|
Name |
Accession |
Description |
Interval |
E-value |
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
19-608 |
2.27e-111 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 345.25 E-value: 2.27e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 19 QFLQRFLQIQKvlfPSWSSQNALMFLTLLFVALLEQLVIYQVGLIPSQYYGV----LGNKDLDGFKTLTFLAVMLIVLNS 94
Cdd:COG4178 2 SLLRQFWRLAR---PYWRSEEKWKAWGLLALLLLLTLASVGLNVLLNFWNRDfydaLQARDAAAFWQQLGVFALLAAISI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 95 MLKSFDQFTCNLLYVSWRKDLTEHLHHLYFQGRVYYTLNVLRDDVDNPDQRISQDVERFCRQLSSMASKLIISPFTLIYY 174
Cdd:COG4178 79 LLAVYQTYLRQRLQIRWREWLTERLLDRWLSNRAYYRLQLSGGEIDNPDQRIAEDIRLFTETTLSLSLGLLSSVVTLISF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 175 TY------QCFQSTGWLGPMSIFGYF--------ILGTLVNkTLMG-PIVAKLVQQEKLEGDFRFKHMQIRVNAESAAFF 239
Cdd:COG4178 159 IGilwslsGSLTFTLGGYSITIPGYMvwaaliyaIIGTLLT-HLIGrPLIRLNFEQQRREADFRFALVRVRENAESIALY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 240 RAGHVEHQRTDRRLQRLLQTQRELMSKELWLYIGVNTFDYLGSILSYVVIAIPIFSGvygDLSPTELSTLVSknAFV--- 316
Cdd:COG4178 238 RGEAAERRRLRRRFDAVIANWRRLIRRQRNLTFFTTGYGQLAVIFPILVAAPRYFAG---EITLGGLMQAAS--AFGqvq 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 317 --CIYLISCFTRLIDLSSTLSdvagythRIGELQETLLDMSlklrggggeildesewnmDRAPGWPAAEPADTAFLSSSG 394
Cdd:COG4178 313 gaLSWFVDNYQSLAEWRATVD-------RLAGFEEALEAAD------------------ALPEAASRIETSEDGALALED 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 395 SPLCPPSsHKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQMltdfgPHG--VLFLPQKPFFTDGT 472
Cdd:COG4178 368 LTLRTPD-GRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR-----PAGarVLFLPQRPYLPLGT 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 473 LREQVSdiyplkeiYPDS-GSTDDERILRFLELAGLSSLVTRtegLDQQVDWNwyDVLSPGEMQRLSFARLFYLQPKYAV 551
Cdd:COG4178 442 LREALL--------YPATaEAFSDAELREALEAVGLGHLAER---LDEEADWD--QVLSLGEQQRLAFARLLLHKPDWLF 508
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1953408514 552 LDEATSALTEEVESELYR-IGQQL-GMTFISVGHRHSLEKFHSLVLKLYGEGRWELSRI 608
Cdd:COG4178 509 LDEATSALDEENEAALYQlLREELpGTTVISVGHRSTLAAFHDRVLELTGDGSWQLLPA 567
|
|
| ABC_membrane_2 |
pfam06472 |
ABC transporter transmembrane region 2; This domain covers the transmembrane of a small family ... |
27-294 |
8.24e-97 |
|
ABC transporter transmembrane region 2; This domain covers the transmembrane of a small family of ABC transporters and shares sequence similarity with pfam00664. Mutations in this domain in Swiss:P28288 are believed responsible for Zellweger Syndrome-2; mutations in Swiss:P33897 are responsible for recessive X-linked adrenoleukodystrophy. A Saccharomyces cerevisiae homolog is involved in the import of long-chain fatty acids.
Pssm-ID: 399466 Cd Length: 269 Bit Score: 296.83 E-value: 8.24e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 27 IQKVLFPSWSSQNALMFLTLLFVALLEQLVIYQVGLIPSQYYGVLGNKDLDGFKTLTFLAVMLIVLNSMLKSFDQFTCNL 106
Cdd:pfam06472 1 LLKILFPRWFSKEAGLLLALAALLVLRTFLSVLVAQLDGQIVKALVAKNGRGFIRLLLKWALLAVPASFVNSALKYLTQR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 107 LYVSWRKDLTEHLHHLYFQGRVYYTLNVLRDDVDNPDQRISQDVERFCRQLSSMASKLIISPFTLIYYTYQCFQSTGWLG 186
Cdd:pfam06472 81 LALRFRTRLTRHLHDEYLKGRTYYKMSNLDGRIDNPDQRITQDVEKFCSSLSDLYSNLLKPILDIILFTFRLWRLSGWRG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 187 PMSIFGYFILGTLVNKTLMGPIVAKLVQQEKLEGDFRFKHMQIRVNAESAAFFRAGHVEHQRTDRRLQRLLQTQRELMSK 266
Cdd:pfam06472 161 PAILFLYVLLSAVILRRLSPPFGKLVAEEQKLEGEFRYLHSRLITNAEEIAFYRGEKREKKQLQRSFKSLIDHMRRILRR 240
|
250 260
....*....|....*....|....*....
gi 1953408514 267 ELWLYIGVNTF-DYLGSILSYVVIAIPIF 294
Cdd:pfam06472 241 RLWYGFIEDFVlKYTWSILGYVLVALPIF 269
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
16-605 |
4.72e-92 |
|
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: 297.43 E-value: 4.72e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 16 LDLQFLQRFLQIQKVLFPSWSSQNALMFLTLLFVALLEQLVIYQVGLIPSQYYGVLGNKDLDGFKTLTFLAVMLIVLNSM 95
Cdd:TIGR00954 71 VNGVFLGKLDFLLKILIPRVFCKETGLLILIAFLLVSRTYLSVYVATLDGQIESSIVRRSPRNFAWILFKWFLIAPPASF 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 96 LKSFDQFTCNLLYVSWRKDLTEHLHHLYFQGRVYYTLNVLRDDVDNPDQRISQDVERFCRQLSSMASKLIISPFTLIYYT 175
Cdd:TIGR00954 151 INSAIKYLLKELKLRFRVRLTRYLYSKYLSGFTFYKVSNLDSRIQNPDQLLTQDVEKFCDSVVELYSNLTKPILDVILYS 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 176 YQCFQSTGWLGPMSIFGYFILGTLVNKTLMGPIVAKLVQQEKLEGDFRFKHMQIRVNAESAAFFRAGHVEHQRTDRRLQR 255
Cdd:TIGR00954 231 FKLLTALGSVGPAGLFAYLFATGVVLTKLRPPIGKLTVEEQALEGEYRYVHSRLIMNSEEIAFYQGNKVEKETVMSSFYR 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 256 LLQTQRELMSKELWlYIGVNTF--DYLGSILSYVVIAIPIFSGV---YGDLSPTELSTLVSKNAFVCIYLISCFTRLIDL 330
Cdd:TIGR00954 311 LVEHLNLIIKFRFS-YGFLDNIvaKYTWSAVGLVAVSIPIFDKThpaFLEMSEEELMQEFYNNGRLLLKAADALGRLMLA 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 331 SSTLSDVAGYTHRIGELQETLLDM-SLKL-RGGGGEILDESEW--NMDRAPGWPAAEPADTAfLSSSGSPLCPPSSHKpL 406
Cdd:TIGR00954 390 GRDMTRLAGFTARVDTLLQVLDDVkSGNFkRPRVEEIESGREGgrNSNLVPGRGIVEYQDNG-IKFENIPLVTPNGDV-L 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 407 IKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGsvqMLTDFGPHGVLFLPQKPFFTDGTLREQVsdiyplkeI 486
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGG---RLTKPAKGKLFYVPQRPYMTLGTLRDQI--------I 536
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 487 YPDSgSTD-------DERILRFLELAGLSSLVTRTEGLDQQVDWNwyDVLSPGEMQRLSFARLFYLQPKYAVLDEATSAL 559
Cdd:TIGR00954 537 YPDS-SEDmkrrglsDKDLEQILDNVQLTHILEREGGWSAVQDWM--DVLSGGEKQRIAMARLFYHKPQFAILDECTSAV 613
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1953408514 560 TEEVESELYRIGQQLGMTFISVGHRHSLEKFHSLVLKLYGEGRWEL 605
Cdd:TIGR00954 614 SVDVEGYMYRLCREFGITLFSVSHRKSLWKYHEYLLYMDGRGGYQF 659
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
396-603 |
1.61e-71 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 227.42 E-value: 1.61e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 396 PLCPPSsHKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQMLTDfgpHGVLFLPQKPFFTDGTLRE 475
Cdd:cd03223 7 SLATPD-GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEG---EDLLFLPQRPYLPLGTLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 476 QVsdiyplkeIYPdsgstdderilrflelaglsslvtrtegldqqvdwnWYDVLSPGEMQRLSFARLFYLQPKYAVLDEA 555
Cdd:cd03223 83 QL--------IYP------------------------------------WDDVLSGGEQQRLAFARLLLHKPKFVFLDEA 118
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1953408514 556 TSALTEEVESELYRIGQQLGMTFISVGHRHSLEKFHSLVLKLYGEGRW 603
Cdd:cd03223 119 TSALDEESEDRLYQLLKELGITVISVGHRPSLWKFHDRVLDLDGEGGW 166
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
397-583 |
2.59e-31 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 121.08 E-value: 2.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 397 LCPPSSHKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV----QMLTDFGPHG----VLFLPQKPFF 468
Cdd:COG4619 6 LSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIyldgKPLSAMPPPEwrrqVAYVPQEPAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 469 TDGTLREQVSDIYPLKEIYPDsgstdDERILRFLELAGLSSLVtrtegLDQQVDwnwydVLSPGEMQRLSFARLFYLQPK 548
Cdd:COG4619 86 WGGTVRDNLPFPFQLRERKFD-----RERALELLERLGLPPDI-----LDKPVE-----RLSGGERQRLALIRALLLQPD 150
|
170 180 190
....*....|....*....|....*....|....*....
gi 1953408514 549 YAVLDEATSAL----TEEVESELYRIGQQLGMTFISVGH 583
Cdd:COG4619 151 VLLLDEPTSALdpenTRRVEELLREYLAEEGRAVLWVSH 189
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
21-587 |
1.31e-29 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 124.18 E-value: 1.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 21 LQRFLQIqkvLFPSWSSqnalmFLTLLFVALLEQLViyqvGLIPSQYYG-----VLGNKDLDGFKTLTFLAVMLIVLNSM 95
Cdd:COG2274 144 LRWFLRL---LRRYRRL-----LLQVLLASLLINLL----ALATPLFTQvvidrVLPNQDLSTLWVLAIGLLLALLFEGL 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 96 LKSFDQF----TCNLLYVSWRKDLTEHLHHL---YFQGRvyYTlnvlrddvdnPD--QRIsQDVERFCRQLSSMASKLII 166
Cdd:COG2274 212 LRLLRSYlllrLGQRIDLRLSSRFFRHLLRLplsFFESR--SV----------GDlaSRF-RDVESIREFLTGSLLTALL 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 167 S-PFTLIYYTYQCFQStGWLGPMSIFGyFILGTLVNKtLMGPIVAKLVQQEklegdfrfkhmqIRVNAESAAF------- 238
Cdd:COG2274 279 DlLFVLIFLIVLFFYS-PPLALVVLLL-IPLYVLLGL-LFQPRLRRLSREE------------SEASAKRQSLlvetlrg 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 239 ---FRAGHVEHQ---RTDRRLQRLLQTQRELMSKELWLYIGVNTFdylgSILSYVVIaipIFSGVY----GDLSpteLST 308
Cdd:COG2274 344 ietIKALGAESRfrrRWENLLAKYLNARFKLRRLSNLLSTLSGLL----QQLATVAL---LWLGAYlvidGQLT---LGQ 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 309 LVsknAFVCI--YLISCFTRLIDLSSTLSDVAGYTHRIGELQETlldmslklrggggeildESEWNMDRAPGWPAAEPAD 386
Cdd:COG2274 414 LI---AFNILsgRFLAPVAQLIGLLQRFQDAKIALERLDDILDL-----------------PPEREEGRSKLSLPRLKGD 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 387 TAF--LSssgspLCPPSSHKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQM----LTDFGPH--- 457
Cdd:COG2274 474 IELenVS-----FRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIdgidLRQIDPAslr 548
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 458 ---GVlfLPQKPFFTDGTLREQVSDIYPlkeiypdsgSTDDERILRFLELAGLSSLVTR-TEGLDQQVDwNWYDVLSPGE 533
Cdd:COG2274 549 rqiGV--VLQDVFLFSGTIRENITLGDP---------DATDEEIIEAARLAGLHDFIEAlPMGYDTVVG-EGGSNLSGGQ 616
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 1953408514 534 MQRLSFARLFYLQPKYAVLDEATSALTEEVESELYRIGQQL--GMTFISVGHRHSL 587
Cdd:COG2274 617 RQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLlkGRTVIIIAHRLST 672
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
18-584 |
1.26e-25 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 111.41 E-value: 1.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 18 LQFLQRFLQIQKVLFpswssqnALMFLTLLFVALLEQLVIYQVGLIPSQyygVLGNKDLDGFKTLTFLAVMLIVLNSMLK 97
Cdd:COG1132 9 LRRLLRYLRPYRGLL-------ILALLLLLLSALLELLLPLLLGRIIDA---LLAGGDLSALLLLLLLLLGLALLRALLS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 98 SFDQFTCNLLYVS----WRKDLTEHLHHL---YFQG-RVYYTLNVLRDDVDNpdqrisqdVERFcrqLSSMASKLIISPF 169
Cdd:COG1132 79 YLQRYLLARLAQRvvadLRRDLFEHLLRLplsFFDRrRTGDLLSRLTNDVDA--------VEQF---LAHGLPQLVRSVV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 170 TLIYYTYQCFQSTGWLGPMSIFGyFILGTLVNKTLMGPIVAKLVQQEKLEGDFrFKHMQ--------IRVnaesaafFRA 241
Cdd:COG1132 148 TLIGALVVLFVIDWRLALIVLLV-LPLLLLVLRLFGRRLRKLFRRVQEALAEL-NGRLQeslsgirvVKA-------FGR 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 242 GHVEHQRTDRRLQRLLQTQRELMSKELWLYIGVNTFDYLGSILSYVVIAIPIFSGvygDLSPTELSTLVSknafvciYLI 321
Cdd:COG1132 219 EERELERFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSG---SLTVGDLVAFIL-------YLL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 322 SCFTRLIDLSSTLSDV---AGYTHRIGElqetlldmslklrggggeILDESEwnmdrapgwPAAEPADTAFLSSSGSPLC 398
Cdd:COG1132 289 RLFGPLRQLANVLNQLqraLASAERIFE------------------LLDEPP---------EIPDPPGAVPLPPVRGEIE 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 399 --------PPSshKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQM----LTDFGPHG----VLFL 462
Cdd:COG1132 342 fenvsfsyPGD--RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIdgvdIRDLTLESlrrqIGVV 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 463 PQKPFFTDGTLREQVSdiyplkeiYPDSGSTDDErILRFLELAGLSSLVTR-TEGLDQQVDWNWYDvLSPGEMQRLSFAR 541
Cdd:COG1132 420 PQDTFLFSGTIRENIR--------YGRPDATDEE-VEEAAKAAQAHEFIEAlPDGYDTVVGERGVN-LSGGQRQRIAIAR 489
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1953408514 542 LFYLQPKYAVLDEATSAL---TE-EVESELYRIGQqlGMTFISVGHR 584
Cdd:COG1132 490 ALLKDPPILILDEATSALdteTEaLIQEALERLMK--GRTTIVIAHR 534
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
400-587 |
4.07e-23 |
|
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: 98.05 E-value: 4.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 400 PSSHKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVqML--TDFGP-------HGVLFLPQKPFFTD 470
Cdd:cd03245 13 PNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSV-LLdgTDIRQldpadlrRNIGYVPQDVTLFY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 471 GTLREQVSDIYPlkeiypdsgSTDDERILRFLELAGLSSLVTR-TEGLDQQVDWNWYDvLSPGEMQRLSFARLFYLQPKY 549
Cdd:cd03245 92 GTLRDNITLGAP---------LADDERILRAAELAGVTDFVNKhPNGLDLQIGERGRG-LSGGQRQAVALARALLNDPPI 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1953408514 550 AVLDEATSALTEEVESELYRIGQQL--GMTFISVGHRHSL 587
Cdd:cd03245 162 LLLDEPTSAMDMNSEERLKERLRQLlgDKTLIIITHRPSL 201
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
400-587 |
1.34e-22 |
|
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: 94.76 E-value: 1.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 400 PSSHKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV----QMLTDFGPHG----VLFLPQKPFFTDG 471
Cdd:cd03228 11 PGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEIlidgVDLRDLDLESlrknIAYVPQDPFLFSG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 472 TLREqvsdiyplkeiypdsgstdderilrflelaglsslvtrtegldqqvdwNwydVLSPGEMQRLSFARLFYLQPKYAV 551
Cdd:cd03228 91 TIRE------------------------------------------------N---ILSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1953408514 552 LDEATSAL---TE-EVESELYRIGQqlGMTFISVGHRHSL 587
Cdd:cd03228 120 LDEATSALdpeTEaLILEALRALAK--GKTVIVIAHRLST 157
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
404-584 |
1.76e-21 |
|
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: 98.29 E-value: 1.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 404 KPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV----QMLTDFGP----HGVLFLPQKPFFTDGTLRE 475
Cdd:COG4988 350 RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSIlingVDLSDLDPaswrRQIAWVPQNPYLFAGTIRE 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 476 QVSdiyplkeIY-PDSgstDDERILRFLELAGLSSLVTR-TEGLDQQVD---WNwydvLSPGEMQRLSFARLFYLQPKYA 550
Cdd:COG4988 430 NLR-------LGrPDA---SDEELEAALEAAGLDEFVAAlPDGLDTPLGeggRG----LSGGQAQRLALARALLRDAPLL 495
|
170 180 190
....*....|....*....|....*....|....*.
gi 1953408514 551 VLDEATSALTEEVESELYRIGQQL--GMTFISVGHR 584
Cdd:COG4988 496 LLDEPTAHLDAETEAEILQALRRLakGRTVILITHR 531
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
399-587 |
4.95e-21 |
|
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: 90.35 E-value: 4.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 399 PPSSHKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQM---------LTDFGPHgVLFLPQKPFFT 469
Cdd:cd03246 10 YPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLdgadisqwdPNELGDH-VGYLPQDDELF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 470 DGTLREqvsdiyplkeiypdsgstdderilrflelaglsslvtrtegldqqvdwnwyDVLSPGEMQRLSFARLFYLQPKY 549
Cdd:cd03246 89 SGSIAE---------------------------------------------------NILSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1953408514 550 AVLDEATSALTEEVESELYRIGQQL---GMTFISVGHRHSL 587
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALkaaGATRIVIAHRPET 158
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
405-584 |
4.96e-21 |
|
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: 96.97 E-value: 4.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 405 PLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQM----LTDFGPHG----VLFLPQKPFFTDGTLREQ 476
Cdd:TIGR02857 336 PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVngvpLADADADSwrdqIAWVPQHPFLFAGTIAEN 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 477 VSdiyplkeiYPDSGSTDDErILRFLELAGLSSLV-TRTEGLDQQVDWNWYDvLSPGEMQRLSFARLFYLQPKYAVLDEA 555
Cdd:TIGR02857 416 IR--------LARPDASDAE-IREALERAGLDEFVaALPQGLDTPIGEGGAG-LSGGQAQRLALARAFLRDAPLLLLDEP 485
|
170 180 190
....*....|....*....|....*....|.
gi 1953408514 556 TSALTEEVESELYRIGQQL--GMTFISVGHR 584
Cdd:TIGR02857 486 TAHLDAETEAEVLEALRALaqGRTVLLVTHR 516
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
400-584 |
5.86e-21 |
|
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: 91.37 E-value: 5.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 400 PSSHKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQM----LTDFGPH------GVLFlpQKP--- 466
Cdd:cd03225 10 PDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVdgkdLTKLSLKelrrkvGLVF--QNPddq 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 467 FFTDgTLREQVSdiYPLkEIYPDSGSTDDERILRFLELAGLSSLvtrtegldqqVDWNWYDvLSPGEMQRLSFARLFYLQ 546
Cdd:cd03225 88 FFGP-TVEEEVA--FGL-ENLGLPEEEIEERVEEALELVGLEGL----------RDRSPFT-LSGGQKQRVAIAGVLAMD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1953408514 547 PKYAVLDEATSAL----TEEVESELYRIGQQlGMTFISVGHR 584
Cdd:cd03225 153 PDILLLDEPTAGLdpagRRELLELLKKLKAE-GKTIIIVTHD 193
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
403-602 |
5.91e-20 |
|
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: 86.92 E-value: 5.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 403 HKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQmltdFGPHGVLFLPQKPfftdgtLREQVSdiyp 482
Cdd:cd00267 11 GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEIL----IDGKDIAKLPLEE------LRRRIG---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 483 lkeiypdsgstdderilrflelaglsslvtrteGLDQqvdwnwydvLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEE 562
Cdd:cd00267 77 ---------------------------------YVPQ---------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPA 114
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1953408514 563 VESELYRIGQQL---GMTFISVGHRHSLEKFHSLVLKLYGEGR 602
Cdd:cd00267 115 SRERLLELLRELaeeGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
407-557 |
8.44e-19 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 83.47 E-value: 8.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 407 IKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQ-----MLTDFGPH---GVLFLPQKP-FFTDGTLREQV 477
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILldgqdLTDDERKSlrkEIGYVFQDPqLFPRLTVRENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 478 SDIYPLKEIYPDsgsTDDERILRFLELAGLSSLVTRTEGldqqvdwNWYDVLSPGEMQRLSFARLFYLQPKYAVLDEATS 557
Cdd:pfam00005 81 RLGLLLKGLSKR---EKDARAEEALEKLGLGDLADRPVG-------ERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
404-597 |
8.98e-18 |
|
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: 82.66 E-value: 8.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 404 KPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGsvQMLTDFGP----------HGVLFLPQKPFFTDGTL 473
Cdd:cd03254 16 KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKG--QILIDGIDirdisrkslrSMIGVVLQDTFLFSGTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 474 REQVSdiyplkeiYPDSGSTDDErILRFLELAGLSSLVTR-TEGLDQQVDWNWyDVLSPGEMQRLSFARLFYLQPKYAVL 552
Cdd:cd03254 94 MENIR--------LGRPNATDEE-VIEAAKEAGAHDFIMKlPNGYDTVLGENG-GNLSQGERQLLAIARAMLRDPKILIL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1953408514 553 DEATSAL---TEE-VESELYRIGQqlGMTFISVGHRHSLEKFHSLVLKL 597
Cdd:cd03254 164 DEATSNIdteTEKlIQEALEKLMK--GRTSIIIAHRLSTIKNADKILVL 210
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
403-607 |
8.20e-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: 8.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 403 HKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSvqmltdfgphGVLFLPQKPFFTDGTLREQVsdiyp 482
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVA----------GCVDVPDNQFGREASLIDAI----- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 483 lkeiyPDSGSTDDerILRFLELAGLSSLvtrtegldqqvdWNW---YDVLSPGEMQRLSFARLFYLQPKYAVLDEATSAL 559
Cdd:COG2401 107 -----GRKGDFKD--AVELLNAVGLSDA------------VLWlrrFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1953408514 560 TEEVESELYRIGQQL----GMTFISVGHRHSLEKFHS---LVLKLYGeGRWELSR 607
Cdd:COG2401 168 DRQTAKRVARNLQKLarraGITLVVATHHYDVIDDLQpdlLIFVGYG-GVPEEKR 221
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
402-596 |
9.34e-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: 79.50 E-value: 9.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 402 SHKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQML---TDFGPHGVLFLPQKPFFtDGTLREQVS 478
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFgkpLEKERKRIGYVPQRRSI-DRDFPISVR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 479 DI-----YPLKEIYPDSGSTDDERILRFLELAGLSSLVTRTegLDQqvdwnwydvLSPGEMQRLSFARLFYLQPKYAVLD 553
Cdd:cd03235 89 DVvlmglYGHKGLFRRLSKADKAKVDEALERVGLSELADRQ--IGE---------LSGGQQQRVLLARALVQDPDLLLLD 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1953408514 554 EATSALTEEVESELYRIGQQL---GMTFISVGH-RHSLEKF--HSLVLK 596
Cdd:cd03235 158 EPFAGVDPKTQEDIYELLRELrreGMTILVVTHdLGLVLEYfdRVLLLN 206
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
405-583 |
1.05e-16 |
|
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: 79.55 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 405 PLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV----QMLTDFGPHGVLFLPQK--------PFFTDGT 472
Cdd:cd03258 19 TALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVlvdgTDLTLLSGKELRKARRRigmifqhfNLLSSRT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 473 LREQVSdiYPLkEIYPDSGSTDDERILRFLELAGLSSLVTRtegldqqvdwnwY-DVLSPGEMQRLSFARLFYLQPKYAV 551
Cdd:cd03258 99 VFENVA--LPL-EIAGVPKAEIEERVLELLELVGLEDKADA------------YpAQLSGGQKQRVGIARALANNPKVLL 163
|
170 180 190
....*....|....*....|....*....|....*.
gi 1953408514 552 LDEATSAL----TEEVESELYRIGQQLGMTFISVGH 583
Cdd:cd03258 164 CDEATSALdpetTQSILALLRDINRELGLTIVLITH 199
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
404-559 |
1.10e-16 |
|
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: 79.06 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 404 KPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV--------QMLTDFGPHgVLFLPQKPFFTDG-TLR 474
Cdd:COG4133 15 RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVlwngepirDAREDYRRR-LAYLGHADGLKPElTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 475 EQ---VSDIYPLkeiypdsgSTDDERILRFLELAGLSSLvtrtegLDQQVdwnwyDVLSPGEMQRLSFARLFYLQPKYAV 551
Cdd:COG4133 94 ENlrfWAALYGL--------RADREAIDEALEAVGLAGL------ADLPV-----RQLSAGQKRRVALARLLLSPAPLWL 154
|
....*...
gi 1953408514 552 LDEATSAL 559
Cdd:COG4133 155 LDEPFTAL 162
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
403-590 |
2.11e-16 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 78.30 E-value: 2.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 403 HKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV------------QMLTDFGPHGVLFLPQK----P 466
Cdd:cd03255 16 KVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVrvdgtdisklseKELAAFRRRHIGFVFQSfnllP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 467 FFtdgTLREQVSdiYPLkEIYPDSGSTDDERILRFLELAGLsslvtrTEGLDQQVDWnwydvLSPGEMQRLSFARLFYLQ 546
Cdd:cd03255 96 DL---TALENVE--LPL-LLAGVPKKERRERAEELLERVGL------GDRLNHYPSE-----LSGGQQQRVAIARALAND 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1953408514 547 PKYAVLDEATSAL----TEEVESELYRIGQQLGMTFISVGHRHSLEKF 590
Cdd:cd03255 159 PKIILADEPTGNLdsetGKEVMELLRELNKEAGTTIVVVTHDPELAEY 206
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
400-586 |
2.76e-16 |
|
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: 78.43 E-value: 2.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 400 PSSHKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQM----LTDFGPHG----VLFLPQKPFFTDG 471
Cdd:cd03251 11 PGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIdghdVRDYTLASlrrqIGLVSQDVFLFND 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 472 TLREQVSdiyplkeiYPDSGSTDDErILRFLELAGLSSLVTRT-EGLDQQVDWNWYDvLSPGEMQRLSFARLFYLQPKYA 550
Cdd:cd03251 91 TVAENIA--------YGRPGATREE-VEEAARAANAHEFIMELpEGYDTVIGERGVK-LSGGQRQRIAIARALLKDPPIL 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 1953408514 551 VLDEATSALTEEVESELYRIGQQL--GMTFISVGHRHS 586
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLmkNRTTFVIAHRLS 198
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
404-584 |
3.12e-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: 3.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 404 KPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQM----LTDFGPHgVL-----FLPQKPFFTDGTLR 474
Cdd:cd03244 17 PPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIdgvdISKIGLH-DLrsrisIIPQDPVLFSGTIR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 475 EqvsDIYPLKEiypdsgsTDDERILRFLELAGLSSLV-TRTEGLDQQVDWNWyDVLSPGEMQRLSFARLFYLQPKYAVLD 553
Cdd:cd03244 96 S---NLDPFGE-------YSDEELWQALERVGLKEFVeSLPGGLDTVVEEGG-ENLSVGQRQLLCLARALLRKSKILVLD 164
|
170 180 190
....*....|....*....|....*....|....*..
gi 1953408514 554 EATSAlteeVESELYRIGQQL------GMTFISVGHR 584
Cdd:cd03244 165 EATAS----VDPETDALIQKTireafkDCTVLTIAHR 197
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
282-567 |
4.29e-16 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 81.25 E-value: 4.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 282 SILSYVVIAIPIFSGvyGDLSPTELSTLVsknaFVCIYLISCFTRLIDLSSTLSDVAGYTHRIGELQETlldmslklRGG 361
Cdd:TIGR02868 251 AVLGALWAGGPAVAD--GRLAPVTLAVLV----LLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVLDA--------AGP 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 362 GGEILDESEwnMDRAPGWPAAEPADTAFlSSSGSPlcppsshkPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLW 441
Cdd:TIGR02868 317 VAEGSAPAA--GAVGLGKPTLELRDLSA-GYPGAP--------PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLL 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 442 ASTQGSVqMLTDFGPHG---------VLFLPQKPFFTDGTLREQvsdiypLKEIYPDSgstDDERILRFLELAGLSSLVT 512
Cdd:TIGR02868 386 DPLQGEV-TLDGVPVSSldqdevrrrVSVCAQDAHLFDTTVREN------LRLARPDA---TDEELWAALERVGLADWLR 455
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1953408514 513 RT-EGLDQQVDWNWyDVLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEVESEL 567
Cdd:TIGR02868 456 ALpDGLDTVLGEGG-ARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADEL 510
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
407-583 |
7.26e-16 |
|
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: 77.38 E-value: 7.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 407 IKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQM----LTDFGP--HGVLFLPQ-KPFFTDGTLREQVSd 479
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLngkdITNLPPekRDISYVPQnYALFPHMTVYKNIA- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 480 iYPLKEIYPDSgSTDDERILRFLELAGLSSLVTRTEGldqqvdwnwydVLSPGEMQRLSFARLFYLQPKYAVLDEATSAL 559
Cdd:cd03299 94 -YGLKKRKVDK-KEIERKVLEIAEMLGIDHLLNRKPE-----------TLSGGEQQRVAIARALVVNPKILLLDEPFSAL 160
|
170 180
....*....|....*....|....*...
gi 1953408514 560 ----TEEVESELYRIGQQLGMTFISVGH 583
Cdd:cd03299 161 dvrtKEKLREELKKIRKEFGVTVLHVTH 188
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
403-586 |
2.25e-15 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 75.73 E-value: 2.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 403 HKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQM---------LTDFGPH-GVLflPQK-PFFTDg 471
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIdgqdirevtLDSLRRAiGVV--PQDtVLFND- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 472 TLREQVSdiyplkeiYPDSGSTDDERIlrflELAGLSSLVTRTEGLDQQvdwnwYDV--------LSPGEMQRLSFARLF 543
Cdd:cd03253 90 TIGYNIR--------YGRPDATDEEVI----EAAKAAQIHDKIMRFPDG-----YDTivgerglkLSGGEKQRVAIARAI 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1953408514 544 YLQPKYAVLDEATSALTEEVESELYRIGQQL--GMTFISVGHRHS 586
Cdd:cd03253 153 LKNPPILLLDEATSALDTHTEREIQAALRDVskGRTTIVIAHRLS 197
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
407-588 |
4.43e-15 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 74.91 E-value: 4.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 407 IKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLW-----ASTQGSVQML------TDFGPH------GVLFlpQKPFFT 469
Cdd:cd03260 16 LKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDgkdiydLDVDVLelrrrvGMVF--QKPNPF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 470 DGTLREQVSdiYPLKEIYPDSGSTDDERILRFLELAGLSSLV-TRTEGLDqqvdwnwydvLSPGEMQRLSFARLFYLQPK 548
Cdd:cd03260 94 PGSIYDNVA--YGLRLHGIKLKEELDERVEEALRKAALWDEVkDRLHALG----------LSGGQQQRLCLARALANEPE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1953408514 549 YAVLDEATSAL----TEEVESELYRIGQQLGMTFISvghrHSLE 588
Cdd:cd03260 162 VLLLDEPTSALdpisTAKIEELIAELKKEYTIVIVT----HNMQ 201
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
404-583 |
5.88e-15 |
|
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: 74.09 E-value: 5.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 404 KPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV----QMLTDFGPH--GVLFLPQKP-FFTDGTLREQ 476
Cdd:cd03259 13 VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEIlidgRDVTGVPPErrNIGMVFQDYaLFPHLTVAEN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 477 VSdiYPLKEIYPDSGSTdDERILRFLELAGLSSLVTRtegldqqvdwnWYDVLSPGEMQRLSFARLFYLQPKYAVLDEAT 556
Cdd:cd03259 93 IA--FGLKLRGVPKAEI-RARVRELLELVGLEGLLNR-----------YPHELSGGQQQRVALARALAREPSLLLLDEPL 158
|
170 180 190
....*....|....*....|....*....|.
gi 1953408514 557 SAL----TEEVESELYRIGQQLGMTFISVGH 583
Cdd:cd03259 159 SALdaklREELREELKELQRELGITTIYVTH 189
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
403-583 |
6.14e-15 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 74.58 E-value: 6.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 403 HKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV----QMLTDFGPH----GVLFlpQK-PFFTDGTL 473
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEIlldgKDITNLPPHkrpvNTVF--QNyALFPHLTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 474 REQVSdiYPLKeIYPDSGSTDDERILRFLELAGLSSLVTRTEgldqqvdwnwyDVLSPGEMQRLSFARLFYLQPKYAVLD 553
Cdd:cd03300 90 FENIA--FGLR-LKKLPKAEIKERVAEALDLVQLEGYANRKP-----------SQLSGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190
....*....|....*....|....*....|....
gi 1953408514 554 EATSALT----EEVESELYRIGQQLGMTFISVGH 583
Cdd:cd03300 156 EPLGALDlklrKDMQLELKRLQKELGITFVFVTH 189
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
404-583 |
8.74e-15 |
|
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: 74.08 E-value: 8.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 404 KPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQM----LTDFGPH---------GVLFlpQKP-FFT 469
Cdd:cd03261 13 RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIdgedISGLSEAelyrlrrrmGMLF--QSGaLFD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 470 DGTLREQVSdiYPLKEIYPDSGSTDDERILRFLELAGLSslvtrtegldQQVDwnwydvLSPGE----MQ-RLSFARLFY 544
Cdd:cd03261 91 SLTVFENVA--FPLREHTRLSEEEIREIVLEKLEAVGLR----------GAED------LYPAElsggMKkRVALARALA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1953408514 545 LQPKYAVLDEATSAL----TEEVESELYRIGQQLGMTFISVGH 583
Cdd:cd03261 153 LDPELLLYDEPTAGLdpiaSGVIDDLIRSLKKELGLTSIMVTH 195
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
405-586 |
2.37e-14 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 72.96 E-value: 2.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 405 PLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV----QMLTDFGPHGVL----FLPQKPFFTDGTLREQ 476
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEIlldgVDIRDLNLRWLRsqigLVSQEPVLFDGTIAEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 477 VSdiyplkeiYPDSGSTDDERIlRFLELAGLSSLVTR-TEGLDQQVDWNwYDVLSPGEMQRLSFARLFYLQPKYAVLDEA 555
Cdd:cd03249 97 IR--------YGKPDATDEEVE-EAAKKANIHDFIMSlPDGYDTLVGER-GSQLSGGQKQRIAIARALLRNPKILLLDEA 166
|
170 180 190
....*....|....*....|....*....|...
gi 1953408514 556 TSALTEEVESELYRIGQQL--GMTFISVGHRHS 586
Cdd:cd03249 167 TSALDAESEKLVQEALDRAmkGRTTIVIAHRLS 199
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
400-586 |
2.63e-14 |
|
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: 75.91 E-value: 2.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 400 PSSHKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQM---------LTDFGPHgVLFLPQKPFFTD 470
Cdd:TIGR02203 341 PGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLdghdladytLASLRRQ-VALVSQDVVLFN 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 471 GTLREQVSdiyplkeiYPDSGSTDDERILRFLELAGLSSLVTRT-EGLDQQVDWNWyDVLSPGEMQRLSFARLFYLQPKY 549
Cdd:TIGR02203 420 DTIANNIA--------YGRTEQADRAEIERALAAAYAQDFVDKLpLGLDTPIGENG-VLLSGGQRQRLAIARALLKDAPI 490
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1953408514 550 AVLDEATSALTEE----VESELYRIGQqlGMTFISVGHRHS 586
Cdd:TIGR02203 491 LILDEATSALDNEserlVQAALERLMQ--GRTTLVIAHRLS 529
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
402-583 |
4.73e-14 |
|
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: 71.77 E-value: 4.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 402 SHKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV------------QMLTDFGpHGVLFLPQKPFft 469
Cdd:cd03257 16 GSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIifdgkdllklsrRLRKIRR-KEIQMVFQDPM-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 470 dGTL--REQVSDIypLKEIYPDSGSTDDERILRFLELAGLSSLVTRTEGLDQ---QvdwnwydvLSPGEMQRLSFARLFY 544
Cdd:cd03257 93 -SSLnpRMTIGEQ--IAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRyphE--------LSGGQRQRVAIARALA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1953408514 545 LQPKYAVLDEATSAL---TE-EVESELYRIGQQLGMTFISVGH 583
Cdd:cd03257 162 LNPKLLIADEPTSALdvsVQaQILDLLKKLQEELGLTLLFITH 204
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
406-599 |
6.01e-14 |
|
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: 71.75 E-value: 6.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 406 LIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQM----LTDFGPH------GVLFlpQKPFFTDGTLRE 475
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVdghdLALADPAwlrrqvGVVL--QENVLFNRSIRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 476 QVSDIYPlkeiypdsgSTDDERILRFLELAGLSSLVTRT-EGLDQQVDWNWYDvLSPGEMQRLSFARLFYLQPKYAVLDE 554
Cdd:cd03252 95 NIALADP---------GMSMERVIEAAKLAGAHDFISELpEGYDTIVGEQGAG-LSGGQRQRIAIARALIHNPRILIFDE 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1953408514 555 ATSALTEEVESELYRIGQQL--GMTFISVGHRHSLEKFHSLVLKLYG 599
Cdd:cd03252 165 ATSALDYESEHAIMRNMHDIcaGRTVIIIAHRLSTVKNADRIIVMEK 211
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
399-596 |
9.16e-14 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 74.37 E-value: 9.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 399 PPSSHKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV----QMLTDFGPH----GVLFLPQKPFFTD 470
Cdd:TIGR00958 489 PNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVlldgVPLVQYDHHylhrQVALVGQEPVLFS 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 471 GTLREQVSdiYPLKeiypdsgSTDDERILRFLELAGLSSLVTR-TEGLDQQVDWNWyDVLSPGEMQRLSFARLFYLQPKY 549
Cdd:TIGR00958 569 GSVRENIA--YGLT-------DTPDEEIMAAAKAANAHDFIMEfPNGYDTEVGEKG-SQLSGGQKQRIAIARALVRKPRV 638
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1953408514 550 AVLDEATSALTEEVESELYRIGQQLGMTFISVGHR-HSLEKFHS-LVLK 596
Cdd:TIGR00958 639 LILDEATSALDAECEQLLQESRSRASRTVLLIAHRlSTVERADQiLVLK 687
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
400-595 |
4.32e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 72.16 E-value: 4.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 400 PSSHKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQM----LTDFGP----HGVLFLPQKPFFTDG 471
Cdd:PRK11160 349 PDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLngqpIADYSEaalrQAISVVSQRVHLFSA 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 472 TLREQvsdiypLKEIYPDSgstDDERILRFLELAGLSSLVTRTEGLDQqvdwnWYD----VLSPGEMQRLSFARLFYLQP 547
Cdd:PRK11160 429 TLRDN------LLLAAPNA---SDEALIEVLQQVGLEKLLEDDKGLNA-----WLGeggrQLSGGEQRRLGIARALLHDA 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1953408514 548 KYAVLDEATSALTEEVESELYRIGQQL--GMTFISVGHR-HSLEKFHSLVL 595
Cdd:PRK11160 495 PLLLLDEPTEGLDAETERQILELLAEHaqNKTVLMITHRlTGLEQFDRICV 545
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
400-583 |
5.93e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 69.66 E-value: 5.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 400 PSSHKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQMltdfgphGVLFLPQKpffTDGTLREQVSD 479
Cdd:PRK13635 16 PDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITV-------GGMVLSEE---TVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 480 IYPlkeiYPDS---GSTDDERILRFLELAGlsslVTRTEGLdQQVDWNWYDV------------LSPGEMQRLSFARLFY 544
Cdd:PRK13635 86 VFQ----NPDNqfvGATVQDDVAFGLENIG----VPREEMV-ERVDQALRQVgmedflnrephrLSGGQKQRVAIAGVLA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1953408514 545 LQPKYAVLDEATSALT----EEVESELYRIGQQLGMTFISVGH 583
Cdd:PRK13635 157 LQPDIIILDEATSMLDprgrREVLETVRQLKEQKGITVLSITH 199
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
400-584 |
6.84e-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: 67.34 E-value: 6.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 400 PSSHKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQM-------LTDFGPHGVLFLPQKPFFTDGT 472
Cdd:cd03247 11 PEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLdgvpvsdLEKALSSLISVLNQRPYLFDTT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 473 LREQVSdiyplkeiypdsgstdderiLRFlelaglsslvtrtegldqqvdwnwydvlSPGEMQRLSFARLFYLQPKYAVL 552
Cdd:cd03247 91 LRNNLG--------------------RRF----------------------------SGGERQRLALARILLQDAPIVLL 122
|
170 180 190
....*....|....*....|....*....|....
gi 1953408514 553 DEATSALTEEVESELYR-IGQQL-GMTFISVGHR 584
Cdd:cd03247 123 DEPTVGLDPITERQLLSlIFEVLkDKTLIWITHH 156
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
404-583 |
7.13e-13 |
|
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: 68.27 E-value: 7.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 404 KPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQM----LTDFGPH-GVLF-----LPQKpfftdgTL 473
Cdd:cd03293 17 VTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVdgepVTGPGPDrGYVFqqdalLPWL------TV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 474 REQVSdiYPLkEIYPDSGSTDDERILRFLELAGLSSLVTRtegldqqvdwnWYDVLSPGEMQRLSFARLFYLQPKYAVLD 553
Cdd:cd03293 91 LDNVA--LGL-ELQGVPKAEARERAEELLELVGLSGFENA-----------YPHQLSGGMRQRVALARALAVDPDVLLLD 156
|
170 180 190
....*....|....*....|....*....|....
gi 1953408514 554 EATSAL---T-EEVESELYRIGQQLGMTFISVGH 583
Cdd:cd03293 157 EPFSALdalTrEQLQEELLDIWRETGKTVLLVTH 190
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
406-559 |
1.47e-12 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 66.90 E-value: 1.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 406 LIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQMLTDFGPHGVL-----FLPQKP---FFTDGTLREqv 477
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERrksigYVMQDVdyqLFTDSVREE-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 478 sdIYPLKEIYPDSGsTDDERILRFLELAGLsslvtrtegldqqVDWNWYDvLSPGEMQRLSFARLFYLQPKYAVLDEATS 557
Cdd:cd03226 93 --LLLGLKELDAGN-EQAETVLKDLDLYAL-------------KERHPLS-LSGGQKQRLAIAAALLSGKDLLIFDEPTS 155
|
..
gi 1953408514 558 AL 559
Cdd:cd03226 156 GL 157
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
400-584 |
1.75e-12 |
|
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: 69.93 E-value: 1.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 400 PSSHKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLW---ASTQGSV----QMLTDFGPHG----VLFLPQKPF- 467
Cdd:COG1123 15 PGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLphgGRISGEVlldgRDLLELSEALrgrrIGMVFQDPMt 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 468 -FTDGTLREQVSDIYPLKEIypdSGSTDDERILRFLELAGLSSLVTRtegldqqvdwnwY-DVLSPGEMQRLSFARLFYL 545
Cdd:COG1123 95 qLNPVTVGDQIAEALENLGL---SRAEARARVLELLEAVGLERRLDR------------YpHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1953408514 546 QPKYAVLDEATSAL----TEEVESELYRIGQQLGMTFISVGHR 584
Cdd:COG1123 160 DPDLLIADEPTTALdvttQAEILDLLRELQRERGTTVLLITHD 202
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
403-583 |
2.72e-12 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 65.53 E-value: 2.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 403 HKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQMltdfgphgvlflpqkpfftDGTLREQvsdiYP 482
Cdd:cd03214 11 GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILL-------------------DGKDLAS----LS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 483 LKEIypdsgstddERILRF----LELAGLSSLVTRTegldqqvdwnwYDVLSPGEMQRLSFARLFYLQPKYAVLDEATSA 558
Cdd:cd03214 68 PKEL---------ARKIAYvpqaLELLGLAHLADRP-----------FNELSGGERQRVLLARALAQEPPILLLDEPTSH 127
|
170 180
....*....|....*....|....*....
gi 1953408514 559 L----TEEVESELYRIGQQLGMTFISVGH 583
Cdd:cd03214 128 LdiahQIELLELLRRLARERGKTVVMVLH 156
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
403-583 |
3.06e-12 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 68.44 E-value: 3.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 403 HKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV----QMLTDFGPHgvlflpQKP---------FFT 469
Cdd:PRK09452 26 GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRImldgQDITHVPAE------NRHvntvfqsyaLFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 470 DGTLREQVSdiYPLK-------EIYPdsgstddeRILRFLELAGLSSLVTRTEgldQQvdwnwydvLSPGEMQRLSFARL 542
Cdd:PRK09452 100 HMTVFENVA--FGLRmqktpaaEITP--------RVMEALRMVQLEEFAQRKP---HQ--------LSGGQQQRVAIARA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1953408514 543 FYLQPKYAVLDEATSALT----EEVESELYRIGQQLGMTFISVGH 583
Cdd:PRK09452 159 VVNKPKVLLLDESLSALDyklrKQMQNELKALQRKLGITFVFVTH 203
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
401-595 |
4.61e-12 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 66.63 E-value: 4.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 401 SSHKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQG----------------------SVQMLTDFGPHG 458
Cdd:PRK10419 22 HQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGnvswrgeplaklnraqrkafrrDIQMVFQDSISA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 459 VLflPQKpfftdgTLREQVSDiyPLKEIYPDSGSTDDERILRFLELAGLS-SLVTRtegLDQQvdwnwydvLSPGEMQRL 537
Cdd:PRK10419 102 VN--PRK------TVREIIRE--PLRHLLSLDKAERLARASEMLRAVDLDdSVLDK---RPPQ--------LSGGQLQRV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953408514 538 SFARLFYLQPKYAVLDEATS----ALTEEVESELYRIGQQLGMTFISVGHRHSL-EKFHSLVL 595
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSnldlVLQAGVIRLLKKLQQQFGTACLFITHDLRLvERFCQRVM 223
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
406-583 |
4.75e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 66.73 E-value: 4.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 406 LIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV----QMLTDFGPHG----VLFLPQKPFFTDG-TLREQ 476
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEIlldaQPLESWSSKAfarkVAYLPQQLPAAEGmTVREL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 477 VS-DIYPLKEIYPDSGSTDDERILRFLELAGLSSLVTRTegldqqvdwnwYDVLSPGEMQRLSFARLFYLQPKYAVLDEA 555
Cdd:PRK10575 106 VAiGRYPWHGALGRFGAADREKVEEAISLVGLKPLAHRL-----------VDSLSGGERQRAWIAMLVAQDSRCLLLDEP 174
|
170 180 190
....*....|....*....|....*....|..
gi 1953408514 556 TSAL----TEEVESELYRIGQQLGMTFISVGH 583
Cdd:PRK10575 175 TSALdiahQVDVLALVHRLSQERGLTVIAVLH 206
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
404-583 |
6.83e-12 |
|
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: 64.97 E-value: 6.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 404 KPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV----QMLTDFGPH----GVLF-----LPQKpfftd 470
Cdd:cd03301 13 VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIyiggRDVTDLPPKdrdiAMVFqnyalYPHM----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 471 gTLREQVSdiYPLK-------EIypdsgstdDERILRFLELAGLSSLvtrtegLDQQVDwnwydVLSPGEMQRLSFARLF 543
Cdd:cd03301 88 -TVYDNIA--FGLKlrkvpkdEI--------DERVREVAELLQIEHL------LDRKPK-----QLSGGQRQRVALGRAI 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1953408514 544 YLQPKYAVLDEATSALT----EEVESELYRIGQQLGMTFISVGH 583
Cdd:cd03301 146 VREPKVFLMDEPLSNLDaklrVQMRAELKRLQQRLGTTTIYVTH 189
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
403-583 |
9.69e-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: 63.75 E-value: 9.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 403 HKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQMltdfgpHGVLFlpQKPFFTDGTLREQVSDIYP 482
Cdd:cd03229 12 QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILI------DGEDL--TDLEDELPPLRRRIGMVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 483 LKEIYPdsgstdderilrflelaGLSSLVTRTEGLdqqvdwnwydvlSPGEMQRLSFARLFYLQPKYAVLDEATSAL--- 559
Cdd:cd03229 84 DFALFP-----------------HLTVLENIALGL------------SGGQQQRVALARALAMDPDVLLLDEPTSALdpi 134
|
170 180
....*....|....*....|....*
gi 1953408514 560 -TEEVESELYRIGQQLGMTFISVGH 583
Cdd:cd03229 135 tRREVRALLKSLQAQLGITVVLVTH 159
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
399-580 |
1.40e-11 |
|
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: 67.24 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 399 PPSSHKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQM------------LTDFGPH-GVLFlpQK 465
Cdd:COG1123 273 RGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFdgkdltklsrrsLRELRRRvQMVF--QD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 466 P---FFTDGTLREQVSdiYPLKEIYPDSGSTDDERILRFLELAGLSSLVtrtegldqqvdWNWY-DVLSPGEMQRLSFAR 541
Cdd:COG1123 351 PyssLNPRMTVGDIIA--EPLRLHGLLSRAERRERVAELLERVGLPPDL-----------ADRYpHELSGGQRQRVAIAR 417
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1953408514 542 LFYLQPKYAVLDEATSAL----TEEVESELYRIGQQLGMT--FIS 580
Cdd:COG1123 418 ALALEPKLLILDEPTSALdvsvQAQILNLLRDLQRELGLTylFIS 462
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
407-583 |
1.65e-11 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 65.89 E-value: 1.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 407 IKDLSLKISEGQ--SLLitGNTGTGKSSLLRVLGGLWASTQGSV----QMLTDFGPH----GVLFlpQK----PFFtdgT 472
Cdd:COG3842 21 LDDVSLSIEPGEfvALL--GPSGCGKTTLLRMIAGFETPDSGRIlldgRDVTGLPPEkrnvGMVF--QDyalfPHL---T 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 473 LREQVSdiYPLK-------EIypdsgstdDERILRFLELAGLSSLVTR--TEgldqqvdwnwydvLSPGEMQRLSFARLF 543
Cdd:COG3842 94 VAENVA--FGLRmrgvpkaEI--------RARVAELLELVGLEGLADRypHQ-------------LSGGQQQRVALARAL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1953408514 544 YLQPKYAVLDEATSAL----TEEVESELYRIGQQLGMTFISVGH 583
Cdd:COG3842 151 APEPRVLLLDEPLSALdaklREEMREELRRLQRELGITFIYVTH 194
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
404-583 |
1.82e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 65.14 E-value: 1.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 404 KPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV----QMLT-----DFGPH-GVLFlpQKP--FFTDG 471
Cdd:PRK13650 20 KYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIiidgDLLTeenvwDIRHKiGMVF--QNPdnQFVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 472 TLREQVS-----DIYPLKEIypdsgstdDERILRFLELAGLSSLVTRTEGLdqqvdwnwydvLSPGEMQRLSFARLFYLQ 546
Cdd:PRK13650 98 TVEDDVAfglenKGIPHEEM--------KERVNEALELVGMQDFKEREPAR-----------LSGGQKQRVAIAGAVAMR 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1953408514 547 PKYAVLDEATSALTEEVESELYR----IGQQLGMTFISVGH 583
Cdd:PRK13650 159 PKIIILDEATSMLDPEGRLELIKtikgIRDDYQMTVISITH 199
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
403-559 |
2.64e-11 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 64.41 E-value: 2.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 403 HKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQM----LTDFGPH------GVlfLPQK-----PF 467
Cdd:PRK13548 14 GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLngrpLADWSPAelarrrAV--LPQHsslsfPF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 468 ftdgTLREQVS-DIYPLkeiyPDSGSTDDERILRFLELAGLSSLVTRTegldqqvdwnwYDVLSPGEMQRLSFAR-LFYL 545
Cdd:PRK13548 92 ----TVEEVVAmGRAPH----GLSRAEDDALVAAALAQVDLAHLAGRD-----------YPQLSGGEQQRVQLARvLAQL 152
|
170
....*....|....*....
gi 1953408514 546 -----QPKYAVLDEATSAL 559
Cdd:PRK13548 153 wepdgPPRWLLLDEPTSAL 171
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
404-595 |
3.29e-11 |
|
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: 62.87 E-value: 3.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 404 KPLIKDLSLKISEGQSLLITGNTGTGKSSLLR-VLGGLWAsTQGSVQMltdfgPHGVLFLPQKPFFTDGTLREQVSDIYP 482
Cdd:cd03250 18 SFTLKDINLEVPKGELVAIVGPVGSGKSSLLSaLLGELEK-LSGSVSV-----PGSIAYVSQEPWIQNGTIRENILFGKP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 483 LkeiypdsgstDDERILRFLELAGLSSLVTRTEGLDQQVdwnwydV------LSPGEMQRLSFARLFYLQPKYAVLDEAT 556
Cdd:cd03250 92 F----------DEERYEKVIKACALEPDLEILPDGDLTE------IgekginLSGGQKQRISLARAVYSDADIYLLDDPL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1953408514 557 SALTEEVESELYR--IGQQL--GMTFISVGHR-HSLEKFHSLVL 595
Cdd:cd03250 156 SAVDAHVGRHIFEncILGLLlnNKTRILVTHQlQLLPHADQIVV 199
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
405-583 |
6.54e-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: 62.74 E-value: 6.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 405 PLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV----QMLTDFGPH--GVLFLPQK-PFFTDGTLREQV 477
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTIlfggEDATDVPVQerNVGFVFQHyALFRHMTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 478 S---DIYPLKEIYPDsgSTDDERILRFLELAGLSSLVTRtegldqqvdwnWYDVLSPGEMQRLSFARLFYLQPKYAVLDE 554
Cdd:cd03296 96 AfglRVKPRSERPPE--AEIRAKVHELLKLVQLDWLADR-----------YPAQLSGGQRQRVALARALAVEPKVLLLDE 162
|
170 180 190
....*....|....*....|....*....|...
gi 1953408514 555 ATSALTEEVESEL----YRIGQQLGMTFISVGH 583
Cdd:cd03296 163 PFGALDAKVRKELrrwlRRLHDELHVTTVFVTH 195
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
406-565 |
8.28e-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: 65.35 E-value: 8.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 406 LIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQM----LTDFGPHGVLF----LPQKPFFTDGTLREQV 477
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIdglnIAKIGLHDLRFkitiIPQDPVLFSGSLRMNL 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 478 SDIyplkeiypdsGSTDDERILRFLELAGLSSLVT-RTEGLDQQVDWNWYDvLSPGEMQRLSFARLFYLQPKYAVLDEAT 556
Cdd:TIGR00957 1381 DPF----------SQYSDEEVWWALELAHLKTFVSaLPDKLDHECAEGGEN-LSVGQRQLVCLARALLRKTKILVLDEAT 1449
|
....*....
gi 1953408514 557 SALTEEVES 565
Cdd:TIGR00957 1450 AAVDLETDN 1458
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
403-581 |
8.75e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 62.88 E-value: 8.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 403 HKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVqMLTD----FGPHGVLFLPQKPFFTDGTL----R 474
Cdd:PRK15112 25 TVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGEL-LIDDhplhFGDYSYRSQRIRMIFQDPSTslnpR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 475 EQVSDI--YPLKEIYPDSGSTDDERILRFLELAGLsslvtrtegLDQQVdwNWY-DVLSPGEMQRLSFARLFYLQPKYAV 551
Cdd:PRK15112 104 QRISQIldFPLRLNTDLEPEQREKQIIETLRQVGL---------LPDHA--SYYpHMLAPGQKQRLGLARALILRPKVII 172
|
170 180 190
....*....|....*....|....*....|....
gi 1953408514 552 LDEATSALTEEVESELYRIGQQL----GMTFISV 581
Cdd:PRK15112 173 ADEALASLDMSMRSQLINLMLELqekqGISYIYV 206
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
406-583 |
1.30e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 62.29 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 406 LIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV-------QMLTDfgPHGVLFLPQKPFFTdgTLREQVS 478
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIvvngqtiNLVRD--KDGQLKVADKNQLR--LLRTRLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 479 DIYPLKEIYpdSGSTDDERILRF-LELAGLSSLVTRTE--------GLDQQVDWNWYDVLSPGEMQRLSFARLFYLQPKY 549
Cdd:PRK10619 96 MVFQHFNLW--SHMTVLENVMEApIQVLGLSKQEARERavkylakvGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEV 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 1953408514 550 AVLDEATSALTEEVESELYRIGQQL---GMTFISVGH 583
Cdd:PRK10619 174 LLFDEPTSALDPELVGEVLRIMQQLaeeGKTMVVVTH 210
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
379-584 |
1.48e-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: 61.27 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 379 WPAAEPADTAFLSSSGSPLCPPsshkpLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQM-------- 450
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPP-----VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIdgidisti 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 451 -LTDFgPHGVLFLPQKPFFTDGTLREQVsDIYplkeiypdsGSTDDERILRFLELaglsslvtrTEGLDQqvdwnwydvL 529
Cdd:cd03369 76 pLEDL-RSSLTIIPQDPTLFSGTIRSNL-DPF---------DEYSDEEIYGALRV---------SEGGLN---------L 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1953408514 530 SPGEMQRLSFARLFYLQPKYAVLDEATSALTEEVESELYRIGQQL--GMTFISVGHR 584
Cdd:cd03369 127 SQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREEftNSTILTIAHR 183
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
403-583 |
1.79e-10 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 61.65 E-value: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 403 HKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGS--VQMLTDFGPH----------GVLFlPQKPFFTD 470
Cdd:PRK09493 13 PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDliVDGLKVNDPKvderlirqeaGMVF-QQFYLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 471 GTLREQVSdIYPLKeiYPDSGSTDDERILRflELAGLSSLVTRTEGLDQQvdwnwydvLSPGEMQRLSFARLFYLQPKYA 550
Cdd:PRK09493 92 LTALENVM-FGPLR--VRGASKEEAEKQAR--ELLAKVGLAERAHHYPSE--------LSGGQQQRVAIARALAVKPKLM 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 1953408514 551 VLDEATSALTEEVESELYRIGQQL---GMTFISVGH 583
Cdd:PRK09493 159 LFDEPTSALDPELRHEVLKVMQDLaeeGMTMVIVTH 194
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
404-583 |
1.89e-10 |
|
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: 61.53 E-value: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 404 KPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV----QMLTDFGPH---------GVLF----Lpqkp 466
Cdd:COG1127 18 RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEIlvdgQDITGLSEKelyelrrriGMLFqggaL---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 467 fFTDGTLREQVSdiYPLKEIYPDSGSTDDERILRFLELAGLSSLVTrtegldqqvdwnwydvLSPGE----MQ-RLSFAR 541
Cdd:COG1127 94 -FDSLTVFENVA--FPLREHTDLSEAEIRELVLEKLELVGLPGAAD----------------KMPSElsggMRkRVALAR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1953408514 542 LFYLQPKYAVLDEATSAL----TEEVESELYRIGQQLGMTFISVGH 583
Cdd:COG1127 155 ALALDPEILLYDEPTAGLdpitSAVIDELIRELRDELGLTSVVVTH 200
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
407-583 |
2.31e-10 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 62.74 E-value: 2.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 407 IKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGsvQMLTDfgphGVLFLPqkpfFTDGTLRE----QVSDIYP 482
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRG--QVLID----GVDIAK----ISDAELREvrrkKIAMVFQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 483 LKEIYPDSGSTDDERIlrFLELAGLSSLVTRTEGLD--QQVDWNWY-----DVLSPGEMQRLSFARLFYLQPKYAVLDEA 555
Cdd:PRK10070 114 SFALMPHMTVLDNTAF--GMELAGINAEERREKALDalRQVGLENYahsypDELSGGMRQRVGLARALAINPDILLMDEA 191
|
170 180 190
....*....|....*....|....*....|..
gi 1953408514 556 TSALT----EEVESELYRIGQQLGMTFISVGH 583
Cdd:PRK10070 192 FSALDplirTEMQDELVKLQAKHQRTIVFISH 223
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
401-583 |
2.32e-10 |
|
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: 61.04 E-value: 2.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 401 SSHKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQmltdFGPHGVLFLPQKPF----------FTD 470
Cdd:cd03256 11 PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVL----IDGTDINKLKGKALrqlrrqigmiFQQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 471 GTLREQVSDI--------------------YPLKEIypdsgstddERILRFLELAGLSSLV-TRTegldqqvdwnwyDVL 529
Cdd:cd03256 87 FNLIERLSVLenvlsgrlgrrstwrslfglFPKEEK---------QRALAALERVGLLDKAyQRA------------DQL 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1953408514 530 SPGEMQRLSFARLFYLQPKYAVLDEATSAL----TEEVESELYRIGQQLGMTFISVGH 583
Cdd:cd03256 146 SGGQQQRVAIARALMQQPKLILADEPVASLdpasSRQVMDLLKRINREEGITVIVSLH 203
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
405-586 |
2.43e-10 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 63.30 E-value: 2.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 405 PLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV----QMLTDFGPH------GVLflPQKP-FFTDgTL 473
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRIlidgQDIRDVTQAslraaiGIV--PQDTvLFND-TI 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 474 REQVsdiyplkeIYPDSGSTDDErILRFLELAGLSSLVTRT-EGLDQQVdwnwydvLSPGEMQRLSFARLFYLQPKYAVL 552
Cdd:COG5265 449 AYNI--------AYGRPDASEEE-VEAAARAAQIHDFIESLpDGYDTRVger-glkLSGGEKQRVAIARTLLKNPPILIF 518
|
170 180 190
....*....|....*....|....*....|....*...
gi 1953408514 553 DEATSAL---TE-EVESELYRIGQqlGMTFISVGHRHS 586
Cdd:COG5265 519 DEATSALdsrTErAIQAALREVAR--GRTTLVIAHRLS 554
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
405-589 |
2.93e-10 |
|
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: 63.22 E-value: 2.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 405 PLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQM----LTDFGPHG----VLFLPQKPFFTDGTLREQ 476
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLngfsLKDIDRHTlrqfINYLPQEPYIFSGSILEN 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 477 VsdIYPLKEiypdsGSTDDErILRFLELAGLSSLVTR-TEGLDQQVDWNWYDvLSPGEMQRLSFARLFYLQPKYAVLDEA 555
Cdd:TIGR01193 568 L--LLGAKE-----NVSQDE-IWAACEIAEIKDDIENmPLGYQTELSEEGSS-ISGGQKQRIALARALLTDSKVLILDES 638
|
170 180 190
....*....|....*....|....*....|....*..
gi 1953408514 556 TSALTEEVESELyrIGQQLGM---TFISVGHRHSLEK 589
Cdd:TIGR01193 639 TSNLDTITEKKI--VNNLLNLqdkTIIFVAHRLSVAK 673
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
403-583 |
3.91e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 60.85 E-value: 3.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 403 HKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGsvQMLTDFGPHGVLFLPQKPFFTDGTLreqvsdiYP 482
Cdd:PRK11247 24 ERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAG--ELLAGTAPLAEAREDTRLMFQDARL-------LP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 483 LKEIYPDSG---STD-DERILRFLELAGLSSLVTrtegldqqvdwNWYDVLSPGEMQRLSFARLFYLQPKYAVLDE---A 555
Cdd:PRK11247 95 WKKVIDNVGlglKGQwRDAALQALAAVGLADRAN-----------EWPAALSGGQKQRVALARALIHRPGLLLLDEplgA 163
|
170 180
....*....|....*....|....*....
gi 1953408514 556 TSALTE-EVESELYRIGQQLGMTFISVGH 583
Cdd:PRK11247 164 LDALTRiEMQDLIESLWQQHGFTVLLVTH 192
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
404-583 |
4.29e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 60.11 E-value: 4.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 404 KPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV----QMLTDFGPHG----VLFLPQKPFFTDGTLRE 475
Cdd:PRK10247 20 AKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLlfegEDISTLKPEIyrqqVSYCAQTPTLFGDTVYD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 476 QVSDIYPLKEIYPdsgstDDERILRFLELAGLSSlvtrtEGLDQQVdwnwyDVLSPGEMQRLSFARLFYLQPKYAVLDEA 555
Cdd:PRK10247 100 NLIFPWQIRNQQP-----DPAIFLDDLERFALPD-----TILTKNI-----AELSGGEKQRISLIRNLQFMPKVLLLDEI 164
|
170 180 190
....*....|....*....|....*....|..
gi 1953408514 556 TSALTEE----VESELYRIGQQLGMTFISVGH 583
Cdd:PRK10247 165 TSALDESnkhnVNEIIHRYVREQNIAVLWVTH 196
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
408-583 |
5.07e-10 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 59.62 E-value: 5.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 408 KDLSLKIS---EGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV----------QMLTDFGPH----GVLFlPQKPFFTD 470
Cdd:cd03297 11 PDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIvlngtvlfdsRKKINLPPQqrkiGLVF-QQYALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 471 GTLREQVSDIYPLKEIYPDSGSTDDerilrFLELAGLSSLVTRteGLDQqvdwnwydvLSPGEMQRLSFARLFYLQPKYA 550
Cdd:cd03297 90 LNVRENLAFGLKRKRNREDRISVDE-----LLDLLGLDHLLNR--YPAQ---------LSGGEKQRVALARALAAQPELL 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 1953408514 551 VLDEATSAL----TEEVESELYRIGQQLGMTFISVGH 583
Cdd:cd03297 154 LLDEPFSALdralRLQLLPELKQIKKNLNIPVIFVTH 190
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
400-583 |
5.21e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 60.39 E-value: 5.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 400 PSSHKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQMltdFGphgvLFLPQKPFFtdgTLREQVSD 479
Cdd:PRK13632 18 PNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKI---DG----ITISKENLK---EIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 480 IYPlkeiYPDS---GSTDDERILRFLElaglSSLVTRTE------GLDQQVDWNWY-----DVLSPGEMQRLSFARLFYL 545
Cdd:PRK13632 88 IFQ----NPDNqfiGATVEDDIAFGLE----NKKVPPKKmkdiidDLAKKVGMEDYldkepQNLSGGQKQRVAIASVLAL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1953408514 546 QPKYAVLDEATSALTEEVESELYRIGQQL----GMTFISVGH 583
Cdd:PRK13632 160 NPEIIIFDESTSMLDPKGKREIKKIMVDLrktrKKTLISITH 201
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
407-584 |
5.76e-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: 59.76 E-value: 5.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 407 IKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV----QMLTDFGPH-----GVL--FlpQKP-FFTDGTLR 474
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVlfdgEDITGLPPHeiarlGIGrtF--QIPrLFPELTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 475 EQV-------SDIYPLKEIYPDSGSTDDERILRFLELAGLSSLVTRTEGLdqqvdwnwydvLSPGEMQRLSFARLFYLQP 547
Cdd:cd03219 94 ENVmvaaqarTGSGLLLARARREEREARERAEELLERVGLADLADRPAGE-----------LSYGQQRRLEIARALATDP 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1953408514 548 KYAVLDEATSALT-EEVESELYRIGQ--QLGMTFISVGHR 584
Cdd:cd03219 163 KLLLLDEPAAGLNpEETEELAELIRElrERGITVLLVEHD 202
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
409-583 |
6.86e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 60.52 E-value: 6.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 409 DLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQM----LTDFGPH----------GVLF-LPQKPFFTDGTL 473
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgdivVSSTSKQkeikpvrkkvGVVFqFPESQLFEETVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 474 ReqvsDIYPLKEIYPDSGSTDDERILRFLELAGLSSLVTRTEGLDqqvdwnwydvLSPGEMQRLSFARLFYLQPKYAVLD 553
Cdd:PRK13643 104 K----DVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFE----------LSGGQMRRVAIAGILAMEPEVLVLD 169
|
170 180 190
....*....|....*....|....*....|...
gi 1953408514 554 EATSALTEEVESELYRIGQ---QLGMTFISVGH 583
Cdd:PRK13643 170 EPTAGLDPKARIEMMQLFEsihQSGQTVVLVTH 202
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
399-567 |
1.02e-09 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 59.02 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 399 PPSSHKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGsvQMLTDFGP---------HGVLFL-PQKPFF 468
Cdd:cd03248 22 PTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGG--QVLLDGKPisqyehkylHSKVSLvGQEPVL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 469 TDGTLREQVSdiYPLkeiypdsGSTDDERILRFLELAGLSSLVTRTE-GLDQQVDWNWyDVLSPGEMQRLSFARLFYLQP 547
Cdd:cd03248 100 FARSLQDNIA--YGL-------QSCSFECVKEAAQKAHAHSFISELAsGYDTEVGEKG-SQLSGGQKQRVAIARALIRNP 169
|
170 180
....*....|....*....|
gi 1953408514 548 KYAVLDEATSALteEVESEL 567
Cdd:cd03248 170 QVLILDEATSAL--DAESEQ 187
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
407-583 |
1.32e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 59.65 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 407 IKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQ----MLT------DFGPH----GVLF-LPQKPFFTDG 471
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTigerVITagkknkKLKPLrkkvGIVFqFPEHQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 472 TLReqvsDIY--PLkeiypDSGSTDDERILR---FLELAGLS-SLVTRTEgldqqvdwnwYDvLSPGEMQRLSFARLFYL 545
Cdd:PRK13634 103 VEK----DICfgPM-----NFGVSEEDAKQKareMIELVGLPeELLARSP----------FE-LSGGQMRRVAIAGVLAM 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1953408514 546 QPKYAVLDEATSAL----TEEVESELYRIGQQLGMTFISVGH 583
Cdd:PRK13634 163 EPEVLVLDEPTAGLdpkgRKEMMEMFYKLHKEKGLTTVLVTH 204
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
408-583 |
2.82e-09 |
|
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: 57.54 E-value: 2.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 408 KDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQMltdfgpHG-VLFLPQKPFFTdgtLREQVS------DI 480
Cdd:cd03262 17 KGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIII------DGlKLTDDKKNINE---LRQKVGmvfqqfNL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 481 YP-----------LKEIYPDSGSTDDERILRFLELAGLSslvtrteglDQQvdwNWY-DVLSPGEMQRLSFARLFYLQPK 548
Cdd:cd03262 88 FPhltvlenitlaPIKVKGMSKAEAEERALELLEKVGLA---------DKA---DAYpAQLSGGQQQRVAIARALAMNPK 155
|
170 180 190
....*....|....*....|....*....|....*...
gi 1953408514 549 YAVLDEATSALTEEVESELYRIGQQL---GMTFISVGH 583
Cdd:cd03262 156 VMLFDEPTSALDPELVGEVLDVMKDLaeeGMTMVVVTH 193
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
405-584 |
4.82e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 59.60 E-value: 4.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 405 PLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQM----LTDFG----PHGVLFLPQKPFFTDGTLReq 476
Cdd:PLN03232 1250 PVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIddcdVAKFGltdlRRVLSIIPQSPVLFSGTVR-- 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 477 vSDIYPLKEiypdsgsTDDERILRFLELAGLSSLVTRTE-GLDQQVdWNWYDVLSPGEMQRLSFARLFYLQPKYAVLDEA 555
Cdd:PLN03232 1328 -FNIDPFSE-------HNDADLWEALERAHIKDVIDRNPfGLDAEV-SEGGENFSVGQRQLLSLARALLRRSKILVLDEA 1398
|
170 180 190
....*....|....*....|....*....|.
gi 1953408514 556 TSALTEEVESELYR-IGQQL-GMTFISVGHR 584
Cdd:PLN03232 1399 TASVDVRTDSLIQRtIREEFkSCTMLVIAHR 1429
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
407-606 |
7.52e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 57.36 E-value: 7.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 407 IKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQMltdfgpHGVLFLPQKPFFTDgtLREQVSDI--YP-- 482
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIII------DGVDITDKKVKLSD--IRKKVGLVfqYPey 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 483 -LKE--IYPD-------SGSTDDE---RILRFLELAGLSslvtrtegLDQQVDWNWYDvLSPGEMQRLSFARLFYLQPKY 549
Cdd:PRK13637 95 qLFEetIEKDiafgpinLGLSEEEienRVKRAMNIVGLD--------YEDYKDKSPFE-LSGGQKRRVAIAGVVAMEPKI 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953408514 550 AVLDEATSALT----EEVESELYRIGQQLGMTFISVGhrHSLEKFHSLVLKLY--GEGRWELS 606
Cdd:PRK13637 166 LILDEPTAGLDpkgrDEILNKIKELHKEYNMTIILVS--HSMEDVAKLADRIIvmNKGKCELQ 226
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
403-556 |
7.96e-09 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 58.15 E-value: 7.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 403 HKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQMltdfgPHG--VLFLPQKPFFTDG-TLREQV-- 477
Cdd:COG0488 10 GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI-----PKGlrIGYLPQEPPLDDDlTVLDTVld 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 478 --SDIYPLKEIY------PDSGSTDDERIL----RFLELAG----------LSSLVTRTEGLDQQVdwnwyDVLSPGEMQ 535
Cdd:COG0488 85 gdAELRALEAELeeleakLAEPDEDLERLAelqeEFEALGGweaearaeeiLSGLGFPEEDLDRPV-----SELSGGWRR 159
|
170 180
....*....|....*....|.
gi 1953408514 536 RLSFARLFYLQPKYAVLDEAT 556
Cdd:COG0488 160 RVALARALLSEPDLLLLDEPT 180
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
404-559 |
9.83e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 55.65 E-value: 9.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 404 KPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQmLTDFGPHGVLFLPQ----------KPFFtdgTL 473
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIK-LDGGDIDDPDVAEAchylghrnamKPAL---TV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 474 REQVS---DIYplkeiypdsgSTDDERILRFLELAGLSSLVTRTegldqqvdwnwYDVLSPGEMQRLSFARLFYLQPKYA 550
Cdd:PRK13539 91 AENLEfwaAFL----------GGEELDIAAALEAVGLAPLAHLP-----------FGYLSAGQKRRVALARLLVSNRPIW 149
|
....*....
gi 1953408514 551 VLDEATSAL 559
Cdd:PRK13539 150 ILDEPTAAL 158
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
405-568 |
1.13e-08 |
|
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: 58.38 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 405 PLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQmltdfgpHG--VLFLPQKPFFTDGTLREQVsdIYP 482
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIK-------HSgrISFSPQTSWIMPGTIKDNI--IFG 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 483 LkeiypdsgSTDDERILRFLELAGLSSLVTRTEGLDQQVDWNWYDVLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEE 562
Cdd:TIGR01271 511 L--------SYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVV 582
|
....*.
gi 1953408514 563 VESELY 568
Cdd:TIGR01271 583 TEKEIF 588
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
409-583 |
1.28e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 56.68 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 409 DLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV----QMLTDFGPH----------GVLF-LPQKPFFTDGTL 473
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVrvddTLITSTSKNkdikqirkkvGLVFqFPESQLFEETVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 474 ReqvsDIYPLKEIYPDSGSTDDERILRFLELAGLSslvtrteglDQQVDWNWYDvLSPGEMQRLSFARLFYLQPKYAVLD 553
Cdd:PRK13649 105 K----DVAFGPQNFGVSQEEAEALAREKLALVGIS---------ESLFEKNPFE-LSGGQMRRVAIAGILAMEPKILVLD 170
|
170 180 190
....*....|....*....|....*....|...
gi 1953408514 554 EATSALTEEVESELYRIGQQL---GMTFISVGH 583
Cdd:PRK13649 171 EPTAGLDPKGRKELMTLFKKLhqsGMTIVLVTH 203
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
396-559 |
2.28e-08 |
|
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: 54.97 E-value: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 396 PLCPPSSHKP--LIKDLSLKISEGQSLLITGNTGTGKSSLL-----RVLGGlwASTQGSV----------QMLTDFGphg 458
Cdd:cd03234 10 GLKAKNWNKYarILNDVSLHVESGQVMAILGSSGSGKTTLLdaisgRVEGG--GTTSGQIlfngqprkpdQFQKCVA--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 459 vlFLPQKPFFTDG-TLREQV--SDIYPLKEIYPDSGSTDDERILRFLELAglsslvtrteglDQQVDWNWYDVLSPGEMQ 535
Cdd:cd03234 85 --YVRQDDILLPGlTVRETLtyTAILRLPRKSSDAIRKKRVEDVLLRDLA------------LTRIGGNLVKGISGGERR 150
|
170 180
....*....|....*....|....
gi 1953408514 536 RLSFARLFYLQPKYAVLDEATSAL 559
Cdd:cd03234 151 RVSIAVQLLWDPKVLILDEPTSGL 174
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
407-577 |
3.22e-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: 54.36 E-value: 3.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 407 IKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQM----LTDFGPH-----GVLFLPQ-KPFFTDGTLRE- 475
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFdgrdITGLPPHeraraGIGYVPEgRRIFPELTVEEn 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 476 -QVSdiyplkeIYPDSGSTDDERILRFLELagLSSLVTRtegLDQQVdwnwyDVLSPGEMQRLSFARLFYLQPKYAVLDE 554
Cdd:cd03224 96 lLLG-------AYARRRAKRKARLERVYEL--FPRLKER---RKQLA-----GTLSGGEQQMLAIARALMSRPKLLLLDE 158
|
170 180
....*....|....*....|....*..
gi 1953408514 555 ATSAL----TEEVESELYRIgQQLGMT 577
Cdd:cd03224 159 PSEGLapkiVEEIFEAIREL-RDEGVT 184
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
396-598 |
3.76e-08 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 55.48 E-value: 3.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 396 PLCPPSSHKPlIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV----QMLTDFGPHG---------VLFl 462
Cdd:PRK15079 27 FWQPPKTLKA-VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVawlgKDLLGMKDDEwravrsdiqMIF- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 463 pQKPFftdGTL--REQVSDIY--PLKEIYPD-SGSTDDERILRFLELAGLsslvtrtegLDQQVdwNWY-DVLSPGEMQR 536
Cdd:PRK15079 105 -QDPL---ASLnpRMTIGEIIaePLRTYHPKlSRQEVKDRVKAMMLKVGL---------LPNLI--NRYpHEFSGGQCQR 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953408514 537 LSFARLFYLQPKYAVLDEATSALTEEVESELYRIGQQL----GMTFISVGHRHSLEKFHS-LVLKLY 598
Cdd:PRK15079 170 IGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLqremGLSLIFIAHDLAVVKHISdRVLVMY 236
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
404-559 |
4.81e-08 |
|
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: 56.46 E-value: 4.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 404 KPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLwASTQG----------SVQMLTDFGPHGVlfLPQKPFFTDGTL 473
Cdd:TIGR01271 1232 RAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGeiqidgvswnSVTLQTWRKAFGV--IPQKVFIFSGTF 1308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 474 REQVsDIYplkEIYpdsgstDDERILRFLELAGLSSLVTRTEG-LDQQVDWNWYdVLSPGEMQRLSFARLFYLQPKYAVL 552
Cdd:TIGR01271 1309 RKNL-DPY---EQW------SDEEIWKVAEEVGLKSVIEQFPDkLDFVLVDGGY-VLSNGHKQLMCLARSILSKAKILLL 1377
|
....*..
gi 1953408514 553 DEATSAL 559
Cdd:TIGR01271 1378 DEPSAHL 1384
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
403-588 |
5.72e-08 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 55.09 E-value: 5.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 403 HKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQMltdfgpHG------------VLFLPQK-PFFT 469
Cdd:PRK10851 14 RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRF------HGtdvsrlhardrkVGFVFQHyALFR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 470 DGTLREQVS---DIYPLKEiYPDSGSTDdERILRFLELAGLSSLVTRtegldqqvdwnWYDVLSPGEMQRLSFARLFYLQ 546
Cdd:PRK10851 88 HMTVFDNIAfglTVLPRRE-RPNAAAIK-AKVTQLLEMVQLAHLADR-----------YPAQLSGGQKQRVALARALAVE 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1953408514 547 PKYAVLDEATSALTEEVESELYRIGQQLG--MTFISVGHRHSLE 588
Cdd:PRK10851 155 PQILLLDEPFGALDAQVRKELRRWLRQLHeeLKFTSVFVTHDQE 198
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
406-574 |
6.30e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 53.96 E-value: 6.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 406 LIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQMltdfgPHG--VLFLPQKpFFTDGTLREQVSDIYPL 483
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKR-----NGKlrIGYVPQK-LYLDTTLPLTVNRFLRL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 484 KeiyPDSGSTDderILRFLELAGLSSLvtrtegLDQQVDwnwydVLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEV 563
Cdd:PRK09544 93 R---PGTKKED---ILPALKRVQAGHL------IDAPMQ-----KLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNG 155
|
170
....*....|.
gi 1953408514 564 ESELYRIGQQL 574
Cdd:PRK09544 156 QVALYDLIDQL 166
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
408-577 |
7.98e-08 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 54.70 E-value: 7.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 408 KDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV----QMLTDFGPH---------GVLF-----LPQKpfft 469
Cdd:COG1135 22 DDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVlvdgVDLTALSERelraarrkiGMIFqhfnlLSSR---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 470 dgTLREQVSdiYPLK-------EIypdsgstdDERILRFLELAGLSslvtrteglDQQvdWNWYDVLSPGEMQRLSFARL 542
Cdd:COG1135 98 --TVAENVA--LPLEiagvpkaEI--------RKRVAELLELVGLS---------DKA--DAYPSQLSGGQKQRVGIARA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1953408514 543 FYLQPKyaVL--DEATSAL----TEEVESELYRIGQQLGMT 577
Cdd:COG1135 155 LANNPK--VLlcDEATSALdpetTRSILDLLKDINRELGLT 193
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
400-583 |
8.06e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 54.04 E-value: 8.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 400 PSSHKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQMLTDFGphgvLFLPQKpffTDGTLREQVSD 479
Cdd:PRK13640 16 PDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDG----ITLTAK---TVWDIREKVGI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 480 IYPlkeiYPDS---GSTDDERILRFLELAGL--SSLVTRTEGLDQQVDWNWY-----DVLSPGEMQRLSFARLFYLQPKY 549
Cdd:PRK13640 89 VFQ----NPDNqfvGATVGDDVAFGLENRAVprPEMIKIVRDVLADVGMLDYidsepANLSGGQKQRVAIAGILAVEPKI 164
|
170 180 190
....*....|....*....|....*....|....*...
gi 1953408514 550 AVLDEATSALTEEVESELYRIGQQL----GMTFISVGH 583
Cdd:PRK13640 165 IILDESTSMLDPAGKEQILKLIRKLkkknNLTVISITH 202
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
150-568 |
8.30e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 55.75 E-value: 8.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 150 VERFCRQLSSMASkliiSPFTLIYYTYQCFQStgwLGPMSIFGYFILGTLVnkTLMGPIVAKLVQQEKLEGDFRFKHMQI 229
Cdd:PLN03232 411 LQQIAEQLHGLWS----APFRIIVSMVLLYQQ---LGVASLFGSLILFLLI--PLQTLIVRKMRKLTKEGLQWTDKRVGI 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 230 RVNAESAAFFRAGHVEHQRTDRRLQRLLQTQRELMSKELWLYiGVNTFdYLGSILSYV-VIAIPIFSGVYGDLSPTElst 308
Cdd:PLN03232 482 INEILASMDTVKCYAWEKSFESRIQGIRNEELSWFRKAQLLS-AFNSF-ILNSIPVVVtLVSFGVFVLLGGDLTPAR--- 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 309 lvsknAFVCIYLISCF-TRLIDLSSTLSDVAGYTHRIGELQETLLDMSlklrggggEILDEsewNMDRAPGWPAAEPADT 387
Cdd:PLN03232 557 -----AFTSLSLFAVLrSPLNMLPNLLSQVVNANVSLQRIEELLLSEE--------RILAQ---NPPLQPGAPAISIKNG 620
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 388 AFLSSSgsplcppSSHKPLIKDLSLKISEGQSLLITGNTGTGKSSLLR-VLGGLWASTQGSVQMLTDfgphgVLFLPQKP 466
Cdd:PLN03232 621 YFSWDS-------KTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRGS-----VAYVPQVS 688
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 467 FFTDGTLREQV---SDIYPlkeiypdsgstddERILRFLELAGLSSLVTRTEGLDQQVDWNWYDVLSPGEMQRLSFARLF 543
Cdd:PLN03232 689 WIFNATVRENIlfgSDFES-------------ERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAV 755
|
410 420
....*....|....*....|....*
gi 1953408514 544 YLQPKYAVLDEATSALTEEVESELY 568
Cdd:PLN03232 756 YSNSDIYIFDDPLSALDAHVAHQVF 780
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
405-568 |
9.21e-08 |
|
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: 54.09 E-value: 9.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 405 PLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQmltdfgpHG--VLFLPQKPFFTDGTLREQVsdIYP 482
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK-------HSgrISFSSQFSWIMPGTIKENI--IFG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 483 LkeiypdsgSTDDERILRFLELAGLSSLVTRTEGLDQQVDWNWYDVLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEE 562
Cdd:cd03291 122 V--------SYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVF 193
|
....*.
gi 1953408514 563 VESELY 568
Cdd:cd03291 194 TEKEIF 199
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
404-583 |
9.49e-08 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 54.46 E-value: 9.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 404 KPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV----QMLTDFGPHgvlflpQKP---------FFTD 470
Cdd:PRK11607 32 QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQImldgVDLSHVPPY------QRPinmmfqsyaLFPH 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 471 GTLREQVS-----DIYPLKEIypdsgstdDERILRFLELAGLSSLVTRTEgldQQvdwnwydvLSPGEMQRLSFARLFYL 545
Cdd:PRK11607 106 MTVEQNIAfglkqDKLPKAEI--------ASRVNEMLGLVHMQEFAKRKP---HQ--------LSGGQRQRVALARSLAK 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1953408514 546 QPKYAVLDEATSALT----EEVESELYRIGQQLGMTFISVGH 583
Cdd:PRK11607 167 RPKLLLLDEPMGALDkklrDRMQLEVVDILERVGVTCVMVTH 208
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
406-559 |
1.07e-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: 52.50 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 406 LIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQM-------LTDFGPHGVLFLPQKPfftdgTLREQVS 478
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLnggpldfQRDSIARGLLYLGHAP-----GIKTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 479 DIYPLKEIYPDSGstdDERILRFLELAGLSSLVTRTEGldqqvdwnwydVLSPGEMQRLSFARLFYLQPKYAVLDEATSA 558
Cdd:cd03231 90 VLENLRFWHADHS---DEQVEEALARVGLNGFEDRPVA-----------QLSAGQQRRVALARLLLSGRPLWILDEPTTA 155
|
.
gi 1953408514 559 L 559
Cdd:cd03231 156 L 156
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
406-559 |
1.12e-07 |
|
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: 53.70 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 406 LIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLwASTQGSVQM-------------LTDFGphgvlFLPQKPFFTDGT 472
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQIdgvswnsvplqkwRKAFG-----VIPQKVFIFSGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 473 LREQVsDIYplkeiypdsGSTDDERILRFLELAGLSSLVTRTEG-LDQQVDWNWYdVLSPGEMQRLSFARLFYLQPKYAV 551
Cdd:cd03289 93 FRKNL-DPY---------GKWSDEEIWKVAEEVGLKSVIEQFPGqLDFVLVDGGC-VLSHGHKQLMCLARSVLSKAKILL 161
|
....*...
gi 1953408514 552 LDEATSAL 559
Cdd:cd03289 162 LDEPSAHL 169
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
404-559 |
2.00e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 54.08 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 404 KPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGlWASTQGSVQM----LTDFGP----HGVLFLPQKPFFTDGTLRE 475
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLG-FLPYQGSLKIngieLRELDPeswrKHLSWVGQNPQLPHGTLRD 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 476 QVSdiyplkeiyPDSGSTDDERILRFLELAGLSSLVTR-TEGLDQQV-DWNwyDVLSPGEMQRLSFARLFYLQPKYAVLD 553
Cdd:PRK11174 442 NVL---------LGNPDASDEQLQQALENAWVSEFLPLlPQGLDTPIgDQA--AGLSVGQAQRLALARALLQPCQLLLLD 510
|
....*.
gi 1953408514 554 EATSAL 559
Cdd:PRK11174 511 EPTASL 516
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
409-583 |
2.90e-07 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 51.94 E-value: 2.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 409 DLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQMLT---DFGphgvlflpQKPFFTDG-TLREQVSDIYPLK 484
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfDFS--------KTPSDKAIrELRRNVGMVFQQY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 485 EIYPD--------------SGSTDDERILRFLELagLSSLvtrteGLDQQVDwNWYDVLSPGEMQRLSFARLFYLQPKYA 550
Cdd:PRK11124 92 NLWPHltvqqnlieapcrvLGLSKDQALARAEKL--LERL-----RLKPYAD-RFPLHLSGGQQQRVAIARALMMEPQVL 163
|
170 180 190
....*....|....*....|....*....|....*.
gi 1953408514 551 VLDEATSALTEEVESELYRIGQQL---GMTFISVGH 583
Cdd:PRK11124 164 LFDEPTAALDPEITAQIVSIIRELaetGITQVIVTH 199
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
384-586 |
3.12e-07 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 53.18 E-value: 3.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 384 PADTAFLSSSGSPLCPPSSHKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV----QMLTDFGPHG- 458
Cdd:PRK10789 308 PEGRGELDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIrfhdIPLTKLQLDSw 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 459 ---VLFLPQKPF-FTDgtlreQVSDIYPLKEiyPDSGSTDDERILRfleLAGLSSLVTR-TEGLDQQVDWNWYdVLSPGE 533
Cdd:PRK10789 388 rsrLAVVSQTPFlFSD-----TVANNIALGR--PDATQQEIEHVAR---LASVHDDILRlPQGYDTEVGERGV-MLSGGQ 456
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1953408514 534 MQRLSFARLFYLQPKYAVLDEATSAL---TE-EVESELYRIGQqlGMTFISVGHRHS 586
Cdd:PRK10789 457 KQRISIARALLLNAEILILDDALSAVdgrTEhQILHNLRQWGE--GRTVIISAHRLS 511
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
377-558 |
3.30e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 53.59 E-value: 3.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 377 PGWPAAEPADTAFLSSSGSPLCPPSSHkplikDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQM------ 450
Cdd:PLN03130 1230 PGWPSSGSIKFEDVVLRYRPELPPVLH-----GLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIdgcdis 1304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 451 ---LTDFgpHGVL-FLPQKPFFTDGTLReqvSDIYPLKEiypdsgsTDDERILRFLELAGLSSLVTR-TEGLDQQVDwNW 525
Cdd:PLN03130 1305 kfgLMDL--RKVLgIIPQAPVLFSGTVR---FNLDPFNE-------HNDADLWESLERAHLKDVIRRnSLGLDAEVS-EA 1371
|
170 180 190
....*....|....*....|....*....|...
gi 1953408514 526 YDVLSPGEMQRLSFARLFYLQPKYAVLDEATSA 558
Cdd:PLN03130 1372 GENFSVGQRQLLSLARALLRRSKILVLDEATAA 1404
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
407-583 |
4.99e-07 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 52.00 E-value: 4.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 407 IKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV----QMLTDFGPH--GVLFLPQK----PFFtdgTLREQ 476
Cdd:COG3839 19 LKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEIliggRDVTDLPPKdrNIAMVFQSyalyPHM---TVYEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 477 VSdiYPLK-------EIypdsgstdDERILRFLELAGLSSLvtrtegLDQ---QvdwnwydvLSPGEMQRLSFARLFYLQ 546
Cdd:COG3839 96 IA--FPLKlrkvpkaEI--------DRRVREAAELLGLEDL------LDRkpkQ--------LSGGQRQRVALGRALVRE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1953408514 547 PKYAVLDEATS----ALTEEVESELYRIGQQLGMTFISVGH 583
Cdd:COG3839 152 PKVFLLDEPLSnldaKLRVEMRAEIKRLHRRLGTTTIYVTH 192
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
404-567 |
6.18e-07 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 52.27 E-value: 6.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 404 KPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQM----LTDFGPH------GVLFlpQKPFFTDGTL 473
Cdd:PRK13657 348 RQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIdgtdIRTVTRAslrrniAVVF--QDAGLFNRSI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 474 REQVSdiyplkeiypdSGSTD--DERILRFLELAGLSSLVTRTE-GLDQQVDWNWyDVLSPGEMQRLSFARLFYLQPKYA 550
Cdd:PRK13657 426 EDNIR-----------VGRPDatDEEMRAAAERAQAHDFIERKPdGYDTVVGERG-RQLSGGERQRLAIARALLKDPPIL 493
|
170
....*....|....*..
gi 1953408514 551 VLDEATSALTEEVESEL 567
Cdd:PRK13657 494 ILDEATSALDVETEAKV 510
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
403-559 |
6.32e-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: 50.27 E-value: 6.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 403 HKPLIKDLSLKISEGQSLLItGNTGTGKSSLLRVLGGLWASTQGSVQML------TDFGPHGVL-FLPQKP-FFTDGTLR 474
Cdd:cd03264 12 KKRALDGVSLTLGPGMYGLL-GPNGAGKTTLMRILATLTPPSSGTIRIDgqdvlkQPQKLRRRIgYLPQEFgVYPNFTVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 475 EQVSDIYPLKEIypdSGSTDDERILRFLELAGLSSLVTRTEGldqqvdwnwydVLSPGEMQRLSFARLFYLQPKYAVLDE 554
Cdd:cd03264 91 EFLDYIAWLKGI---PSKEVKARVDEVLELVNLGDRAKKKIG-----------SLSGGMRRRVGIAQALVGDPSILIVDE 156
|
....*
gi 1953408514 555 ATSAL 559
Cdd:cd03264 157 PTAGL 161
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
406-583 |
8.30e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 50.61 E-value: 8.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 406 LIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLW-----ASTQGSVQMltdFGPHgvLFLPQ-KPFftdgTLREQVSD 479
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLelneeARVEGEVRL---FGRN--IYSPDvDPI----EVRREVGM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 480 IYPLKEIYPDSGSTDDERIlrfleLAGLSSLVTRTEGLDQQVDWN------WYDV----------LSPGEMQRLSFARLF 543
Cdd:PRK14267 90 VFQYPNPFPHLTIYDNVAI-----GVKLNGLVKSKKELDERVEWAlkkaalWDEVkdrlndypsnLSGGQRQRLVIARAL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1953408514 544 YLQPKYAVLDEATSAL----TEEVESELYRIGQQLgmTFISVGH 583
Cdd:PRK14267 165 AMKPKILLMDEPTANIdpvgTAKIEELLFELKKEY--TIVLVTH 206
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
404-580 |
8.38e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 50.82 E-value: 8.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 404 KPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQMltdfgPHGVLFLPQKPFFTDG-TLREQVSDIYP 482
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKV-----DGKVLYFGKDIFQIDAiKLRKEVGMVFQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 483 LKEIYPDSGSTDD-------ERILRFLELAGLSSLVTRTEGLDQQVdwnwYD-------VLSPGEMQRLSFARLFYLQPK 548
Cdd:PRK14246 98 QPNPFPHLSIYDNiayplksHGIKEKREIKKIVEECLRKVGLWKEV----YDrlnspasQLSGGQQQRLTIARALALKPK 173
|
170 180 190
....*....|....*....|....*....|....*.
gi 1953408514 549 YAVLDEATSAL----TEEVESELYRIGQQLGMTFIS 580
Cdd:PRK14246 174 VLLMDEPTSMIdivnSQAIEKLITELKNEIAIVIVS 209
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
400-589 |
1.00e-06 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 51.56 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 400 PSSHKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQM----LTDfgphgvlflpqkpfFTDGTLRE 475
Cdd:PRK11176 352 PGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLdghdLRD--------------YTLASLRN 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 476 QVSDI----------------YPLKEIYpdsgstDDERILRFLELAGLSSLVTRTE-GLDQQVDWNWYdVLSPGEMQRLS 538
Cdd:PRK11176 418 QVALVsqnvhlfndtianniaYARTEQY------SREQIEEAARMAYAMDFINKMDnGLDTVIGENGV-LLSGGQRQRIA 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1953408514 539 FARLFYLQPKYAVLDEATSALteEVESElyRIGQ------QLGMTFISVGHRHS-LEK 589
Cdd:PRK11176 491 IARALLRDSPILILDEATSAL--DTESE--RAIQaaldelQKNRTSLVIAHRLStIEK 544
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
404-586 |
1.08e-06 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 51.64 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 404 KPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQMltDFGP-----HGVL-----FLPQKP------F 467
Cdd:PRK10790 354 NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRL--DGRPlsslsHSVLrqgvaMVQQDPvvladtF 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 468 FTDGTLREQVSdiyplkeiypdsgstdDERILRFLELAGLSSLV-TRTEGLDQQVDwNWYDVLSPGEMQRLSFARLFYLQ 546
Cdd:PRK10790 432 LANVTLGRDIS----------------EEQVWQALETVQLAELArSLPDGLYTPLG-EQGNNLSVGQKQLLALARVLVQT 494
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1953408514 547 PKYAVLDEATSAL---TEE-VESELYRIGQQlgMTFISVGHRHS 586
Cdd:PRK10790 495 PQILILDEATANIdsgTEQaIQQALAAVREH--TTLVVIAHRLS 536
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
404-580 |
1.21e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 50.39 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 404 KPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV---QMLTDFGPHGVLflpqkpfftdgTLREQVSDI 480
Cdd:PRK13638 14 EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVlwqGKPLDYSKRGLL-----------ALRQQVATV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 481 Y--PLKEIYPDSGSTDDERILRFLELAGlSSLVTRTEGLDQQVDWNWY-----DVLSPGEMQRLSFARLFYLQPKYAVLD 553
Cdd:PRK13638 83 FqdPEQQIFYTDIDSDIAFSLRNLGVPE-AEITRRVDEALTLVDAQHFrhqpiQCLSHGQKKRVAIAGALVLQARYLLLD 161
|
170 180 190
....*....|....*....|....*....|.
gi 1953408514 554 EATSALTEEVESELY----RIGQQLGMTFIS 580
Cdd:PRK13638 162 EPTAGLDPAGRTQMIaiirRIVAQGNHVIIS 192
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
146-568 |
1.63e-06 |
|
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: 51.48 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 146 ISQDVERFcRQLSSMASKLIISPFTLIYYTYQCFQStgwLGPMSIFG--YFILGTLVNKTLMGPIVAKLVQQEKLEgDFR 223
Cdd:TIGR00957 421 MSVDAQRF-MDLATYINMIWSAPLQVILALYFLWLN---LGPSVLAGvaVMVLMVPLNAVMAMKTKTYQVAHMKSK-DNR 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 224 FKHMQIRVNAESAAFFRAGHVEHQRtdrRLQRLLQTQRELMSKELWLYiGVNTFDYLGSILSYVVIAIPIFsgVYGDlsp 303
Cdd:TIGR00957 496 IKLMNEILNGIKVLKLYAWELAFLD---KVEGIRQEELKVLKKSAYLH-AVGTFTWVCTPFLVALITFAVY--VTVD--- 566
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 304 tELSTLVSKNAFVCIYLISCF----TRLIDLSSTLSDVAGYTHRIGEL--QETLLDMSLKLR----GGGGEILDESEwnm 373
Cdd:TIGR00957 567 -ENNILDAEKAFVSLALFNILrfplNILPMVISSIVQASVSLKRLRIFlsHEELEPDSIERRtikpGEGNSITVHNA--- 642
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 374 drAPGWPAAEPadtaflsssgsplcppsshkPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQMltd 453
Cdd:TIGR00957 643 --TFTWARDLP--------------------PTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHM--- 697
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 454 fgPHGVLFLPQKPFFTDGTLREQVSDIYPLKEIYPDSgSTDDERILRFLELagLSSlVTRTEGLDQQVDwnwydvLSPGE 533
Cdd:TIGR00957 698 --KGSVAYVPQQAWIQNDSLRENILFGKALNEKYYQQ-VLEACALLPDLEI--LPS-GDRTEIGEKGVN------LSGGQ 765
|
410 420 430
....*....|....*....|....*....|....*
gi 1953408514 534 MQRLSFARLFYLQPKYAVLDEATSALTEEVESELY 568
Cdd:TIGR00957 766 KQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIF 800
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
404-583 |
2.07e-06 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 49.63 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 404 KPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV----QMLTDFGP----HGVLFLPQKPFFTDG-TLR 474
Cdd:PRK11231 15 KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVflgdKPISMLSSrqlaRRLALLPQHHLTPEGiTVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 475 EQVSdiY---PLKEIYPDSGSTDDERILRFLELAGLSSLVtrteglDQQVdwnwyDVLSPGEMQRLSFARLFYLQPKYAV 551
Cdd:PRK11231 95 ELVA--YgrsPWLSLWGRLSAEDNARVNQAMEQTRINHLA------DRRL-----TDLSGGQRQRAFLAMVLAQDTPVVL 161
|
170 180 190
....*....|....*....|....*....|....*
gi 1953408514 552 LDEATSALTEEVESELYRIGQQL---GMTFISVGH 583
Cdd:PRK11231 162 LDEPTTYLDINHQVELMRLMRELntqGKTVVTVLH 196
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
408-583 |
2.11e-06 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 50.41 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 408 KDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV----QMLTDFGPH----GVLFlpqkpfftdgtlreQVSD 479
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLfigeKRMNDVPPAergvGMVF--------------QSYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 480 IYP-----------LKEIYPDSGSTDD--ERILRFLELAGLsslvtrtegLDQQVdwnwyDVLSPGEMQRLSFARLFYLQ 546
Cdd:PRK11000 86 LYPhlsvaenmsfgLKLAGAKKEEINQrvNQVAEVLQLAHL---------LDRKP-----KALSGGQRQRVAIGRTLVAE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1953408514 547 PKYAVLDEATS----ALTEEVESELYRIGQQLGMTFISVGH 583
Cdd:PRK11000 152 PSVFLLDEPLSnldaALRVQMRIEISRLHKRLGRTMIYVTH 192
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
403-558 |
2.42e-06 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 49.07 E-value: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 403 HKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQM------LTDFGpHGvlFLPqkpfftDGTLREq 476
Cdd:cd03220 34 EFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVrgrvssLLGLG-GG--FNP------ELTGRE- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 477 vsDIYPLKEIYPDSGSTDDERILRFLELAGLsslvtrTEGLDQQVdwnwyDVLSPGEMQRLSFARLFYLQPKYAVLDEAT 556
Cdd:cd03220 104 --NIYLNGRLLGLSRKEIDEKIDEIIEFSEL------GDFIDLPV-----KTYSSGMKARLAFAIATALEPDILLIDEVL 170
|
..
gi 1953408514 557 SA 558
Cdd:cd03220 171 AV 172
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
404-601 |
2.83e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 50.32 E-value: 2.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 404 KPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQMLTDFgphGVLFLPQKPFFTDG-TLREQVSD--- 479
Cdd:TIGR03719 18 KEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGI---KVGYLPQEPQLDPTkTVRENVEEgva 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 480 -----IYPLKEIYPDSGSTDDERILRFLELAGLSSLVTRTEG--LDQQVD----------WNWyDV--LSPGEMQRLSFA 540
Cdd:TIGR03719 95 eikdaLDRFNEISAKYAEPDADFDKLAAEQAELQEIIDAADAwdLDSQLEiamdalrcppWDA-DVtkLSGGERRRVALC 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953408514 541 RLFYLQPKYAVLDEATSALTEEVESELYRIGQQLGMTFISVGH-RHSLEKFHSLVLKL-YGEG 601
Cdd:TIGR03719 174 RLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHdRYFLDNVAGWILELdRGRG 236
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
403-589 |
3.42e-06 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 48.66 E-value: 3.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 403 HKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSvqmltdfgphgVLF----LPQKPFFTDGTLR-EQV 477
Cdd:PRK11629 21 QTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGD-----------VIFngqpMSKLSSAAKAELRnQKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 478 SDIYPLKEIYPD-------------SGSTDDERILRFLELAGLSSLVTRTEGLDQQvdwnwydvLSPGEMQRLSFARLFY 544
Cdd:PRK11629 90 GFIYQFHHLLPDftalenvamplliGKKKPAEINSRALEMLAAVGLEHRANHRPSE--------LSGGERQRVAIARALV 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1953408514 545 LQPKYAVLDEATSALTEEVESELYRIGQQL----GMTFISVGHRHSLEK 589
Cdd:PRK11629 162 NNPRLVLADEPTGNLDARNADSIFQLLGELnrlqGTAFLVVTHDLQLAK 210
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
408-577 |
3.50e-06 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 49.41 E-value: 3.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 408 KDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV----QMLTDFGPH---------GVLF-----LPQKpfft 469
Cdd:PRK11153 22 NNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVlvdgQDLTALSEKelrkarrqiGMIFqhfnlLSSR---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 470 dgTLREQVSdiYPLK-------EIypdsgstdDERILRFLELAGLSSLVTRtegldqqvdwnwYDV-LSPGEMQRLSFAR 541
Cdd:PRK11153 98 --TVFDNVA--LPLElagtpkaEI--------KARVTELLELVGLSDKADR------------YPAqLSGGQKQRVAIAR 153
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1953408514 542 LFYLQPKyaVL--DEATSAL----TEEVESELYRIGQQLGMT 577
Cdd:PRK11153 154 ALASNPK--VLlcDEATSALdpatTRSILELLKDINRELGLT 193
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
405-586 |
4.31e-06 |
|
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: 49.95 E-value: 4.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 405 PLI-KDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV----QMLTDFGPH------GVLFlpQKPFFTDGTL 473
Cdd:TIGR03797 466 PLIlDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVfydgQDLAGLDVQavrrqlGVVL--QNGRLMSGSI 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 474 REQVSDIYPLkeiypdsgsTDDErILRFLELAGLSSLVTR---------TEGLDQqvdwnwydvLSPGEMQRLSFARLFY 544
Cdd:TIGR03797 544 FENIAGGAPL---------TLDE-AWEAARMAGLAEDIRAmpmgmhtviSEGGGT---------LSGGQRQRLLIARALV 604
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1953408514 545 LQPKYAVLDEATSAL---TEEVESELYrigQQLGMTFISVGHRHS 586
Cdd:TIGR03797 605 RKPRILLFDEATSALdnrTQAIVSESL---ERLKVTRIVIAHRLS 646
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
407-601 |
6.30e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 48.21 E-value: 6.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 407 IKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV---------QMLTDFGPH-GVLFL-PQKPFFtdgtlre 475
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqaitdDNFEKLRKHiGIVFQnPDNQFV------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 476 qvsdiyplkeiypdsGStdderILRFLELAGLSSLVTRTEGLDQQVDWNWYDV------------LSPGEMQRLSFARLF 543
Cdd:PRK13648 98 ---------------GS-----IVKYDVAFGLENHAVPYDEMHRRVSEALKQVdmleradyepnaLSGGQKQRVAIAGVL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953408514 544 YLQPKYAVLDEATSALTEEVESELYRIGQQL----GMTFISVGH--RHSLEKFHSLVL---KLYGEG 601
Cdd:PRK13648 158 ALNPSVIILDEATSMLDPDARQNLLDLVRKVksehNITIISITHdlSEAMEADHVIVMnkgTVYKEG 224
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
404-559 |
7.00e-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: 47.71 E-value: 7.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 404 KPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQMLtDFGPH----------GVLFLPQKPFFTDGTL 473
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVA-GLVPWkrrkkflrriGVVFGQKTQLWWDLPV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 474 REQvsdIYPLKEIYpdsgSTDDERILRflELAGLSSLVTRTEGLDQQVdwnwyDVLSPGEMQRLSFARLFYLQPKYAVLD 553
Cdd:cd03267 113 IDS---FYLLAAIY----DLPPARFKK--RLDELSELLDLEELLDTPV-----RQLSLGQRMRAEIAAALLHEPEILFLD 178
|
....*.
gi 1953408514 554 EATSAL 559
Cdd:cd03267 179 EPTIGL 184
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
411-580 |
7.15e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 48.42 E-value: 7.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 411 SLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV----QMLTDFGPHGVLFLPQK-------PFftdGTL--REQV 477
Cdd:PRK11308 35 SFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELyyqgQDLLKADPEAQKLLRQKiqivfqnPY---GSLnpRKKV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 478 SDIY--PLKEIYPDSGSTDDERILRFLELAGLsslvtRTEgldqqvdwnWYD----VLSPGEMQRLSFARLFYLQPKYAV 551
Cdd:PRK11308 112 GQILeePLLINTSLSAAERREKALAMMAKVGL-----RPE---------HYDryphMFSGGQRQRIAIARALMLDPDVVV 177
|
170 180 190
....*....|....*....|....*....|....*
gi 1953408514 552 LDEATSALTEEVESE----LYRIGQQLGMT--FIS 580
Cdd:PRK11308 178 ADEPVSALDVSVQAQvlnlMMDLQQELGLSyvFIS 212
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
364-563 |
8.89e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 49.01 E-value: 8.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 364 EILDESEWNMDRAPGWPAAEPA-DTAFLSSSGSPLCPPSSH--------KPLIKDLSLKISEGQSLLITGNTGTGKSSLL 434
Cdd:PTZ00243 624 EDTDYGSPSSASRHIVEGGTGGgHEATPTSERSAKTPKMKTddffelepKVLLRDVSVSVPRGKLTVVLGATGSGKSTLL 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 435 RVLGGLWASTQGSVqmltdFGPHGVLFLPQKPFFTDGTLReqvSDIYPLKEiypdsgsTDDERI---LRFLEL-AGLSSL 510
Cdd:PTZ00243 704 QSLLSQFEISEGRV-----WAERSIAYVPQQAWIMNATVR---GNILFFDE-------EDAARLadaVRVSQLeADLAQL 768
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1953408514 511 VT--RTEGLDQQVDwnwydvLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEV 563
Cdd:PTZ00243 769 GGglETEIGEKGVN------LSGGQKARVSLARAVYANRDVYLLDDPLSALDAHV 817
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
408-584 |
9.64e-06 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 45.88 E-value: 9.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 408 KDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQMltdfgphgvlflpqkpfftDGtlreqvsdiyplKEIY 487
Cdd:cd03216 17 DGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILV-------------------DG------------KEVS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 488 PDSgSTDDERilrflelAGLSsLVTrtegldqQvdwnwydvLSPGEMQRLSFARLFYLQPKYAVLDEATSALT-EEVEsE 566
Cdd:cd03216 66 FAS-PRDARR-------AGIA-MVY-------Q--------LSVGERQMVEIARALARNARLLILDEPTAALTpAEVE-R 120
|
170 180
....*....|....*....|.
gi 1953408514 567 LYRIGQQL---GMTFISVGHR 584
Cdd:cd03216 121 LFKVIRRLraqGVAVIFISHR 141
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
403-559 |
1.24e-05 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 46.34 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 403 HKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV---------------QMLTDFGPH-GVlflpqKP 466
Cdd:PRK13538 13 ERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVlwqgepirrqrdeyhQDLLYLGHQpGI-----KT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 467 fftDGTLREQvsdiypLKEIYPDSGSTDDERILRFLELAGLSslvtRTEgldqqvdwnwyDV----LSPGEMQRLSFARL 542
Cdd:PRK13538 88 ---ELTALEN------LRFYQRLHGPGDDEALWEALAQVGLA----GFE-----------DVpvrqLSAGQQRRVALARL 143
|
170
....*....|....*..
gi 1953408514 543 FYLQPKYAVLDEATSAL 559
Cdd:PRK13538 144 WLTRAPLWILDEPFTAI 160
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
408-559 |
1.26e-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: 48.14 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 408 KDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLwASTQGSVQM----LTDFGPHG---------VLFlpQKPFftdGTL- 473
Cdd:COG4172 303 DGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFdgqdLDGLSRRAlrplrrrmqVVF--QDPF---GSLs 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 474 -REQVSDIY--PLKEIYPD-SGSTDDERILRFLELAGLS-SLVTR--TEgldqqvdwnwydvLSPGEMQRLSFARLFYLQ 546
Cdd:COG4172 377 pRMTVGQIIaeGLRVHGPGlSAAERRARVAEALEEVGLDpAARHRypHE-------------FSGGQRQRIAIARALILE 443
|
170
....*....|...
gi 1953408514 547 PKYAVLDEATSAL 559
Cdd:COG4172 444 PKLLVLDEPTSAL 456
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
404-554 |
1.36e-05 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 46.77 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 404 KPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV----QMLTDFGPH-----GVLFLPQKP-FFTDGTL 473
Cdd:cd03218 13 RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKIlldgQDITKLPMHkrarlGIGYLPQEAsIFRKLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 474 REqvsDIYPLKEIYPDSGSTDDERILRFLELAGLSSLvtrtegLDQQVDwnwydVLSPGEMQRLSFARLFYLQPKYAVLD 553
Cdd:cd03218 93 EE---NILAVLEIRGLSKKEREEKLEELLEEFHITHL------RKSKAS-----SLSGGERRRVEIARALATNPKFLLLD 158
|
.
gi 1953408514 554 E 554
Cdd:cd03218 159 E 159
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
405-584 |
1.51e-05 |
|
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: 46.56 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 405 PLIKDLSLKISEGQSLLITGNTGTGKSS-LLRVLGGL--------WASTQGSVQMLTDFGP---HGVLFLPQKPFFTDGT 472
Cdd:cd03290 15 ATLSNINIRIPTGQLTMIVGQVGCGKSSlLLAILGEMqtlegkvhWSNKNESEPSFEATRSrnrYSVAYAAQKPWLLNAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 473 LREQVSDIYPL-KEIYP---DSGSTD-DERILRFLElaglsslvtRTEGLDQQVDwnwydvLSPGEMQRLSFARLFYLQP 547
Cdd:cd03290 95 VEENITFGSPFnKQRYKavtDACSLQpDIDLLPFGD---------QTEIGERGIN------LSGGQRQRICVARALYQNT 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1953408514 548 KYAVLDEATSALTEEVESELYRIG-----QQLGMTFISVGHR 584
Cdd:cd03290 160 NIVFLDDPFSALDIHLSDHLMQEGilkflQDDKRTLVLVTHK 201
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
403-593 |
2.18e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 47.39 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 403 HKPLIKDLSLKISEGQSLLITGNTGTGKSS----LLRVL---GGLWASTQ-----GSVQMLTDFGPHGVLFlpQKPfftD 470
Cdd:PRK15134 298 HNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLInsqGEIWFDGQplhnlNRRQLLPVRHRIQVVF--QDP---N 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 471 GTL--REQVSDIYP--LKEIYPD-SGSTDDERILRFLELAGLsslvtrteglDQQVDWNWYDVLSPGEMQRLSFARLFYL 545
Cdd:PRK15134 373 SSLnpRLNVLQIIEegLRVHQPTlSAAQREQQVIAVMEEVGL----------DPETRHRYPAEFSGGQRQRIAIARALIL 442
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1953408514 546 QPKYAVLDEATSALTEEVESE---LYRIGQQ---LGMTFISvghrHSLEKFHSL 593
Cdd:PRK15134 443 KPSLIILDEPTSSLDKTVQAQilaLLKSLQQkhqLAYLFIS----HDLHVVRAL 492
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
407-583 |
2.75e-05 |
|
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: 45.82 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 407 IKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSvqmLTDFGpHGVL-----------FLPQKPFFTDG-TLR 474
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGR---ATVAG-HDVVreprevrrrigIVFQDLSVDDElTGW 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 475 EQVsdiYPLKEIYPDSGSTDDERILRFLELAGLsslvtrTEGLDQQVdwnwyDVLSPGEMQRLSFARLFYLQPKYAVLDE 554
Cdd:cd03265 92 ENL---YIHARLYGVPGAERRERIDELLDFVGL------LEAADRLV-----KTYSGGMRRRLEIARSLVHRPEVLFLDE 157
|
170 180 190
....*....|....*....|....*....|...
gi 1953408514 555 ATSALTEEVESELYRIGQQL----GMTFISVGH 583
Cdd:cd03265 158 PTIGLDPQTRAHVWEYIEKLkeefGMTILLTTH 190
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
407-559 |
2.78e-05 |
|
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: 45.35 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 407 IKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQM----LTDFGPHGVLFLPQ-KPFFTDGTLREQVsdIY 481
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFdgkpLDIAARNRIGYLPEeRGLYPKMKVIDQL--VY 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953408514 482 pLKEIYPDSGSTDDERILRFLELAGLSSLvtRTEGLDQqvdwnwydvLSPGEMQRLSFARLFYLQPKYAVLDEATSAL 559
Cdd:cd03269 94 -LAQLKGLKKEEARRRIDEWLERLELSEY--ANKRVEE---------LSKGNQQKVQFIAAVIHDPELLILDEPFSGL 159
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
404-556 |
2.79e-05 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 46.98 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 404 KPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVqmltDFGPHGVL-FLPQ--KPFFTDGTLREQVSDI 480
Cdd:COG0488 328 KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV----KLGETVKIgYFDQhqEELDPDKTVLDELRDG 403
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953408514 481 YPlkeiypdsgsTDDERILR-FLELAGLSSlvtrtEGLDQQVdwnwyDVLSPGEMQRLSFARLFYLQPKYAVLDEAT 556
Cdd:COG0488 404 AP----------GGTEQEVRgYLGRFLFSG-----DDAFKPV-----GVLSGGEKARLALAKLLLSPPNVLLLDEPT 460
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
404-583 |
2.82e-05 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 46.13 E-value: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 404 KPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV----QMLTDFGPHGV-----LFLPQKPFFTDGTLR 474
Cdd:PRK10253 20 YTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVwldgEHIQHYASKEVarrigLLAQNATTPGDITVQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 475 EQVS-DIYPLKEIYPDSGSTDDERILRFLELAGLSSLVtrteglDQQVdwnwyDVLSPGEMQRLSFARLFYLQPKYAVLD 553
Cdd:PRK10253 100 ELVArGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLA------DQSV-----DTLSGGQRQRAWIAMVLAQETAIMLLD 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 1953408514 554 EATSALT-------EEVESELYRigqQLGMTFISVGH 583
Cdd:PRK10253 169 EPTTWLDishqidlLELLSELNR---EKGYTLAAVLH 202
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
417-602 |
3.00e-05 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 45.64 E-value: 3.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 417 GQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQmltdFGPHGVLFLPQK--PFftdgtLREQVSDIYPLKEIYPDSGSTD 494
Cdd:PRK10908 28 GEMAFLTGHSGAGKSTLLKLICGIERPSAGKIW----FSGHDITRLKNRevPF-----LRRQIGMIFQDHHLLMDRTVYD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 495 DERILRFLELAGLSSLVTRTEGLDQQVDW-----NWYDVLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEVESELYR 569
Cdd:PRK10908 99 NVAIPLIIAGASGDDIRRRVSAALDKVGLldkakNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILR 178
|
170 180 190
....*....|....*....|....*....|....*.
gi 1953408514 570 IGQQ---LGMTFISVGHRHSLEKFHSLVLKLYGEGR 602
Cdd:PRK10908 179 LFEEfnrVGVTVLMATHDIGLISRRSYRMLTLSDGH 214
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
409-603 |
4.14e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 46.26 E-value: 4.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 409 DLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQML---TDFGP------HGVLFLPQKpffTDGTLREQVSD 479
Cdd:PRK10982 16 NVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQgkeIDFKSskealeNGISMVHQE---LNLVLQRSVMD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 480 -----IYPLKEIYPDSGSTDDERILRFLELaglsslvtrteglDQQVDWN-WYDVLSPGEMQRLSFARLFYLQPKYAVLD 553
Cdd:PRK10982 93 nmwlgRYPTKGMFVDQDKMYRDTKAIFDEL-------------DIDIDPRaKVATLSVSQMQMIEIAKAFSYNAKIVIMD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1953408514 554 EATSALTEEVESELYRIGQQL-----GMTFISvghrHSLEKFHSLV--LKLYGEGRW 603
Cdd:PRK10982 160 EPTSSLTEKEVNHLFTIIRKLkergcGIVYIS----HKMEEIFQLCdeITILRDGQW 212
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
407-583 |
5.83e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 46.00 E-value: 5.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 407 IKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQmltdFGPHGVLFLPqkpfftDGTLREQVSDIyplKEI 486
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEII----FNGQRIDTLS------PGKLQALRRDI---QFI 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 487 YPDSGSTDDER------ILRFLELAGL----------SSLVTRTeGLDQQVDWNWYDVLSPGEMQRLSFARLFYLQPKYA 550
Cdd:PRK10261 407 FQDPYASLDPRqtvgdsIMEPLRVHGLlpgkaaaarvAWLLERV-GLLPEHAWRYPHEFSGGQRQRICIARALALNPKVI 485
|
170 180 190
....*....|....*....|....*....|....*..
gi 1953408514 551 VLDEATSALTEEVESE----LYRIGQQLGMTFISVGH 583
Cdd:PRK10261 486 IADEAVSALDVSIRGQiinlLLDLQRDFGIAYLFISH 522
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
408-449 |
6.91e-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: 6.91e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1953408514 408 KDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQ 449
Cdd:COG1134 43 KDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
404-567 |
8.72e-05 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 44.69 E-value: 8.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 404 KPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQM--LTDFGP---HGVLF-----LPQKPFFTDGTL 473
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLdgKPVEGPgaeRGVVFqneglLPWRNVQDNVAF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 474 REQVsdiyplkeiypdSGSTDDERILRFLELAGLSSLvtrtEGLDQQVDWNwydvLSPGEMQRLSFARLFYLQPKYAVLD 553
Cdd:PRK11248 94 GLQL------------AGVEKMQRLEIAHQMLKKVGL----EGAEKRYIWQ----LSGGQRQRVGIARALAANPQLLLLD 153
|
170
....*....|....*..
gi 1953408514 554 E---ATSALTEEVESEL 567
Cdd:PRK11248 154 EpfgALDAFTREQMQTL 170
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
496-584 |
2.10e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 44.63 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 496 ERILRFLELAGLSSLVtrtEGLDQQVDWN---WYDVLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEE----VESELY 568
Cdd:PTZ00265 1326 EDVKRACKFAAIDEFI---ESLPNKYDTNvgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNseklIEKTIV 1402
|
90
....*....|....*.
gi 1953408514 569 RIGQQLGMTFISVGHR 584
Cdd:PTZ00265 1403 DIKDKADKTIITIAHR 1418
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
404-589 |
2.23e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 43.23 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 404 KPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLW-----ASTQGSVqmltDFGPHGVlFLPQkpffTDGT-LREQV 477
Cdd:PRK14239 18 KKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNdlnpeVTITGSI----VYNGHNI-YSPR----TDTVdLRKEI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 478 SDIYPLKEIYPDSGStddERILRFLELAGlsslVTRTEGLDQQVDWN------WYDV----------LSPGEMQRLSFAR 541
Cdd:PRK14239 89 GMVFQQPNPFPMSIY---ENVVYGLRLKG----IKDKQVLDEAVEKSlkgasiWDEVkdrlhdsalgLSGGQQQRVCIAR 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1953408514 542 LFYLQPKYAVLDEATSAL----TEEVESELYRIGQQLGMTFISvghrHSLEK 589
Cdd:PRK14239 162 VLATSPKIILLDEPTSALdpisAGKIEETLLGLKDDYTMLLVT----RSMQQ 209
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
405-584 |
2.85e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 44.00 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 405 PLI-KDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQML-TDFGPHGV-----LF--LPQKPFFTDGTLRE 475
Cdd:PTZ00243 1323 PLVlRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNgREIGAYGLrelrrQFsmIPQDPVLFDGTVRQ 1402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 476 QVSdiyPLKEIYPdsgstddERILRFLELAGLSSLV-TRTEGLDQQV---DWNWydvlSPGEMQRLSFAR-LFYLQPKYA 550
Cdd:PTZ00243 1403 NVD---PFLEASS-------AEVWAALELVGLRERVaSESEGIDSRVlegGSNY----SVGQRQLMCMARaLLKKGSGFI 1468
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1953408514 551 VLDEATSalteEVESELYRIGQQLGM------TFISVGHR 584
Cdd:PTZ00243 1469 LMDEATA----NIDPALDRQIQATVMsafsayTVITIAHR 1504
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
404-565 |
2.90e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 43.73 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 404 KPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQML--TDFGphgvlFLPQ---KPFFTDGTLREQVS 478
Cdd:PRK15064 332 GPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSenANIG-----YYAQdhaYDFENDLTLFDWMS 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 479 DiyplkeiYPDSGstDDERILRflelAGLSSLVTRTEGLDQQVdwnwyDVLSPGEMQRLSFARLFYLQPKYAVLDEATSA 558
Cdd:PRK15064 407 Q-------WRQEG--DDEQAVR----GTLGRLLFSQDDIKKSV-----KVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNH 468
|
....*...
gi 1953408514 559 L-TEEVES 565
Cdd:PRK15064 469 MdMESIES 476
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
405-450 |
4.03e-04 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 42.14 E-value: 4.03e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1953408514 405 PLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQM 450
Cdd:PRK13543 25 PVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQI 70
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
529-584 |
8.57e-04 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 42.31 E-value: 8.57e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 529 LSPGEMQRLSFARLFYLQPKYAVLDEATSALTE-EVESeLYRIGQQL---GMTFISVGHR 584
Cdd:COG1129 141 LSVAQQQLVEIARALSRDARVLILDEPTASLTErEVER-LFRIIRRLkaqGVAIIYISHR 199
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
529-580 |
9.35e-04 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 41.94 E-value: 9.35e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1953408514 529 LSPGEMQRLSFARLFYLQPKYAVLDEATSALT-EEVEsELYRIGQQL---GMT--FIS 580
Cdd:COG3845 142 LSVGEQQRVEILKALYRGARILILDEPTAVLTpQEAD-ELFEILRRLaaeGKSiiFIT 198
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
407-584 |
1.45e-03 |
|
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: 41.35 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 407 IKDLSLKISEGQSLLITGNTGTGKSSLLRVLGG-----------LWASTQGSVQMLTDFGPHGVLFLPQKPfftdgTLRE 475
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyphgtwdgeiYWSGSPLKASNIRDTERAGIVIIHQEL-----TLVP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 476 QVS---DIYPLKEIYPDSGSTDDerilrflelaglSSLVTRTEGLDQQVDWNWYDVLSP------GEMQRLSFARLFYLQ 546
Cdd:TIGR02633 92 ELSvaeNIFLGNEITLPGGRMAY------------NAMYLRAKNLLRELQLDADNVTRPvgdyggGQQQLVEIAKALNKQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1953408514 547 PKYAVLDEATSALTE---EVESELYRIGQQLGMTFISVGHR 584
Cdd:TIGR02633 160 ARLLILDEPSSSLTEketEILLDIIRDLKAHGVACVYISHK 200
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
407-583 |
2.62e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 40.15 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 407 IKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQmLTDFGPH---------------GVLF-LPQKPFFTD 470
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVT-VDDITIThktkdkyirpvrkriGMVFqFPESQLFED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 471 GTLREQV----SDIYPLKEIypdsgstdDERILRFLELAGLSSLVTRTEGLDqqvdwnwydvLSPGEMQRLSFARLFYLQ 546
Cdd:PRK13646 102 TVEREIIfgpkNFKMNLDEV--------KNYAHRLLMDLGFSRDVMSQSPFQ----------MSGGQMRKIAIVSILAMN 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1953408514 547 PKYAVLDEATSALTEEVESELYRIGQQL----GMTFISVGH 583
Cdd:PRK13646 164 PDIIVLDEPTAGLDPQSKRQVMRLLKSLqtdeNKTIILVSH 204
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
404-583 |
2.74e-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: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 404 KPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGL--WASTQGS----VQMLTDFGPHGV-LFLPQKPFFTDGTLREQ 476
Cdd:TIGR03269 13 KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRiiyhVALCEKCGYVERpSKVGEPCPVCGGTLEPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953408514 477 VSDIYPLKEIY--------------------------------PDSGSTDDERILRFLELAGLSSLVTRTEGLDQQvdwn 524
Cdd:TIGR03269 93 EVDFWNLSDKLrrrirkriaimlqrtfalygddtvldnvlealEEIGYEGKEAVGRAVDLIEMVQLSHRITHIARD---- 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953408514 525 wydvLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEE----VESELYRIGQQLGMTFISVGH 583
Cdd:TIGR03269 169 ----LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQtaklVHNALEEAVKASGISMVLTSH 227
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
405-448 |
3.80e-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: 3.80e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1953408514 405 PLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSV 448
Cdd:PRK11650 18 QVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEI 61
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
402-439 |
3.92e-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: 3.92e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1953408514 402 SHKPLIKDLSLKISEGQSLLITGNTGTGKSSLLRVLGG 439
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALAN 55
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
409-449 |
9.53e-03 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 38.74 E-value: 9.53e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1953408514 409 DLSLKISEGQSLLITGNTGTGKSSLLRVLGGLWASTQGSVQ 449
Cdd:PRK11288 22 DISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSIL 62
|
|
| |
