SVGHRHSLEKFHSLVLKLYGEGRWELSRI 340
Cdd:COG4178 539 SVGHRSTLAAFHDRVLELTGDGSWQLLPA 567
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1-337 |
2.89e-62 |
|
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: 209.99 E-value: 2.89e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 1 MLNLLLFSVGVNTFD-----YLGSILSYVVIAIPIFSGV---YGDLSPTELSTLVSKNAFVCIYLISCFTRLIDLSSTLS 72
Cdd:TIGR00954 315 LNLIIKFRFSYGFLDnivakYTWSAVGLVAVSIPIFDKThpaFLEMSEEELMQEFYNNGRLLLKAADALGRLMLAGRDMT 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 73 DVAGYTHRIGELQETLLDMSL----KLRGGEILDESEW--NMDRAPGWPAAEPADTAFLLERVSVCAPSSHKpLIKDLSL 146
Cdd:TIGR00954 395 RLAGFTARVDTLLQVLDDVKSgnfkRPRVEEIESGREGgrNSNLVPGRGIVEYQDNGIKFENIPLVTPNGDV-LIESLSF 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 147 KISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGsvqMLTDFGPHGVLFLPQKPFFTDGTLREQVIYPL-KEIYPDSGST 225
Cdd:TIGR00954 474 EVPSGNNLLICGPNGCGKSSLFRILGELWPVYGG---RLTKPAKGKLFYVPQRPYMTLGTLRDQIIYPDsSEDMKRRGLS 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 226 DDERIlRFLELAGLSSLVTRTEGLDQQVDWNwyDVLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEVESELYRIGQQ 305
Cdd:TIGR00954 551 DKDLE-QILDNVQLTHILEREGGWSAVQDWM--DVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCRE 627
|
330 340 350
....*....|....*....|....*....|..
gi 1239915452 306 LGMTFISVGHRHSLEKFHSLVLKLYGEGRWEL 337
Cdd:TIGR00954 628 FGITLFSVSHRKSLWKYHEYLLYMDGRGGYQF 659
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
131-315 |
4.57e-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: 4.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 131 VCAPSSHKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV----QMLTDFGPHG----VLFLPQKPFF 202
Cdd:COG4619 6 LSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIyldgKPLSAMPPPEwrrqVAYVPQEPAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 203 TDGTLREQVIYP--LKEIYPDsgstdDERILRFLELAGLSSLVtrtegLDQQVDwnwydVLSPGEMQRLSFARLFYLQPK 280
Cdd:COG4619 86 WGGTVRDNLPFPfqLRERKFD-----RERALELLERLGLPPDI-----LDKPVE-----RLSGGERQRLALIRALLLQPD 150
|
170 180 190
....*....|....*....|....*....|....*....
gi 1239915452 281 YAVLDEATSAL----TEEVESELYRIGQQLGMTFISVGH 315
Cdd:COG4619 151 VLLLDEPTSALdpenTRRVEELLREYLAEEGRAVLWVSH 189
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
12-319 |
1.13e-27 |
|
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: 113.78 E-value: 1.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 12 NTFDYLGSILSYVVIAIPIFSGVY----GDLSpteLSTLVsknAFVCI--YLISCFTRLIDLSSTLSDVAGYTHRIGELQ 85
Cdd:COG2274 379 NLLSTLSGLLQQLATVALLWLGAYlvidGQLT---LGQLI---AFNILsgRFLAPVAQLIGLLQRFQDAKIALERLDDIL 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 86 ETlldmslklrggeildESEWNMDRAPgwPAAEPADTAFLLERVSVCAPSSHKPLIKDLSLKISEGQSLLITGNTGTGKS 165
Cdd:COG2274 453 DL---------------PPEREEGRSK--LSLPRLKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKS 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 166 SLLRVLGGLWASTQGSVQM----LTDFGPH------GVlfLPQKPFFTDGTLREQVIYPLKEIypdsgstDDERILRFLE 235
Cdd:COG2274 516 TLLKLLLGLYEPTSGRILIdgidLRQIDPAslrrqiGV--VLQDVFLFSGTIRENITLGDPDA-------TDEEIIEAAR 586
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 236 LAGLSSLVTR-TEGLDQQVDwNWYDVLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEVESELYRIGQQL--GMTFIS 312
Cdd:COG2274 587 LAGLHDFIEAlPMGYDTVVG-EGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLlkGRTVII 665
|
....*..
gi 1239915452 313 VGHRHSL 319
Cdd:COG2274 666 IAHRLST 672
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
126-316 |
5.06e-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: 100.23 E-value: 5.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 126 LERVSVCAPSSHKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQM----LTDFGPH------GVLF 195
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVdgkdLTKLSLKelrrkvGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 196 lpQKP---FFTDgTLREQVIYPLkEIYPDSGSTDDERILRFLELAGLSSLvtrtegldqqVDWNWYDvLSPGEMQRLSFA 272
Cdd:cd03225 82 --QNPddqFFGP-TVEEEVAFGL-ENLGLPEEEIEERVEEALELVGLEGL----------RDRSPFT-LSGGQKQRVAIA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1239915452 273 RLFYLQPKYAVLDEATSAL----TEEVESELYRIGQQlGMTFISVGHR 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 |
6.03e-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: 98.99 E-value: 6.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 126 LERVSVCAPSSHKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV----QMLTDFGPHG----VLFLP 197
Cdd:cd03228 3 FKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEIlidgVDLRDLDLESlrknIAYVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 198 QKPFFTDGTLREqviyplkeiypdsgstdderilrflelaglsslvtrtegldqqvdwNwydVLSPGEMQRLSFARLFYL 277
Cdd:cd03228 83 QDPFLFSGTIRE----------------------------------------------N---ILSGGQRQRIAIARALLR 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1239915452 278 QPKYAVLDEATSAL---TE-EVESELYRIGQqlGMTFISVGHRHSL 319
Cdd:cd03228 114 DPPILILDEATSALdpeTEaLILEALRALAK--GKTVIVIAHRLST 157
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
126-319 |
2.22e-24 |
|
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: 98.82 E-value: 2.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 126 LERVSVCAPSSHKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQM----LTDFGP----HGVLFLP 197
Cdd:cd03245 5 FRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLdgtdIRQLDPadlrRNIGYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 198 QKPFFTDGTLREQVIYPLKEIypdsgstDDERILRFLELAGLSSLVTR-TEGLDQQVDWNWYDvLSPGEMQRLSFARLFY 276
Cdd:cd03245 85 QDVTLFYGTLRDNITLGAPLA-------DDERILRAAELAGVTDFVNKhPNGLDLQIGERGRG-LSGGQRQAVALARALL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1239915452 277 LQPKYAVLDEATSALTEEVESELYRIGQQL--GMTFISVGHRHSL 319
Cdd:cd03245 157 NDPPILLLDEPTSAMDMNSEERLKERLRQLlgDKTLIIITHRPSL 201
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
99-316 |
6.19e-24 |
|
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: 102.53 E-value: 6.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 99 EILDESEWNMDR-APGWPAAEPADTAFllERVSVCAPSShKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWAS 177
Cdd:COG4988 313 ALLDAPEPAAPAgTAPLPAAGPPSIEL--EDVSFSYPGG-RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPP 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 178 TQGSV----QMLTDFGPH----GVLFLPQKPFFTDGTLREQV-IYplkeiYPDSgstDDERILRFLELAGLSSLVTR-TE 247
Cdd:COG4988 390 YSGSIlingVDLSDLDPAswrrQIAWVPQNPYLFAGTIRENLrLG-----RPDA---SDEELEAALEAAGLDEFVAAlPD 461
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1239915452 248 GLDQQVD---WNwydvLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEVESELYRIGQQL--GMTFISVGHR 316
Cdd:COG4988 462 GLDTPLGeggRG----LSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLakGRTVILITHR 531
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
6-316 |
1.92e-23 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 101.01 E-value: 1.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 6 LFSVGVNTFDYLGSILSYVVIAIPIFSGvygDLSPTELSTLVSknafvciYLISCFTRLIDLSSTLSDvagythrigeLQ 85
Cdd:COG1132 246 LFFPLMELLGNLGLALVLLVGGLLVLSG---SLTVGDLVAFIL-------YLLRLFGPLRQLANVLNQ----------LQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 86 ETLLDMSlklRGGEILDESEwNMDRAPGWPAAEPADTAFLLERVSVCAPSShKPLIKDLSLKISEGQSLLITGNTGTGKS 165
Cdd:COG1132 306 RALASAE---RIFELLDEPP-EIPDPPGAVPLPPVRGEIEFENVSFSYPGD-RPVLKDISLTIPPGETVALVGPSGSGKS 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 166 SLLRVLGGLWASTQGSVQM----LTDFGPHG----VLFLPQKPFFTDGTLREQVIYPLKEIypdsgstDDERILRFLELA 237
Cdd:COG1132 381 TLVNLLLRFYDPTSGRILIdgvdIRDLTLESlrrqIGVVPQDTFLFSGTIRENIRYGRPDA-------TDEEVEEAAKAA 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 238 GLSSLVTR-TEGLDQQVDWNWYDvLSPGEMQRLSFARLFYLQPKYAVLDEATSAL---TE-EVESELYRIGQqlGMTFIS 312
Cdd:COG1132 454 QAHEFIEAlPDGYDTVVGERGVN-LSGGQRQRIAIARALLKDPPILILDEATSALdteTEaLIQEALERLMK--GRTTIV 530
|
....
gi 1239915452 313 VGHR 316
Cdd:COG1132 531 IAHR 534
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
126-319 |
2.53e-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: 94.59 E-value: 2.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 126 LERVSVCAPSSHKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQM---------LTDFGPHgVLFL 196
Cdd:cd03246 3 VENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLdgadisqwdPNELGDH-VGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 197 PQKPFFTDGTLREqviyplkeiypdsgstdderilrflelaglsslvtrtegldqqvdwnwyDVLSPGEMQRLSFARLFY 276
Cdd:cd03246 82 PQDDELFSGSIAE-------------------------------------------------NILSGGQRQRLGLARALY 112
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1239915452 277 LQPKYAVLDEATSALTEEVESELYRIGQQL---GMTFISVGHRHSL 319
Cdd:cd03246 113 GNPRILVLDEPNSHLDVEGERALNQAIAALkaaGATRIVIAHRPET 158
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
111-316 |
6.24e-23 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 99.28 E-value: 6.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 111 APGWPAAEPADTAFLLERVSVCAPSShKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQM----LT 186
Cdd:TIGR02857 309 AGKAPVTAAPASSLEFSGVSVAYPGR-RPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVngvpLA 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 187 DFGPHG----VLFLPQKPFFTDGTLREQVIYPLKEiypdsgsTDDERILRFLELAGLSSLV-TRTEGLDQQVDWNWYDvL 261
Cdd:TIGR02857 388 DADADSwrdqIAWVPQHPFLFAGTIAENIRLARPD-------ASDAEIREALERAGLDEFVaALPQGLDTPIGEGGAG-L 459
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1239915452 262 SPGEMQRLSFARLFYLQPKYAVLDEATSALTEEVESELYRIGQQL--GMTFISVGHR 316
Cdd:TIGR02857 460 SGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALaqGRTVLLVTHR 516
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
137-334 |
1.45e-21 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 89.61 E-value: 1.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 137 HKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQmltdFGPHGVLFLPQKPfftdgtLREQVIYplk 216
Cdd:cd00267 11 GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEIL----IDGKDIAKLPLEE------LRRRIGY--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 217 eiypdsgstdderilrflelaglsslvtrtegLDQqvdwnwydvLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEVE 296
Cdd:cd00267 78 --------------------------------VPQ---------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASR 116
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1239915452 297 SELYRIGQQL---GMTFISVGHRHSLEKFHSLVLKLYGEGR 334
Cdd:cd00267 117 ERLLELLRELaeeGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
141-289 |
5.70e-20 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 85.01 E-value: 5.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 141 IKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQ-----MLTDFGPH---GVLFLPQKP-FFTDGTLREQV 211
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILldgqdLTDDERKSlrkEIGYVFQDPqLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1239915452 212 IYPLKEIYPDSgSTDDERILRFLELAGLSSLVTRTEGldqqvdwNWYDVLSPGEMQRLSFARLFYLQPKYAVLDEATS 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 ... |
138-329 |
2.42e-19 |
|
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: 85.35 E-value: 2.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 138 KPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGsvQMLTDFGP----------HGVLFLPQKPFFTDGTL 207
Cdd:cd03254 16 KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKG--QILIDGIDirdisrkslrSMIGVVLQDTFLFSGTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 208 REQVIYplkeiypDSGSTDDERILRFLELAGLSSLVTR-TEGLDQQVDWNWyDVLSPGEMQRLSFARLFYLQPKYAVLDE 286
Cdd:cd03254 94 MENIRL-------GRPNATDEEVIEAAKEAGAHDFIMKlPNGYDTVLGENG-GNLSQGERQLLAIARAMLRDPKILILDE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1239915452 287 ATSAL---TEE-VESELYRIGQqlGMTFISVGHRHSLEKFHSLVLKL 329
Cdd:cd03254 166 ATSNIdteTEKlIQEALEKLMK--GRTSIIIAHRLSTIKNADKILVL 210
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
126-315 |
1.37e-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: 83.40 E-value: 1.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 126 LERVSVCAPSSHK--PLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV----QMLTDFGPHGVLFLPQK 199
Cdd:cd03258 4 LKNVSKVFGDTGGkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVlvdgTDLTLLSGKELRKARRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 200 --------PFFTDGTLREQVIYPLkEIYPDSGSTDDERILRFLELAGLSSLVTRtegldqqvdwnwY-DVLSPGEMQRLS 270
Cdd:cd03258 84 igmifqhfNLLSSRTVFENVALPL-EIAGVPKAEIEERVLELLELVGLEDKADA------------YpAQLSGGQKQRVG 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1239915452 271 FARLFYLQPKYAVLDEATSAL----TEEVESELYRIGQQLGMTFISVGH 315
Cdd:cd03258 151 IARALANNPKVLLCDEATSALdpetTQSILALLRDINRELGLTIVLITH 199
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
128-322 |
1.59e-18 |
|
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: 82.92 E-value: 1.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 128 RVSVCAPSSHKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV------------QMLTDFGPHGVLF 195
Cdd:cd03255 7 SKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVrvdgtdisklseKELAAFRRRHIGF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 196 LPQK----PFFtdgTLREQVIYPLkEIYPDSGSTDDERILRFLELAGLsslvtrTEGLDQQVDWnwydvLSPGEMQRLSF 271
Cdd:cd03255 87 VFQSfnllPDL---TALENVELPL-LLAGVPKKERRERAEELLERVGL------GDRLNHYPSE-----LSGGQQQRVAI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1239915452 272 ARLFYLQPKYAVLDEATSAL----TEEVESELYRIGQQLGMTFISVGHRHSLEKF 322
Cdd:cd03255 152 ARALANDPKIILADEPTGNLdsetGKEVMELLRELNKEAGTTIVVVTHDPELAEY 206
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
19-299 |
1.09e-17 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 83.95 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 19 SILSYVVIAIPIFSGvyGDLSPTELSTLVsknaFVCIYLISCFTRLIDLSSTLSDVAGYTHRIGELQETlldmslKLRGG 98
Cdd:TIGR02868 251 AVLGALWAGGPAVAD--GRLAPVTLAVLV----LLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVLDA------AGPVA 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 99 EIldesewnmdRAPGWPAAEPADTAFLLERVSVCAPSShKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWAST 178
Cdd:TIGR02868 319 EG---------SAPAAGAVGLGKPTLELRDLSAGYPGA-PPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPL 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 179 QGSVqMLTDFGPHG---------VLFLPQKPFFTDGTLREQVIYPLKEIypdsgstDDERILRFLELAGLSSLVTRT-EG 248
Cdd:TIGR02868 389 QGEV-TLDGVPVSSldqdevrrrVSVCAQDAHLFDTTVRENLRLARPDA-------TDEELWAALERVGLADWLRALpDG 460
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1239915452 249 LDQQVDWNWyDVLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEVESEL 299
Cdd:TIGR02868 461 LDTVLGEGG-ARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADEL 510
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
141-315 |
1.26e-17 |
|
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: 80.84 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 141 IKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQM----LTDFGP--HGVLFLPQ-KPFFTDGTLREQVIY 213
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLngkdITNLPPekRDISYVPQnYALFPHMTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 214 PLKEIYPDSgSTDDERILRFLELAGLSSLVTRTEGldqqvdwnwydVLSPGEMQRLSFARLFYLQPKYAVLDEATSAL-- 291
Cdd:cd03299 95 GLKKRKVDK-KEIERKVLEIAEMLGIDHLLNRKPE-----------TLSGGEQQRVAIARALVVNPKILLLDEPFSALdv 162
|
170 180
....*....|....*....|....*.
gi 1239915452 292 --TEEVESELYRIGQQLGMTFISVGH 315
Cdd:cd03299 163 rtKEKLREELKKIRKEFGVTVLHVTH 188
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
137-339 |
2.44e-17 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 79.62 E-value: 2.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 137 HKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSvqmltdfgphGVLFLPQKPFFTDGTLREQViyplk 216
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVA----------GCVDVPDNQFGREASLIDAI----- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 217 eiyPDSGSTDDerILRFLELAGLSSLvtrtegldqqvdWNW---YDVLSPGEMQRLSFARLFYLQPKYAVLDEATSALTE 293
Cdd:COG2401 107 ---GRKGDFKD--AVELLNAVGLSDA------------VLWlrrFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDR 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1239915452 294 EVESELYRIGQQL----GMTFISVGHRHSLEKFHS---LVLKLYGeGRWELSR 339
Cdd:COG2401 170 QTAKRVARNLQKLarraGITLVVATHHYDVIDDLQpdlLIFVGYG-GVPEEKR 221
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
126-318 |
3.13e-17 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 79.58 E-value: 3.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 126 LERVSVCAPSSHKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQM----LTDFGPHG----VLFLP 197
Cdd:cd03251 3 FKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIdghdVRDYTLASlrrqIGLVS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 198 QKPFFTDGTLREQVIYPLKEIypdsgstDDERILRFLELAGLSSLVTRT-EGLDQQVDWNWYDvLSPGEMQRLSFARLFY 276
Cdd:cd03251 83 QDVFLFNDTVAENIAYGRPGA-------TREEVEEAARAANAHEFIMELpEGYDTVIGERGVK-LSGGQRQRIAIARALL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1239915452 277 LQPKYAVLDEATSALTEEVESELYRIGQQL--GMTFISVGHRHS 318
Cdd:cd03251 155 KDPPILILDEATSALDTESERLVQAALERLmkNRTTFVIAHRLS 198
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
138-291 |
3.75e-17 |
|
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: 78.67 E-value: 3.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 138 KPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV--------QMLTDFGPHgVLFLPQKPFFTDG-TLR 208
Cdd:COG4133 15 RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVlwngepirDAREDYRRR-LAYLGHADGLKPElTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 209 EQVIYpLKEIYPDSGstDDERILRFLELAGLSSLvtrtegLDQQVdwnwyDVLSPGEMQRLSFARLFYLQPKYAVLDEAT 288
Cdd:COG4133 94 ENLRF-WAALYGLRA--DREAIDEALEAVGLAGL------ADLPV-----RQLSAGQKRRVALARLLLSPAPLWLLDEPF 159
|
...
gi 1239915452 289 SAL 291
Cdd:COG4133 160 TAL 162
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
137-315 |
3.97e-17 |
|
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: 79.20 E-value: 3.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 137 HKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV----QMLTDFGPH----GVLFlpQK-PFFTDGTL 207
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEIlldgKDITNLPPHkrpvNTVF--QNyALFPHLTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 208 REQVIYPLKeIYPDSGSTDDERILRFLELAGLSSLVTRTEgldqqvdwnwyDVLSPGEMQRLSFARLFYLQPKYAVLDEA 287
Cdd:cd03300 90 FENIAFGLR-LKKLPKAEIKERVAEALDLVQLEGYANRKP-----------SQLSGGQQQRVAIARALVNEPKVLLLDEP 157
|
170 180 190
....*....|....*....|....*....|..
gi 1239915452 288 TSALT----EEVESELYRIGQQLGMTFISVGH 315
Cdd:cd03300 158 LGALDlklrKDMQLELKRLQKELGITFVFVTH 189
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
136-328 |
4.61e-17 |
|
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: 78.73 E-value: 4.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 136 SHKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQML---TDFGPHGVLFLPQKPFF-TD--GTLRE 209
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFgkpLEKERKRIGYVPQRRSIdRDfpISVRD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 210 QV---IYPLKEIYPDSGSTDDERILRFLELAGLSSLVTRTegLDQqvdwnwydvLSPGEMQRLSFARLFYLQPKYAVLDE 286
Cdd:cd03235 90 VVlmgLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQ--IGE---------LSGGQQQRVLLARALVQDPDLLLLDE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1239915452 287 ATSALTEEVESELYRIGQQL---GMTFISVGH-RHSLEKF--HSLVLK 328
Cdd:cd03235 159 PFAGVDPKTQEDIYELLRELrreGMTILVVTHdLGLVLEYfdRVLLLN 206
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
138-315 |
8.96e-17 |
|
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: 77.94 E-value: 8.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 138 KPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV----QMLTDFGPH--GVLFLPQKP-FFTDGTLREQ 210
Cdd:cd03259 13 VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEIlidgRDVTGVPPErrNIGMVFQDYaLFPHLTVAEN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 211 VIYPLKEIYPDSGSTdDERILRFLELAGLSSLVTRtegldqqvdwnWYDVLSPGEMQRLSFARLFYLQPKYAVLDEATSA 290
Cdd:cd03259 93 IAFGLKLRGVPKAEI-RARVRELLELVGLEGLLNR-----------YPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180
....*....|....*....|....*....
gi 1239915452 291 L----TEEVESELYRIGQQLGMTFISVGH 315
Cdd:cd03259 161 LdaklREELREELKELQRELGITTIYVTH 189
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
127-316 |
1.04e-16 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 77.92 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 127 ERVSVCAPSSHKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQM----LTDFGPHgVL-----FLP 197
Cdd:cd03244 6 KNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIdgvdISKIGLH-DLrsrisIIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 198 QKPFFTDGTLREQvIYPLKEiypdsgsTDDERILRFLELAGLSSLV-TRTEGLDQQVDWNWyDVLSPGEMQRLSFARLFY 276
Cdd:cd03244 85 QDPVLFSGTIRSN-LDPFGE-------YSDEELWQALERVGLKEFVeSLPGGLDTVVEEGG-ENLSVGQRQLLCLARALL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1239915452 277 LQPKYAVLDEATSAlteeVESELYRIGQQL------GMTFISVGHR 316
Cdd:cd03244 156 RKSKILVLDEATAS----VDPETDALIQKTireafkDCTVLTIAHR 197
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
141-320 |
2.32e-16 |
|
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: 76.84 E-value: 2.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 141 IKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLW-----ASTQGSVQML------TDFGPH------GVLFlpQKPFFT 203
Cdd:cd03260 16 LKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDgkdiydLDVDVLelrrrvGMVF--QKPNPF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 204 DGTLREQVIYPLKEIYPDSGSTDDERILRFLELAGLSSLV-TRTEGLDqqvdwnwydvLSPGEMQRLSFARLFYLQPKYA 282
Cdd:cd03260 94 PGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVkDRLHALG----------LSGGQQQRLCLARALANEPEVL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1239915452 283 VLDEATSAL----TEEVESELYRIGQQLGMTFISvghrHSLE 320
Cdd:cd03260 164 LLDEPTSALdpisTAKIEELIAELKKEYTIVIVT----HNMQ 201
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
138-315 |
3.81e-16 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 76.39 E-value: 3.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 138 KPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQM----LTDFGPH---------GVLFlpQKP-FFT 203
Cdd:cd03261 13 RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIdgedISGLSEAelyrlrrrmGMLF--QSGaLFD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 204 DGTLREQVIYPLKEIYPDSGSTDDERILRFLELAGLSslvtrtegldQQVDwnwydvLSPGE----MQ-RLSFARLFYLQ 278
Cdd:cd03261 91 SLTVFENVAFPLREHTRLSEEEIREIVLEKLEAVGLR----------GAED------LYPAElsggMKkRVALARALALD 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1239915452 279 PKYAVLDEATSAL----TEEVESELYRIGQQLGMTFISVGH 315
Cdd:cd03261 155 PELLLYDEPTAGLdpiaSGVIDDLIRSLKKELGLTSIMVTH 195
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
17-318 |
3.88e-16 |
|
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: 79.38 E-value: 3.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 17 LGSILSYVVIAIPIFSGVYGDLSPTELSTLVSKnafvCIYLISCFTRLIDLSSTLSDVAGYTHRIGelqeTLLDMSLKLr 96
Cdd:TIGR02203 247 IASLALAVVLFIALFQAQAGSLTAGDFTAFITA----MIALIRPLKSLTNVNAPMQRGLAAAESLF----TLLDSPPEK- 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 97 ggeilDESEWNMDRAPGwpaaepaDTAFllERVSVCAPSSHKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWA 176
Cdd:TIGR02203 318 -----DTGTRAIERARG-------DVEF--RNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 177 STQGSVQM---------LTDFGPHgVLFLPQKPFFTDGTLREQVIYPlkeiypDSGSTDDERILRFLELAGLSSLVTRT- 246
Cdd:TIGR02203 384 PDSGQILLdghdladytLASLRRQ-VALVSQDVVLFNDTIANNIAYG------RTEQADRAEIERALAAAYAQDFVDKLp 456
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1239915452 247 EGLDQQVDWNWyDVLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEE----VESELYRIGQqlGMTFISVGHRHS 318
Cdd:TIGR02203 457 LGLDTPIGENG-VLLSGGQRQRLAIARALLKDAPILILDEATSALDNEserlVQAALERLMQ--GRTTLVIAHRLS 529
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
129-328 |
7.83e-16 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 78.61 E-value: 7.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 129 VSVCAPS-SHKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV----QMLTDFGPH----GVLFLPQK 199
Cdd:TIGR00958 484 VSFSYPNrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVlldgVPLVQYDHHylhrQVALVGQE 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 200 PFFTDGTLREQVIYPLKeiypdsgSTDDERILRFLELAGLSSLVTR-TEGLDQQVDWNWyDVLSPGEMQRLSFARLFYLQ 278
Cdd:TIGR00958 564 PVLFSGSVRENIAYGLT-------DTPDEEIMAAAKAANAHDFIMEfPNGYDTEVGEKG-SQLSGGQKQRIAIARALVRK 635
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1239915452 279 PKYAVLDEATSALTEEVESELYRIGQQLGMTFISVGHR-HSLEKFHS-LVLK 328
Cdd:TIGR00958 636 PRVLILDEATSALDAECEQLLQESRSRASRTVLLIAHRlSTVERADQiLVLK 687
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
137-318 |
8.48e-16 |
|
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: 75.73 E-value: 8.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 137 HKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQM---------LTDFGPH-GVLflPQK-PFFTDg 205
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIdgqdirevtLDSLRRAiGVV--PQDtVLFND- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 206 TLREQVIYplkeiypdsGSTD--DERILRFLELAGLSSLVTR-TEGLDQQV-DWNWYdvLSPGEMQRLSFARLFYLQPKY 281
Cdd:cd03253 90 TIGYNIRY---------GRPDatDEEVIEAAKAAQIHDKIMRfPDGYDTIVgERGLK--LSGGEKQRVAIARAILKNPPI 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 1239915452 282 AVLDEATSALTEEVESELYRIGQQL--GMTFISVGHRHS 318
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAALRDVskGRTTIVIAHRLS 197
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
128-315 |
1.55e-15 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 74.85 E-value: 1.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 128 RVSVCAPSSHKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV------------QMLTDFGpHGVLF 195
Cdd:cd03257 8 SVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIifdgkdllklsrRLRKIRR-KEIQM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 196 LPQKPF------FTdgtLREQVIYPLKEIYPDSGSTD-DERILRFLELAGLSSLVtrtegLDQ---QvdwnwydvLSPGE 265
Cdd:cd03257 87 VFQDPMsslnprMT---IGEQIAEPLRIHGKLSKKEArKEAVLLLLVGVGLPEEV-----LNRyphE--------LSGGQ 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1239915452 266 MQRLSFARLFYLQPKYAVLDEATSAL----TEEVESELYRIGQQLGMTFISVGH 315
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALdvsvQAQILDLLKKLQEELGLTLLFITH 204
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
140-331 |
2.31e-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: 74.44 E-value: 2.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 140 LIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVqmLTDfGPHGVLFLPQkpfftdgTLREQVIYPLKEIY 219
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRV--LVD-GHDLALADPA-------WLRRQVGVVLQENV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 220 PDSGSTDD-----------ERILRFLELAGLSSLVTRT-EGLDQQVDWNWYDvLSPGEMQRLSFARLFYLQPKYAVLDEA 287
Cdd:cd03252 87 LFNRSIRDnialadpgmsmERVIEAAKLAGAHDFISELpEGYDTIVGEQGAG-LSGGQRQRIAIARALIHNPRILIFDEA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1239915452 288 TSALTEEVESELYRIGQQL--GMTFISVGHRHSLEKFHSLVLKLYG 331
Cdd:cd03252 166 TSALDYESEHAIMRNMHDIcaGRTVIIIAHRLSTVKNADRIIVMEK 211
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
139-318 |
3.52e-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: 73.73 E-value: 3.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 139 PLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV----QMLTDFGPHGVL----FLPQKPFFTDGTLREQ 210
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEIlldgVDIRDLNLRWLRsqigLVSQEPVLFDGTIAEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 211 VIYPLkeiyPDSGSTDDERILRfleLAGLSSLVTR-TEGLDQQVDWNwYDVLSPGEMQRLSFARLFYLQPKYAVLDEATS 289
Cdd:cd03249 97 IRYGK----PDATDEEVEEAAK---KANIHDFIMSlPDGYDTLVGER-GSQLSGGQKQRIAIARALLRNPKILLLDEATS 168
|
170 180 190
....*....|....*....|....*....|.
gi 1239915452 290 ALTEEVESELYRIGQQL--GMTFISVGHRHS 318
Cdd:cd03249 169 ALDAESEKLVQEALDRAmkGRTTIVIAHRLS 199
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
126-316 |
5.79e-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: 75.71 E-value: 5.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 126 LERVSVCAPSSHKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLW---ASTQGSV----QMLTDFGPHG----VL 194
Cdd:COG1123 7 VRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLphgGRISGEVlldgRDLLELSEALrgrrIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 195 FLPQKPF--FTDGTLREQVIYPLkEIYPDSGSTDDERILRFLELAGLSSLVTRtegldqqvdwnWYDVLSPGEMQRLSFA 272
Cdd:COG1123 87 MVFQDPMtqLNPVTVGDQIAEAL-ENLGLSRAEARARVLELLEAVGLERRLDR-----------YPHQLSGGQRQRVAIA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1239915452 273 RLFYLQPKYAVLDEATSAL----TEEVESELYRIGQQLGMTFISVGHR 316
Cdd:COG1123 155 MALALDPDLLIADEPTTALdvttQAEILDLLRELQRERGTTVLLITHD 202
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
121-315 |
8.27e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 73.28 E-value: 8.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 121 DTAFLLERVSVCAPSshKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV----QMLTDFGPHG---- 192
Cdd:PRK10575 9 DTTFALRNVSFRVPG--RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEIlldaQPLESWSSKAfark 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 193 VLFLPQKPFFTDG-TLREQVI---YPLKEIYPDSGSTDDERILRFLELAGLSSLVTRTegldqqvdwnwYDVLSPGEMQR 268
Cdd:PRK10575 87 VAYLPQQLPAAEGmTVRELVAigrYPWHGALGRFGAADREKVEEAISLVGLKPLAHRL-----------VDSLSGGERQR 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1239915452 269 LSFARLFYLQPKYAVLDEATSAL----TEEVESELYRIGQQLGMTFISVGH 315
Cdd:PRK10575 156 AWIAMLVAQDSRCLLLDEPTSALdiahQVDVLALVHRLSQERGLTVIAVLH 206
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
112-327 |
1.15e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 74.86 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 112 PGWPAAEPADTAFLLERVSVCAPSSHKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQM----LTD 187
Cdd:PRK11160 327 PTTSTAAADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLngqpIAD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 188 FGP----HGVLFLPQKPFFTDGTLREQVIYPLKEIypdsgstDDERILRFLELAGLSSLVTRTEGLDQqvdwnWYD---- 259
Cdd:PRK11160 407 YSEaalrQAISVVSQRVHLFSATLRDNLLLAAPNA-------SDEALIEVLQQVGLEKLLEDDKGLNA-----WLGeggr 474
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1239915452 260 VLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEVESELYRIGQQL--GMTFISVGHR-HSLEKFHSLVL 327
Cdd:PRK11160 475 QLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHaqNKTVLMITHRlTGLEQFDRICV 545
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
138-315 |
1.21e-14 |
|
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: 72.12 E-value: 1.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 138 KPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQM----LTDFGPH-GVLF-----LPQKpfftdgTL 207
Cdd:cd03293 17 VTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVdgepVTGPGPDrGYVFqqdalLPWL------TV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 208 REQVIYPLkEIYPDSGSTDDERILRFLELAGLSSLVTRtegldqqvdwnWYDVLSPGEMQRLSFARLFYLQPKYAVLDEA 287
Cdd:cd03293 91 LDNVALGL-ELQGVPKAEARERAEELLELVGLSGFENA-----------YPHQLSGGMRQRVALARALAVDPDVLLLDEP 158
|
170 180 190
....*....|....*....|....*....|..
gi 1239915452 288 TSAL---T-EEVESELYRIGQQLGMTFISVGH 315
Cdd:cd03293 159 FSALdalTrEQLQEELLDIWRETGKTVLLVTH 190
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
137-315 |
3.59e-14 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 72.67 E-value: 3.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 137 HKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV----QMLTDFGPHgvlflpQKP---------FFT 203
Cdd:PRK09452 26 GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRImldgQDITHVPAE------NRHvntvfqsyaLFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 204 DGTLREQVIYPLK-------EIYPdsgstddeRILRFLELAGLSSLVTRTEgldQQvdwnwydvLSPGEMQRLSFARLFY 276
Cdd:PRK09452 100 HMTVFENVAFGLRmqktpaaEITP--------RVMEALRMVQLEEFAQRKP---HQ--------LSGGQQQRVAIARAVV 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1239915452 277 LQPKYAVLDEATSALT----EEVESELYRIGQQLGMTFISVGH 315
Cdd:PRK09452 161 NKPKVLLLDESLSALDyklrKQMQNELKALQRKLGITFVFVTH 203
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
140-291 |
6.74e-14 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 69.59 E-value: 6.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 140 LIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQMLTDFGPHGVL-----FLPQKP---FFTDgTLREQV 211
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERrksigYVMQDVdyqLFTD-SVREEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 212 IYPLKEiyPDSGSTDDERILRFLELAGLsslvtrtegldqqVDWNWYDvLSPGEMQRLSFARLFYLQPKYAVLDEATSAL 291
Cdd:cd03226 94 LLGLKE--LDAGNEQAETVLKDLDLYAL-------------KERHPLS-LSGGQKQRLAIAAALLSGKDLLIFDEPTSGL 157
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
78-312 |
7.96e-14 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 72.24 E-value: 7.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 78 THRIGELQEtLLDMSLKLRGGEILDE--------------SEWNMDRAPGWPAAEPADTAFLLE--RVSV---CAPSSHK 138
Cdd:COG1123 200 THDLGVVAE-IADRVVVMDDGRIVEDgppeeilaapqalaAVPRLGAARGRAAPAAAAAEPLLEvrNLSKrypVRGKGGV 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 139 PLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQM------------LTDFGPHgVLFLPQKP---FFT 203
Cdd:COG1123 279 RAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFdgkdltklsrrsLRELRRR-VQMVFQDPyssLNP 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 204 DGTLREQVIYPLKEIYPDSGSTDDERILRFLELAGLSSLVtrtegldqqvdWNWY-DVLSPGEMQRLSFARLFYLQPKYA 282
Cdd:COG1123 358 RMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPDL-----------ADRYpHELSGGQRQRVAIARALALEPKLL 426
|
250 260 270
....*....|....*....|....*....|....*.
gi 1239915452 283 VLDEATSAL----TEEVESELYRIGQQLGMT--FIS 312
Cdd:COG1123 427 ILDEPTSALdvsvQAQILNLLRDLQRELGLTylFIS 462
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
134-315 |
1.13e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 70.04 E-value: 1.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 134 PSSHKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQMltdFGPH-------------GVLFlpQKP 200
Cdd:PRK13635 16 PDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITV---GGMVlseetvwdvrrqvGMVF--QNP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 201 --FFTDGTLREQVIYPLKeiypDSGSTDDERILRF---LELAGLSSLVTRTEGLdqqvdwnwydvLSPGEMQRLSFARLF 275
Cdd:PRK13635 91 dnQFVGATVQDDVAFGLE----NIGVPREEMVERVdqaLRQVGMEDFLNREPHR-----------LSGGQKQRVAIAGVL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1239915452 276 YLQPKYAVLDEATSALT----EEVESELYRIGQQLGMTFISVGH 315
Cdd:PRK13635 156 ALQPDIIILDEATSMLDprgrREVLETVRQLKEQKGITVLSITH 199
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
138-315 |
1.64e-13 |
|
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: 68.82 E-value: 1.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 138 KPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV----QMLTDFGPH----GVLF-----LPQKpfftd 204
Cdd:cd03301 13 VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIyiggRDVTDLPPKdrdiAMVFqnyalYPHM----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 205 gTLREQVIYPLK-------EIypdsgstdDERILRFLELAGLSSLvtrtegLDQQVdwnwyDVLSPGEMQRLSFARLFYL 277
Cdd:cd03301 88 -TVYDNIAFGLKlrkvpkdEI--------DERVREVAELLQIEHL------LDRKP-----KQLSGGQRQRVALGRAIVR 147
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1239915452 278 QPKYAVLDEATSALT----EEVESELYRIGQQLGMTFISVGH 315
Cdd:cd03301 148 EPKVFLMDEPLSNLDaklrVQMRAELKRLQQRLGTTTIYVTH 189
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
129-327 |
2.48e-13 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 68.95 E-value: 2.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 129 VSVCAPSSHKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQG----------------------SVQMLT 186
Cdd:PRK10419 16 GGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGnvswrgeplaklnraqrkafrrDIQMVF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 187 DFGPHGVLflPQKpfftdgTLREQVIYPLKEIYPDSGSTDDERILRFLELAGLS-SLVTRtegLDQQvdwnwydvLSPGE 265
Cdd:PRK10419 96 QDSISAVN--PRK------TVREIIREPLRHLLSLDKAERLARASEMLRAVDLDdSVLDK---RPPQ--------LSGGQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1239915452 266 MQRLSFARLFYLQPKYAVLDEATS----ALTEEVESELYRIGQQLGMTFISVGHRHSL-EKFHSLVL 327
Cdd:PRK10419 157 LQRVCLARALAVEPKLLILDEAVSnldlVLQAGVIRLLKKLQQQFGTACLFITHDLRLvERFCQRVM 223
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
134-316 |
3.70e-13 |
|
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: 66.95 E-value: 3.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 134 PSSHKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQM-------LTDFGPHGVLFLPQKPFFTDGT 206
Cdd:cd03247 11 PEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLdgvpvsdLEKALSSLISVLNQRPYLFDTT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 207 LREQViyplkeiypdsGstdderiLRFlelaglsslvtrtegldqqvdwnwydvlSPGEMQRLSFARLFYLQPKYAVLDE 286
Cdd:cd03247 91 LRNNL-----------G-------RRF----------------------------SGGERQRLALARILLQDAPIVLLDE 124
|
170 180 190
....*....|....*....|....*....|..
gi 1239915452 287 ATSALTEEVESELYR-IGQQL-GMTFISVGHR 316
Cdd:cd03247 125 PTVGLDPITERQLLSlIFEVLkDKTLIWITHH 156
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
137-315 |
6.43e-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: 66.30 E-value: 6.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 137 HKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQMltdfgphgvlflpqkpfftDGTLREQviYPLK 216
Cdd:cd03214 11 GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILL-------------------DGKDLAS--LSPK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 217 EIypdsgstddERILRF----LELAGLSSLVTRTegldqqvdwnwYDVLSPGEMQRLSFARLFYLQPKYAVLDEATSAL- 291
Cdd:cd03214 70 EL---------ARKIAYvpqaLELLGLAHLADRP-----------FNELSGGERQRVLLARALAQEPPILLLDEPTSHLd 129
|
170 180
....*....|....*....|....*..
gi 1239915452 292 ---TEEVESELYRIGQQLGMTFISVGH 315
Cdd:cd03214 130 iahQIELLELLRRLARERGKTVVMVLH 156
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
138-327 |
7.56e-13 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 66.34 E-value: 7.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 138 KPLIKDLSLKISEGQSLLITGNTGTGKSSLLR-VLGGLWAsTQGSVQMltdfgPHGVLFLPQKPFFTDGTLREQVIYplk 216
Cdd:cd03250 18 SFTLKDINLEVPKGELVAIVGPVGSGKSSLLSaLLGELEK-LSGSVSV-----PGSIAYVSQEPWIQNGTIRENILF--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 217 eiypdsGST-DDERILRFLELAGLSSLVTRTEGLDQQVdwnwydV------LSPGEMQRLSFARLFYLQPKYAVLDEATS 289
Cdd:cd03250 89 ------GKPfDEERYEKVIKACALEPDLEILPDGDLTE------IgekginLSGGQKQRISLARAVYSDADIYLLDDPLS 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1239915452 290 ALTEEVESELYR--IGQQL--GMTFISVGHR-HSLEKFHSLVL 327
Cdd:cd03250 157 AVDAHVGRHIFEncILGLLlnNKTRILVTHQlQLLPHADQIVV 199
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
141-315 |
7.94e-13 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 68.59 E-value: 7.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 141 IKDLSLKISEGQ--SLLitGNTGTGKSSLLRVLGGLWASTQGSV----QMLTDFGPH----GVLFlpQK----PFFtdgT 206
Cdd:COG3842 21 LDDVSLSIEPGEfvALL--GPSGCGKTTLLRMIAGFETPDSGRIlldgRDVTGLPPEkrnvGMVF--QDyalfPHL---T 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 207 LREQVIYPLK-------EIypdsgstdDERILRFLELAGLSSLVTR--TEgldqqvdwnwydvLSPGEMQRLSFARLFYL 277
Cdd:COG3842 94 VAENVAFGLRmrgvpkaEI--------RARVAELLELVGLEGLADRypHQ-------------LSGGQQQRVALARALAP 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1239915452 278 QPKYAVLDEATSAL----TEEVESELYRIGQQLGMTFISVGH 315
Cdd:COG3842 153 EPRVLLLDEPLSALdaklREEMREELRRLQRELGITFIYVTH 194
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
139-321 |
1.02e-12 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 69.00 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 139 PLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQM----LTDFGPHG----VLFLPQKPFFTDGTLREQ 210
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLngfsLKDIDRHTlrqfINYLPQEPYIFSGSILEN 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 211 VIYPLKEiypdsGSTDDErILRFLELAGLSSLVTR-TEGLDQQVDWNWYDvLSPGEMQRLSFARLFYLQPKYAVLDEATS 289
Cdd:TIGR01193 568 LLLGAKE-----NVSQDE-IWAACEIAEIKDDIENmPLGYQTELSEEGSS-ISGGQKQRIALARALLTDSKVLILDESTS 640
|
170 180 190
....*....|....*....|....*....|....*
gi 1239915452 290 ALTEEVESELyrIGQQLGM---TFISVGHRHSLEK 321
Cdd:TIGR01193 641 NLDTITEKKI--VNNLLNLqdkTIIFVAHRLSVAK 673
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
138-315 |
1.38e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 67.06 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 138 KPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV----QMLT-----DFGPH-GVLFlpQKP--FFTDG 205
Cdd:PRK13650 20 KYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIiidgDLLTeenvwDIRHKiGMVF--QNPdnQFVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 206 TLREQVIY-------PLKEIypdsgstdDERILRFLELAGLSSLVTRTEGLdqqvdwnwydvLSPGEMQRLSFARLFYLQ 278
Cdd:PRK13650 98 TVEDDVAFglenkgiPHEEM--------KERVNEALELVGMQDFKEREPAR-----------LSGGQKQRVAIAGAVAMR 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1239915452 279 PKYAVLDEATSALTEEVESELYR----IGQQLGMTFISVGH 315
Cdd:PRK13650 159 PKIIILDEATSMLDPEGRLELIKtikgIRDDYQMTVISITH 199
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
137-315 |
2.29e-12 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 64.52 E-value: 2.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 137 HKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQML-TDFGPHGVLFLPQKP----FFTDGTL---- 207
Cdd:cd03229 12 QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDgEDLTDLEDELPPLRRrigmVFQDFALfphl 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 208 --REQVIYPLkeiypdSGstdderilrflelaglsslvtrtegldqqvdwnwydvlspGEMQRLSFARLFYLQPKYAVLD 285
Cdd:cd03229 92 tvLENIALGL------SG----------------------------------------GQQQRVALARALAMDPDVLLLD 125
|
170 180 190
....*....|....*....|....*....|....
gi 1239915452 286 EATSAL----TEEVESELYRIGQQLGMTFISVGH 315
Cdd:cd03229 126 EPTSALdpitRREVRALLKSLQAQLGITVVLVTH 159
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
137-291 |
3.87e-12 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 65.56 E-value: 3.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 137 HKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQM----LTDFGPH------GVlfLPQK-----PF 201
Cdd:PRK13548 14 GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLngrpLADWSPAelarrrAV--LPQHsslsfPF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 202 ftdgTLREQV---IYPLkeiyPDSGSTDDERILRFLELAGLSSLVTRTegldqqvdwnwYDVLSPGEMQRLSFAR-LFYL 277
Cdd:PRK13548 92 ----TVEEVVamgRAPH----GLSRAEDDALVAAALAQVDLAHLAGRD-----------YPQLSGGEQQRVQLARvLAQL 152
|
170
....*....|....*....
gi 1239915452 278 -----QPKYAVLDEATSAL 291
Cdd:PRK13548 153 wepdgPPRWLLLDEPTSAL 171
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
142-315 |
4.99e-12 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 64.24 E-value: 4.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 142 KDLSLKIS---EGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV----------QMLTDFGPH----GVLFlPQKPFFTD 204
Cdd:cd03297 11 PDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIvlngtvlfdsRKKINLPPQqrkiGLVF-QQYALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 205 GTLREQVIYPLKEIypdSGSTDDERILRFLELAGLSSLVTRteGLDQqvdwnwydvLSPGEMQRLSFARLFYLQPKYAVL 284
Cdd:cd03297 90 LNVRENLAFGLKRK---RNREDRISVDELLDLLGLDHLLNR--YPAQ---------LSGGEKQRVALARALAAQPELLLL 155
|
170 180 190
....*....|....*....|....*....|....*
gi 1239915452 285 DEATSAL----TEEVESELYRIGQQLGMTFISVGH 315
Cdd:cd03297 156 DEPFSALdralRLQLLPELKQIKKNLNIPVIFVTH 190
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
138-315 |
5.96e-12 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 64.35 E-value: 5.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 138 KPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV----QMLTDFGPHG----VLFLPQKPFFTDGTLRE 209
Cdd:PRK10247 20 AKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLlfegEDISTLKPEIyrqqVSYCAQTPTLFGDTVYD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 210 QVIYP--LKEIYPdsgstDDERILRFLELAGLSSlvtrtEGLDQQVdwnwyDVLSPGEMQRLSFARLFYLQPKYAVLDEA 287
Cdd:PRK10247 100 NLIFPwqIRNQQP-----DPAIFLDDLERFALPD-----TILTKNI-----AELSGGEKQRISLIRNLQFMPKVLLLDEI 164
|
170 180 190
....*....|....*....|....*....|..
gi 1239915452 288 TSALTEE----VESELYRIGQQLGMTFISVGH 315
Cdd:PRK10247 165 TSALDESnkhnVNEIIHRYVREQNIAVLWVTH 196
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
137-315 |
6.71e-12 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 64.34 E-value: 6.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 137 HKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGS--VQMLTDFGPH----------GVLFlPQKPFFTD 204
Cdd:PRK09493 13 PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDliVDGLKVNDPKvderlirqeaGMVF-QQFYLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 205 GTLREQVIY-PLKeiYPDSGSTDDERILRflELAGLSSLVTRTEGLDQQvdwnwydvLSPGEMQRLSFARLFYLQPKYAV 283
Cdd:PRK09493 92 LTALENVMFgPLR--VRGASKEEAEKQAR--ELLAKVGLAERAHHYPSE--------LSGGQQQRVAIARALAVKPKLML 159
|
170 180 190
....*....|....*....|....*....|....*
gi 1239915452 284 LDEATSALTEEVESELYRIGQQL---GMTFISVGH 315
Cdd:PRK09493 160 FDEPTSALDPELRHEVLKVMQDLaeeGMTMVIVTH 194
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
138-315 |
6.75e-12 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 64.62 E-value: 6.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 138 KPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV----QMLTDFGPH---------GVLF----Lpqkp 200
Cdd:COG1127 18 RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEIlvdgQDITGLSEKelyelrrriGMLFqggaL---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 201 fFTDGTLREQVIYPLKEIYPDSGSTDDERILRFLELAGLSSLVTrtegldqqvdwnwydvLSPGE----MQ-RLSFARLF 275
Cdd:COG1127 94 -FDSLTVFENVAFPLREHTDLSEAEIRELVLEKLELVGLPGAAD----------------KMPSElsggMRkRVALARAL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1239915452 276 YLQPKYAVLDEATSAL----TEEVESELYRIGQQLGMTFISVGH 315
Cdd:COG1127 157 ALDPEILLYDEPTAGLdpitSAVIDELIRELRDELGLTSVVVTH 200
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
139-315 |
1.12e-11 |
|
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: 63.90 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 139 PLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV----QMLTDFGPH--GVLFLPQK-PFFTDGTLREQV 211
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTIlfggEDATDVPVQerNVGFVFQHyALFRHMTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 212 IYPLKE---IYPDSGSTDDERILRFLELAGLSSLVTRtegldqqvdwnWYDVLSPGEMQRLSFARLFYLQPKYAVLDEAT 288
Cdd:cd03296 96 AFGLRVkprSERPPEAEIRAKVHELLKLVQLDWLADR-----------YPAQLSGGQRQRVALARALAVEPKVLLLDEPF 164
|
170 180 190
....*....|....*....|....*....|.
gi 1239915452 289 SALTEEVESELYR----IGQQLGMTFISVGH 315
Cdd:cd03296 165 GALDAKVRKELRRwlrrLHDELHVTTVFVTH 195
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
140-297 |
2.31e-11 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 64.97 E-value: 2.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 140 LIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQM----LTDFGPHGVLF----LPQKPFFTDGTLREQv 211
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIdglnIAKIGLHDLRFkitiIPQDPVLFSGSLRMN- 1379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 212 IYPLkeiypdsGSTDDERILRFLELAGLSSLVT-RTEGLDQQVDWNWYDvLSPGEMQRLSFARLFYLQPKYAVLDEATSA 290
Cdd:TIGR00957 1380 LDPF-------SQYSDEEVWWALELAHLKTFVSaLPDKLDHECAEGGEN-LSVGQRQLVCLARALLRKTKILVLDEATAA 1451
|
....*..
gi 1239915452 291 LTEEVES 297
Cdd:TIGR00957 1452 VDLETDN 1458
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
139-318 |
3.01e-11 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 64.46 E-value: 3.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 139 PLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV----QMLTDFGPH------GVLflPQKP-FFTDgTL 207
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRIlidgQDIRDVTQAslraaiGIV--PQDTvLFND-TI 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 208 REQVIY--PlkeiypdsGSTDDErILRFLELAGLSSLVTRT-EGLDQQVdwnwydvLSPGEMQRLSFARLFYLQPKYAVL 284
Cdd:COG5265 449 AYNIAYgrP--------DASEEE-VEAAARAAQIHDFIESLpDGYDTRVger-glkLSGGEKQRVAIARTLLKNPPILIF 518
|
170 180 190
....*....|....*....|....*....|....*...
gi 1239915452 285 DEATSAL---TE-EVESELYRIGQqlGMTFISVGHRHS 318
Cdd:COG5265 519 DEATSALdsrTErAIQAALREVAR--GRTTLVIAHRLS 554
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
133-315 |
3.35e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 63.21 E-value: 3.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 133 APSSHKPLIkDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQ----MLTDFGPH----------GVLF-LP 197
Cdd:PRK13643 15 SPFASRALF-DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTvgdiVVSSTSKQkeikpvrkkvGVVFqFP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 198 QKPFFTDGTLREQVIYPlkEIYPDSGSTDDERILRFLELAGLSSLVTRTEGLDqqvdwnwydvLSPGEMQRLSFARLFYL 277
Cdd:PRK13643 94 ESQLFEETVLKDVAFGP--QNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFE----------LSGGQMRRVAIAGILAM 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1239915452 278 QPKYAVLDEATSALTEEVESELYRIGQ---QLGMTFISVGH 315
Cdd:PRK13643 162 EPEVLVLDEPTAGLDPKARIEMMQLFEsihQSGQTVVLVTH 202
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
121-315 |
3.55e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 62.70 E-value: 3.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 121 DTAFLLERVSVCAPSSHKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQMltdfgphgvlflpqkp 200
Cdd:PRK13632 5 SVMIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKI---------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 201 fftDGTL--REQVIYPLKEI-----YPDS---GSTDDERILRFLElaglSSLVTRTE------GLDQQVDWNWY-----D 259
Cdd:PRK13632 69 ---DGITisKENLKEIRKKIgiifqNPDNqfiGATVEDDIAFGLE----NKKVPPKKmkdiidDLAKKVGMEDYldkepQ 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 260 VLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEVESELYRIGQQL----GMTFISVGH 315
Cdd:PRK13632 142 NLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLrktrKKTLISITH 201
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
126-315 |
4.32e-11 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 62.20 E-value: 4.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 126 LERVSVCAPSSHKPLiKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV--------------------QML 185
Cdd:cd03256 3 VENLSKTYPNGKKAL-KDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVlidgtdinklkgkalrqlrrQIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 186 TDFGPHG----------VL--FLPQKPFFtdgtlreQVI---YPLKEIypdsgstddERILRFLELAGLSSLV-TRTegl 249
Cdd:cd03256 82 MIFQQFNlierlsvlenVLsgRLGRRSTW-------RSLfglFPKEEK---------QRALAALERVGLLDKAyQRA--- 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 250 dqqvdwnwyDVLSPGEMQRLSFARLFYLQPKYAVLDEATSAL----TEEVESELYRIGQQLGMTFISVGH 315
Cdd:cd03256 143 ---------DQLSGGQQQRVAIARALMQQPKLILADEPVASLdpasSRQVMDLLKRINREEGITVIVSLH 203
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
140-315 |
4.96e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 62.29 E-value: 4.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 140 LIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV-------QMLTDfgPHGVLFLPQKPFFTdgTLREQVI 212
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIvvngqtiNLVRD--KDGQLKVADKNQLR--LLRTRLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 213 YPLKEIYPDSGSTDDERILRF-LELAGLSSLVTRTE--------GLDQQVDWNWYDVLSPGEMQRLSFARLFYLQPKYAV 283
Cdd:PRK10619 96 MVFQHFNLWSHMTVLENVMEApIQVLGLSKQEARERavkylakvGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLL 175
|
170 180 190
....*....|....*....|....*....|....*
gi 1239915452 284 LDEATSALTEEVESELYRIGQQL---GMTFISVGH 315
Cdd:PRK10619 176 FDEPTSALDPELVGEVLRIMQQLaeeGKTMVVVTH 210
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
142-315 |
5.19e-11 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 61.39 E-value: 5.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 142 KDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV----QMLTDFGPH--------GVLFlPQKPFFTDGTLRE 209
Cdd:cd03262 17 KGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIiidgLKLTDDKKNinelrqkvGMVF-QQFNLFPHLTVLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 210 QVIYPLKEIYPDSGSTDDERILRFLELAGLSslvtrteglDQQvdwNWY-DVLSPGEMQRLSFARLFYLQPKYAVLDEAT 288
Cdd:cd03262 96 NITLAPIKVKGMSKAEAEERALELLEKVGLA---------DKA---DAYpAQLSGGQQQRVAIARALAMNPKVMLFDEPT 163
|
170 180 190
....*....|....*....|....*....|
gi 1239915452 289 SALTEEVESELYRIGQQL---GMTFISVGH 315
Cdd:cd03262 164 SALDPELVGEVLDVMKDLaeeGMTMVVVTH 193
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
139-300 |
6.66e-11 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 63.78 E-value: 6.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 139 PLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQmltdfgpHG--VLFLPQKPFFTDGTLREQVIYPLk 216
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIK-------HSgrISFSPQTSWIMPGTIKDNIIFGL- 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 217 eiypdsgSTDDERILRFLELAGLSSLVTRTEGLDQQVDWNWYDVLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEVE 296
Cdd:TIGR01271 512 -------SYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTE 584
|
....
gi 1239915452 297 SELY 300
Cdd:TIGR01271 585 KEIF 588
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
141-315 |
1.18e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 61.57 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 141 IKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQ----MLT------DFGPH----GVLF-LPQKPFFTDG 205
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTigerVITagkknkKLKPLrkkvGIVFqFPEHQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 206 TLREQVIYPLkeiypDSGSTDDERILR---FLELAGLS-SLVTRTEgldqqvdwnwYDvLSPGEMQRLSFARLFYLQPKY 281
Cdd:PRK13634 103 VEKDICFGPM-----NFGVSEEDAKQKareMIELVGLPeELLARSP----------FE-LSGGQMRRVAIAGVLAMEPEV 166
|
170 180 190
....*....|....*....|....*....|....*...
gi 1239915452 282 AVLDEATSAL----TEEVESELYRIGQQLGMTFISVGH 315
Cdd:PRK13634 167 LVLDEPTAGLdpkgRKEMMEMFYKLHKEKGLTTVLVTH 204
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
136-299 |
1.21e-10 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 60.56 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 136 SHKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGsvQMLTDFGP---------HGVLFL-PQKPFFTDG 205
Cdd:cd03248 25 PDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGG--QVLLDGKPisqyehkylHSKVSLvGQEPVLFAR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 206 TLREQVIYPLkeiypdsGSTDDERILRFLELAGLSSLVTRTE-GLDQQVDWNWyDVLSPGEMQRLSFARLFYLQPKYAVL 284
Cdd:cd03248 103 SLQDNIAYGL-------QSCSFECVKEAAQKAHAHSFISELAsGYDTEVGEKG-SQLSGGQKQRVAIARALIRNPQVLIL 174
|
170
....*....|....*
gi 1239915452 285 DEATSALteEVESEL 299
Cdd:cd03248 175 DEATSAL--DAESEQ 187
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
115-315 |
1.24e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 60.85 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 115 PAAEPADTAFLLERVSvcAPSSHKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGsvQMLTDFGPHGVL 194
Cdd:PRK11247 4 TARLNQGTPLLLNAVS--KRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAG--ELLAGTAPLAEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 195 FLPQKPFFTDGTLreqviYPLKEIYPDSG---STD-DERILRFLELAGLSSLVTrtegldqqvdwNWYDVLSPGEMQRLS 270
Cdd:PRK11247 80 REDTRLMFQDARL-----LPWKKVIDNVGlglKGQwRDAALQALAAVGLADRAN-----------EWPAALSGGQKQRVA 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1239915452 271 FARLFYLQPKYAVLDE---ATSALTE-EVESELYRIGQQLGMTFISVGH 315
Cdd:PRK11247 144 LARALIHRPGLLLLDEplgALDALTRiEMQDLIESLWQQHGFTVLLVTH 192
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
141-316 |
1.60e-10 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 60.53 E-value: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 141 IKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV----QMLTDFGPH-----GVL--FlpQKP-FFTDGTLR 208
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVlfdgEDITGLPPHeiarlGIGrtF--QIPrLFPELTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 209 EQVI---------YPLKEIYPDSGSTDDERILRFLELAGLSSLVTRTEGLdqqvdwnwydvLSPGEMQRLSFARLFYLQP 279
Cdd:cd03219 94 ENVMvaaqartgsGLLLARARREEREARERAEELLERVGLADLADRPAGE-----------LSYGQQRRLEIARALATDP 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1239915452 280 KYAVLDEATSALT-EEVESELYRIGQ--QLGMTFISVGHR 316
Cdd:cd03219 163 KLLLLDEPAAGLNpEETEELAELIRElrERGITVLLVEHD 202
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
137-313 |
2.61e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 60.19 E-value: 2.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 137 HKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVqMLTDFGPHgvlflpqkpfFTDGTLREQVIyplK 216
Cdd:PRK15112 25 TVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGEL-LIDDHPLH----------FGDYSYRSQRI---R 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 217 EIYPDSGSTDDER-----ILRF-LELAGLSSLVTRTEGLDQ---QVDW-----NWY-DVLSPGEMQRLSFARLFYLQPKY 281
Cdd:PRK15112 91 MIFQDPSTSLNPRqrisqILDFpLRLNTDLEPEQREKQIIEtlrQVGLlpdhaSYYpHMLAPGQKQRLGLARALILRPKV 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 1239915452 282 AVLDEATSALTEEVESELYRIGQQL----GMTFISV 313
Cdd:PRK15112 171 IIADEALASLDMSMRSQLINLMLELqekqGISYIYV 206
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
137-288 |
4.01e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 60.85 E-value: 4.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 137 HKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQMltdfgPHG--VLFLPQKPFFTDG-TLREQVIY 213
Cdd:COG0488 10 GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI-----PKGlrIGYLPQEPPLDDDlTVLDTVLD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 214 PLKEIY------------PDSGSTDDERIL----RFLELAG----------LSSLVTRTEGLDQQVdwnwyDVLSPGEMQ 267
Cdd:COG0488 85 GDAELRaleaeleeleakLAEPDEDLERLAelqeEFEALGGweaearaeeiLSGLGFPEEDLDRPV-----SELSGGWRR 159
|
170 180
....*....|....*....|.
gi 1239915452 268 RLSFARLFYLQPKYAVLDEAT 288
Cdd:COG0488 160 RVALARALLSEPDLLLLDEPT 180
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
141-315 |
4.30e-10 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 60.43 E-value: 4.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 141 IKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGsvQMLTDfgphGVLFLPqkpfFTDGTLRE------QVIYP 214
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRG--QVLID----GVDIAK----ISDAELREvrrkkiAMVFQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 215 LKEIYPDSGSTDDERIlrFLELAGLSSLVTRTEGLD--QQVDWNWY-----DVLSPGEMQRLSFARLFYLQPKYAVLDEA 287
Cdd:PRK10070 114 SFALMPHMTVLDNTAF--GMELAGINAEERREKALDalRQVGLENYahsypDELSGGMRQRVGLARALAINPDILLMDEA 191
|
170 180 190
....*....|....*....|....*....|..
gi 1239915452 288 TSALT----EEVESELYRIGQQLGMTFISVGH 315
Cdd:PRK10070 192 FSALDplirTEMQDELVKLQAKHQRTIVFISH 223
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
119-316 |
6.35e-10 |
|
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: 58.19 E-value: 6.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 119 PADTAFLLERVSVCAPSSHKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQM---------LTDFg 189
Cdd:cd03369 2 PEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIdgidistipLEDL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 190 PHGVLFLPQKPFFTDGTLREQViyplkEIYpdsGSTDDERILRFLELaglsslvtrTEGLDQqvdwnwydvLSPGEMQRL 269
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNL-----DPF---DEYSDEEIYGALRV---------SEGGLN---------LSQGQRQLL 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1239915452 270 SFARLFYLQPKYAVLDEATSALTEEVESELYRIGQQL--GMTFISVGHR 316
Cdd:cd03369 135 CLARALLKRPRVLVLDEATASIDYATDALIQKTIREEftNSTILTIAHR 183
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
143-315 |
9.94e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 58.60 E-value: 9.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 143 DLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV----QMLTDFGPH----------GVLF-LPQKPFFTDGTL 207
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVrvddTLITSTSKNkdikqirkkvGLVFqFPESQLFEETVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 208 REQVIYPL-----KEiypdsgstDDERILR-FLELAGLSslvtrteglDQQVDWNWYDvLSPGEMQRLSFARLFYLQPKY 281
Cdd:PRK13649 105 KDVAFGPQnfgvsQE--------EAEALAReKLALVGIS---------ESLFEKNPFE-LSGGQMRRVAIAGILAMEPKI 166
|
170 180 190
....*....|....*....|....*....|....*..
gi 1239915452 282 AVLDEATSALTEEVESELYRIGQQL---GMTFISVGH 315
Cdd:PRK13649 167 LVLDEPTAGLDPKGRKELMTLFKKLhqsGMTIVLVTH 203
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
139-300 |
1.05e-09 |
|
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: 58.71 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 139 PLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQmltdfgpHG--VLFLPQKPFFTDGTLREQVIYPLk 216
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK-------HSgrISFSSQFSWIMPGTIKENIIFGV- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 217 eiypdsgSTDDERILRFLELAGLSSLVTRTEGLDQQVDWNWYDVLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEVE 296
Cdd:cd03291 123 -------SYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTE 195
|
....
gi 1239915452 297 SELY 300
Cdd:cd03291 196 KEIF 199
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
119-315 |
1.69e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 57.89 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 119 PADTAFLLERVSVCAPSSHKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLwastqgsvqMLTDFGPHGVLFLpq 198
Cdd:PRK13640 1 MKDNIVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGL---------LLPDDNPNSKITV-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 199 kpfftDG-TLREQVIYPLKEIY------PDS---GSTDDERILRFLELAGL--SSLVTRTEGLDQQVDWNWY-----DVL 261
Cdd:PRK13640 70 -----DGiTLTAKTVWDIREKVgivfqnPDNqfvGATVGDDVAFGLENRAVprPEMIKIVRDVLADVGMLDYidsepANL 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1239915452 262 SPGEMQRLSFARLFYLQPKYAVLDEATSALTEEVESELYRIGQQL----GMTFISVGH 315
Cdd:PRK13640 145 SGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLkkknNLTVISITH 202
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
139-316 |
1.77e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 59.22 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 139 PLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQM----LTDFGPHGVL----FLPQKPFFTDGTLREQ 210
Cdd:PLN03232 1250 PVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIddcdVAKFGLTDLRrvlsIIPQSPVLFSGTVRFN 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 211 vIYPLKEiypdsgsTDDERILRFLELAGLSSLVTRTE-GLDQQVdWNWYDVLSPGEMQRLSFARLFYLQPKYAVLDEATS 289
Cdd:PLN03232 1330 -IDPFSE-------HNDADLWEALERAHIKDVIDRNPfGLDAEV-SEGGENFSVGQRQLLSLARALLRRSKILVLDEATA 1400
|
170 180
....*....|....*....|....*....
gi 1239915452 290 ALTEEVESELYR-IGQQL-GMTFISVGHR 316
Cdd:PLN03232 1401 SVDVRTDSLIQRtIREEFkSCTMLVIAHR 1429
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
126-291 |
2.48e-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: 56.90 E-value: 2.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 126 LERVSVCAPSSHKP--LIKDLSLKISEGQSLLITGNTGTGKSSLL-----RVLGGlwASTQGSV----------QMLTDF 188
Cdd:cd03234 6 WWDVGLKAKNWNKYarILNDVSLHVESGQVMAILGSSGSGKTTLLdaisgRVEGG--GTTSGQIlfngqprkpdQFQKCV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 189 GphgvlFLPQKPFFTDG-TLREQVIY----PLKEIYPDSGSTDDERILRFLELAglsslvtrteglDQQVDWNWYDVLSP 263
Cdd:cd03234 84 A-----YVRQDDILLPGlTVRETLTYtailRLPRKSSDAIRKKRVEDVLLRDLA------------LTRIGGNLVKGISG 146
|
170 180
....*....|....*....|....*...
gi 1239915452 264 GEMQRLSFARLFYLQPKYAVLDEATSAL 291
Cdd:cd03234 147 GERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
138-315 |
2.55e-09 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 57.92 E-value: 2.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 138 KPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV----QMLTDFGPHgvlflpQKP---------FFTD 204
Cdd:PRK11607 32 QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQImldgVDLSHVPPY------QRPinmmfqsyaLFPH 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 205 GTLREQVIYPLKEIYPDSGSTDDeRILRFLELAGLSSLVTRTEgldQQvdwnwydvLSPGEMQRLSFARLFYLQPKYAVL 284
Cdd:PRK11607 106 MTVEQNIAFGLKQDKLPKAEIAS-RVNEMLGLVHMQEFAKRKP---HQ--------LSGGQRQRVALARSLAKRPKLLLL 173
|
170 180 190
....*....|....*....|....*....|....*
gi 1239915452 285 DEATSALT----EEVESELYRIGQQLGMTFISVGH 315
Cdd:PRK11607 174 DEPMGALDkklrDRMQLEVVDILERVGVTCVMVTH 208
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
141-338 |
3.51e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 56.98 E-value: 3.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 141 IKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQM----LTDFGPH--------GVLFlpQKPFFtdgTLR 208
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIdgvdITDKKVKlsdirkkvGLVF--QYPEY---QLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 209 EQVIYplKEIY--PDS-GSTDDE---RILRFLELAGLSslvtrtegLDQQVDWNWYDvLSPGEMQRLSFARLFYLQPKYA 282
Cdd:PRK13637 98 EETIE--KDIAfgPINlGLSEEEienRVKRAMNIVGLD--------YEDYKDKSPFE-LSGGQKRRVAIAGVVAMEPKIL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1239915452 283 VLDEATSALT----EEVESELYRIGQQLGMTFISVGhrHSLEKFHSLVLKLY--GEGRWELS 338
Cdd:PRK13637 167 ILDEPTAGLDpkgrDEILNKIKELHKEYNMTIILVS--HSMEDVAKLADRIIvmNKGKCELQ 226
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
142-309 |
4.81e-09 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 57.01 E-value: 4.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 142 KDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV----QMLTDFGPH---------GVLF-----LPQKpfft 203
Cdd:COG1135 22 DDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVlvdgVDLTALSERelraarrkiGMIFqhfnlLSSR---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 204 dgTLREQVIYPLK-------EIypdsgstdDERILRFLELAGLSslvtrteglDQQvdWNWYDVLSPGEMQRLSFARLFY 276
Cdd:COG1135 98 --TVAENVALPLEiagvpkaEI--------RKRVAELLELVGLS---------DKA--DAYPSQLSGGQKQRVGIARALA 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 1239915452 277 LQPKyaVL--DEATSAL----TEEVESELYRIGQQLGMT 309
Cdd:COG1135 157 NNPK--VLlcDEATSALdpetTRSILDLLKDINRELGLT 193
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
138-291 |
6.44e-09 |
|
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: 57.61 E-value: 6.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 138 KPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLwASTQG----------SVQMLTDFGPHGVlfLPQKPFFTDGTL 207
Cdd:TIGR01271 1232 RAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGeiqidgvswnSVTLQTWRKAFGV--IPQKVFIFSGTF 1308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 208 ReqviyplKEIYPDSGSTDDErILRFLELAGLSSLVTRTEG-LDQQVDWNWYdVLSPGEMQRLSFARLFYLQPKYAVLDE 286
Cdd:TIGR01271 1309 R-------KNLDPYEQWSDEE-IWKVAEEVGLKSVIEQFPDkLDFVLVDGGY-VLSNGHKQLMCLARSILSKAKILLLDE 1379
|
....*
gi 1239915452 287 ATSAL 291
Cdd:TIGR01271 1380 PSAHL 1384
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
138-291 |
6.85e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 55.27 E-value: 6.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 138 KPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQmLTDFGPHGVLFLPQ----------KPFFtdgTL 207
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIK-LDGGDIDDPDVAEAchylghrnamKPAL---TV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 208 REQVIYpLKEIYpdsgSTDDERILRFLELAGLSSLVTRTegldqqvdwnwYDVLSPGEMQRLSFARLFYLQPKYAVLDEA 287
Cdd:PRK13539 91 AENLEF-WAAFL----GGEELDIAAALEAVGLAPLAHLP-----------FGYLSAGQKRRVALARLLVSNRPIWILDEP 154
|
....
gi 1239915452 288 TSAL 291
Cdd:PRK13539 155 TAAL 158
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
137-320 |
7.63e-09 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 56.25 E-value: 7.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 137 HKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQMltdfgpHG------------VLFLPQK-PFFT 203
Cdd:PRK10851 14 RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRF------HGtdvsrlhardrkVGFVFQHyALFR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 204 DGTLREQVIYPLKeIYP----DSGSTDDERILRFLELAGLSSLVTRtegldqqvdwnWYDVLSPGEMQRLSFARLFYLQP 279
Cdd:PRK10851 88 HMTVFDNIAFGLT-VLPrrerPNAAAIKAKVTQLLEMVQLAHLADR-----------YPAQLSGGQKQRVALARALAVEP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1239915452 280 KYAVLDEATSALTEEVESELYRIGQQLG--MTFISVGHRHSLE 320
Cdd:PRK10851 156 QILLLDEPFGALDAQVRKELRRWLRQLHeeLKFTSVFVTHDQE 198
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
141-309 |
1.01e-08 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 54.75 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 141 IKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQM----LTDFGPH-----GVLFLPQ-KPFFTDGTLREQ 210
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFdgrdITGLPPHeraraGIGYVPEgRRIFPELTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 211 VIYPLKEIYPDSGSTDDERIL-RFLELAglsslvtrtEGLDQQVdwnwyDVLSPGEMQRLSFARLFYLQPKYAVLDEATS 289
Cdd:cd03224 96 LLLGAYARRRAKRKARLERVYeLFPRLK---------ERRKQLA-----GTLSGGEQQMLAIARALMSRPKLLLLDEPSE 161
|
170 180
....*....|....*....|....
gi 1239915452 290 AL----TEEVESELYRIgQQLGMT 309
Cdd:cd03224 162 GLapkiVEEIFEAIREL-RDEGVT 184
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
129-321 |
1.35e-08 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 56.18 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 129 VSVCAPSSHKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQM---------LTDFGPHGVLFLPQK 199
Cdd:PRK11176 347 VTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLdghdlrdytLASLRNQVALVSQNV 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 200 PFFTDgTLREQVIYPLKEIYpdsgstDDERILRFLELAGLSSLVTRTE-GLDQQVDWNWYdVLSPGEMQRLSFARLFYLQ 278
Cdd:PRK11176 427 HLFND-TIANNIAYARTEQY------SREQIEEAARMAYAMDFINKMDnGLDTVIGENGV-LLSGGQRQRIAIARALLRD 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1239915452 279 PKYAVLDEATSALteEVESElyRIGQ------QLGMTFISVGHRHS-LEK 321
Cdd:PRK11176 499 SPILILDEATSAL--DTESE--RAIQaaldelQKNRTSLVIAHRLStIEK 544
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
138-291 |
1.91e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 55.62 E-value: 1.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 138 KPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGlWASTQGSVQM----LTDFGP----HGVLFLPQKPFFTDGTLRE 209
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLG-FLPYQGSLKIngieLRELDPeswrKHLSWVGQNPQLPHGTLRD 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 210 QVIYPLKEIypdsgstDDERILRFLELAGLSSLVTR-TEGLDQQV-DWNwyDVLSPGEMQRLSFARLFYLQPKYAVLDEA 287
Cdd:PRK11174 442 NVLLGNPDA-------SDEQLQQALENAWVSEFLPLlPQGLDTPIgDQA--AGLSVGQAQRLALARALLQPCQLLLLDEP 512
|
....
gi 1239915452 288 TSAL 291
Cdd:PRK11174 513 TASL 516
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
22-300 |
1.98e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 56.14 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 22 SYVVIAIPIFS-----GVY----GDLSPTElstlvsknAFVCIYLISCF-TRLIDLSSTLSDVAGYTHRIGELQETLLDM 91
Cdd:PLN03232 527 SFILNSIPVVVtlvsfGVFvllgGDLTPAR--------AFTSLSLFAVLrSPLNMLPNLLSQVVNANVSLQRIEELLLSE 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 92 SlklrggEILDEsewNMDRAPGWPAAEPADTAFLLERvsvcapSSHKPLIKDLSLKISEGQSLLITGNTGTGKSSLLR-V 170
Cdd:PLN03232 599 E------RILAQ---NPPLQPGAPAISIKNGYFSWDS------KTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISaM 663
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 171 LGGLWASTQGSVQMLTDfgphgVLFLPQKPFFTDGTLREQVIYplkeiypdsGST-DDERILRFLELAGLSSLVTRTEGL 249
Cdd:PLN03232 664 LGELSHAETSSVVIRGS-----VAYVPQVSWIFNATVRENILF---------GSDfESERYWRAIDVTALQHDLDLLPGR 729
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1239915452 250 DQQVDWNWYDVLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEVESELY 300
Cdd:PLN03232 730 DLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVF 780
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
143-315 |
3.09e-08 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 53.86 E-value: 3.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 143 DLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQMLT---DF----GPHGVLFLPQK-----------PFFtd 204
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfDFsktpSDKAIRELRRNvgmvfqqynlwPHL-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 205 gTLREQVI-YPLKEIypdsGSTDDERILRFLELagLSSLvtrteGLDQQVDwNWYDVLSPGEMQRLSFARLFYLQPKYAV 283
Cdd:PRK11124 98 -TVQQNLIeAPCRVL----GLSKDQALARAEKL--LERL-----RLKPYAD-RFPLHLSGGQQQRVAIARALMMEPQVLL 164
|
170 180 190
....*....|....*....|....*....|....*
gi 1239915452 284 LDEATSALTEEVESELYRIGQQL---GMTFISVGH 315
Cdd:PRK11124 165 FDEPTAALDPEITAQIVSIIRELaetGITQVIVTH 199
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
141-315 |
3.64e-08 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 54.31 E-value: 3.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 141 IKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV----QMLTDFGPH--GVLFLPQK----PFFtdgTLREQ 210
Cdd:COG3839 19 LKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEIliggRDVTDLPPKdrNIAMVFQSyalyPHM---TVYEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 211 VIYPLK-------EIypdsgstdDERILRFLELAGLSSLvtrtegLDQ---QvdwnwydvLSPGEMQRLSFARLFYLQPK 280
Cdd:COG3839 96 IAFPLKlrkvpkaEI--------DRRVREAAELLGLEDL------LDRkpkQ--------LSGGQRQRVALGRALVREPK 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 1239915452 281 YAVLDEATS----ALTEEVESELYRIGQQLGMTFISVGH 315
Cdd:COG3839 154 VFLLDEPLSnldaKLRVEMRAEIKRLHRRLGTTTIYVTH 192
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
140-291 |
4.94e-08 |
|
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: 53.32 E-value: 4.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 140 LIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLwASTQGSVQM-------------LTDFGphgvlFLPQKPFFTDGT 206
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQIdgvswnsvplqkwRKAFG-----VIPQKVFIFSGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 207 LReqviyplKEIYPdSGSTDDERILRFLELAGLSSLVTRTEG-LDQQVDWNWYdVLSPGEMQRLSFARLFYLQPKYAVLD 285
Cdd:cd03289 93 FR-------KNLDP-YGKWSDEEIWKVAEEVGLKSVIEQFPGqLDFVLVDGGC-VLSHGHKQLMCLARSVLSKAKILLLD 163
|
....*.
gi 1239915452 286 EATSAL 291
Cdd:cd03289 164 EPSAHL 169
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
116-312 |
6.09e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 53.13 E-value: 6.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 116 AAEPADTAFLLERVSVCApsSHKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQM---LTDFGPH- 191
Cdd:PRK14246 3 AGKSAEDVFNISRLYLYI--NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVdgkVLYFGKDi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 192 ------------GVLFLPQKPFfTDGTLREQVIYPLKEiypdSGSTDDERILRFLELAglsslvTRTEGLDQQVdwnwYD 259
Cdd:PRK14246 81 fqidaiklrkevGMVFQQPNPF-PHLSIYDNIAYPLKS----HGIKEKREIKKIVEEC------LRKVGLWKEV----YD 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1239915452 260 -------VLSPGEMQRLSFARLFYLQPKYAVLDEATSAL----TEEVESELYRIGQQLGMTFIS 312
Cdd:PRK14246 146 rlnspasQLSGGQQQRLTIARALALKPKVLLMDEPTSMIdivnSQAIEKLITELKNEIAIVIVS 209
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
138-315 |
7.52e-08 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 52.71 E-value: 7.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 138 KPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV----QMLTDFGP----HGVLFLPQKPFFTDG-TLR 208
Cdd:PRK11231 15 KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVflgdKPISMLSSrqlaRRLALLPQHHLTPEGiTVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 209 EQVIY---PLKEIYPDSGSTDDERILRFLELAGLSSLVtrteglDQQVdwnwyDVLSPGEMQRLSFARLFYLQPKYAVLD 285
Cdd:PRK11231 95 ELVAYgrsPWLSLWGRLSAEDNARVNQAMEQTRINHLA------DRRL-----TDLSGGQRQRAFLAMVLAQDTPVVLLD 163
|
170 180 190
....*....|....*....|....*....|...
gi 1239915452 286 EATSALTEEVESELYRIGQQL---GMTFISVGH 315
Cdd:PRK11231 164 EPTTYLDINHQVELMRLMRELntqGKTVVTVLH 196
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
112-290 |
1.23e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 53.59 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 112 PGWPAAepadTAFLLERVSVCAPSSHKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQM------- 184
Cdd:PLN03130 1230 PGWPSS----GSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIdgcdisk 1305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 185 --LTDFgpHGVL-FLPQKPFFTDGTLREQvIYPLKEiypdsgsTDDERILRFLELAGLSSLVTR-TEGLDQQVDwNWYDV 260
Cdd:PLN03130 1306 fgLMDL--RKVLgIIPQAPVLFSGTVRFN-LDPFNE-------HNDADLWESLERAHLKDVIRRnSLGLDAEVS-EAGEN 1374
|
170 180 190
....*....|....*....|....*....|
gi 1239915452 261 LSPGEMQRLSFARLFYLQPKYAVLDEATSA 290
Cdd:PLN03130 1375 FSVGQRQLLSLARALLRRSKILVLDEATAA 1404
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
140-291 |
1.50e-07 |
|
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: 50.95 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 140 LIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQM-------LTDFGPHGVLFLPQKPFFTdGTLreQVI 212
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLnggpldfQRDSIARGLLYLGHAPGIK-TTL--SVL 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1239915452 213 YPLKEIYPDSGstdDERILRFLELAGLSSLVTRTEGldqqvdwnwydVLSPGEMQRLSFARLFYLQPKYAVLDEATSAL 291
Cdd:cd03231 92 ENLRFWHADHS---DEQVEEALARVGLNGFEDRPVA-----------QLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
142-309 |
1.69e-07 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 52.11 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 142 KDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV----QMLTDFGPH---------GVLF-----LPQKpfft 203
Cdd:PRK11153 22 NNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVlvdgQDLTALSEKelrkarrqiGMIFqhfnlLSSR---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 204 dgTLREQVIYPLK-------EIypdsgstdDERILRFLELAGLSSLVTRtegldqqvdwnwYDV-LSPGEMQRLSFARLF 275
Cdd:PRK11153 98 --TVFDNVALPLElagtpkaEI--------KARVTELLELVGLSDKADR------------YPAqLSGGQKQRVAIARAL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1239915452 276 YLQPKyaVL--DEATSAL----TEEVESELYRIGQQLGMT 309
Cdd:PRK11153 156 ASNPK--VLlcDEATSALdpatTRSILELLKDINRELGLT 193
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
132-318 |
1.73e-07 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 52.79 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 132 CAPSSHKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV----QMLTDFGPHG----VLFLPQKPF-F 202
Cdd:PRK10789 322 TYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIrfhdIPLTKLQLDSwrsrLAVVSQTPFlF 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 203 TDgtlreQVIYPLKEIYPDSGSTDDERILRfleLAGLSSLVTR-TEGLDQQVDWNWYdVLSPGEMQRLSFARLFYLQPKY 281
Cdd:PRK10789 402 SD-----TVANNIALGRPDATQQEIEHVAR---LASVHDDILRlPQGYDTEVGERGV-MLSGGQKQRISIARALLLNAEI 472
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1239915452 282 AVLDEATSAL---TE-EVESELYRIGQqlGMTFISVGHRHS 318
Cdd:PRK10789 473 LILDDALSAVdgrTEhQILHNLRQWGE--GRTVIISAHRLS 511
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
141-333 |
2.12e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 51.68 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 141 IKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV---------QMLTDFGPH-GVLFlpQKP--FFTDGTLR 208
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqaitdDNFEKLRKHiGIVF--QNPdnQFVGSIVK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 209 EQVIYPLKEiypDSGSTDD-ERILrflelaglSSLVTRTEGLDQQVDWNwyDVLSPGEMQRLSFARLFYLQPKYAVLDEA 287
Cdd:PRK13648 103 YDVAFGLEN---HAVPYDEmHRRV--------SEALKQVDMLERADYEP--NALSGGQKQRVAIAGVLALNPSVIILDEA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1239915452 288 TSALTEEVESELYRIGQQL----GMTFISVGH--RHSLEKFHSLVL---KLYGEG 333
Cdd:PRK13648 170 TSMLDPDARQNLLDLVRKVksehNITIISITHdlSEAMEADHVIVMnkgTVYKEG 224
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
139-300 |
2.38e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 52.64 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 139 PLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQMltdfgPHGVLFLPQKPFFTDGTLREQVIY--PLK 216
Cdd:TIGR00957 652 PTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHM-----KGSVAYVPQQAWIQNDSLRENILFgkALN 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 217 EIYPDSgSTDDERILRFLELagLSSlVTRTEGLDQQVDwnwydvLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEVE 296
Cdd:TIGR00957 727 EKYYQQ-VLEACALLPDLEI--LPS-GDRTEIGEKGVN------LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVG 796
|
....
gi 1239915452 297 SELY 300
Cdd:TIGR00957 797 KHIF 800
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
113-325 |
2.52e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 52.01 E-value: 2.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 113 GWPAAEPADTAFLL--ERVSVCAP---------SSHKPLIKDLSLKISEGQSLLITGNTGTGKSS----LLRVL---GGL 174
Cdd:PRK15134 263 GDPVPLPEPASPLLdvEQLQVAFPirkgilkrtVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLInsqGEI 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 175 WASTQ-----GSVQMLTDFGPHGVLFlpQKPfftDGTLR-----EQVIYP-LKEIYPD-SGSTDDERILRFLELAGLssl 242
Cdd:PRK15134 343 WFDGQplhnlNRRQLLPVRHRIQVVF--QDP---NSSLNprlnvLQIIEEgLRVHQPTlSAAQREQQVIAVMEEVGL--- 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 243 vtrteglDQQVDWNWYDVLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEVESE---LYRIGQQ---LGMTFISvghr 316
Cdd:PRK15134 415 -------DPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQilaLLKSLQQkhqLAYLFIS---- 483
|
....*....
gi 1239915452 317 HSLEKFHSL 325
Cdd:PRK15134 484 HDLHVVRAL 492
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
141-291 |
2.61e-07 |
|
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: 50.36 E-value: 2.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 141 IKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQM----LTDFGPHGVLFLPQ-KPFFTDGTLREQVIYpL 215
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFdgkpLDIAARNRIGYLPEeRGLYPKMKVIDQLVY-L 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1239915452 216 KEIYPDSGSTDDERILRFLELAGLSSLvtRTEGLDQqvdwnwydvLSPGEMQRLSFARLFYLQPKYAVLDEATSAL 291
Cdd:cd03269 95 AQLKGLKKEEARRRIDEWLERLELSEY--ANKRVEE---------LSKGNQQKVQFIAAVIHDPELLILDEPFSGL 159
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
143-315 |
3.01e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 50.98 E-value: 3.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 143 DLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQMLtdfGPH-----------------GVLF-LPQKPFFTD 204
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIA---GYHitpetgnknlkklrkkvSLVFqFPEAQLFEN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 205 GTLREQVIYPLkeiypDSGSTDDE---RILRFLELAGLSSLVTRTEGLDqqvdwnwydvLSPGEMQRLSFARLFYLQPKY 281
Cdd:PRK13641 102 TVLKDVEFGPK-----NFGFSEDEakeKALKWLKKVGLSEDLISKSPFE----------LSGGQMRRVAIAGVMAYEPEI 166
|
170 180 190
....*....|....*....|....*....|....*..
gi 1239915452 282 AVLDEATSALTEEVESELYRI---GQQLGMTFISVGH 315
Cdd:PRK13641 167 LCLDEPAAGLDPEGRKEMMQLfkdYQKAGHTVILVTH 203
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
141-315 |
3.46e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 51.00 E-value: 3.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 141 IKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV---QMLTDFGPHGVLFL----------PQKPFFTdGTL 207
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRIlfdGKPIDYSRKGLMKLresvgmvfqdPDNQLFS-ASV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 208 REQVIY-------PLKEIYpdsgstddERILRFLELAGLSSLVtrteglDQQVDWnwydvLSPGEMQRLSFARLFYLQPK 280
Cdd:PRK13636 101 YQDVSFgavnlklPEDEVR--------KRVDNALKRTGIEHLK------DKPTHC-----LSFGQKKRVAIAGVLVMEPK 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 1239915452 281 YAVLDEATSAL----TEEVESELYRIGQQLGMTFISVGH 315
Cdd:PRK13636 162 VLVLDEPTAGLdpmgVSEIMKLLVEMQKELGLTIIIATH 200
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
126-318 |
3.56e-07 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 51.88 E-value: 3.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 126 LERVSVCAPSSHKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVqmltdfgphgvlflpqkpfFTDG 205
Cdd:TIGR03797 454 VDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSV-------------------FYDG 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 206 ---------TLREQVIYPLKEIYPDSGStdderILRflELAGLSSL-------VTRTEGLDQQVD---WNWYDV------ 260
Cdd:TIGR03797 515 qdlagldvqAVRRQLGVVLQNGRLMSGS-----IFE--NIAGGAPLtldeaweAARMAGLAEDIRampMGMHTViseggg 587
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1239915452 261 -LSPGEMQRLSFARLFYLQPKYAVLDEATSAL---TEEVESELYrigQQLGMTFISVGHRHS 318
Cdd:TIGR03797 588 tLSGGQRQRLLIARALVRKPRILLFDEATSALdnrTQAIVSESL---ERLKVTRIVIAHRLS 646
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
141-330 |
3.61e-07 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 51.25 E-value: 3.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 141 IKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV----QMLTDFGPHG---------VLFlpQKPFFTDG-- 205
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVawlgKDLLGMKDDEwravrsdiqMIF--QDPLASLNpr 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 206 -TLREQVIYPLKEIYPD-SGSTDDERILRFLELAGLsslvtrtegLDQQVdwNWY-DVLSPGEMQRLSFARLFYLQPKYA 282
Cdd:PRK15079 115 mTIGEIIAEPLRTYHPKlSRQEVKDRVKAMMLKVGL---------LPNLI--NRYpHEFSGGQCQRIGIARALILEPKLI 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1239915452 283 VLDEATSALTEEVESELYRIGQQL----GMTFISVGHRHSLEKFHS-LVLKLY 330
Cdd:PRK15079 184 ICDEPVSALDVSIQAQVVNLLQQLqremGLSLIFIAHDLAVVKHISdRVLVMY 236
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
138-299 |
3.99e-07 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 51.50 E-value: 3.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 138 KPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQM----LTDFGPH------GVLFlpQKPFFTDGTL 207
Cdd:PRK13657 348 RQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIdgtdIRTVTRAslrrniAVVF--QDAGLFNRSI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 208 REQviypLKEIYPDSgsTDDErILRFLELAGLSSLVTRTE-GLDQQVDWNWyDVLSPGEMQRLSFARLFYLQPKYAVLDE 286
Cdd:PRK13657 426 EDN----IRVGRPDA--TDEE-MRAAAERAQAHDFIERKPdGYDTVVGERG-RQLSGGERQRLAIARALLKDPPILILDE 497
|
170
....*....|...
gi 1239915452 287 ATSALTEEVESEL 299
Cdd:PRK13657 498 ATSALDVETEAKV 510
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
138-318 |
4.00e-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: 4.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 138 KPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQMltDFGP-----HGVL-----FLPQKP------F 201
Cdd:PRK10790 354 NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRL--DGRPlsslsHSVLrqgvaMVQQDPvvladtF 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 202 FTDGTLREQViyplkeiypdsgstDDERILRFLELAGLSSLV-TRTEGLDQQVDwNWYDVLSPGEMQRLSFARLFYLQPK 280
Cdd:PRK10790 432 LANVTLGRDI--------------SEEQVWQALETVQLAELArSLPDGLYTPLG-EQGNNLSVGQKQLLALARVLVQTPQ 496
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1239915452 281 YAVLDEATSAL---TEE-VESELYRIGQQlgMTFISVGHRHS 318
Cdd:PRK10790 497 ILILDEATANIdsgTEQaIQQALAAVREH--TTLVVIAHRLS 536
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
142-315 |
4.81e-07 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 50.80 E-value: 4.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 142 KDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV----QMLTDFGP--HGVLFLPQK-PFFTDGTLREQVIYP 214
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLfigeKRMNDVPPaeRGVGMVFQSyALYPHLSVAENMSFG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 215 LKEIYPDSGSTDD--ERILRFLELAGLsslvtrtegLDQQVdwnwyDVLSPGEMQRLSFARLFYLQPKYAVLDEATS--- 289
Cdd:PRK11000 100 LKLAGAKKEEINQrvNQVAEVLQLAHL---------LDRKP-----KALSGGQRQRVAIGRTLVAEPSVFLLDEPLSnld 165
|
170 180
....*....|....*....|....*..
gi 1239915452 290 -ALTEEVESELYRIGQQLGMTFISVGH 315
Cdd:PRK11000 166 aALRVQMRIEISRLHKRLGRTMIYVTH 192
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
142-343 |
5.25e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.57 E-value: 5.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 142 KDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV-----QMLTDFGPH------GVLflPQKPFFTDGTLREQ 210
Cdd:PTZ00265 402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIiindsHNLKDINLKwwrskiGVV--SQDPLLFSNSIKNN 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 211 V---IYPLKEI--------------YPDSGSTDDERILRFLELAGLSSLVTRTEGLDQQVDWNW---------------- 257
Cdd:PTZ00265 480 IkysLYSLKDLealsnyynedgndsQENKNKRNSCRAKCAGDLNDMSNTTDSNELIEMRKNYQTikdsevvdvskkvlih 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 258 ---------YDVL--------SPGEMQRLSFARLFYLQPKYAVLDEATSALTEEVESELYRI-----GQQLGMTFIsVGH 315
Cdd:PTZ00265 560 dfvsalpdkYETLvgsnasklSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTinnlkGNENRITII-IAH 638
|
250 260
....*....|....*....|....*...
gi 1239915452 316 RHSLEKFHSLVLKLYGEGRWELSRIKVE 343
Cdd:PTZ00265 639 RLSTIRYANTIFVLSNRERGSTVDVDII 666
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
137-321 |
5.62e-07 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 49.81 E-value: 5.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 137 HKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV----QMLT--------DFGPHGVLFLPQ-KPFFT 203
Cdd:PRK11629 21 QTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVifngQPMSklssaakaELRNQKLGFIYQfHHLLP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 204 DGTLREQVIYPLKeIYPDSGSTDDERILRFLELAGLSSlvtRTEGLDQQvdwnwydvLSPGEMQRLSFARLFYLQPKYAV 283
Cdd:PRK11629 101 DFTALENVAMPLL-IGKKKPAEINSRALEMLAAVGLEH---RANHRPSE--------LSGGERQRVAIARALVNNPRLVL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1239915452 284 LDEATSALTEEVESELYRIGQQL----GMTFISVGHRHSLEK 321
Cdd:PRK11629 169 ADEPTGNLDARNADSIFQLLGELnrlqGTAFLVVTHDLQLAK 210
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
126-323 |
7.10e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 49.99 E-value: 7.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 126 LERVSVCAPSShKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQM----LTDFGPH-------GVL 194
Cdd:PRK13644 4 LENVSYSYPDG-TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVsgidTGDFSKLqgirklvGIV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 195 FLPQKPFFTDGTLREQVIY-------PLKEIypdsgstdDERILRFLELAGLSSLVTRTEgldqqvdwnwyDVLSPGEMQ 267
Cdd:PRK13644 83 FQNPETQFVGRTVEEDLAFgpenlclPPIEI--------RKRVDRALAEIGLEKYRHRSP-----------KTLSGGQGQ 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1239915452 268 RLSFARLFYLQPKYAVLDEATSALTEEV-ESELYRIGQ--QLGMTFISVghRHSLEKFH 323
Cdd:PRK13644 144 CVALAGILTMEPECLIFDEVTSMLDPDSgIAVLERIKKlhEKGKTIVYI--THNLEELH 200
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
118-290 |
7.51e-07 |
|
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: 49.45 E-value: 7.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 118 EPADTAFLLERVSVCAPSSHKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQM------LTDFGpH 191
Cdd:cd03220 15 GGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVrgrvssLLGLG-G 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 192 GvlFLPqkpfftDGTLREQvIYPLKEIYPDSGSTDDERILRFLELAGLsslvtrTEGLDQQVdwnwyDVLSPGEMQRLSF 271
Cdd:cd03220 94 G--FNP------ELTGREN-IYLNGRLLGLSRKEIDEKIDEIIEFSEL------GDFIDLPV-----KTYSSGMKARLAF 153
|
170
....*....|....*....
gi 1239915452 272 ARLFYLQPKYAVLDEATSA 290
Cdd:cd03220 154 AIATALEPDILLIDEVLAV 172
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
137-291 |
7.85e-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: 7.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 137 HKPLIKDLSLKISEGQSLLItGNTGTGKSSLLRVLGGLWASTQGSVQML------TDFGPHGVL-FLPQKP-FFTDGTLR 208
Cdd:cd03264 12 KKRALDGVSLTLGPGMYGLL-GPNGAGKTTLMRILATLTPPSSGTIRIDgqdvlkQPQKLRRRIgYLPQEFgVYPNFTVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 209 EQVIYP--LKEIypdSGSTDDERILRFLELAGLSSLVTRTEGldqqvdwnwydVLSPGEMQRLSFARLFYLQPKYAVLDE 286
Cdd:cd03264 91 EFLDYIawLKGI---PSKEVKARVDEVLELVNLGDRAKKKIG-----------SLSGGMRRRVGIAQALVGDPSILIVDE 156
|
....*
gi 1239915452 287 ATSAL 291
Cdd:cd03264 157 PTAGL 161
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
141-315 |
1.02e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 49.32 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 141 IKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQM----LTDFG------PHGVLFLPQKPFFTDGTLREQ 210
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIdgelLTAENvwnlrrKIGMVFQNPDNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 211 VIYPLKeiypDSGSTDDERILRFLE-LAGLSSLVTRTEGLDQqvdwnwydvLSPGEMQRLSFARLFYLQPKYAVLDEATS 289
Cdd:PRK13642 103 VAFGME----NQGIPREEMIKRVDEaLLAVNMLDFKTREPAR---------LSGGQKQRVAVAGIIALRPEIIILDESTS 169
|
170 180 190
....*....|....*....|....*....|
gi 1239915452 290 ALTEEVESELYRIGQQLG----MTFISVGH 315
Cdd:PRK13642 170 MLDPTGRQEIMRVIHEIKekyqLTVLSITH 199
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
124-315 |
1.02e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 49.46 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 124 FLLERVSVCAPSSHKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLW-----ASTQGSVQML------TDFGP-- 190
Cdd:PRK14267 3 FAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLelneeARVEGEVRLFgrniysPDVDPie 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 191 ----HGVLFLPQKPFfTDGTLREQVIYPLKeiypdsgstdderilrflelagLSSLVTRTEGLDQQVDWN------WYDV 260
Cdd:PRK14267 83 vrreVGMVFQYPNPF-PHLTIYDNVAIGVK----------------------LNGLVKSKKELDERVEWAlkkaalWDEV 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1239915452 261 ----------LSPGEMQRLSFARLFYLQPKYAVLDEATSAL----TEEVESELYRIGQQLgmTFISVGH 315
Cdd:PRK14267 140 kdrlndypsnLSGGQRQRLVIARALAMKPKILLMDEPTANIdpvgTAKIEELLFELKKEY--TIVLVTH 206
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
138-291 |
1.89e-06 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 48.48 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 138 KPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQMLtDFGPH----------GVLFLPQKPFFTDGTL 207
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVA-GLVPWkrrkkflrriGVVFGQKTQLWWDLPV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 208 REQvIYPLKEIYpdsgSTDDERILRflELAGLSSLVTRTEGLDQQVdwnwyDVLSPGEMQRLSFARLFYLQPKYAVLDEA 287
Cdd:cd03267 113 IDS-FYLLAAIY----DLPPARFKK--RLDELSELLDLEELLDTPV-----RQLSLGQRMRAEIAAALLHEPEILFLDEP 180
|
....
gi 1239915452 288 TSAL 291
Cdd:cd03267 181 TIGL 184
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
124-333 |
2.58e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 49.16 E-value: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 124 FLLERVSVCAPSShKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQMLTDFgphGVLFLPQKPFFT 203
Cdd:TIGR03719 5 YTMNRVSKVVPPK-KEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGI---KVGYLPQEPQLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 204 DG-TLREQV----------IYPLKEIYPDSGSTDDERILRFLELAGLSSLVTRTEG--LDQQVD----------WNWyDV 260
Cdd:TIGR03719 81 PTkTVRENVeegvaeikdaLDRFNEISAKYAEPDADFDKLAAEQAELQEIIDAADAwdLDSQLEiamdalrcppWDA-DV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1239915452 261 --LSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEVESELYRIGQQLGMTFISVGH-RHSLEKFHSLVLKL-YGEG 333
Cdd:TIGR03719 160 tkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHdRYFLDNVAGWILELdRGRG 236
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
138-295 |
2.83e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 49.39 E-value: 2.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 138 KPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVqmltdFGPHGVLFLPQKPFFTDGTLREQVIYplke 217
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-----WAERSIAYVPQQAWIMNATVRGNILF---- 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 218 iypdsgsTDDERILRF--------LE--LAGLSSLVtRTEGLDQQVDwnwydvLSPGEMQRLSFARLFYLQPKYAVLDEA 287
Cdd:PTZ00243 744 -------FDEEDAARLadavrvsqLEadLAQLGGGL-ETEIGEKGVN------LSGGQKARVSLARAVYANRDVYLLDDP 809
|
....*...
gi 1239915452 288 TSALTEEV 295
Cdd:PTZ00243 810 LSALDAHV 817
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
142-316 |
3.15e-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: 46.65 E-value: 3.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 142 KDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQMltdfgphgvlflpqkpfftDGtlreqviyplKEIYPD 221
Cdd:cd03216 17 DGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILV-------------------DG----------KEVSFA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 222 SgSTDDERilrflelAGLSsLVTrtegldqQvdwnwydvLSPGEMQRLSFARLFYLQPKYAVLDEATSALT-EEVEsELY 300
Cdd:cd03216 68 S-PRDARR-------AGIA-MVY-------Q--------LSVGERQMVEIARALARNARLLILDEPTAALTpAEVE-RLF 122
|
170
....*....|....*....
gi 1239915452 301 RIGQQL---GMTFISVGHR 316
Cdd:cd03216 123 KVIRRLraqGVAVIFISHR 141
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
139-316 |
3.16e-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: 47.33 E-value: 3.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 139 PLIKDLSLKISEGQSLLITGNTGTGKSS-LLRVLGGL--------WASTQGSVQMLTDFGP---HGVLFLPQKPFFTDGT 206
Cdd:cd03290 15 ATLSNINIRIPTGQLTMIVGQVGCGKSSlLLAILGEMqtlegkvhWSNKNESEPSFEATRSrnrYSVAYAAQKPWLLNAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 207 LREQVIY--PL-KEIYP---DSGSTD-DERILRFLElaglsslvtRTEGLDQQVDwnwydvLSPGEMQRLSFARLFYLQP 279
Cdd:cd03290 95 VEENITFgsPFnKQRYKavtDACSLQpDIDLLPFGD---------QTEIGERGIN------LSGGQRQRICVARALYQNT 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1239915452 280 KYAVLDEATSALTEEVESELYRIG-----QQLGMTFISVGHR 316
Cdd:cd03290 160 NIVFLDDPFSALDIHLSDHLMQEGilkflQDDKRTLVLVTHK 201
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
137-291 |
4.73e-06 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 46.72 E-value: 4.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 137 HKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV---------------QMLTDFGPH-GVlflpqKP 200
Cdd:PRK13538 13 ERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVlwqgepirrqrdeyhQDLLYLGHQpGI-----KT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 201 fftDGTLREQviypLKEIYPDSGSTDDERILRFLELAGLSslvtRTEgldqqvdwnwyDV----LSPGEMQRLSFARLFY 276
Cdd:PRK13538 88 ---ELTALEN----LRFYQRLHGPGDDEALWEALAQVGLA----GFE-----------DVpvrqLSAGQQRRVALARLWL 145
|
170
....*....|....*
gi 1239915452 277 LQPKYAVLDEATSAL 291
Cdd:PRK13538 146 TRAPLWILDEPFTAI 160
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
125-299 |
5.32e-06 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 47.00 E-value: 5.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 125 LLERVSVCAPSSHKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQM--LTDFGP---HGVLF---- 195
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLdgKPVEGPgaeRGVVFqneg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 196 -LPQKpfftdgTLREQVIYPLKEiypdSGSTDDERILRFLELAGLSSLvtrtEGLDQQVDWNwydvLSPGEMQRLSFARL 274
Cdd:PRK11248 81 lLPWR------NVQDNVAFGLQL----AGVEKMQRLEIAHQMLKKVGL----EGAEKRYIWQ----LSGGQRQRVGIARA 142
|
170 180
....*....|....*....|....*...
gi 1239915452 275 FYLQPKYAVLDE---ATSALTEEVESEL 299
Cdd:PRK11248 143 LAANPQLLLLDEpfgALDAFTREQMQTL 170
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
122-315 |
5.54e-06 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 48.18 E-value: 5.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 122 TAFL-LERVSVCAPSSHKPL--IKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV----QMLTDFGPHGVL 194
Cdd:PRK10535 2 TALLeLKDIRRSYPSGEEQVevLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYrvagQDVATLDADALA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 195 FLPQKPF---------FTDGTLREQVIYPlkEIYpdSGSTDDERILRFLElaglssLVTRTeGLDQQVDWNwYDVLSPGE 265
Cdd:PRK10535 82 QLRREHFgfifqryhlLSHLTAAQNVEVP--AVY--AGLERKQRLLRAQE------LLQRL-GLEDRVEYQ-PSQLSGGQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1239915452 266 MQRLSFARLFYLQPKYAVLDEATSAL----TEEVESELYRIGQQlGMTFISVGH 315
Cdd:PRK10535 150 QQRVSIARALMNGGQVILADEPTGALdshsGEEVMAILHQLRDR-GHTVIIVTH 202
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
138-286 |
6.07e-06 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 46.77 E-value: 6.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 138 KPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV----QMLTDFGPH-----GVLFLPQKP-FFTDGTL 207
Cdd:cd03218 13 RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKIlldgQDITKLPMHkrarlGIGYLPQEAsIFRKLTV 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1239915452 208 REQVIYPLkEIYPDSGSTDDERILRFLELAGLSSLvtrtegLDQQVDwnwydVLSPGEMQRLSFARLFYLQPKYAVLDE 286
Cdd:cd03218 93 EENILAVL-EIRGLSKKEREEKLEELLEEFHITHL------RKSKAS-----SLSGGERRRVEIARALATNPKFLLLDE 159
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
141-315 |
9.32e-06 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 46.21 E-value: 9.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 141 IKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSvqmLTDFGpHGVL-----------FLPQKPFFTDG-TLR 208
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGR---ATVAG-HDVVreprevrrrigIVFQDLSVDDElTGW 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 209 EQViYPLKEIYPDSGSTDDERILRFLELAGLsslvtrTEGLDQQVdwnwyDVLSPGEMQRLSFARLFYLQPKYAVLDEAT 288
Cdd:cd03265 92 ENL-YIHARLYGVPGAERRERIDELLDFVGL------LEAADRLV-----KTYSGGMRRRLEIARSLVHRPEVLFLDEPT 159
|
170 180 190
....*....|....*....|....*....|.
gi 1239915452 289 SALTEEVESELYRIGQQL----GMTFISVGH 315
Cdd:cd03265 160 IGLDPQTRAHVWEYIEKLkeefGMTILLTTH 190
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
138-312 |
9.48e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 46.54 E-value: 9.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 138 KPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV---QMLTDFGPHGVLFLPQK--PFFTDgtlreqvi 212
Cdd:PRK13638 14 EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVlwqGKPLDYSKRGLLALRQQvaTVFQD-------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 213 yPLKEIYPDSGSTDDERILRFLELAGlSSLVTRTEGLDQQVDWNWY-----DVLSPGEMQRLSFARLFYLQPKYAVLDEA 287
Cdd:PRK13638 86 -PEQQIFYTDIDSDIAFSLRNLGVPE-AEITRRVDEALTLVDAQHFrhqpiQCLSHGQKKRVAIAGALVLQARYLLLDEP 163
|
170 180
....*....|....*....|....*....
gi 1239915452 288 TSALTEEVESELY----RIGQQLGMTFIS 312
Cdd:PRK13638 164 TAGLDPAGRTQMIaiirRIVAQGNHVIIS 192
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
137-291 |
1.01e-05 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 45.67 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 137 HKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVqmlTDFGPH-----------GVLFlpQKPFFTDG 205
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEI---TFDGKSyqkniealrriGALI--EAPGFYPN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 206 -TLREQVIYPLKEIypdsgSTDDERILRFLELAGLSSLVTRTEGLdqqvdwnwydvLSPGEMQRLSFARLFYLQPKYAVL 284
Cdd:cd03268 87 lTARENLRLLARLL-----GIRKKRIDEVLDVVGLKDSAKKKVKG-----------FSLGMKQRLGIALALLGNPDLLIL 150
|
....*..
gi 1239915452 285 DEATSAL 291
Cdd:cd03268 151 DEPTNGL 157
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
138-315 |
1.42e-05 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 45.75 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 138 KPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV----QMLTDFGPHGV-----LFLPQKPFFTDGTLR 208
Cdd:PRK10253 20 YTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVwldgEHIQHYASKEVarrigLLAQNATTPGDITVQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 209 EQVI---YPLKEIYPDSGSTDDERILRFLELAGLSSLVtrteglDQQVdwnwyDVLSPGEMQRLSFARLFYLQPKYAVLD 285
Cdd:PRK10253 100 ELVArgrYPHQPLFTRWRKEDEEAVTKAMQATGITHLA------DQSV-----DTLSGGQRQRAWIAMVLAQETAIMLLD 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 1239915452 286 EATSALT-------EEVESELYRigqQLGMTFISVGH 315
Cdd:PRK10253 169 EPTTWLDishqidlLELLSELNR---EKGYTLAAVLH 202
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
115-288 |
2.03e-05 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 46.21 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 115 PAAEPADTAFLLERVSVCAPSshKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVqmltDFGPHGVL 194
Cdd:COG0488 307 PPERLGKKVLELEGLSKSYGD--KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV----KLGETVKI 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 195 -FLPQKPFFTDGTLReqviyPLKEIYPDSGSTDDERILRFLELAGLSSlvtrtEGLDQQVdwnwyDVLSPGEMQRLSFAR 273
Cdd:COG0488 381 gYFDQHQEELDPDKT-----VLDELRDGAPGGTEQEVRGYLGRFLFSG-----DDAFKPV-----GVLSGGEKARLALAK 445
|
170
....*....|....*
gi 1239915452 274 LFYLQPKYAVLDEAT 288
Cdd:COG0488 446 LLLSPPNVLLLDEPT 460
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
138-315 |
2.50e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 45.08 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 138 KPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV---QMLTDFGPH--------GVLFlpQKPfftDGT 206
Cdd:PRK13633 23 KLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVyvdGLDTSDEENlwdirnkaGMVF--QNP---DNQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 207 L-----REQVIY-------PLKEIypdsgstdDERILRFLELAGLSSLVTRTEGLdqqvdwnwydvLSPGEMQRLSFARL 274
Cdd:PRK13633 98 IvativEEDVAFgpenlgiPPEEI--------RERVDESLKKVGMYEYRRHAPHL-----------LSGGQKQRVAIAGI 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1239915452 275 FYLQPKYAVLDEATSALT----EEVESELYRIGQQLGMTFISVGH 315
Cdd:PRK13633 159 LAMRPECIIFDEPTAMLDpsgrREVVNTIKELNKKYGITIILITH 203
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
11-300 |
2.82e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 45.88 E-value: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 11 VNTFdYLGSILSYV-VIAIPIFSGVYGDLSPTElstlvsknAFVCIYLISCFT-RLIDLSSTLSDVAGYTHRIGELQETL 88
Cdd:PLN03130 525 FNSF-ILNSIPVLVtVVSFGVFTLLGGDLTPAR--------AFTSLSLFAVLRfPLFMLPNLITQAVNANVSLKRLEELL 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 89 LDMSLKLRGGEILDesewnmdraPGWPAAEPADTAFLLErvsvcaPSSHKPLIKDLSLKISEGQSLLITGNTGTGKSSLL 168
Cdd:PLN03130 596 LAEERVLLPNPPLE---------PGLPAISIKNGYFSWD------SKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLI 660
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 169 R-VLGGLWASTQGSVQMLTDfgphgVLFLPQKPFFTDGTLREQVIYplkeiypdsGST-DDERILRFLELAGLSSLVTRT 246
Cdd:PLN03130 661 SaMLGELPPRSDASVVIRGT-----VAYVPQVSWIFNATVRDNILF---------GSPfDPERYERAIDVTALQHDLDLL 726
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 247 EGLDQQ------VDwnwydvLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEVESELY 300
Cdd:PLN03130 727 PGGDLTeigergVN------ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVF 780
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
141-315 |
3.10e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 45.16 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 141 IKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQmLTDFGPH---------------GVLF-LPQKPFFTD 204
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVT-VDDITIThktkdkyirpvrkriGMVFqFPESQLFED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 205 GTLREQVIYP------LKEIypdsgstdDERILRFLELAGLSSLVTRTEGLDqqvdwnwydvLSPGEMQRLSFARLFYLQ 278
Cdd:PRK13646 102 TVEREIIFGPknfkmnLDEV--------KNYAHRLLMDLGFSRDVMSQSPFQ----------MSGGQMRKIAIVSILAMN 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1239915452 279 PKYAVLDEATSALTEEVESELYRIGQQL----GMTFISVGH 315
Cdd:PRK13646 164 PDIIVLDEPTAGLDPQSKRQVMRLLKSLqtdeNKTIILVSH 204
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
142-291 |
3.37e-05 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 45.45 E-value: 3.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 142 KDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWAStQGSVQM----LTDFGPHG---------VLFlpQKPFftdGTL- 207
Cdd:COG4172 303 DGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPS-EGEIRFdgqdLDGLSRRAlrplrrrmqVVF--QDPF---GSLs 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 208 -R---EQVIY-PLKEIYPD-SGSTDDERILRFLELAGLS-SLVTR--TEgldqqvdwnwydvLSPGEMQRLSFARLFYLQ 278
Cdd:COG4172 377 pRmtvGQIIAeGLRVHGPGlSAAERRARVAEALEEVGLDpAARHRypHE-------------FSGGQRQRIAIARALILE 443
|
170
....*....|...
gi 1239915452 279 PKYAVLDEATSAL 291
Cdd:COG4172 444 PKLLVLDEPTSAL 456
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
142-183 |
3.43e-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: 3.43e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1239915452 142 KDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQ 183
Cdd:COG1134 43 KDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
143-335 |
3.53e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.49 E-value: 3.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 143 DLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQML---TDFGP------HGVLFLPQKpffTDGTLREQVI- 212
Cdd:PRK10982 16 NVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQgkeIDFKSskealeNGISMVHQE---LNLVLQRSVMd 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 213 ------YPLKEIYPDSGSTDDERILRFLELaglsslvtrteglDQQVDWN-WYDVLSPGEMQRLSFARLFYLQPKYAVLD 285
Cdd:PRK10982 93 nmwlgrYPTKGMFVDQDKMYRDTKAIFDEL-------------DIDIDPRaKVATLSVSQMQMIEIAKAFSYNAKIVIMD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1239915452 286 EATSALTEEVESELYRIGQQL-----GMTFISvghrHSLEKFHSLV--LKLYGEGRW 335
Cdd:PRK10982 160 EPTSSLTEKEVNHLFTIIRKLkergcGIVYIS----HKMEEIFQLCdeITILRDGQW 212
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
141-315 |
3.55e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 45.62 E-value: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 141 IKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQmltdFGPHGVLFLPQKPFftdGTLREQVIYPLKEIYP 220
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEII----FNGQRIDTLSPGKL---QALRRDIQFIFQDPYA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 221 --DSGSTDDERILRFLELAGL----------SSLVTRTeGLDQQVDWNWYDVLSPGEMQRLSFARLFYLQPKYAVLDEAT 288
Cdd:PRK10261 413 slDPRQTVGDSIMEPLRVHGLlpgkaaaarvAWLLERV-GLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAV 491
|
170 180 190
....*....|....*....|....*....|.
gi 1239915452 289 SALTEEVESE----LYRIGQQLGMTFISVGH 315
Cdd:PRK10261 492 SALDVSIRGQiinlLLDLQRDFGIAYLFISH 522
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
141-315 |
4.41e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 44.39 E-value: 4.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 141 IKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGL-----WASTQGSVQMLTD--FGPH----------GVLFlpQKPFFT 203
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndlipGFRVEGKVTFHGKnlYAPDvdpvevrrriGMVF--QKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 204 DGTLREQVIYPLKeIYPDSGSTDdERILRFLELAGLSSLVT---RTEGLDqqvdwnwydvLSPGEMQRLSFARLFYLQPK 280
Cdd:PRK14243 104 PKSIYDNIAYGAR-INGYKGDMD-ELVERSLRQAALWDEVKdklKQSGLS----------LSGGQQQRLCIARAIAVQPE 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 1239915452 281 YAVLDEATSAL----TEEVESELYRIGQQlgMTFISVGH 315
Cdd:PRK14243 172 VILMDEPCSALdpisTLRIEELMHELKEQ--YTIIIVTH 208
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
198-316 |
6.06e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.02 E-value: 6.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 198 QKPFFTDGTLREQVIYPlKEiypDSGSTDDERILRFlelAGLSSLVtrtEGLDQQVDWN---WYDVLSPGEMQRLSFARL 274
Cdd:PTZ00265 1303 QEPMLFNMSIYENIKFG-KE---DATREDVKRACKF---AAIDEFI---ESLPNKYDTNvgpYGKSLSGGQKQRIAIARA 1372
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1239915452 275 FYLQPKYAVLDEATSALTEE----VESELYRIGQQLGMTFISVGHR 316
Cdd:PTZ00265 1373 LLREPKILLLDEATSSLDSNseklIEKTIVDIKDKADKTIITIAHR 1418
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
151-334 |
1.15e-04 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 42.94 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 151 GQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQmltdFGPHGVLFLPQK--PF--------------FTDGTLREQVIYP 214
Cdd:PRK10908 28 GEMAFLTGHSGAGKSTLLKLICGIERPSAGKIW----FSGHDITRLKNRevPFlrrqigmifqdhhlLMDRTVYDNVAIP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 215 LKeIYPDSGSTDDERILRFLELAGLsslvtrtegLDQQVdwNWYDVLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEE 294
Cdd:PRK10908 104 LI-IAGASGDDIRRRVSAALDKVGL---------LDKAK--NFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1239915452 295 VESELYRIGQQ---LGMTFISVGHRHSLEKFHSLVLKLYGEGR 334
Cdd:PRK10908 172 LSEGILRLFEEfnrVGVTVLMATHDIGLISRRSYRMLTLSDGH 214
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
115-197 |
1.70e-04 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 43.09 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 115 PAAEPADTAFLLERVSVcAPSSHKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQM----LTDFGP 190
Cdd:COG3845 249 APAEPGEVVLEVENLSV-RDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLdgedITGLSP 327
|
90
....*....|..
gi 1239915452 191 -----HGVLFLP 197
Cdd:COG3845 328 rerrrLGVAYIP 339
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
138-321 |
1.83e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 42.46 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 138 KPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLW-----ASTQGSVqmltDFGPH----------------GVLFL 196
Cdd:PRK14239 18 KKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNdlnpeVTITGSI----VYNGHniysprtdtvdlrkeiGMVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 197 PQKPFftDGTLREQVIYPLKEiypdSGSTDDERilrfLELAGLSSLvtRTEGLDQQVDWNWYDV---LSPGEMQRLSFAR 273
Cdd:PRK14239 94 QPNPF--PMSIYENVVYGLRL----KGIKDKQV----LDEAVEKSL--KGASIWDEVKDRLHDSalgLSGGQQQRVCIAR 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1239915452 274 LFYLQPKYAVLDEATSAL----TEEVESELYRIGQQLGMTFISvghrHSLEK 321
Cdd:PRK14239 162 VLATSPKIILLDEPTSALdpisAGKIEETLLGLKDDYTMLLVT----RSMQQ 209
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
138-297 |
2.57e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 42.57 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 138 KPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQML--TDFGphgvlFLPQ---KPFFTDGTLREQVI 212
Cdd:PRK15064 332 GPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSenANIG-----YYAQdhaYDFENDLTLFDWMS 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 213 YPLKEiypdsgsTDDERILRflelAGLSSLVTRTEGLDQQVdwnwyDVLSPGEMQRLSFARLFYLQPKYAVLDEATSAL- 291
Cdd:PRK15064 407 QWRQE-------GDDEQAVR----GTLGRLLFSQDDIKKSV-----KVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMd 470
|
....*.
gi 1239915452 292 TEEVES 297
Cdd:PRK15064 471 MESIES 476
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
139-184 |
2.64e-04 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 41.76 E-value: 2.64e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1239915452 139 PLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQM 184
Cdd:PRK13543 25 PVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQI 70
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
139-316 |
2.78e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 42.84 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 139 PLI-KDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQML-TDFGPHGV-----LF--LPQKPFFTDGTLRE 209
Cdd:PTZ00243 1323 PLVlRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNgREIGAYGLrelrrQFsmIPQDPVLFDGTVRQ 1402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 210 QViYPLKEIYPdsgstddERILRFLELAGLSSLV-TRTEGLDQQV---DWNWydvlSPGEMQRLSFAR-LFYLQPKYAVL 284
Cdd:PTZ00243 1403 NV-DPFLEASS-------AEVWAALELVGLRERVaSESEGIDSRVlegGSNY----SVGQRQLMCMARaLLKKGSGFILM 1470
|
170 180 190
....*....|....*....|....*....|....*...
gi 1239915452 285 DEATSalteEVESELYRIGQQLGM------TFISVGHR 316
Cdd:PTZ00243 1471 DEATA----NIDPALDRQIQATVMsafsayTVITIAHR 1504
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
138-315 |
3.29e-04 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 41.67 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 138 KPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQMLTDFGP---HGVLFLPQK---------PFFTDG 205
Cdd:PRK11831 20 RCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPamsRSRLYTVRKrmsmlfqsgALFTDM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 206 TLREQVIYPLKEIYPDSGSTDDERILRFLELAGL--SSLVTRTEgldqqvdwnwydvLSPGEMQRLSFARLFYLQPKYAV 283
Cdd:PRK11831 100 NVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLrgAAKLMPSE-------------LSGGMARRAALARAIALEPDLIM 166
|
170 180 190
....*....|....*....|....*....|....*....
gi 1239915452 284 LDEA-------TSALTEEVESELyriGQQLGMTFISVGH 315
Cdd:PRK11831 167 FDEPfvgqdpiTMGVLVKLISEL---NSALGVTCVVVSH 202
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
138-293 |
5.20e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 40.70 E-value: 5.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 138 KPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQML-----TDFGPH--GVLFLPQK----PFFtdgT 206
Cdd:PRK13540 14 QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFErqsikKDLCTYqkQLCFVGHRsginPYL---T 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 207 LREQVIYplkEIYPDSGSTDDERILRFLElagLSSLVTRTEGLdqqvdwnwydvLSPGEMQRLSFARLFYLQPKYAVLDE 286
Cdd:PRK13540 91 LRENCLY---DIHFSPGAVGITELCRLFS---LEHLIDYPCGL-----------LSSGQKRQVALLRLWMSKAKLWLLDE 153
|
....*..
gi 1239915452 287 ATSALTE 293
Cdd:PRK13540 154 PLVALDE 160
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
261-316 |
5.55e-04 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 41.54 E-value: 5.55e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 261 LSPGEMQRLSFARLFYLQPKYAVLDEATSALTE-EVESeLYRIGQQL---GMTFISVGHR 316
Cdd:COG1129 141 LSVAQQQLVEIARALSRDARVLILDEPTASLTErEVER-LFRIIRRLkaqGVAIIYISHR 199
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
140-318 |
5.91e-04 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 40.89 E-value: 5.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 140 LIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQMLTDFGPHGVLFLPQKPFFTDgtLREQV-------- 211
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQQKGLIRQ--LRQHVgfvfqnfn 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 212 IYPLKEIYPD--------SGSTDDERILRFLELAGLSSLVTRTEGLDQQvdwnwydvLSPGEMQRLSFARLFYLQPKYAV 283
Cdd:PRK11264 96 LFPHRTVLENiiegpvivKGEPKEEATARARELLAKVGLAGKETSYPRR--------LSGGQQQRVAIARALAMRPEVIL 167
|
170 180 190
....*....|....*....|....*....|....*...
gi 1239915452 284 LDEATSALTEEVESELYRIGQQLG---MTFISVGHRHS 318
Cdd:PRK11264 168 FDEPTSALDPELVGEVLNTIRQLAqekRTMVIVTHEMS 205
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
261-312 |
6.61e-04 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 41.17 E-value: 6.61e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1239915452 261 LSPGEMQRLSFARLFYLQPKYAVLDEATSALT-EEVEsELYRIGQQL---GMT--FIS 312
Cdd:COG3845 142 LSVGEQQRVEILKALYRGARILILDEPTAVLTpQEAD-ELFEILRRLaaeGKSiiFIT 198
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
141-316 |
9.89e-04 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 40.96 E-value: 9.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 141 IKDLSLKISEGQSLLITGNTGTGKSSLLRVLGG-----------LWASTQGSVQMLTDFGPHGVLFLPQKPFFTDGTLRE 209
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyphgtwdgeiYWSGSPLKASNIRDTERAGIVIIHQELTLVPELSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 210 QVIYPLKEIYPDSGSTDDerilrflelaglSSLVTRTEGLDQQVDWNWYDVLSP------GEMQRLSFARLFYLQPKYAV 283
Cdd:TIGR02633 97 ENIFLGNEITLPGGRMAY------------NAMYLRAKNLLRELQLDADNVTRPvgdyggGQQQLVEIAKALNKQARLLI 164
|
170 180 190
....*....|....*....|....*....|....*.
gi 1239915452 284 LDEATSALTE---EVESELYRIGQQLGMTFISVGHR 316
Cdd:TIGR02633 165 LDEPSSSLTEketEILLDIIRDLKAHGVACVYISHK 200
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
138-315 |
1.35e-03 |
|
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: 40.56 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 138 KPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGL--WASTQGSV-------------------------------QM 184
Cdd:TIGR03269 13 KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpskvgepcpvcggtlePE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239915452 185 LTDF-GPHGVLF---------LPQKPF--FTDGTLREQVIYPLKEIypdsGSTDDERILRFLELAGLSSLVTRTEGLDQQ 252
Cdd:TIGR03269 93 EVDFwNLSDKLRrrirkriaiMLQRTFalYGDDTVLDNVLEALEEI----GYEGKEAVGRAVDLIEMVQLSHRITHIARD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1239915452 253 vdwnwydvLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEE----VESELYRIGQQLGMTFISVGH 315
Cdd:TIGR03269 169 --------LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQtaklVHNALEEAVKASGISMVLTSH 227
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
139-182 |
1.71e-03 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 39.83 E-value: 1.71e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1239915452 139 PLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV 182
Cdd:PRK11650 18 QVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEI 61
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
136-173 |
1.92e-03 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 38.78 E-value: 1.92e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1239915452 136 SHKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGG 173
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALAN 55
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
143-183 |
5.23e-03 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 38.35 E-value: 5.23e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1239915452 143 DLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQ 183
Cdd:PRK11288 22 DISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSIL 62
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
141-185 |
8.31e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 37.41 E-value: 8.31e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1239915452 141 IKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQML 185
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVM 65
|
|
| |
