|
Name |
Accession |
Description |
Interval |
E-value |
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
289-572 |
4.02e-120 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350042 [Multi-domain] Cd Length: 288 Bit Score: 368.80 E-value: 4.02e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 289 LGLLKMVGTMLGFSGPLLLSLLVGFLEEGQEPLSHGLLYVLGLAGGTVISAVLQNQYGYEVRKVTLQARVAVLSTLYRKA 368
Cdd:cd18598 2 LGLLKLLADVLGFAGPLLLNKLVEFLEDSSEPLSDGYLYALGLVLSSLLGALLSSHYNFQMNKVSLKVRAALVTAVYRKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 369 LKLGPSR---PPTGEVLNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGMAFLAGLVLALLLVPVNKVIATRI 445
Cdd:cd18598 82 LRVRSSSlskFSTGEIVNLMSTDADRIVNFCPSFHDLWSLPLQIIVALYLLYQQVGVAFLAGLVFALVLIPINKWIAKRI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 446 MASNQEMLRHKDARVKLMTELLSGIRVIKFFRWEQALGDRVKACRTKELGRLRVIKYLDAACVYLWAALPVVICITIFIT 525
Cdd:cd18598 162 GALSEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELKALKGRKYLDALCVYFWATTPVLISILTFAT 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1039753390 526 YVLMGHQLTATKVFTALALVRMLILPLNNFPWVINGLLESKVSLDRI 572
Cdd:cd18598 242 YVLMGNTLTAAKVFTSLALFNMLIGPLNAFPWVLNGLVEAWVSLKRL 288
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
203-911 |
6.81e-114 |
|
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: 384.68 E-value: 6.81e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 203 PFLSSESQE-TEVAEDGESWLSRFSYAWLAPLLARGVRGELQQP----------------------RDTCRLPRRlHPAF 259
Cdd:TIGR00957 190 PLFSETNHDpNPCPESSASFLSRITFWWITGMAVYGYRQPLEESdlwslnkedtsemvvpvlvenwKKECKKTRK-QPVS 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 260 LA--RVFQAHWKEGAQ----------------------LWRALYRAFGCCYLALGLLKMVGTMLGFSGPLLLSLLVGFLE 315
Cdd:TIGR00957 269 AVygKKDPSKPKGSSQldaneevealivksphkprkpsLFKVLYKTFGPYFLMSFCFKAIHDLMMFIGPQILSLLIRFVN 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 316 EGQEPLSHGLLYvlglAGGTVISAVLQ----NQYGYEVRKVTLQARVAVLSTLYRKALKLGPS--RPPT-GEVLNLLGTD 388
Cdd:TIGR00957 349 DPMAPDWQGYFY----TGLLFVCACLQtlilHQYFHICFVSGMRIKTAVMGAVYRKALVITNSarKSSTvGEIVNLMSVD 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 389 SERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGMAFLAGLVLALLLVPVNKVIATRIMASNQEMLRHKDARVKLMTELLS 468
Cdd:TIGR00957 425 AQRFMDLATYINMIWSAPLQVILALYFLWLNLGPSVLAGVAVMVLMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILN 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 469 GIRVIKFFRWEQALGDRVKACRTKELGRLRVIKYLDAACVYLWAALPVVICITIFITYVLMGHQ--LTATKVFTALALVR 546
Cdd:TIGR00957 505 GIKVLKLYAWELAFLDKVEGIRQEELKVLKKSAYLHAVGTFTWVCTPFLVALITFAVYVTVDENniLDAEKAFVSLALFN 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 547 MLILPLNNFPWVINGLLESKVSLDRIQRFLDLPSYSPEAYYSPDPPAEPSTALELHEALFSW---DPIGASQKTFishlQ 623
Cdd:TIGR00957 585 ILRFPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDSIERRTIKPGEGNSITVHNATFTWardLPPTLNGITF----S 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 624 VKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVselsKG-FGLATQEPWIQCATIRDNILFGKTFDAQLYREVLEA 702
Cdd:TIGR00957 661 IPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHM----KGsVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEA 736
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 703 CALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHRCI--LGVLSHTTRL 780
Cdd:TIGR00957 737 CALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIgpEGVLKNKTRI 816
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 781 LCTHRTEYLERADVVLLMEAGQLVRTGPPSEILPLVQAVPT-----AWAEKEQ---------VATSGQSP-------SVC 839
Cdd:TIGR00957 817 LVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEflrtyAPDEQQGhledswtalVSGEGKEAkliengmLVT 896
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 840 DLERTTEEELEVEQST-----------------------CGCLVQEESKSEGAVALHVYRAYWRAMGSGLAAAILVSLLL 896
Cdd:TIGR00957 897 DVVGKQLQRQLSASSSdsgdqsrhhgssaelqkaeakeeTWKLMEADKAQTGQVELSVYWDYMKAIGLFITFLSIFLFVC 976
|
810
....*....|....*
gi 1039753390 897 MQATRNGADWWLAHW 911
Cdd:TIGR00957 977 NHVSALASNYWLSLW 991
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
288-572 |
5.55e-109 |
|
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents the 6-transmembrane (6TM) domain of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides.
Pssm-ID: 350003 [Multi-domain] Cd Length: 290 Bit Score: 339.96 E-value: 5.55e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 288 ALGLLKMVGTMLGFSGPLLLSLLVGFLEEGQEPLSHGLLYVLGLAGGTVISAVLQNQYGYEVRKVTLQARVAVLSTLYRK 367
Cdd:cd18559 1 SFLLIKLVLCNHVFSGPSNLWLLLWFDDPVNGPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 368 ALKLGPS---RPPTGEVLNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGMAFLAGLVLALLLVPVNKVIATR 444
Cdd:cd18559 81 ALRSPISffeRTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVPVNRVYAAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 445 IMASNQEMLRHKDARVKLMTELLSGIRVIKFFRWEQALGDRVKACRTKELGRLRVIKYLDAACVYLWAALPVVICITIFI 524
Cdd:cd18559 161 SRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYLRALAVRLWCVGPCIVLFASFF 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1039753390 525 TYVLMGH--QLTATKVFTALALVRMLILPLNNFPWVINGLLESKVSLDRI 572
Cdd:cd18559 241 AYVSRHSlaGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
599-802 |
2.22e-98 |
|
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: 308.24 E-value: 2.22e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 599 LELHEALFSWDPiGASQKTFISH---LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVSelsKGFGLATQEPW 675
Cdd:cd03250 1 ISVEDASFTWDS-GEQETSFTLKdinLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVP---GSIAYVSQEPW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 676 IQCATIRDNILFGKTFDAQLYREVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLA 755
Cdd:cd03250 77 IQNGTIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLS 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1039753390 756 AVDADVANHLLHRCILGVLSHT-TRLLCTHRTEYLERADVVLLMEAGQ 802
Cdd:cd03250 157 AVDAHVGRHIFENCILGLLLNNkTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
216-932 |
1.10e-97 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 338.10 E-value: 1.10e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 216 EDGESWLSRFSYAWLAPLLARGVRGELQQpRDTCRLPRRLHPAFLARVFQAHWKEGAQ-----LWRALYRAFGCCYLALG 290
Cdd:PLN03232 229 ERYASIFSRIYFSWMTPLMQLGYRKPITE-KDVWQLDQWDQTETLIKRFQRCWTEESRrpkpwLLRALNNSLGGRFWLGG 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 291 LLKMVGTMLGFSGPLLLSLLVGFLEEGqEPLSHGLLYVLGLAGGTVISAVLQNQYGYEVRKVTLQARVAVLSTLYRKALK 370
Cdd:PLN03232 308 IFKIGHDLSQFVGPVILSHLLQSMQEG-DPAWVGYVYAFLIFFGVTFGVLCESQYFQNVGRVGFRLRSTLVAAIFHKSLR 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 371 L---GPSRPPTGEVLNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGMAFLAGLVLALLLVPVNKVIATRIMA 447
Cdd:PLN03232 387 LtheARKNFASGKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMVLLYQQLGVASLFGSLILFLLIPLQTLIVRKMRK 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 448 SNQEMLRHKDARVKLMTELLSGIRVIKFFRWEQALGDRVKACRTKELGRLRVIKYLDAACVYLWAALPVVICITIFITYV 527
Cdd:PLN03232 467 LTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWFRKAQLLSAFNSFILNSIPVVVTLVSFGVFV 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 528 LMGHQLTATKVFTALALVRMLILPLNNFPWVINGLLESKVSLDRIQRFLdlpsYSPEAYYSPDPPAEPST-ALELHEALF 606
Cdd:PLN03232 547 LLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELL----LSEERILAQNPPLQPGApAISIKNGYF 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 607 SWDPIGASQKTFISHLQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVSELSKGFglATQEPWIQCATIRDNIL 686
Cdd:PLN03232 623 SWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVIRGSVAY--VPQVSWIFNATVRENIL 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 687 FGKTFDAQLYREVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLL 766
Cdd:PLN03232 701 FGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVF 780
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 767 HRCILGVLSHTTRLLCTHRTEYLERADVVLLM------EAGQLVRTGPPSEILPLVQAVPTAWAEKEQVATSGQ-----S 835
Cdd:PLN03232 781 DSCMKDELKGKTRVLVTNQLHFLPLMDRIILVsegmikEEGTFAELSKSGSLFKKLMENAGKMDATQEVNTNDEnilklG 860
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 836 PSV-CDLERTTEEELEVEQSTCGCLVQEESKSEGAVALHVYRAYWRAMGSGLAAAIL-VSLLLMQATRNGADWWLAHWLS 913
Cdd:PLN03232 861 PTVtIDVSERNLGSTKQGKRGRSVLVKQEERETGIISWNVLMRYNKAVGGLWVVMILlVCYLTTEVLRVSSSTWLSIWTD 940
|
730
....*....|....*....
gi 1039753390 914 QlkagrngsrEDPASCSPG 932
Cdd:PLN03232 941 Q---------STPKSYSPG 950
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
206-914 |
6.74e-97 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 336.71 E-value: 6.74e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 206 SSESQETEVAEDGE--------SWLSRFSYAWLAPLLARGVRGELQQPrDTCRLPRRLHPAFLARVFQAHWKEGAQ---- 273
Cdd:PLN03130 211 SVDDYEYEELPGGEqicperhaNIFSRIFFGWMTPLMQLGYKRPLTEK-DVWKLDTWDQTETLYRSFQKCWDEELKkpkp 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 274 -LWRALYRAFGCCYLALGLLKMVGTMLGFSGPLLLSLLVGFLEEGqEPLSHGLLYVLGLAGGTVISAVLQNQYGYEVRKV 352
Cdd:PLN03130 290 wLLRALNNSLGGRFWLGGFFKIGNDLSQFVGPLLLNLLLESMQNG-EPAWIGYIYAFSIFVGVVLGVLCEAQYFQNVMRV 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 353 TLQARVAVLSTLYRKALKL---GPSRPPTGEVLNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGMAFLAGLV 429
Cdd:PLN03130 369 GFRLRSTLVAAVFRKSLRLtheGRKKFTSGKITNLMTTDAEALQQICQQLHTLWSAPFRIIIAMVLLYQQLGVASLIGSL 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 430 LALLLVPVNKVIATRIMASNQEMLRHKDARVKLMTELLSGIRVIKFFRWEQALGDRVKACRTKELGRLRVIKYLDAACVY 509
Cdd:PLN03130 449 MLVLMFPIQTFIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELSWFRKAQLLSAFNSF 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 510 LWAALPVVICITIFITYVLMGHQLTATKVFTALALVRMLILPLNNFPWVINGLLESKVSLDRIQRFLdlpsYSPEAYYSP 589
Cdd:PLN03130 529 ILNSIPVLVTVVSFGVFTLLGGDLTPARAFTSLSLFAVLRFPLFMLPNLITQAVNANVSLKRLEELL----LAEERVLLP 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 590 DPPAEPST-ALELHEALFSWDPigASQKTFISH--LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVSELSKG 666
Cdd:PLN03130 605 NPPLEPGLpAISIKNGYFSWDS--KAERPTLSNinLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVVIRGTVA 682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 667 FglATQEPWIQCATIRDNILFGKTFDAQLYREVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKA 746
Cdd:PLN03130 683 Y--VPQVSWIFNATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSD 760
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 747 LYLLDDPLAAVDADVANHLLHRCILGVLSHTTRLLCTHRTEYLERADVVLLMEAGQLVRTGPPSEIL---PLVQAV---- 819
Cdd:PLN03130 761 VYIFDDPLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSnngPLFQKLmena 840
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 820 --------PTAWAEKEQVATSGQSPSVCDLERTTEEELEVEQSTCGCLVQEESKSEGAVALHVYRAYWRAMGSGLAAAIL 891
Cdd:PLN03130 841 gkmeeyveENGEEEDDQTSSKPVANGNANNLKKDSSSKKKSKEGKSVLIKQEERETGVVSWKVLERYKNALGGAWVVMIL 920
|
730 740
....*....|....*....|....
gi 1039753390 892 V-SLLLMQATRNGADWWLAHWLSQ 914
Cdd:PLN03130 921 FlCYVLTEVFRVSSSTWLSEWTDQ 944
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
289-572 |
1.90e-78 |
|
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350023 [Multi-domain] Cd Length: 289 Bit Score: 258.18 E-value: 1.90e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 289 LGLLKMVGTMLGFSGPLLLSLLVGFLEE-GQEPLSHGLLYVLGLAGGTVISAVLQNQYGYEVRKVTLQARVAVLSTLYRK 367
Cdd:cd18579 2 AGLLKLLEDLLSLAQPLLLGLLISYLSSyPDEPLSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIYRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 368 ALKLGPS---RPPTGEVLNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGMAFLAGLVLALLLVPVNKVIATR 444
Cdd:cd18579 82 ALRLSSSarqETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAFLAKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 445 IMASNQEMLRHKDARVKLMTELLSGIRVIKFFRWEQALGDRVKACRTKELGRLRVIKYLDAACVYLWAALPVVICITIFI 524
Cdd:cd18579 162 ISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTPVLVSLATFA 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1039753390 525 TYVLMGHQLTATKVFTALALVRMLILPLNNFPWVINGLLESKVSLDRI 572
Cdd:cd18579 242 TYVLLGNPLTAAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKRI 289
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
274-911 |
2.03e-74 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 269.34 E-value: 2.03e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 274 LWRALYRAFGCCYLALGLLKMVGTMLGFSGPLLLSLLVGFLEEGQEPLSHGLLYVLGLAGGTVISAVLQNQYGYEVRKVT 353
Cdd:PTZ00243 234 LLRTLFAALPYYVWWQIPFKLLSDVCTLTLPVLLKYFVKFLDADNATWGRGLGLVLTLFLTQLIQSVCLHRFYYISIRCG 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 354 LQARVAVLSTLYRKALKLGP---SRPP--TGEVLNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGMAFLAGL 428
Cdd:PTZ00243 314 LQYRSALNALIFEKCFTISSkslAQPDmnTGRIINMMSTDVERINSFMQYCMYLWSSPMVLLLSILLLSRLVGWCALMAV 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 429 VLALLLVPVNKVIATRIMASNQEMLRHKDARVKLMTELLSGIRVIKFFRWEQALGDRVKACRTKELGRLRVIKYLDAACV 508
Cdd:PTZ00243 394 AVLLVTLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRARELRYLRDVQLARVATS 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 509 YLWAALPVVICITIFITYVLMGHQLTATKVFTALALVRMLILPLNNFPWVINGLLESKVSLDRIQRFL-----------D 577
Cdd:PTZ00243 474 FVNNATPTLMIAVVFTVYYLLGHELTPEVVFPTIALLGVLRMPFFMIPWVFTTVLQFLVSIKRISTFLecdnatcstvqD 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 578 LPSYSPEAYYSP---------------------------------------------DPPAEPSTALELHEALFSWDPIG 612
Cdd:PTZ00243 554 MEEYWREQREHStacqlaavlenvdvtafvpvklprapkvktsllsralrmlcceqcRPTKRHPSPSVVVEDTDYGSPSS 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 613 AS------------QKTFIS--------------------------HLQVKKGMLVGIVGKVGCGKSSLLAAITGELhrl 654
Cdd:PTZ00243 634 ASrhiveggtggghEATPTSersaktpkmktddffelepkvllrdvSVSVPRGKLTVVLGATGSGKSTLLQSLLSQF--- 710
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 655 cgwvavsELSKG-------FGLATQEPWIQCATIRDNILFGKTFDAQLYREVLEACALNDDLSILPAGDQTEVGEKGVTL 727
Cdd:PTZ00243 711 -------EISEGrvwaersIAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNL 783
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 728 SGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHRCILGVLSHTTRLLCTHRTEYLERADVVLLMEAGQLVRTG 807
Cdd:PTZ00243 784 SGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSG 863
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 808 PPSEIL--PLVQAVPTAWAEKEQVATSGQSPSVCDLERTTEEELEVEQS------------------TCGCLVQEESKSE 867
Cdd:PTZ00243 864 SSADFMrtSLYATLAAELKENKDSKEGDADAEVAEVDAAPGGAVDHEPPvakqegnaeggdgaaldaAAGRLMTREEKAS 943
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 1039753390 868 GAVALHVYRAYWRAMGSGLAAAILVSLLLMQATRNGAD-WWLAHW 911
Cdd:PTZ00243 944 GSVPWSTYVAYLRFCGGLHAAGFVLATFAVTELVTVSSgVWLSMW 988
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
290-572 |
8.24e-68 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350039 [Multi-domain] Cd Length: 290 Bit Score: 228.89 E-value: 8.24e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 290 GLLKMVGTMLGFSGPLLLSLLVGFLEEGQEPLSHGLLYVLGLAGGTVISAVLQNQYGYEVRKVTLQARVAVLSTLYRKAL 369
Cdd:cd18595 3 ALLKLLSDILLFASPQLLKLLINFVEDPDEPLWKGYLYAVLLFLVSIIQSLLLHQYFHRCFRLGMRIRTALTSAIYRKAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 370 KLGP-SRP--PTGEVLNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGMAFLAGLVLALLLVPVNKVIATRIM 446
Cdd:cd18595 83 RLSNsARKksTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILALYFLWQTLGPSVLAGLGVMILLIPLNAVLARKIK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 447 ASNQEMLRHKDARVKLMTELLSGIRVIKFFRWEQALGDRVKACRTKELGRLRVIKYLDAACVYLWAALPVVICITIFITY 526
Cdd:cd18595 163 KLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAYLNAVSSFLWTCAPFLVSLATFATY 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1039753390 527 VLMG--HQLTATKVFTALALVRMLILPLNNFPWVINGLLESKVSLDRI 572
Cdd:cd18595 243 VLSDpdNVLDAEKAFVSLSLFNILRFPLSMLPMVISNLVQASVSLKRL 290
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
220-812 |
6.00e-62 |
|
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: 230.95 E-value: 6.00e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 220 SWLSRFSYAWLAPLLARGVRGELQQPrDTCRLPRRLHPAFLARVFQAHW-------KEGAQLWRALYRAFGCCYLALGLL 292
Cdd:TIGR01271 10 NFLSKLFFWWTRPILRKGYRQKLELS-DIYQIPSFDSADNLSERLEREWdrelasaKKNPKLLNALRRCFFWRFVFYGIL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 293 KMVGTMLGFSGPLLLSLLVG-FLEEGQEPLSHGLLYVLGLAGGTVISAVLQNQYGYEVRKVTLQARVAVLSTLYRKALKL 371
Cdd:TIGR01271 89 LYFGEATKAVQPLLLGRIIAsYDPFNAPEREIAYYLALGLCLLFIVRTLLLHPAIFGLHHLGMQMRIALFSLIYKKTLKL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 372 GP---SRPPTGEVLNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGMAFLAGLVLALLLVPVNKVIATRIMAS 448
Cdd:TIGR01271 169 SSrvlDKISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILLMGLIWELLEVNGFCGLGFLILLALFQACLGQKMMPY 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 449 NQEMLRHKDARVKLMTELLSGIRVIKFFRWEQALGDRVKACRTKELGRLRVI---KYLDAACVYLWAALPVVICItifIT 525
Cdd:TIGR01271 249 RDKRAGKISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRKIaylRYFYSSAFFFSGFFVVFLSV---VP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 526 YVLMgHQLTATKVFTALALVRMLILPLN-NFPWVINGLLESKVSLDRIQRFLDLPSYSPEAYyspdppAEPSTALELHEA 604
Cdd:TIGR01271 326 YALI-KGIILRRIFTTISYCIVLRMTVTrQFPGAIQTWYDSLGAITKIQDFLCKEEYKTLEY------NLTTTEVEMVNV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 605 LFSWDP-IG----------ASQKT-------FISHL-------------QVKKGMLVGIVGKVGCGKSSLLAAITGELHR 653
Cdd:TIGR01271 399 TASWDEgIGelfekikqnnKARKQpngddglFFSNFslyvtpvlknisfKLEKGQLLAVAGSTGSGKSSLLMMIMGELEP 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 654 LCGWVavsELSKGFGLATQEPWIQCATIRDNILFGKTFDAQLYREVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRA 733
Cdd:TIGR01271 479 SEGKI---KHSGRISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRA 555
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039753390 734 RIALARAVYQEKALYLLDDPLAAVDADVANHLLHRCILGVLSHTTRLLCTHRTEYLERADVVLLMEAGQLVRTGPPSEI 812
Cdd:TIGR01271 556 RISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSEL 634
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
288-572 |
1.63e-58 |
|
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350040 [Multi-domain] Cd Length: 309 Bit Score: 203.50 E-value: 1.63e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 288 ALGLLKMVGTMLGFSGPLLLSLLVGFLEE-GQEPLSHGLLYVLGLAGGTVISAVLQNQYGYEVRKVTLQARVAVLSTLYR 366
Cdd:cd18596 1 LQALLAVLSSVLSFAPPFFLNRLLRYLEDpGEDATVRPWVWVLLLFLGPLLSSLLDQQYLWIGRRLSVRLRAILTQLIFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 367 KALKL----GPSRPP------------------TGEVLNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGMAF 424
Cdd:cd18596 81 KALRRrdksGSSKSSeskkkdkeededekssasVGKINNLMSVDANRISEFAAFLHLLVSAPLQIVIAIVFLYRLLGWSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 425 LAGLVLALLLVPVNKVIATRIMASNQEMLRHKDARVKLMTELLSGIRVIKFFRWEQALGDRVKACRTKELGRLRVIKYLD 504
Cdd:cd18596 161 LVGLAVMVLLLPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEELKWLRKRFLLD 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039753390 505 AACVYLWAALPVVICITIFITYVL-MGHQLTATKVFTALALVRMLILPLNNFPWVINGLLESKVSLDRI 572
Cdd:cd18596 241 LLLSLLWFLIPILVTVVTFATYTLvMGQELTASVAFTSLALFNMLRGPLNVLPELITQLLQAKVSLDRI 309
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
290-572 |
1.02e-53 |
|
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350041 [Multi-domain] Cd Length: 293 Bit Score: 189.20 E-value: 1.02e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 290 GLLKMVGTMLGFSGPLLLSLLVGFLEEGQE-----PLSHGLLYVLGLAGGTVISAVLQNQYGYEVRKVTLQARVAVLSTL 364
Cdd:cd18597 3 GLLKLLADVLQVLSPLLLKYLINFVEDAYLggpppSIGYGIGYAIGLFLLQLLSSLLLNHFFYRSMLTGAQVRAALTKAI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 365 YRKALKL-GPSR--PPTGEVLNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGMAFLAGLVLALLLVPVNKVI 441
Cdd:cd18597 83 YRKSLRLsGKSRheFPNGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIALLIVNLGPSALVGIGVLILSIPLQGFL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 442 ATRIMASNQEMLRHKDARVKLMTELLSGIRVIKFFRWEQALGDRVKACRTKELGRLRVIKYLDAACVYLWAALPVVICIT 521
Cdd:cd18597 163 MKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELKYVRKLQILRSILTAVAFSLPVLASML 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1039753390 522 IFITYVLMGHQLTATKVFTALALVRMLILPLNNFPWVINGLLESKVSLDRI 572
Cdd:cd18597 243 SFITYYATGHTLDPANIFSSLALFNVLRMPLMFLPLALSSLADALVALKRI 293
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
606-801 |
1.55e-52 |
|
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: 183.30 E-value: 1.55e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 606 FSWDPiGASQKTFIShLQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCG---WVAVSELSKGF-----------GLAT 671
Cdd:cd03290 8 FSWGS-GLATLSNIN-IRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGkvhWSNKNESEPSFeatrsrnrysvAYAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 672 QEPWIQCATIRDNILFGKTFDAQLYREVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLD 751
Cdd:cd03290 86 QKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1039753390 752 DPLAAVDADVANHLLHRCILGVLSHTTR--LLCTHRTEYLERADVVLLMEAG 801
Cdd:cd03290 166 DPFSALDIHLSDHLMQEGILKFLQDDKRtlVLVTHKLQYLPHADWIIAMKDG 217
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
269-813 |
1.63e-51 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 191.15 E-value: 1.63e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 269 KEGAQLWRALYRAFGCC---YLALGLLKMVGTMLGFSGPLLLSLLVGFLEEGQePLSHGLLYVLGLAGGTVISAVLQNQY 345
Cdd:COG1132 3 KSPRKLLRRLLRYLRPYrglLILALLLLLLSALLELLLPLLLGRIIDALLAGG-DLSALLLLLLLLLGLALLRALLSYLQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 346 GYEVRKVTLQARVAVLSTLYRKALKLGPS---RPPTGEVLNLLGTDSERLLNFAG-SFHEAWGLPLQLAITL-YLLYQQV 420
Cdd:COG1132 82 RYLLARLAQRVVADLRRDLFEHLLRLPLSffdRRRTGDLLSRLTNDVDAVEQFLAhGLPQLVRSVVTLIGALvVLFVIDW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 421 GMAFLAGLVLALLLVPVnKVIATRIMASNQEMLRHKDARVKLMTELLSGIRVIKFFRWEQALGDRVKAcRTKELGR--LR 498
Cdd:COG1132 162 RLALIVLLVLPLLLLVL-RLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFRE-ANEELRRanLR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 499 VIKYLDA--ACVYLWAALPVVICITIFITYVLMGhQLTATKVFTALALVRMLILPLNNFPWVINGLLESKVSLDRIQRFL 576
Cdd:COG1132 240 AARLSALffPLMELLGNLGLALVLLVGGLLVLSG-SLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 577 DLPSYSPEAYySPDPPAEPSTALELHEALFSWDPigaSQKTF--IShLQVKKGMLVGIVGKVGCGKSSLLAAIT------ 648
Cdd:COG1132 319 DEPPEIPDPP-GAVPLPPVRGEIEFENVSFSYPG---DRPVLkdIS-LTIPPGETVALVGPSGSGKSTLVNLLLrfydpt 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 649 -GELhRLCGwVAVSELS-----KGFGLATQEPWIQCATIRDNILFGK---TfDAQLyREVLEACALNDDLSILPAGDQTE 719
Cdd:COG1132 394 sGRI-LIDG-VDIRDLTleslrRQIGVVPQDTFLFSGTIRENIRYGRpdaT-DEEV-EEAAKAAQAHEFIEALPDGYDTV 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 720 VGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVAnHLLHRCILGVLSHTTRLLCTHRTEYLERADVVLLME 799
Cdd:COG1132 470 VGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETE-ALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLD 548
|
570
....*....|....
gi 1039753390 800 AGQLVRTGPPSEIL 813
Cdd:COG1132 549 DGRIVEQGTHEELL 562
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
322-813 |
1.38e-47 |
|
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: 181.96 E-value: 1.38e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 322 SHGLLYVL--GLAGGTVISAVLQNQYGYEVRKVTLQARVAVLSTLYRKALKLGPS---RPPTGEVLNLLGtDSERLLNF- 395
Cdd:COG2274 191 DLSTLWVLaiGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSffeSRSVGDLASRFR-DVESIREFl 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 396 AGSFHEAWGLPLQLAITLYLLYQQVGMAFLAGLVLALLLVPVNKVIATRIMASNQEMLRHKDARVKLMTELLSGIRVIKF 475
Cdd:COG2274 270 TGSLLTALLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 476 F--------RWEQALGDRVKAcrtkelgRLRVIKYLDAAcvYLWA-ALPVV--ICITIFITYVLMGHQLTATKVFTALAL 544
Cdd:COG2274 350 LgaesrfrrRWENLLAKYLNA-------RFKLRRLSNLL--STLSgLLQQLatVALLWLGAYLVIDGQLTLGQLIAFNIL 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 545 VRMLILPLNNFPWVINGLLESKVSLDRIQRFLDLPSySPEAYYSPDPPAEPSTALELHEALFSWDPigASQKTF--IShL 622
Cdd:COG2274 421 SGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPP-EREEGRSKLSLPRLKGDIELENVSFRYPG--DSPPVLdnIS-L 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 623 QVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAV----------SELSKGFGLATQEPWIQCATIRDNILFGKTF- 691
Cdd:COG2274 497 TIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIdgidlrqidpASLRRQIGVVLQDVFLFSGTIRENITLGDPDa 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 692 -DAQLyREVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHRcI 770
Cdd:COG2274 577 tDEEI-IEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILEN-L 654
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1039753390 771 LGVLSHTTRLLCTHRTEYLERADVVLLMEAGQLVRTGPPSEIL 813
Cdd:COG2274 655 RRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELL 697
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
622-812 |
2.27e-44 |
|
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: 162.33 E-value: 2.27e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVavsELSKGFGLATQEPWIQCATIRDNILFGKTFDAQLYREVLE 701
Cdd:cd03291 58 LKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI---KHSGRISFSSQFSWIMPGTIKENIIFGVSYDEYRYKSVVK 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 702 ACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHRCILGVLSHTTRLL 781
Cdd:cd03291 135 ACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCKLMANKTRIL 214
|
170 180 190
....*....|....*....|....*....|.
gi 1039753390 782 CTHRTEYLERADVVLLMEAGQLVRTGPPSEI 812
Cdd:cd03291 215 VTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
313-573 |
2.77e-42 |
|
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; This group represents the six-transmembrane domain 1 (TMD1) of the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), which belongs to the ABCC subfamily. CFTR functions as a chloride channel, in contrast to other ABC transporters, and controls ion and water secretion and absorption in epithelial tissues. ABC proteins are formed from two homologous halves each containing a transmembrane domain (TMD) and a cytosolic nucleotide binding domain (NBD). In CFTR, these two TMD-NBD halves are linked by the unique regulatory (R) domain, which is not present in other ABC transporters. The ion channel only opens when its R-domain is phosphorylated by cyclic AMP-dependent protein kinase (PKA) and ATP is bound at the NBDs. Mutations in CFTR cause cystic fibrosis, the most common lethal genetic disorder in populations of Northern European descent.
Pssm-ID: 350038 [Multi-domain] Cd Length: 291 Bit Score: 156.64 E-value: 2.77e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 313 FLEEGQEPLSHGLLYVLGLAGGTVISAVLQNQYGYEVRKVTLQARVAVLSTLYRKALKLGP---SRPPTGEVLNLLGTDS 389
Cdd:cd18594 27 FVPDSTVTKTEAYLYALGLSLCAFLRVLLHHPYFFGLHRYGMQLRIALSSLIYKKTLKLSSsalSKITTGHIVNLLSNDV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 390 ERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGMAFLAGLVLALLLVPVNKVIATRIMASNQEMLRHKDARVKLMTELLSG 469
Cdd:cd18594 107 QKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPLQAYLGKLFAKYRRKTAGLTDERVKIMNEIISG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 470 IRVIKFFRWEQALGDRVKACRTKELGRLRVIKYLDAACVYLWAALPVVICITIFITYVLMGHQLTATKVFTALAL---VR 546
Cdd:cd18594 187 MRVIKMYTWEESFAKLIENIRKKELKLIRKAAYIRAFNMAFFFFSPTLVSFATFVPYVLTGNTLTARKVFTVISLlnaLR 266
|
250 260
....*....|....*....|....*..
gi 1039753390 547 MLIlpLNNFPWVINGLLESKVSLDRIQ 573
Cdd:cd18594 267 MTI--TRFFPESIQTLSESRVSLKRIQ 291
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
522-813 |
7.05e-40 |
|
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: 156.46 E-value: 7.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 522 IFITYVLMGHQLTATKVFTALALVRMLILPLNNFpwvinGL-----LESKVSLDRIQRFLDLPSYSPEAYYSPDPPAEPS 596
Cdd:COG4988 261 VYIGFRLLGGSLTLFAALFVLLLAPEFFLPLRDL-----GSfyharANGIAAAEKIFALLDAPEPAAPAGTAPLPAAGPP 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 597 TaLELHEALFSWDPIGASQKtFIShLQVKKGMLVGIVGKVGCGKSSLLAAITGELH------RLCGwVAVSELS-----K 665
Cdd:COG4988 336 S-IELEDVSFSYPGGRPALD-GLS-LTIPPGERVALVGPSGAGKSTLLNLLLGFLPpysgsiLING-VDLSDLDpaswrR 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 666 GFGLATQEPWIQCATIRDNILFGKTF--DAQLyREVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQ 743
Cdd:COG4988 412 QIAWVPQNPYLFAGTIRENLRLGRPDasDEEL-EAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLR 490
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 744 EKALYLLDDPLAAVDADVANHLLHRcILGVLSHTTRLLCTHRTEYLERADVVLLMEAGQLVRTGPPSEIL 813
Cdd:COG4988 491 DAPLLLLDEPTAHLDAETEAEILQA-LRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELL 559
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
447-813 |
1.50e-38 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 152.61 E-value: 1.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 447 ASNQEMLRHKDARVKLMTELLSGIRVIKFF-RWEQALG--DRVKACRTKELGRLRVIKYLDAACVYLWAALPVVICITIF 523
Cdd:COG4987 182 RAGRRLAAARAALRARLTDLLQGAAELAAYgALDRALArlDAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLA 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 524 ITYVLMGHQ---LTATKVFTALALVRMLiLPLnnfPWVINGLLESKVSLDRIQRFLDLPSYSPEAYYSPDPPAEPStaLE 600
Cdd:COG4987 262 APLVAAGALsgpLLALLVLAALALFEAL-APL---PAAAQHLGRVRAAARRLNELLDAPPAVTEPAEPAPAPGGPS--LE 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 601 LHEALFSWDpiGASQKTF--IShLQVKKGMLVGIVGKVGCGKSSLLAAITGEL-----------HRLCGWvAVSELSKGF 667
Cdd:COG4987 336 LEDVSFRYP--GAGRPVLdgLS-LTLPPGERVAIVGPSGSGKSTLLALLLRFLdpqsgsitlggVDLRDL-DEDDLRRRI 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 668 GLATQEPWIQCATIRDNILFGK---TfDAQLyREVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQE 744
Cdd:COG4987 412 AVVPQRPHLFDTTLRENLRLARpdaT-DEEL-WAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRD 489
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039753390 745 KALYLLDDPLAAVDADVANHLLHRcILGVLSHTTRLLCTHRTEYLERADVVLLMEAGQLVRTGPPSEIL 813
Cdd:COG4987 490 APILLLDEPTEGLDAATEQALLAD-LLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELL 557
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
290-572 |
1.94e-38 |
|
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group represents the six-transmembrane domain 1 (TMD1) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and they belong to the ABCC subfamily. The ATP-sensitive (K-ATP) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Thus, in contrast to other ABC transporters, the SUR serves as the regulatory subunit of an ion channel. Mutations and deficiencies in the SUR proteins have been observed in patients with hyperinsulinemic hypoglycemia of infancy, an autosomal recessive disorder of unregulated and high insulin secretion. Mutations have also been associated with non-insulin-dependent diabetes mellitus type 2, an autosomal dominant disease of defective insulin secretion.
Pssm-ID: 350035 [Multi-domain] Cd Length: 309 Bit Score: 145.84 E-value: 1.94e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 290 GLLKMVGTMLGFSGPLLLSLLVGFLEEGQEPLS-----HGLLYV-----LG----LAGGTVISAVLQN---QYGYEVRKV 352
Cdd:cd18591 3 GILKLLGDLLGFVGPLCISGIVDYVEENTYSSSnstdkLSVSYVtveefFSngyvLAVILFLALLLQAtfsQASYHIVIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 353 T-LQARVAVLSTLYRKALKLGPSRPP-----TGEVLNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGMAFLA 426
Cdd:cd18591 83 EgIRLKTALQAMIYEKALRLSSWNLSsgsmtIGQITNHMSEDANNIMFFFWLIHYLWAIPLKIIVGLILLYLKLGVSALI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 427 GLVLALLLVPVNKVIATRIMASNQEMLRHKDARVKLMTELLSGIRVIKFFRWEQALGDRVKACRTKELGRLRVIKYLDAA 506
Cdd:cd18591 163 GAALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKELKLLLKDAVYWSL 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039753390 507 CVYLWAALPVVICITIFITYVLMGHQ-LTATKVFTALALVRMLILPLNNFPWVINGLLESKVSLDRI 572
Cdd:cd18591 243 MTFLTQASPILVTLVTFGLYPYLEGEpLTAAKAFSSLALFNQLTVPLFIFPVVIPILINAVVSTRRL 309
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
320-572 |
1.70e-36 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) and similar proteins; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350037 [Multi-domain] Cd Length: 291 Bit Score: 139.66 E-value: 1.70e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 320 PLSHGLLYVLGLAGGTVISAVLQNQYGYEVRKVTLQARVAVLSTLYRKALKLGPS---RPPTGEVLNLLGTDSERLLNFA 396
Cdd:cd18593 35 SLTEAYLYAGGVSLCSFLFIITHHPYFFGMQRIGMRLRVACSSLIYRKALRLSQAalgKTTVGQIVNLLSNDVNRFDQAV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 397 GSFHEAWGLPLQLAITLYLLYQQVGMAFLAGLVLALLLVPVNKVIAtRIMASN-QEMLRHKDARVKLMTELLSGIRVIKF 475
Cdd:cd18593 115 LFLHYLWVAPLQLIAVIYILWFEIGWSCLAGLAVLLILIPLQSFFG-KLFSKLrRKTAARTDKRIRIMNEIINGIRVIKM 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 476 FRWEQALGDRVKACRTKELGRLRVIKYLDAACVYLWAALPVVICITIFITYVLMGHQLTATKVFTALALVRMLILPLNN- 554
Cdd:cd18593 194 YAWEKAFAKLVDDLRRKEIKKVRRTSFLRALNMGLFFVSSKLILFLTFLAYILLGNILTAERVFVTMALYNAVRLTMTLf 273
|
250
....*....|....*...
gi 1039753390 555 FPWVINGLLESKVSLDRI 572
Cdd:cd18593 274 FPFAIQFGSELSVSIRRI 291
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
622-807 |
5.22e-34 |
|
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: 130.02 E-value: 5.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAV----------SELSKGFGLATQEPWIQCATIRDNILFGKTF 691
Cdd:cd03245 25 LTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLdgtdirqldpADLRRNIGYVPQDVTLFYGTLRDNITLGAPL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 692 -DAQLYREVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHRcI 770
Cdd:cd03245 105 aDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKER-L 183
|
170 180 190
....*....|....*....|....*....|....*..
gi 1039753390 771 LGVLSHTTRLLCTHRTEYLERADVVLLMEAGQLVRTG 807
Cdd:cd03245 184 RQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
465-798 |
1.90e-31 |
|
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: 130.10 E-value: 1.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 465 ELLSGIRVIKFFRWEQALGDRVKAC----RTKELGRLRvIKYLDAACVYLWAALPVVIcITIFITYVLMGHQLTATKVFT 540
Cdd:TIGR02857 188 DRLRGLPTLKLFGRAKAQAAAIRRSseeyRERTMRVLR-IAFLSSAVLELFATLSVAL-VAVYIGFRLLAGDLDLATGLF 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 541 ALALVRMLILPLNNFPWVINGLLESKVSLDRIQRFLDLPSysPEAYYSPDPPAEPSTALELHEALFSWDPIGASQKTFis 620
Cdd:TIGR02857 266 VLLLAPEFYLPLRQLGAQYHARADGVAAAEALFAVLDAAP--RPLAGKAPVTAAPASSLEFSGVSVAYPGRRPALRPV-- 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 621 HLQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAV----------SELSKGFGLATQEPWIQCATIRDNILFGKT 690
Cdd:TIGR02857 342 SFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVngvpladadaDSWRDQIAWVPQHPFLFAGTIAENIRLARP 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 691 F-DAQLYREVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHRc 769
Cdd:TIGR02857 422 DaSDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEA- 500
|
330 340
....*....|....*....|....*....
gi 1039753390 770 ILGVLSHTTRLLCTHRTEYLERADVVLLM 798
Cdd:TIGR02857 501 LRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
291-572 |
3.21e-30 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350036 [Multi-domain] Cd Length: 287 Bit Score: 121.51 E-value: 3.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 291 LLKMVGTMLGFSGPLLL-SLLVGFLEEGQEPLSHGLLYVLGLAGGTVISAVLQNQYGYEVRKVTLQARVAVLSTLYRKAL 369
Cdd:cd18592 4 LLLLISLIFGFIGPTILiRKLLEYLEDSDSSVWYGILLVLGLFLTELLRSLFFSLTWAISYRTGIRLRGAVLGLLYKKIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 370 KL-GPSRPPTGEVLNLLGTDSERLLNFAGSFHEAWGLPLQL----AITLYLL--YQQVGMAFLAGLVLAlllvpvnKVIA 442
Cdd:cd18592 84 RLrSLGDKSVGELINIFSNDGQRLFDAAVFGPLVIGGPVVLilgiVYSTYLLgpWALLGMLVFLLFYPL-------QAFI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 443 TRIMAS-NQEMLRHKDARVKLMTELLSGIRVIKFFRWEQALGDRVKACRTKELGRLRVIKYLDAACVYLWAALPVVICIT 521
Cdd:cd18592 157 AKLTGKfRRKAIVITDKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERKILEKAGYLQSISISLAPIVPVIASVV 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1039753390 522 IFITYVLMGHQLTATKVFTALALVRMLILPLNNFPWVINGLLESKVSLDRI 572
Cdd:cd18592 237 TFLAHVALGNDLTAAQAFTVIAVFNSMRFSLRMLPYAVKALAEAKVALQRI 287
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
622-802 |
1.70e-28 |
|
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: 112.48 E-value: 1.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGEL-----------HRLCGWvAVSELSKGFGLATQEPWIQCATIRDNILfgkt 690
Cdd:cd03228 23 LTIKPGEKVAIVGPSGSGKSTLLKLLLRLYdptsgeilidgVDLRDL-DLESLRKNIAYVPQDPFLFSGTIRENIL---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 691 fdaqlyrevleacalnddlsilpagdqtevgekgvtlSGGQRARIALARAVYQEKALYLLDDPLAAVDADvANHLLHRCI 770
Cdd:cd03228 98 -------------------------------------SGGQRQRIAIARALLRDPPILILDEATSALDPE-TEALILEAL 139
|
170 180 190
....*....|....*....|....*....|..
gi 1039753390 771 LGVLSHTTRLLCTHRTEYLERADVVLLMEAGQ 802
Cdd:cd03228 140 RALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
621-813 |
2.10e-27 |
|
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: 111.55 E-value: 2.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 621 HLQVKKGMLVGIVGKVGCGKSSLLAAITgelhRLCGW--------------VAVSELSKGFGLATQEPWIQCATIRDNIL 686
Cdd:cd03254 23 NFSIKPGETVAIVGPTGAGKTTLINLLM----RFYDPqkgqilidgidirdISRKSLRSMIGVVLQDTFLFSGTIMENIR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 687 FGK-TFDAQLYREVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANhL 765
Cdd:cd03254 99 LGRpNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEK-L 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1039753390 766 LHRCILGVLSHTTRLLCTHRTEYLERADVVLLMEAGQLVRTGPPSEIL 813
Cdd:cd03254 178 IQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
622-813 |
2.58e-27 |
|
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: 111.48 E-value: 2.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAI-------TGEL----HRLCGwVAVSELSKGFGLATQEPWIQCATIRDNILFGKt 690
Cdd:cd03249 24 LTIPPGKTVALVGSSGCGKSTVVSLLerfydptSGEIlldgVDIRD-LNLRWLRSQIGLVSQEPVLFDGTIAENIRYGK- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 691 FDAQLyREVLEAC--ALNDDLSI-LPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDAD---VANH 764
Cdd:cd03249 102 PDATD-EEVEEAAkkANIHDFIMsLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAEsekLVQE 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1039753390 765 LLHRCILGvlshTTRLLCTHRTEYLERADVVLLMEAGQLVRTGPPSEIL 813
Cdd:cd03249 181 ALDRAMKG----RTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELM 225
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
621-807 |
7.77e-27 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 116.87 E-value: 7.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 621 HLQVKKGMLVGIVGKVGCGKSSLLAAITG-------------ELHRL--------CGWVAvselskgfglatQEPWIQCA 679
Cdd:PRK11174 370 NFTLPAGQRIALVGPSGAGKTSLLNALLGflpyqgslkingiELRELdpeswrkhLSWVG------------QNPQLPHG 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 680 TIRDNILFGKTF--DAQLYrEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAV 757
Cdd:PRK11174 438 TLRDNVLLGNPDasDEQLQ-QALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASL 516
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1039753390 758 DADVANHLLhRCILGVLSHTTRLLCTHRTEYLERADVVLLMEAGQLVRTG 807
Cdd:PRK11174 517 DAHSEQLVM-QALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQG 565
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
622-813 |
8.96e-27 |
|
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: 109.63 E-value: 8.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAIT-------GEL----HRLCGwVAVSELSKGFGLATQEPWIQCATIRDNILFGKt 690
Cdd:cd03251 23 LDIPAGETVALVGPSGSGKSTLVNLIPrfydvdsGRIlidgHDVRD-YTLASLRRQIGLVSQDVFLFNDTVAENIAYGR- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 691 FDAQL--YREVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDaDVANHLLHR 768
Cdd:cd03251 101 PGATReeVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALD-TESERLVQA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1039753390 769 CILGVLSHTTRLLCTHRTEYLERADVVLLMEAGQLVRTGPPSEIL 813
Cdd:cd03251 180 ALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELL 224
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
503-785 |
2.22e-26 |
|
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: 114.77 E-value: 2.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 503 LDAACVYLWAALPVVICITIFITYVlMGHQLT----ATKVFTALALVRmlilPLNNFPWVINGLLESKVSLDRIQRFLDL 578
Cdd:TIGR02868 239 LGAALTLLAAGLAVLGALWAGGPAV-ADGRLApvtlAVLVLLPLAAFE----AFAALPAAAQQLTRVRAAAERIVEVLDA 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 579 PSYSPEAYYSPDPPAEPSTA-LELHEALFSWDPiGASQKTFIShLQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGW 657
Cdd:TIGR02868 314 AGPVAEGSAPAAGAVGLGKPtLELRDLSAGYPG-APPVLDGVS-LDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGE 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 658 VAV----------SELSKGFGLATQEPWIQCATIRDNILFGK--TFDAQLYReVLEACALNDDLSILPAGDQTEVGEKGV 725
Cdd:TIGR02868 392 VTLdgvpvssldqDEVRRRVSVCAQDAHLFDTTVRENLRLARpdATDEELWA-ALERVGLADWLRALPDGLDTVLGEGGA 470
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 726 TLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHRcILGVLSHTTRLLCTHR 785
Cdd:TIGR02868 471 RLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLED-LLAALSGRTVVLITHH 529
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
622-813 |
2.98e-24 |
|
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: 102.56 E-value: 2.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITG----ELHRLC------GWVAVSELSKGFGLATQEPWIQCATIRDNILFGKTf 691
Cdd:cd03252 23 LRIKPGEVVGIVGRSGSGKSTLTKLIQRfyvpENGRVLvdghdlALADPAWLRRQVGVVLQENVLFNRSIRDNIALADP- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 692 dAQLYREVLEACAL---NDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADvANHLLHR 768
Cdd:cd03252 102 -GMSMERVIEAAKLagaHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYE-SEHAIMR 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1039753390 769 CILGVLSHTTRLLCTHRTEYLERADVVLLMEAGQLVRTGPPSEIL 813
Cdd:cd03252 180 NMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELL 224
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
622-809 |
6.26e-24 |
|
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: 101.03 E-value: 6.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAitgeLHRLcgwvavSELSKG--------------------FGLATQEPWIQCATI 681
Cdd:cd03244 25 FSIKPGEKVGIVGRTGSGKSSLLLA----LFRL------VELSSGsilidgvdiskiglhdlrsrISIIPQDPVLFSGTI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 682 RDNI-LFGKTFDAQLYrEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDAD 760
Cdd:cd03244 95 RSNLdPFGEYSDEELW-QALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1039753390 761 VAnHLLHRCILGVLSHTTRLLCTHRTEYLERADVVLLMEAGQLVRTGPP 809
Cdd:cd03244 174 TD-ALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
599-807 |
4.02e-22 |
|
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: 94.69 E-value: 4.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 599 LELHEALFSWDPigaSQKTFISH--LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVSE---------LSKGF 667
Cdd:cd03247 1 LSINNVSFSYPE---QEQQVLKNlsLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGvpvsdlekaLSSLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 668 GLATQEPWIQCATIRDNIlfgktfdaqlyrevleacalnddlsilpagdqtevgekGVTLSGGQRARIALARAVYQEKAL 747
Cdd:cd03247 78 SVLNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 748 YLLDDPLAAVDADVANHLLhRCILGVLSHTTRLLCTHRTEYLERADVVLLMEAGQLVRTG 807
Cdd:cd03247 120 VLLDEPTVGLDPITERQLL-SLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
621-808 |
1.70e-21 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 99.79 E-value: 1.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 621 HLQVKKGMLVGIVGKVGCGKSSLLAAI-------TGE-------LHRLcgwvAVSELSKGFGLATQEPWIQCATIRDNIL 686
Cdd:PRK10789 335 NFTLKPGQMLGICGPTGSGKSTLLSLIqrhfdvsEGDirfhdipLTKL----QLDSWRSRLAVVSQTPFLFSDTVANNIA 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 687 FGKTfDA--QLYREVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANH 764
Cdd:PRK10789 411 LGRP-DAtqQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQ 489
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1039753390 765 LLHRcilgvLS----HTTRLLCTHRTEYLERADVVLLMEAGQLVRTGP 808
Cdd:PRK10789 490 ILHN-----LRqwgeGRTVIISAHRLSALTEASEILVMQHGHIAQRGN 532
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
624-813 |
3.49e-21 |
|
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: 93.45 E-value: 3.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 624 VKKGMLVGIVGKVGCGKSSLL-------------AAITGELHRLcgwVAVSELSKGFGLATQEPWIQCATIRDNILFGK- 689
Cdd:cd03253 24 IPAGKKVAIVGPSGSGKSTILrllfrfydvssgsILIDGQDIRE---VTLDSLRRAIGVVPQDTVLFNDTIGYNIRYGRp 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 690 -TFDAQLYrEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDAdVANHLLHR 768
Cdd:cd03253 101 dATDEEVI-EAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDT-HTEREIQA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1039753390 769 CILGVLSHTTRLLCTHRTEYLERADVVLLMEAGQLVRTGPPSEIL 813
Cdd:cd03253 179 ALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELL 223
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
541-822 |
3.81e-21 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 98.67 E-value: 3.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 541 ALALVRMLIlplNNfpWviNGLLESKVSLDRIQRFLDlpSYSPEAYYSPDPpaEPSTALELhEALfSWDPIGASQKTF-- 618
Cdd:COG4618 284 ALAPIEQAI---GG--W--KQFVSARQAYRRLNELLA--AVPAEPERMPLP--RPKGRLSV-ENL-TVVPPGSKRPILrg 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 619 IShLQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWV-----AVS-----ELSKGFGLATQEPWIQCATIRDNI-LF 687
Cdd:COG4618 351 VS-FSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVrldgaDLSqwdreELGRHIGYLPQDVELFDGTIAENIaRF 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 688 GKTfDAQlyrEVLEACALND--DLsI--LPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVAN 763
Cdd:COG4618 430 GDA-DPE---KVVAAAKLAGvhEM-IlrLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEA 504
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 764 HLLhRCILGVLSH-TTRLLCTHRTEYLERADVVLLMEAGQLVRTGPPSEILPLVQAVPTA 822
Cdd:COG4618 505 ALA-AAIRALKARgATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLARLARPAAA 563
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
465-812 |
4.30e-21 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 99.41 E-value: 4.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 465 ELLSGIRVIKFFRWEQALGDR--VKACRTKELGRLRVIKYLdaacVYLWAAlpVVICITIFITYVLMGHQLTATKVFTAL 542
Cdd:TIGR00958 345 EALSGMRTVRSFAAEEGEASRfkEALEETLQLNKRKALAYA----GYLWTT--SVLGMLIQVLVLYYGGQLVLTGKVSSG 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 543 ALVRMLILP------LNNFPWVINGLLESKVSLDRIQRFLDL-PSYSPEAYYSPDPPaepSTALELHEALFSWdPIGASQ 615
Cdd:TIGR00958 419 NLVSFLLYQeqlgeaVRVLSYVYSGMMQAVGASEKVFEYLDRkPNIPLTGTLAPLNL---EGLIEFQDVSFSY-PNRPDV 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 616 KTFIS-HLQVKKGMLVGIVGKVGCGKSSLLAAI-------TGELhrLCGWVAVSE-----LSKGFGLATQEPWIQCATIR 682
Cdd:TIGR00958 495 PVLKGlTFTLHPGEVVALVGPSGSGKSTVAALLqnlyqptGGQV--LLDGVPLVQydhhyLHRQVALVGQEPVLFSGSVR 572
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 683 DNILFGKTF--DAQLYREVLEACAlNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDAD 760
Cdd:TIGR00958 573 ENIAYGLTDtpDEEIMAAAKAANA-HDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAE 651
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1039753390 761 VaNHLLH--RCILGvlshTTRLLCTHRTEYLERADVVLLMEAGQLVRTGPPSEI 812
Cdd:TIGR00958 652 C-EQLLQesRSRAS----RTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQL 700
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
622-803 |
1.48e-20 |
|
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: 91.38 E-value: 1.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLlAAITGELHRLC-GWVAVSE----------LSKGFGLATQEPWIQCATIRDNILFG-K 689
Cdd:cd03248 35 FTLHPGEVTALVGPSGSGKSTV-VALLENFYQPQgGQVLLDGkpisqyehkyLHSKVSLVGQEPVLFARSLQDNIAYGlQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 690 TFDAQLYREVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADvANHLLHRC 769
Cdd:cd03248 114 SCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE-SEQQVQQA 192
|
170 180 190
....*....|....*....|....*....|....
gi 1039753390 770 ILGVLSHTTRLLCTHRTEYLERADVVLLMEAGQL 803
Cdd:cd03248 193 LYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
622-807 |
2.37e-19 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 87.57 E-value: 2.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGeLHRLCG---------WVAVSELSKGFGLATQE----PWIqcaTIRDNILFG 688
Cdd:cd03259 21 LTVEPGEFLALLGPSGCGKTTLLRLIAG-LERPDSgeilidgrdVTGVPPERRNIGMVFQDyalfPHL---TVAENIAFG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 689 ----KTFDAQLYREVLEACALNDDLSILpagdqtevGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANH 764
Cdd:cd03259 97 lklrGVPKAEIRARVRELLELVGLEGLL--------NRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREE 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1039753390 765 LLHRcILGVLS--HTTRLLCTH-RTEYLERADVVLLMEAGQLVRTG 807
Cdd:cd03259 169 LREE-LKELQRelGITTIYVTHdQEEALALADRIAVMNEGRIVQVG 213
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
568-813 |
4.07e-19 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 93.50 E-value: 4.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 568 SLDRIQRFLDLPSYSPEAYYSPDPPAepstalelhealfSWdPIGASQKTFISHLQVKKGM---------------LVGI 632
Cdd:PLN03232 1202 SVERVGNYIDLPSEATAIIENNRPVS-------------GW-PSRGSIKFEDVHLRYRPGLppvlhglsffvspseKVGV 1267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 633 VGKVGCGKSSLLAAI--TGELHRlcGWVAV----------SELSKGFGLATQEPWIQCATIRDNI-LFGKTFDAQLYrEV 699
Cdd:PLN03232 1268 VGRTGAGKSSMLNALfrIVELEK--GRIMIddcdvakfglTDLRRVLSIIPQSPVLFSGTVRFNIdPFSEHNDADLW-EA 1344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 700 LEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVaNHLLHRCILGVLSHTTR 779
Cdd:PLN03232 1345 LERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRT-DSLIQRTIREEFKSCTM 1423
|
250 260 270
....*....|....*....|....*....|....
gi 1039753390 780 LLCTHRTEYLERADVVLLMEAGQLVRTGPPSEIL 813
Cdd:PLN03232 1424 LVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELL 1457
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
622-816 |
4.50e-19 |
|
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: 87.14 E-value: 4.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELH------RLCGwVAVSELSKGFGLATQE----PWiqcATIRDNILFGKTF 691
Cdd:cd03293 25 LSVEEGEFVALVGPSGCGKSTLLRIIAGLERptsgevLVDG-EPVTGPGPDRGYVFQQdallPW---LTVLDNVALGLEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 692 ----DAQLYREVLEACALnddlsilpagdqteVGEKGV------TLSGGQRARIALARAVYQEKALYLLDDPLAAVDADV 761
Cdd:cd03293 101 qgvpKAEARERAEELLEL--------------VGLSGFenayphQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 762 ANHlLHRCILGVLSHT--TRLLCTHRTE---YLerADVVLLMeagqlvrTGPPSEILPLV 816
Cdd:cd03293 167 REQ-LQEELLDIWRETgkTVLLVTHDIDeavFL--ADRVVVL-------SARPGRIVAEV 216
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
517-807 |
4.54e-19 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 92.33 E-value: 4.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 517 VICITIFITYVLMGHQLTATKVFTALALVRMLILPLNNFPWVINGLLESKVsldRIQRFLDLPSYSPEAYYSPD--PPAE 594
Cdd:PRK13657 254 MLAILVLGAALVQKGQLRVGEVVAFVGFATLLIGRLDQVVAFINQVFMAAP---KLEEFFEVEDAVPDVRDPPGaiDLGR 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 595 PSTALELHEALFSWDpiGASQKTFISHLQVKKGMLVGIVGKVGCGKSSLLAAitgeLHRL--------------CGWVAV 660
Cdd:PRK13657 331 VKGAVEFDDVSFSYD--NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINL----LQRVfdpqsgrilidgtdIRTVTR 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 661 SELSKGFGLATQEPWIQCATIRDNILFGKT--FDAQLyREVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALA 738
Cdd:PRK13657 405 ASLRRNIAVVFQDAGLFNRSIEDNIRVGRPdaTDEEM-RAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIA 483
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039753390 739 RAVYQEKALYLLDDPLAAVDAdVANHLLHRCILGVLSHTTRLLCTHRTEYLERADVVLLMEAGQLVRTG 807
Cdd:PRK13657 484 RALLKDPPILILDEATSALDV-ETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESG 551
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
622-812 |
5.36e-19 |
|
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: 87.39 E-value: 5.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVA-----VSELS---KGFGLATQE-PWIQCATIRDNILFG---- 688
Cdd:cd03296 23 LDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILfggedATDVPvqeRNVGFVFQHyALFRHMTVFDNVAFGlrvk 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 689 -------KTFDAQLYREVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADV 761
Cdd:cd03296 103 prserppEAEIRAKVHELLKLVQLDWLADRYPA-----------QLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKV 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039753390 762 ANHL------LHRCIlgvlsHTTRLLCTH-RTEYLERADVVLLMEAGQLVRTGPPSEI 812
Cdd:cd03296 172 RKELrrwlrrLHDEL-----HVTTVFVTHdQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
622-813 |
7.48e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 91.42 E-value: 7.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAIT-------GEL----HRLCGWvAVSELSKGFGLATQEPWIQCATIRDNILFGK- 689
Cdd:PRK11160 361 LQIKAGEKVALLGRTGCGKSTLLQLLTrawdpqqGEIllngQPIADY-SEAALRQAISVVSQRVHLFSATLRDNLLLAAp 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 690 -TFDAQLyREVLEACALnDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLhR 768
Cdd:PRK11160 440 nASDEAL-IEVLQQVGL-EKLLEDDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQIL-E 516
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1039753390 769 CILGVLSHTTRLLCTHRTEYLERADVVLLMEAGQLVRTGPPSEIL 813
Cdd:PRK11160 517 LLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELL 561
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
621-755 |
7.62e-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: 84.24 E-value: 7.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 621 HLQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWV----------AVSELSKGFGLATQEPWIQCA-TIRDNILFG- 688
Cdd:pfam00005 5 SLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTIlldgqdltddERKSLRKEIGYVFQDPQLFPRlTVRENLRLGl 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039753390 689 -------KTFDAQLYrEVLEACALNDDLSilpagdqTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLA 755
Cdd:pfam00005 85 llkglskREKDARAE-EALEKLGLGDLAD-------RPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
622-801 |
2.20e-18 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 85.91 E-value: 2.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGeLHR------LCGWVAVSELSKGFGLATQE----PWiqcATIRDNILFG--- 688
Cdd:COG1116 32 LTVAAGEFVALVGPSGCGKSTLLRLIAG-LEKptsgevLVDGKPVTGPGPDRGVVFQEpallPW---LTVLDNVALGlel 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 689 ----KTFDAQLYREVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANH 764
Cdd:COG1116 108 rgvpKAERRERARELLELVGLAGFEDAYPH-----------QLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRER 176
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1039753390 765 lLHRCILGVL--SHTTRLLCTHRTE---YLerADVVLLMEAG 801
Cdd:COG1116 177 -LQDELLRLWqeTGKTVLFVTHDVDeavFL--ADRVVVLSAR 215
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
622-803 |
1.34e-17 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 82.56 E-value: 1.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAI-------TGELH---RLCGWVAVSELSKGFGLATQEP-WIQcATIRDNILF--- 687
Cdd:COG4619 21 LTLEAGECVAITGPSGSGKSTLLRALadldpptSGEIYldgKPLSAMPPPEWRRQVAYVPQEPaLWG-GTVRDNLPFpfq 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 688 --GKTFDAQLYREVLEACALNDDlsILpagdQTEVGEkgvtLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVAnHL 765
Cdd:COG4619 100 lrERKFDRERALELLERLGLPPD--IL----DKPVER----LSGGERQRLALIRALLLQPDVLLLDEPTSALDPENT-RR 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1039753390 766 LHRCILGVLSH--TTRLLCTHRTEYLER-ADVVLLMEAGQL 803
Cdd:COG4619 169 VEELLREYLAEegRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
621-812 |
1.43e-17 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 83.00 E-value: 1.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 621 HLQVKKGMLVGIVGKVGCGKSSLL------------AAITGELH----RLCGW-VAVSELSKGFGLATQEPWIQCATIRD 683
Cdd:cd03260 20 SLDIPKGEITALIGPSGCGKSTLLrllnrlndlipgAPDEGEVLldgkDIYDLdVDVLELRRRVGMVFQKPNPFPGSIYD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 684 NILFG--------KTFDAQLYREVLEACALNDDLSilpagDQTevgeKGVTLSGGQRARIALARAVYQEKALYLLDDPLA 755
Cdd:cd03260 100 NVAYGlrlhgiklKEELDERVEEALRKAALWDEVK-----DRL----HALGLSGGQQQRLCLARALANEPEVLLLDEPTS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039753390 756 AVDAdVANHLLHRCILGVLSHTTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEI 812
Cdd:cd03260 171 ALDP-ISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
622-838 |
1.46e-17 |
|
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: 87.27 E-value: 1.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGEL---HRLCGWVAV----------SELSKGFGLATQEPWIQ--CATIRDNIL 686
Cdd:COG1123 27 LTIAPGETVALVGESGSGKSTLALALMGLLphgGRISGEVLLdgrdllelseALRGRRIGMVFQDPMTQlnPVTVGDQIA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 687 FG----KTFDAQLYREVLEACALnddlsilpAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVA 762
Cdd:COG1123 107 EAlenlGLSRAEARARVLELLEA--------VGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQ 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 763 NHLLHR-CILGVLSHTTRLLCTHRTEY-LERADVVLLMEAGQLVRTGPPSEILPLVQ---AVPTAWAEKEQVATSGQSPS 837
Cdd:COG1123 179 AEILDLlRELQRERGTTVLLITHDLGVvAEIADRVVVMDDGRIVEDGPPEEILAAPQalaAVPRLGAARGRAAPAAAAAE 258
|
.
gi 1039753390 838 V 838
Cdd:COG1123 259 P 259
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
622-802 |
1.98e-17 |
|
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: 82.13 E-value: 1.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVS----------ELSKGFGLATQEPWIQ--CATIRDNILFG- 688
Cdd:cd03225 22 LTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDgkdltklslkELRRKVGLVFQNPDDQffGPTVEEEVAFGl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 689 ------KTFDAQLYREVLEACALND--DLSILpagdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAVDAD 760
Cdd:cd03225 102 enlglpEEEIEERVEEALELVGLEGlrDRSPF-------------TLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1039753390 761 VANHLLHrcILGVL--SHTTRLLCTHRTEYLER-ADVVLLMEAGQ 802
Cdd:cd03225 169 GRRELLE--LLKKLkaEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
622-813 |
3.44e-17 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 81.61 E-value: 3.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELH------RLCGWV----AVSELSKGFGLATQEPWIQ--CATIRDNILFG- 688
Cdd:COG1122 22 LSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKptsgevLVDGKDitkkNLRELRRKVGLVFQNPDDQlfAPTVEEDVAFGp 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 689 -------KTFDAQLyREVLEACALND--DLSILpagdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAVDA 759
Cdd:COG1122 102 enlglprEEIRERV-EEALELVGLEHlaDRPPH-------------ELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039753390 760 DVANHLLHrcILGVL--SHTTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEIL 813
Cdd:COG1122 168 RGRRELLE--LLKRLnkEGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVF 222
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
622-802 |
8.03e-17 |
|
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: 78.83 E-value: 8.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGwvavselskgfglatqepwiqcatirdNILFGKTFDAQLYREvle 701
Cdd:cd00267 20 LTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSG---------------------------EILIDGKDIAKLPLE--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 702 acALNDDLSILPagdQtevgekgvtLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVAnHLLHRCILGVL-SHTTRL 780
Cdd:cd00267 70 --ELRRRIGYVP---Q---------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASR-ERLLELLRELAeEGRTVI 134
|
170 180
....*....|....*....|...
gi 1039753390 781 LCTHRTEYLERA-DVVLLMEAGQ 802
Cdd:cd00267 135 IVTHDPELAELAaDRVIVLKDGK 157
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
621-803 |
1.84e-16 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 80.49 E-value: 1.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 621 HLQVKKGMLVGIVGKVGCGKSSLL-------AAITGELhrLCGWVAVSELSKGFGLATQE----PWiqcATIRDNI---L 686
Cdd:PRK11247 32 DLHIPAGQFVAVVGRSGCGKSTLLrllagleTPSAGEL--LAGTAPLAEAREDTRLMFQDarllPW---KKVIDNVglgL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 687 FGKTFDAQLyrEVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADV---AN 763
Cdd:PRK11247 107 KGQWRDAAL--QALAAVGLADRANEWPA-----------ALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTrieMQ 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1039753390 764 HLLHRciLGVLSHTTRLLCTHR-TEYLERADVVLLMEAGQL 803
Cdd:PRK11247 174 DLIES--LWQQHGFTVLLVTHDvSEAVAMADRVLLIEEGKI 212
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
623-809 |
1.99e-16 |
|
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: 78.99 E-value: 1.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 623 QVKKGMLVGIVGKVGCGKSSLLAAI-------TGELH---RLCGWVAVSELSKGFGLATQEPWIQCATIRDNI-LFGKTF 691
Cdd:cd03369 30 KVKAGEKIGIVGRTGAGKSTLILALfrfleaeEGKIEidgIDISTIPLEDLRSSLTIIPQDPTLFSGTIRSNLdPFDEYS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 692 DAQLYrEVLEacalnddlsilpagdqteVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADvANHLLHRCIL 771
Cdd:cd03369 110 DEEIY-GALR------------------VSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYA-TDALIQKTIR 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 1039753390 772 GVLSHTTRLLCTHRTEYLERADVVLLMEAGQLVRTGPP 809
Cdd:cd03369 170 EEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
567-813 |
2.64e-16 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 83.61 E-value: 2.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 567 VSLDRIQRFLDlpsySPEAYYSPDPPAEPSTALELHEALFSWDpigaSQKTFISH--LQVKKGMLVGIVGKVGCGKSSLL 644
Cdd:PRK10790 313 VAGERVFELMD----GPRQQYGNDDRPLQSGRIDIDNVSFAYR----DDNLVLQNinLSVPSRGFVALVGHTGSGKSTLA 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 645 AAITGELHRLCGWV-----AVSELS-----KGFGLATQEPWIQCATIRDNILFGKTFDAQLYREVLEACALNDDLSILPA 714
Cdd:PRK10790 385 SLLMGYYPLTEGEIrldgrPLSSLShsvlrQGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPD 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 715 GDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADvANHLLHRCILGVLSHTTRLLCTHRTEYLERADV 794
Cdd:PRK10790 465 GLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSG-TEQAIQQALAAVREHTTLVVIAHRLSTIVEADT 543
|
250
....*....|....*....
gi 1039753390 795 VLLMEAGQLVRTGPPSEIL 813
Cdd:PRK10790 544 ILVLHRGQAVEQGTHQQLL 562
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
621-803 |
3.80e-16 |
|
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: 77.26 E-value: 3.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 621 HLQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAV----------SELSKGFGLATQEPWIQCATIRDNILfgkt 690
Cdd:cd03246 22 SFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLdgadisqwdpNELGDHVGYLPQDDELFSGSIAENIL---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 691 fdaqlyrevleacalnddlsilpagdqtevgekgvtlSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHRCI 770
Cdd:cd03246 98 -------------------------------------SGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIA 140
|
170 180 190
....*....|....*....|....*....|...
gi 1039753390 771 LGVLSHTTRLLCTHRTEYLERADVVLLMEAGQL 803
Cdd:cd03246 141 ALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
621-803 |
6.17e-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: 77.92 E-value: 6.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 621 HLQVKKGMLVGIVGKVGCGKSSLLAAIT-------GELhRLCGwVAVSELSKG----------------FGLatqepwIQ 677
Cdd:cd03255 24 SLSIEKGEFVAIVGPSGSGKSTLLNILGgldrptsGEV-RVDG-TDISKLSEKelaafrrrhigfvfqsFNL------LP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 678 CATIRDNILFGKTF-------DAQLYREVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKALYLL 750
Cdd:cd03255 96 DLTALENVELPLLLagvpkkeRRERAEELLERVGLGDRLNHYPS-----------ELSGGQQQRVAIARALANDPKIILA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039753390 751 DDPLAAVDADVANHLLHrcILGVLSH---TTRLLCTHRTEYLERADVVLLMEAGQL 803
Cdd:cd03255 165 DEPTGNLDSETGKEVME--LLRELNKeagTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
622-813 |
8.17e-16 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 78.16 E-value: 8.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAV----------SELSKGFGLATQEPWIQCA-TIRDNILFGKT 690
Cdd:COG1120 22 LSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLdgrdlaslsrRELARRIAYVPQEPPAPFGlTVRELVALGRY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 691 --------FDAQLYREVLEACAlnddlsilpagdQTEVG---EKGV-TLSGGQRARIALARAVYQEKALYLLDDPLAAVD 758
Cdd:COG1120 102 phlglfgrPSAEDREAVEEALE------------RTGLEhlaDRPVdELSGGERQRVLIARALAQEPPLLLLDEPTSHLD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039753390 759 advANHLLHrcILGVLSHTTR------LLCTH------RTeylerADVVLLMEAGQLVRTGPPSEIL 813
Cdd:COG1120 170 ---LAHQLE--VLELLRRLARergrtvVMVLHdlnlaaRY-----ADRLVLLKDGRIVAQGPPEEVL 226
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
568-825 |
1.07e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 82.48 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 568 SLDRIQRFLDLPSYSPEAYYS--PdPPAEPST-ALELHEALFSWDP------------IGASQKtfishlqvkkgmlVGI 632
Cdd:PLN03130 1205 AVERVGTYIDLPSEAPLVIENnrP-PPGWPSSgSIKFEDVVLRYRPelppvlhglsfeISPSEK-------------VGI 1270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 633 VGKVGCGKSSLLAAI--TGELHRLCGWV--------AVSELSKGFGLATQEPWIQCATIRDNI-LFGKTFDAQLYrEVLE 701
Cdd:PLN03130 1271 VGRTGAGKSSMLNALfrIVELERGRILIdgcdiskfGLMDLRKVLGIIPQAPVLFSGTVRFNLdPFNEHNDADLW-ESLE 1349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 702 ACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADvANHLLHRCILGVLSHTTRLL 781
Cdd:PLN03130 1350 RAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVR-TDALIQKTIREEFKSCTMLI 1428
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1039753390 782 CTHRTEYLERADVVLLMEAGQLVRTGPPSEILP--------LVQAVPTAWAE 825
Cdd:PLN03130 1429 IAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSnegsafskMVQSTGAANAQ 1480
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
622-813 |
1.20e-15 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 79.42 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELH------RLCGWVAVSELS---KGFGLATQEPwiqcA-----TIRDNILF 687
Cdd:COG1118 23 LEIASGELVALLGPSGSGKTTLLRIIAGLETpdsgriVLNGRDLFTNLPpreRRVGFVFQHY----AlfphmTVAENIAF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 688 G----KTFDAQLYREVLEacaLnddLSIL---------PAgdQtevgekgvtLSGGQRARIALARAVYQEKALYLLDDPL 754
Cdd:COG1118 99 GlrvrPPSKAEIRARVEE---L---LELVqlegladryPS--Q---------LSGGQRQRVALARALAVEPEVLLLDEPF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039753390 755 AAVDADVANHL------LHRCIlgvlsHTTRLLCTH-RTEYLERADVVLLMEAGQLVRTGPPSEIL 813
Cdd:COG1118 162 GALDAKVRKELrrwlrrLHDEL-----GGTTVFVTHdQEEALELADRVVVMNQGRIEQVGTPDEVY 222
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
621-807 |
1.47e-15 |
|
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: 76.56 E-value: 1.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 621 HLQVK---KGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVS-----ELSKGFGLATQEPWI-----QCA-----TIR 682
Cdd:cd03297 14 TLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNgtvlfDSRKKINLPPQQRKIglvfqQYAlfphlNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 683 DNILFGKTF-----DAQLYREVLEACALnddlsilpagdqTEVGEKGV-TLSGGQRARIALARAVYQEKALYLLDDPLAA 756
Cdd:cd03297 94 ENLAFGLKRkrnreDRISVDELLDLLGL------------DHLLNRYPaQLSGGEKQRVALARALAAQPELLLLDEPFSA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1039753390 757 VDADVANHLLH--RCILGVLsHTTRLLCTHRTEYLER-ADVVLLMEAGQLVRTG 807
Cdd:cd03297 162 LDRALRLQLLPelKQIKKNL-NIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
622-817 |
1.68e-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: 77.16 E-value: 1.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVS-------------ELSKGFGLATQepwiQCA-----TIRD 683
Cdd:cd03261 21 LDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDgedisglseaelyRLRRRMGMLFQ----SGAlfdslTVFE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 684 NILFG----KTFDAQLYREV----LEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLA 755
Cdd:cd03261 97 NVAFPlrehTRLSEEEIREIvlekLEAVGLRGAEDLYPA-----------ELSGGMKKRVALARALALDPELLLYDEPTA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 756 AVD---ADVANHLLHRciLGVLSHTTRLLCTHR-TEYLERADVVLLMEAGQLVRTGPPSEIL----PLVQ 817
Cdd:cd03261 166 GLDpiaSGVIDDLIRS--LKKELGLTSIMVTHDlDTAFAIADRIAVLYDGKIVAEGTPEELRasddPLVR 233
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
621-813 |
9.08e-15 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 74.89 E-value: 9.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 621 HLQVKKGMLVGIVGKVGCGKSSLLAAITGELH------RLCGWVAVSELSK----------GFGLatqePWIQcaTIRDN 684
Cdd:COG4555 21 SFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKpdsgsiLIDGEDVRKEPREarrqigvlpdERGL----YDRL--TVREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 685 ILFgktFdAQLYREVLEACALNDDlSILPAGDQTEVGEKGV-TLSGGQRARIALARAVYQEKALYLLDDPLAAVDADvAN 763
Cdd:COG4555 95 IRY---F-AELYGLFDEELKKRIE-ELIELLGLEEFLDRRVgELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVM-AR 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1039753390 764 HLLHRCILGVLSH-TTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEIL 813
Cdd:COG4555 169 RLLREILRALKKEgKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELR 220
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
507-813 |
1.62e-14 |
|
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: 78.45 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 507 CVYLWAALPVVICitifityvlmGHQLTATKVFTALALVRMLILPLNnfpWVINGLLESKVSLDRIQRFLDLPSYSPEAY 586
Cdd:TIGR00957 1201 CIVLFAALFAVIS----------RHSLSAGLVGLSVSYSLQVTFYLN---WLVRMSSEMETNIVAVERLKEYSETEKEAP 1267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 587 YSPDPPAEPSTalelhealfsWDPIGASQ------------KTFISHLQV--KKGMLVGIVGKVGCGKSSL-------LA 645
Cdd:TIGR00957 1268 WQIQETAPPSG----------WPPRGRVEfrnyclryredlDLVLRHINVtiHGGEKVGIVGRTGAGKSSLtlglfriNE 1337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 646 AITGELhRLCGW----VAVSELSKGFGLATQEPWIQCATIRDNI-LFGKTFDAQLYReVLEACALNDDLSILPAGDQTEV 720
Cdd:TIGR00957 1338 SAEGEI-IIDGLniakIGLHDLRFKITIIPQDPVLFSGSLRMNLdPFSQYSDEEVWW-ALELAHLKTFVSALPDKLDHEC 1415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 721 GEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANhLLHRCILGVLSHTTRLLCTHRTEYLERADVVLLMEA 800
Cdd:TIGR00957 1416 AEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDN-LIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDK 1494
|
330
....*....|...
gi 1039753390 801 GQLVRTGPPSEIL 813
Cdd:TIGR00957 1495 GEVAEFGAPSNLL 1507
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
622-813 |
3.87e-14 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 76.60 E-value: 3.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAIT-------GEL----HRLCGWvAVSELSKGFGLATQEPWIQCATIRDNILFGKT 690
Cdd:PRK11176 364 FKIPAGKTVALVGRSGSGKSTIANLLTrfydideGEIlldgHDLRDY-TLASLRNQVALVSQNVHLFNDTIANNIAYART 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 691 fdAQLYREVLE-----ACALnDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVanhl 765
Cdd:PRK11176 443 --EQYSREQIEeaarmAYAM-DFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTES---- 515
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1039753390 766 lHRCILGVLS----HTTRLLCTHRTEYLERADVVLLMEAGQLVRTGPPSEIL 813
Cdd:PRK11176 516 -ERAIQAALDelqkNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELL 566
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
622-813 |
4.38e-14 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 73.20 E-value: 4.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVselskgFGLATQEPWIQCA--------------TIRDNILF 687
Cdd:COG1121 27 LTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRL------FGKPPRRARRRIGyvpqraevdwdfpiTVRDVVLM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 688 G--------KTFDAQLYREVLEACALnddLSILPAGDQTeVGEkgvtLSGGQRARIALARAVYQEKALYLLDDPLAAVDA 759
Cdd:COG1121 101 GrygrrglfRRPSRADREAVDEALER---VGLEDLADRP-IGE----LSGGQQQRVLLARALAQDPDLLLLDEPFAGVDA 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039753390 760 DVANHLLHrcILGVLSH--TTRLLCTHRTEYLER-ADVVLLMeAGQLVRTGPPSEIL 813
Cdd:COG1121 173 ATEEALYE--LLRELRRegKTILVVTHDLGAVREyFDRVLLL-NRGLVAHGPPEEVL 226
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
287-572 |
6.05e-14 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 73.74 E-value: 6.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 287 LALGLLKM-VGTMLGFSGPLLLSLLVGFLEeGQEPLSHGLLYVLGLAGGTVISAVLQNQYGYEVRKVTLQARVAVLSTLY 365
Cdd:cd07346 1 LLLALLLLlLATALGLALPLLTKLLIDDVI-PAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 366 RKALKLGPS---RPPTGEVLNLLGTDSERLLNFAGS-FHEAWGLPLQLAITL-YLLYQQVGMAFLAGLVLALLLVPvNKV 440
Cdd:cd07346 80 RHLQRLSLSffdRNRTGDLMSRLTSDVDAVQNLVSSgLLQLLSDVLTLIGALvILFYLNWKLTLVALLLLPLYVLI-LRY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 441 IATRIMASNQEmLRHKDARV-KLMTELLSGIRVIKFFRWEQALGDRVKAcRTKELGRLRVIKYLDAACVYLWAALPVVIC 519
Cdd:cd07346 159 FRRRIRKASRE-VRESLAELsAFLQESLSGIRVVKAFAAEEREIERFRE-ANRDLRDANLRAARLSALFSPLIGLLTALG 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039753390 520 ITIFITY----VLMGhQLTATKVFTALALVRMLILPLNNFPWVINGLLESKVSLDRI 572
Cdd:cd07346 237 TALVLLYggylVLQG-SLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
614-807 |
1.20e-13 |
|
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: 71.03 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 614 SQKTFISH--LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAV-----SELSKGFGLATQE---PWIQCATIRD 683
Cdd:cd03235 10 GGHPVLEDvsFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVfgkplEKERKRIGYVPQRrsiDRDFPISVRD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 684 NIL--------FGKTFDAQLYREVLEAcalnddlsiLPAGDQTEVGEKGV-TLSGGQRARIALARAVYQEKALYLLDDPL 754
Cdd:cd03235 90 VVLmglyghkgLFRRLSKADKAKVDEA---------LERVGLSELADRQIgELSGGQQQRVLLARALVQDPDLLLLDEPF 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039753390 755 AAVDADVANHLLHrcILGVLSHTTR--LLCTH-RTEYLERADVVLLMeAGQLVRTG 807
Cdd:cd03235 161 AGVDPKTQEDIYE--LLRELRREGMtiLVVTHdLGLVLEYFDRVLLL-NRTVVASG 213
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
622-803 |
1.25e-13 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 69.73 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVselskgFGlatQEPWIQCATIRDNILFgktfdaqlyreVLE 701
Cdd:cd03230 21 LTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKV------LG---KDIKKEPEEVKRRIGY-----------LPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 702 ACALNDDLSilpagdqtevGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHrcILGVLS--HTTR 779
Cdd:cd03230 81 EPSLYENLT----------VRENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWE--LLRELKkeGKTI 148
|
170 180
....*....|....*....|....*
gi 1039753390 780 LLCTHRTEYLER-ADVVLLMEAGQL 803
Cdd:cd03230 149 LLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
621-807 |
1.63e-13 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 69.77 E-value: 1.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 621 HLQVKKGMLVGIVGKVGCGKSSLLAAITGELhrlcgwvavsELSKGfglatqepwiqcaTIRdniLFGKTFDAQLYREVL 700
Cdd:cd03214 19 SLSIEAGEIVGILGPNGAGKSTLLKTLAGLL----------KPSSG-------------EIL---LDGKDLASLSPKELA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 701 EACAlnddlsILP-AGDQTEVG---EKGV-TLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHrcILGVLS 775
Cdd:cd03214 73 RKIA------YVPqALELLGLAhlaDRPFnELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLE--LLRRLA 144
|
170 180 190
....*....|....*....|....*....|....*....
gi 1039753390 776 H---TTRLLCTHrteYLERA----DVVLLMEAGQLVRTG 807
Cdd:cd03214 145 RergKTVVMVLH---DLNLAaryaDRVILLKDGRIVAQG 180
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
569-822 |
1.70e-13 |
|
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: 74.17 E-value: 1.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 569 LDRIQRFLDLPSYSPEAYYSPDPPAEPSTALELHEALFSWDPIGASQKTFISH--LQVKKGMLVGIVGKVGCGKSSLLAA 646
Cdd:COG1123 231 LAAPQALAAVPRLGAARGRAAPAAAAAEPLLEVRNLSKRYPVRGKGGVRAVDDvsLTLRRGETLGLVGESGSGKSTLARL 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 647 ITG--------------ELHRLCGwVAVSELSKGFGLATQEPWIQ---CATIRDNI-----LFGKTFDAQLY---REVLE 701
Cdd:COG1123 311 LLGllrptsgsilfdgkDLTKLSR-RSLRELRRRVQMVFQDPYSSlnpRMTVGDIIaeplrLHGLLSRAERRervAELLE 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 702 ACALNDD-LSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAVD----ADVANHLLH-RCILGVls 775
Cdd:COG1123 390 RVGLPPDlADRYPH-----------ELSGGQRQRVAIARALALEPKLLILDEPTSALDvsvqAQILNLLRDlQRELGL-- 456
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039753390 776 htTRLLCTH---RTEYLerADVVLLMEAGQLVRTGPPSEIL--P-------LVQAVPTA 822
Cdd:COG1123 457 --TYLFISHdlaVVRYI--ADRVAVMYDGRIVEDGPTEEVFanPqhpytraLLAAVPSL 511
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
622-807 |
1.72e-13 |
|
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: 71.00 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAV-------------SELSKGFGLATQE------PWIqcaTIR 682
Cdd:cd03257 26 FSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFdgkdllklsrrlrKIRRKEIQMVFQDpmsslnPRM---TIG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 683 DNI-----LFGKTFDAQLYREV--LEACALNDDLSIL---PAgdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDD 752
Cdd:cd03257 103 EQIaeplrIHGKLSKKEARKEAvlLLLVGVGLPEEVLnryPH-----------ELSGGQRQRVAIARALALNPKLLIADE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039753390 753 PLAAVDADVAnhllhRCILGVLSH------TTRLLCTHRTEYLER-ADVVLLMEAGQLVRTG 807
Cdd:cd03257 172 PTSALDVSVQ-----AQILDLLKKlqeelgLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
622-812 |
1.75e-13 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 73.21 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVA-----VSELS---KGFGLATQEPwiqcA-----TIRDNILFG 688
Cdd:COG3842 26 LSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILldgrdVTGLPpekRNVGMVFQDY----AlfphlTVAENVAFG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 689 -------KTFDAQLYREVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARA-VYQEKALyLLDDPLAAVDAD 760
Cdd:COG3842 102 lrmrgvpKAEIRARVAELLELVGLEGLADRYPH-----------QLSGGQQQRVALARAlAPEPRVL-LLDEPLSALDAK 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039753390 761 VANHL------LHRcILGVlshTTrLLCTH-RTEYLERADVVLLMEAGQLVRTGPPSEI 812
Cdd:COG3842 170 LREEMreelrrLQR-ELGI---TF-IYVTHdQEEALALADRIAVMNDGRIEQVGTPEEI 223
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
616-813 |
1.93e-13 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 71.48 E-value: 1.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 616 KTFISHLQ--VKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVS----------ELSKGFGLATQEPWIQCATIRD 683
Cdd:cd03288 34 KPVLKHVKayIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDgidisklplhTLRSRLSIILQDPILFSGSIRF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 684 NI-LFGKTFDAQLYrEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVA 762
Cdd:cd03288 114 NLdPECKCTDDRLW-EALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1039753390 763 NhLLHRCILGVLSHTTRLLCTHRTEYLERADVVLLMEAGQLVRTGPPSEIL 813
Cdd:cd03288 193 N-ILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLL 242
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
622-807 |
2.63e-13 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 69.98 E-value: 2.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGeLHR------LCGWVAVSELS---KGFGLATQE----PWIqcaTIRDNILFG 688
Cdd:cd03301 21 LDIADGEFVVLLGPSGCGKTTTLRMIAG-LEEptsgriYIGGRDVTDLPpkdRDIAMVFQNyalyPHM---TVYDNIAFG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 689 ----KTFDAQLYREVLEACALnddLSIlpagdQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANH 764
Cdd:cd03301 97 lklrKVPKDEIDERVREVAEL---LQI-----EHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQ 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1039753390 765 L------LHRcILGvlshTTRLLCTH-RTEYLERADVVLLMEAGQLVRTG 807
Cdd:cd03301 169 MraelkrLQQ-RLG----TTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
287-552 |
3.89e-13 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 70.75 E-value: 3.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 287 LALGLLKMVGTMLGFSGPLLLSLLVGFLEEGQEP----LSHGLLYVLGLAGGTVISAVLQNqygYEVRKVTLQARVAVLS 362
Cdd:pfam00664 2 ILAILLAILSGAISPAFPLVLGRILDVLLPDGDPetqaLNVYSLALLLLGLAQFILSFLQS---YLLNHTGERLSRRLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 363 TLYRKALKLGPS---RPPTGEVLNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGMAFLAGLVLAL-LLVPVN 438
Cdd:pfam00664 79 KLFKKILRQPMSffdTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLpLYILVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 439 KVIATRIMASNQEMLRHKDARVKLMTELLSGIRVIKFFRWEQALGDRVKACRTKELGRLR---VIKYLDAACVYLWAALp 515
Cdd:pfam00664 159 AVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIkkaVANGLSFGITQFIGYL- 237
|
250 260 270
....*....|....*....|....*....|....*..
gi 1039753390 516 VVICITIFITYVLMGHQLTATKVFTALALVRMLILPL 552
Cdd:pfam00664 238 SYALALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
622-807 |
4.23e-13 |
|
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: 69.61 E-value: 4.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELH---RLCGWVAV--SELSKG-----FGLATQ-EPWIQCATIRDNILFGKT 690
Cdd:cd03234 28 LHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFngQPRKPDqfqkcVAYVRQdDILLPGLTVRETLTYTAI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 691 F-----DAQLYREVLEACALNDDLSILPAGDQTEVGekgvtLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHL 765
Cdd:cd03234 108 LrlprkSSDAIRKKRVEDVLLRDLALTRIGGNLVKG-----ISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1039753390 766 LHrcILGVLSHTTRL-LCT-H--RTEYLERADVVLLMEAGQLVRTG 807
Cdd:cd03234 183 VS--TLSQLARRNRIvILTiHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
660-797 |
4.73e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 73.91 E-value: 4.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 660 VSELSKGFGLATQEPWIQCATIRDNILFGKTfDAQLyREVLEAC---ALNDDLSILPAGDQTEVGEKGVTLSGGQRARIA 736
Cdd:PTZ00265 1291 LKDLRNLFSIVSQEPMLFNMSIYENIKFGKE-DATR-EDVKRACkfaAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIA 1368
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039753390 737 LARAVYQEKALYLLDDPLAAVDADvANHLLHRCILGVLSHTTRLLCT--HRTEYLERADVVLL 797
Cdd:PTZ00265 1369 IARALLREPKILLLDEATSSLDSN-SEKLIEKTIVDIKDKADKTIITiaHRIASIKRSDKIVV 1430
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
621-813 |
5.62e-13 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 69.83 E-value: 5.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 621 HLQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAV--SELSKGFGLAT--------QEP-------WiqcaTIRD 683
Cdd:COG1124 25 SLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFdgRPVTRRRRKAFrrrvqmvfQDPyaslhprH----TVDR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 684 NI-----LFGKTFDAQLYREVLEACALNDD-LSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAV 757
Cdd:COG1124 101 ILaeplrIHGLPDREERIAELLEQVGLPPSfLDRYPH-----------QLSGGQRQRVAIARALILEPELLLLDEPTSAL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039753390 758 D----ADVANhLLHRciLGVLSHTTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEIL 813
Cdd:COG1124 170 DvsvqAEILN-LLKD--LREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLL 227
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
622-807 |
5.87e-13 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. 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: 213265 [Multi-domain] Cd Length: 211 Bit Score: 69.06 E-value: 5.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVSELSKGFGLATQEPwiQCATIRDNILFgktfdAQLYREVLE 701
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRP--VSMLFQENNLF-----AHLTVEQNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 702 ACALNDDLSiLPAGDQTEV----GEKGV---------TLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLhR 768
Cdd:cd03298 92 GLGLSPGLK-LTAEDRQAIevalARVGLaglekrlpgELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEML-D 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1039753390 769 CILGVLSHT--TRLLCTHRTEYLER-ADVVLLMEAGQLVRTG 807
Cdd:cd03298 170 LVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
887-994 |
7.53e-13 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350049 [Multi-domain] Cd Length: 300 Bit Score: 70.25 E-value: 7.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 887 AAAILVSLLLMQATRNGADWWLAHWLSQLKagrngsredpascspgstalfsprlllfspgnlytpllstplHKAASNGT 966
Cdd:cd18605 1 LILILLSLILMQASRNLIDFWLSYWVSHSN------------------------------------------NSFFNFIN 38
|
90 100
....*....|....*....|....*...
gi 1039753390 967 ADVHFYLIVYATIAGVNSLCTLLRAVLF 994
Cdd:cd18605 39 DSFNFFLTVYGFLAGLNSLFTLLRAFLF 66
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
622-812 |
8.60e-13 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 70.87 E-value: 8.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAI-------TGELH---RLCGWVAVSElsKGFGLATQEPwiqcA-----TIRDNIL 686
Cdd:COG3839 24 LDIEDGEFLVLLGPSGCGKSTLLRMIagledptSGEILiggRDVTDLPPKD--RNIAMVFQSY----AlyphmTVYENIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 687 FG----KTFDAQLYREVLEACALnddLSI------LPAgdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAA 756
Cdd:COG3839 98 FPlklrKVPKAEIDRRVREAAEL---LGLedlldrKPK-----------QLSGGQRQRVALGRALVREPKVFLLDEPLSN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039753390 757 VDADVANHL------LHRcilgVLSHTTrLLCTH-RTEYLERADVVLLMEAGQLVRTGPPSEI 812
Cdd:COG3839 164 LDAKLRVEMraeikrLHR----RLGTTT-IYVTHdQVEAMTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
511-805 |
9.57e-13 |
|
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: 72.64 E-value: 9.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 511 WAALPVVICITIF---ITYVLMG-HQLTATKVFTALALVrMLILplNNFPWVIN------GLLESkvsLDRIQRFLDLPS 580
Cdd:TIGR01271 1110 WFQMRIDIIFVFFfiaVTFIAIGtNQDGEGEVGIILTLA-MNIL--STLQWAVNssidvdGLMRS---VSRVFKFIDLPQ 1183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 581 YSPEAYYSPDPpAEPSTAL--ELHEALFSWDPIG------------ASQKTFISHLQ--VKKGMLVGIVGKVGCGKSSLL 644
Cdd:TIGR01271 1184 EEPRPSGGGGK-YQLSTVLviENPHAQKCWPSGGqmdvqgltakytEAGRAVLQDLSfsVEGGQRVGLLGRTGSGKSTLL 1262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 645 AAI------TGELH-RLCGWVAVS--ELSKGFGLATQEPWIQCATIRDNI-LFGKTFDAQLYReVLEACALNDDLSILPA 714
Cdd:TIGR01271 1263 SALlrllstEGEIQiDGVSWNSVTlqTWRKAFGVIPQKVFIFSGTFRKNLdPYEQWSDEEIWK-VAEEVGLKSVIEQFPD 1341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 715 GDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDAdVANHLLHRCILGVLSHTTRLLCTHRTEYLERADV 794
Cdd:TIGR01271 1342 KLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDP-VTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQ 1420
|
330
....*....|.
gi 1039753390 795 VLLMEAGQLVR 805
Cdd:TIGR01271 1421 FLVIEGSSVKQ 1431
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
631-825 |
9.61e-13 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 70.90 E-value: 9.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 631 GIVGKVGCGKSSLLAAITGELHRLCGWVAVSElskgfglatqEPWIQCA-------------------------TIRDNI 685
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGLERPDSGRIRLGG----------EVLQDSArgiflpphrrrigyvfqearlfphlSVRGNL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 686 LFG-----KTFDAQLYREVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAVDAD 760
Cdd:COG4148 99 LYGrkrapRAERRISFDEVVELLGIGHLLDRRPA-----------TLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039753390 761 VANHLLHrcILGVLSHTTR---LLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEILPLVQAVPTAWAE 825
Cdd:COG4148 168 RKAEILP--YLERLRDELDipiLYVSHSLDEVARlADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGE 234
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
627-803 |
1.50e-12 |
|
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: 69.11 E-value: 1.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 627 GMLVGIVGKVGCGKSSLLAA------ITGELH-RLCGW--VAVSELSKGFGLATQEPWIQCATIRDNI-LFGKTFDAQLY 696
Cdd:cd03289 30 GQRVGLLGRTGSGKSTLLSAflrllnTEGDIQiDGVSWnsVPLQKWRKAFGVIPQKVFIFSGTFRKNLdPYGKWSDEEIW 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 697 ReVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDAdVANHLLHRCILGVLSH 776
Cdd:cd03289 110 K-VAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDP-ITYQVIRKTLKQAFAD 187
|
170 180
....*....|....*....|....*..
gi 1039753390 777 TTRLLCTHRTEYLERADVVLLMEAGQL 803
Cdd:cd03289 188 CTVILSEHRIEAMLECQRFLVIEENKV 214
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
622-812 |
2.01e-12 |
|
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: 68.03 E-value: 2.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAI-------TGELhrLCGWVAVSEL---SKGFGLATQE----PWIqcaTIRDNILF 687
Cdd:cd03300 21 LDIKEGEFFTLLGPSGCGKTTLLRLIagfetptSGEI--LLDGKDITNLpphKRPVNTVFQNyalfPHL---TVFENIAF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 688 G----KTFDAQLYREVLEACalndDLSILPAGDQTEVGEkgvtLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVAN 763
Cdd:cd03300 96 GlrlkKLPKAEIKERVAEAL----DLVQLEGYANRKPSQ----LSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRK 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039753390 764 HL------LHRcILGvlshTTRLLCTH-RTEYLERADVVLLMEAGQLVRTGPPSEI 812
Cdd:cd03300 168 DMqlelkrLQK-ELG----ITFVFVTHdQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
622-802 |
3.25e-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: 66.06 E-value: 3.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVselskgFGLATQEPWIQCATIRDNIlfGKTF-DAQLYR--E 698
Cdd:cd03229 21 LNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILI------DGEDLTDLEDELPPLRRRI--GMVFqDFALFPhlT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 699 VLEACALnddlsilpagdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHL------LHRcILG 772
Cdd:cd03229 93 VLENIAL--------------------GLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVrallksLQA-QLG 151
|
170 180 190
....*....|....*....|....*....|.
gi 1039753390 773 VlshtTRLLCTHRTEYLER-ADVVLLMEAGQ 802
Cdd:cd03229 152 I----TVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
589-812 |
5.01e-12 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 68.71 E-value: 5.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 589 PDPPAEPSTA----LELHEALFSWDPIGASQKTfisHLQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVSels 664
Cdd:PRK11607 6 PRPQAKTRKAltplLEIRNLTKSFDGQHAVDDV---SLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLD--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 665 kGFGLATQEPWIQC-------------ATIRDNILFGKTFDAQLYREVleACALNDDLSILPAgdQTEVGEKGVTLSGGQ 731
Cdd:PRK11607 80 -GVDLSHVPPYQRPinmmfqsyalfphMTVEQNIAFGLKQDKLPKAEI--ASRVNEMLGLVHM--QEFAKRKPHQLSGGQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 732 RARIALARAVYQEKALYLLDDPLAAVDADVANHLLHRcILGVLSH--TTRLLCTH-RTEYLERADVVLLMEAGQLVRTGP 808
Cdd:PRK11607 155 RQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLE-VVDILERvgVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGE 233
|
....
gi 1039753390 809 PSEI 812
Cdd:PRK11607 234 PEEI 237
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
613-833 |
5.26e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 67.84 E-value: 5.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 613 ASQKTFISHLQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVSEL--------------SKGFGLATQEPWIQC 678
Cdd:PRK13643 18 ASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIvvsstskqkeikpvRKKVGVVFQFPESQL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 679 --ATIRDNILFGKTfDAQLYREVLEACALnDDLSILpaGDQTEVGEKG-VTLSGGQRARIALARAVYQEKALYLLDDPLA 755
Cdd:PRK13643 98 feETVLKDVAFGPQ-NFGIPKEKAEKIAA-EKLEMV--GLADEFWEKSpFELSGGQMRRVAIAGILAMEPEVLVLDEPTA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 756 AVDADVANHLLHrcILGVLSHT--TRLLCTH-RTEYLERADVVLLMEAGQLVRTGPPSEILPLVQ-------AVPTAWAE 825
Cdd:PRK13643 174 GLDPKARIEMMQ--LFESIHQSgqTVVLVTHlMDDVADYADYVYLLEKGHIISCGTPSDVFQEVDflkahelGVPKATHF 251
|
....*...
gi 1039753390 826 KEQVATSG 833
Cdd:PRK13643 252 ADQLQKTG 259
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
622-805 |
5.35e-12 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 66.61 E-value: 5.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAI-------TGELhRLCGwVAVSELSKG----------------FGLatqepwIQC 678
Cdd:COG1136 29 LSIEAGEFVAIVGPSGSGKSTLLNILggldrptSGEV-LIDG-QDISSLSERelarlrrrhigfvfqfFNL------LPE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 679 ATIRDNILF-------GKTFDAQLYREVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKALYLLD 751
Cdd:COG1136 101 LTALENVALplllagvSRKERRERARELLERVGLGDRLDHRPS-----------QLSGGQQQRVAIARALVNRPKLILAD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 752 DPLAAVDADVANHllhrcILGVL------SHTTRLLCTHRTEYLERADVVLLMEAGQLVR 805
Cdd:COG1136 170 EPTGNLDSKTGEE-----VLELLrelnreLGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
621-813 |
5.97e-12 |
|
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: 66.45 E-value: 5.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 621 HLQVKKGMLVGIVGKVGCGKSSLLAAITGeLHR------LCGWVAVSELSK---------------GFGLATQEpwiqca 679
Cdd:cd03258 25 SLSVPKGEIFGIIGRSGAGKSTLIRCING-LERptsgsvLVDGTDLTLLSGkelrkarrrigmifqHFNLLSSR------ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 680 TIRDNILF-------GKTFDAQLYREVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDD 752
Cdd:cd03258 98 TVFENVALpleiagvPKAEIEERVLELLELVGLEDKADAYPA-----------QLSGGQKQRVGIARALANNPKVLLCDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039753390 753 PLAAVDADVANH---LLHR--CILGVlshtTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEIL 813
Cdd:cd03258 167 ATSALDPETTQSilaLLRDinRELGL----TIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVF 229
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
621-813 |
1.14e-11 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 67.94 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 621 HLQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVS----------ELSKGFGLATQEPWIQCA-TIRDNILFGK 689
Cdd:PRK09536 23 DLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAgddvealsarAASRRVASVPQDTSLSFEfDVRQVVEMGR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 690 TfdaqLYREVLEACALNDDLSILPAGDQTEV---GEKGVT-LSGGQRARIALARAVYQEKALYLLDDPLAAVDadvANHL 765
Cdd:PRK09536 103 T----PHRSRFDTWTETDRAAVERAMERTGVaqfADRPVTsLSGGERQRVLLARALAQATPVLLLDEPTASLD---INHQ 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039753390 766 LHrcilgVLSHTTRLLCTHRTEY-----LERA----DVVLLMEAGQLVRTGPPSEIL 813
Cdd:PRK09536 176 VR-----TLELVRRLVDDGKTAVaaihdLDLAarycDELVLLADGRVRAAGPPADVL 227
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
622-812 |
5.34e-11 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 65.49 E-value: 5.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVA-----VSELS---KGFGLATQE-PWIQCATIRDNILFGKTFD 692
Cdd:PRK10851 23 LDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRfhgtdVSRLHardRKVGFVFQHyALFRHMTVFDNIAFGLTVL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 693 AQlyREVLEACALNDDLSILPAGDQTE--VGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHL----- 765
Cdd:PRK10851 103 PR--RERPNAAAIKAKVTQLLEMVQLAhlADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELrrwlr 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1039753390 766 -LHRCIlgvlsHTTRLLCTH-RTEYLERADVVLLMEAGQLVRTGPPSEI 812
Cdd:PRK10851 181 qLHEEL-----KFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
622-812 |
6.04e-11 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 63.74 E-value: 6.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVS--ELSKGFGLATQEPWIQCATI--------R----DNILF 687
Cdd:cd03256 22 LSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDgtDINKLKGKALRQLRRQIGMIfqqfnlieRlsvlENVLS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 688 GKTFDAQLYR---------EVLEACALNDDLSILPAGDQtevgeKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVD 758
Cdd:cd03256 102 GRLGRRSTWRslfglfpkeEKQRALAALERVGLLDKAYQ-----RADQLSGGQQQRVAIARALMQQPKLILADEPVASLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039753390 759 ADVANHLLHrcILGVLSHT---TRLLCTHRTEY-LERADVVLLMEAGQLVRTGPPSEI 812
Cdd:cd03256 177 PASSRQVMD--LLKRINREegiTVIVSLHQVDLaREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
622-813 |
7.34e-11 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 63.57 E-value: 7.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELH------------RLCGWVaVSELSKGFGLAT---QEPWIQCATIRDNIL 686
Cdd:COG1119 24 WTVKPGEHWAILGPNGAGKSTLLSLITGDLPptygndvrlfgeRRGGED-VWELRKRIGLVSpalQLRFPRDETVLDVVL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 687 FGKtFDA-QLYREVLE-----ACALNDDLSILPAGDQTeVGekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAVDaD 760
Cdd:COG1119 103 SGF-FDSiGLYREPTDeqrerARELLELLGLAHLADRP-FG----TLSQGEQRRVLIARALVKDPELLILDEPTAGLD-L 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039753390 761 VANHLLHRCI--LGVLSHTTRLLCTHRTEYL----ERadvVLLMEAGQLVRTGPPSEIL 813
Cdd:COG1119 176 GARELLLALLdkLAAEGAPTLVLVTHHVEEIppgiTH---VLLLKDGRVVAAGPKEEVL 231
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
621-760 |
1.30e-10 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 62.11 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 621 HLQVKKGMLVGIVGKVGCGKSSLLAAITGELH---RLCGWV--------AVSELSKGFGLATQEP-----WiqcaTIRDN 684
Cdd:COG4136 21 SLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVllngrrltALPAEQRRIGILFQDDllfphL----SVGEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 685 ILFG--KTFDAQLYREVLEAcALnddlsilpagdqTEVGEKGV------TLSGGQRARIALARAVYQEKALYLLDDPLAA 756
Cdd:COG4136 97 LAFAlpPTIGRAQRRARVEQ-AL------------EEAGLAGFadrdpaTLSGGQRARVALLRALLAEPRALLLDEPFSK 163
|
....
gi 1039753390 757 VDAD 760
Cdd:COG4136 164 LDAA 167
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
622-797 |
1.97e-10 |
|
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: 61.34 E-value: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVSElsKGFGLATQEPWIQCA------------TIRDNILF-- 687
Cdd:COG4133 23 FTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNG--EPIRDAREDYRRRLAylghadglkpelTVRENLRFwa 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 688 ---GKTFDAQLYREVLEACALnDDLSILPAGdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADvANH 764
Cdd:COG4133 101 alyGLRADREAIDEALEAVGL-AGLADLPVR----------QLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAA-GVA 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 1039753390 765 LLHRCIlgvLSHTTR----LLCTHRTEYLERADVVLL 797
Cdd:COG4133 169 LLAELI---AAHLARggavLLTTHQPLELAAARVLDL 202
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
621-813 |
2.05e-10 |
|
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: 61.79 E-value: 2.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 621 HLQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVSELS-----------KGFGLATQEPWI-QCATIRDNIL-- 686
Cdd:cd03218 20 SLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDitklpmhkrarLGIGYLPQEASIfRKLTVEENILav 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 687 ---FGKTFDAQlyREVLEAcaLNDDLSILPAGDQtevgeKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVD----A 759
Cdd:cd03218 100 leiRGLSKKER--EEKLEE--LLEEFHITHLRKS-----KASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDpiavQ 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039753390 760 DVAN---HLLHRCIlGVL--SHTTRllcthrtEYLERADVVLLMEAGQLVRTGPPSEIL 813
Cdd:cd03218 171 DIQKiikILKDRGI-GVLitDHNVR-------ETLSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
543-807 |
3.30e-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: 64.07 E-value: 3.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 543 ALVRMLILPLNNFPWVINGLLESKVSLDRIQRFLDLPsysPEAYYSPDPPAEPSTALELH-EAL-FSWDPigASQktfIS 620
Cdd:COG5265 303 AYLIQLYIPLNFLGFVYREIRQALADMERMFDLLDQP---PEVADAPDAPPLVVGGGEVRfENVsFGYDP--ERP---IL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 621 H---LQVKKGMLVGIVGKVGCGKSSL---------------------LAAITGE-LHRLCGWVAvselskgfglatQEPW 675
Cdd:COG5265 375 KgvsFEVPAGKTVAIVGPSGAGKSTLarllfrfydvtsgrilidgqdIRDVTQAsLRAAIGIVP------------QDTV 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 676 IQCATIRDNILFGKT--FDAQLyREVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDP 753
Cdd:COG5265 443 LFNDTIAYNIAYGRPdaSEEEV-EAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEA 521
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039753390 754 LAAVDAdvanhllH--RCILGVL-----SHTTrLLCTHRTEYLERADVVLLMEAGQLVRTG 807
Cdd:COG5265 522 TSALDS-------RteRAIQAALrevarGRTT-LVIAHRLSTIVDADEILVLEAGRIVERG 574
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
622-812 |
3.48e-10 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 62.94 E-value: 3.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSL------LAAIT-GELHrLCGWVaVSELskgfglatqEPWIQ-CA------------TI 681
Cdd:PRK11650 25 LDVADGEFIVLVGPSGCGKSTLlrmvagLERITsGEIW-IGGRV-VNEL---------EPADRdIAmvfqnyalyphmSV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 682 RDNILFG----KTFDAQLYREVLEACALnddLSILPAGDQtevgeKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAV 757
Cdd:PRK11650 94 RENMAYGlkirGMPKAEIEERVAEAARI---LELEPLLDR-----KPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039753390 758 DADVANHL------LHRCiLGvlshTTRLLCTH-RTEYLERADVVLLMEAGQLVRTGPPSEI 812
Cdd:PRK11650 166 DAKLRVQMrleiqrLHRR-LK----TTSLYVTHdQVEAMTLADRVVVMNGGVAEQIGTPVEV 222
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
622-818 |
3.97e-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: 61.15 E-value: 3.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCG--WVA---VSELS--------KGFGLATQepwiQCA-----TIRD 683
Cdd:COG1127 26 LDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGeiLVDgqdITGLSekelyelrRRIGMLFQ----GGAlfdslTVFE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 684 NILFG----KTFDAQLYRE----VLEACALNDDLSILPAgdqtevgEkgvtLSGGQRARIALARAVYQEKALYLLDDPLA 755
Cdd:COG1127 102 NVAFPlrehTDLSEAEIRElvleKLELVGLPGAADKMPS-------E----LSGGMRKRVALARALALDPEILLYDEPTA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039753390 756 AVD---ADVANHLLHRC--ILGvlshTTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEIL----PLVQA 818
Cdd:COG1127 171 GLDpitSAVIDELIRELrdELG----LTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLasddPWVRQ 239
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
622-813 |
3.99e-10 |
|
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: 61.20 E-value: 3.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELH------RLCGwVAVSELS---KGFGLATQE----PWIqcaTIRDNILFG 688
Cdd:cd03299 20 LEVERGDYFVILGPTGSGKSVLLETIAGFIKpdsgkiLLNG-KDITNLPpekRDISYVPQNyalfPHM---TVYKNIAYG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 689 ----KTFDAQLYREVLEacaLNDDLSILPAGDQtevgeKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANH 764
Cdd:cd03299 96 lkkrKVDKKEIERKVLE---IAEMLGIDHLLNR-----KPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEK 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1039753390 765 LlhRCILGVLSH---TTRLLCTHR-TEYLERADVVLLMEAGQLVRTGPPSEIL 813
Cdd:cd03299 168 L--REELKKIRKefgVTVLHVTHDfEEAWALADKVAIMLNGKLIQVGKPEEVF 218
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
621-813 |
4.16e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 61.93 E-value: 4.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 621 HLQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVS-----------ELSKGFGLATQEPWIQCA--TIRDNILF 687
Cdd:PRK13644 22 NLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSgidtgdfsklqGIRKLVGIVFQNPETQFVgrTVEEDLAF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 688 GKTFDAQLYREVLEACalndDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLH 767
Cdd:PRK13644 102 GPENLCLPPIEIRKRV----DRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1039753390 768 RCILGVLSHTTRLLCTHRTEYLERADVVLLMEAGQLVRTGPPSEIL 813
Cdd:PRK13644 178 RIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
595-813 |
4.19e-10 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. 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: 213261 [Multi-domain] Cd Length: 269 Bit Score: 61.51 E-value: 4.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 595 PSTALELHEALFSWDPIGASQKTFIS----HLQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWV-----AVSELSK 665
Cdd:cd03294 14 PQKAFKLLAKGKSKEEILKKTGQTVGvndvSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVlidgqDIAAMSR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 666 G----------------FGLATQEpwiqcaTIRDNILFG-------KTFDAQLYREVLEACALNDDLSILPagDQtevge 722
Cdd:cd03294 94 KelrelrrkkismvfqsFALLPHR------TVLENVAFGlevqgvpRAEREERAAEALELVGLEGWEHKYP--DE----- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 723 kgvtLSGGQRARIALARAVYQEKALYLLDDPLAAVD----ADVANHLLHrciLGVLSHTTRLLCTHR-TEYLERADVVLL 797
Cdd:cd03294 161 ----LSGGMQQRVGLARALAVDPDILLMDEAFSALDplirREMQDELLR---LQAELQKTIVFITHDlDEALRLGDRIAI 233
|
250
....*....|....*.
gi 1039753390 798 MEAGQLVRTGPPSEIL 813
Cdd:cd03294 234 MKDGRLVQVGTPEEIL 249
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
622-813 |
6.92e-10 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 60.78 E-value: 6.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAV----------SELSKGFGLATQE----PWIqcaTIRDNI-- 685
Cdd:cd03295 22 LEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIdgedireqdpVELRRKIGYVIQQiglfPHM---TVEENIal 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 686 ---LFGKTfDAQLYREVLEACALNDdlsiLPagDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVA 762
Cdd:cd03295 99 vpkLLKWP-KEKIRERADELLALVG----LD--PAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITR 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039753390 763 NHL------LHRcilgvLSHTTRLLCTHRT-EYLERADVVLLMEAGQLVRTGPPSEIL 813
Cdd:cd03295 172 DQLqeefkrLQQ-----ELGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
621-812 |
7.00e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 61.19 E-value: 7.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 621 HLQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVSE--------------LSKGFGLATQEPWIQC--ATIRDN 684
Cdd:PRK13634 27 NVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGErvitagkknkklkpLRKKVGIVFQFPEHQLfeETVEKD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 685 ILFG-KTF-----DA-QLYREVLEACALNDDLSILPAGDqtevgekgvtLSGGQRARIALARAVYQEKALYLLDDPLAAV 757
Cdd:PRK13634 107 ICFGpMNFgvseeDAkQKAREMIELVGLPEELLARSPFE----------LSGGQMRRVAIAGVLAMEPEVLVLDEPTAGL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039753390 758 DADVANHL------LHRcilgvLSHTTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEI 812
Cdd:PRK13634 177 DPKGRKEMmemfykLHK-----EKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREI 233
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
622-811 |
8.05e-10 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 60.14 E-value: 8.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITG--------------ELHRL------------CGWVAVSelskgFGLatqepw 675
Cdd:COG4181 33 LEVEAGESVAIVGASGSGKSTLLGLLAGldrptsgtvrlagqDLFALdedararlrarhVGFVFQS-----FQL------ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 676 IQCATIRDNI-----LFGKTFDAQLYREVLEACALNDDLSILPAGdqtevgekgvtLSGGQRARIALARAVYQEKALYLL 750
Cdd:COG4181 102 LPTLTALENVmlpleLAGRRDARARARALLERVGLGHRLDHYPAQ-----------LSGGEQQRVALARAFATEPAILFA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039753390 751 DDPLAAVDADVANHllhrcILGVL------SHTTRLLCTHRTEYLERADVVLLMEAGQLVRTGPPSE 811
Cdd:COG4181 171 DEPTGNLDAATGEQ-----IIDLLfelnreRGTTLVLVTHDPALAARCDRVLRLRAGRLVEDTAATA 232
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
622-813 |
8.67e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 60.29 E-value: 8.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVSE-----------LSKGFGLATQEPWI-QCATIRDNILFGK 689
Cdd:PRK10895 24 LTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDedisllplharARRGIGYLPQEASIfRRLSVYDNLMAVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 690 TFDAQLYREVLE--ACALNDDLSILPAGDQTevgekGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVD-------AD 760
Cdd:PRK10895 104 QIRDDLSAEQREdrANELMEEFHIEHLRDSM-----GQSLSGGERRRVEIARALAANPKFILLDEPFAGVDpisvidiKR 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1039753390 761 VANHLLHRCiLGVL--SHTTRllctHRTEYLERADVVllmEAGQLVRTGPPSEIL 813
Cdd:PRK10895 179 IIEHLRDSG-LGVLitDHNVR----ETLAVCERAYIV---SQGHLIAHGTPTEIL 225
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
622-813 |
9.79e-10 |
|
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: 62.13 E-value: 9.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSL---LAAIT----GELHRLCG--WVAVSELS-KGFGLATqePWIqcatirdNILFgKTF 691
Cdd:TIGR03269 305 LEVKEGEIFGIVGTSGAGKTTLskiIAGVLeptsGEVNVRVGdeWVDMTKPGpDGRGRAK--RYI-------GILH-QEY 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 692 DAQLYREVLE------ACALNDDLSILPA-------GDQTEVGEKGV-----TLSGGQRARIALARAVYQEKALYLLDDP 753
Cdd:TIGR03269 375 DLYPHRTVLDnlteaiGLELPDELARMKAvitlkmvGFDEEKAEEILdkypdELSEGERHRVALAQVLIKEPRIVILDEP 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039753390 754 LAAVD----ADVANHLLH-RCILGvlshTTRLLCTHRTEY-LERADVVLLMEAGQLVRTGPPSEIL 813
Cdd:TIGR03269 455 TGTMDpitkVDVTHSILKaREEME----QTFIIVSHDMDFvLDVCDRAALMRDGKIVKIGDPEEIV 516
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
622-813 |
1.06e-09 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 59.77 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVavseLSKGFGLATQEPwiqcA-----------------TIRDN 684
Cdd:COG3840 20 LTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRI----LWNGQDLTALPP----AerpvsmlfqennlfphlTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 685 ILFG-------KTFDAQLYREVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAV 757
Cdd:COG3840 92 IGLGlrpglklTAEQRAQVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVALARCLVRKRPILLLDEPFSAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039753390 758 D-------ADVANHLLHRcilgvlSHTTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEIL 813
Cdd:COG3840 161 DpalrqemLDLVDELCRE------RGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALL 218
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
599-813 |
1.07e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 60.49 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 599 LELHEALFSWDPIGASQKTFISHLQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVS----------ELSKGFG 668
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDgelltaenvwNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 669 LATQEPWIQC--ATIRDNILFGKTFDAQLYREVLEACalndDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKA 746
Cdd:PRK13642 85 MVFQNPDNQFvgATVEDDVAFGMENQGIPREEMIKRV----DEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039753390 747 LYLLDDPLAAVDADVANHLLhRCILGVLS--HTTRLLCTHRTEYLERADVVLLMEAGQLVRTGPPSEIL 813
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIM-RVIHEIKEkyQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELF 228
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
616-812 |
1.28e-09 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 61.12 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 616 KTFISH--LQVKKGMLVGIVGKVGCGKSSLLAAI-------TGELHrLCGwVAVSELSkgfglATQEP----WIQCA--- 679
Cdd:PRK09452 27 KEVISNldLTINNGEFLTLLGPSGCGKTTVLRLIagfetpdSGRIM-LDG-QDITHVP-----AENRHvntvFQSYAlfp 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 680 --TIRDNILFG----KTFDAQLYREVLEACALN--DDLSilpagdqtevGEKGVTLSGGQRARIALARAVYQEKALYLLD 751
Cdd:PRK09452 100 hmTVFENVAFGlrmqKTPAAEITPRVMEALRMVqlEEFA----------QRKPHQLSGGQQQRVAIARAVVNKPKVLLLD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039753390 752 DPLAAVDA----DVANHL--LHRcILGVlshtTRLLCTH-RTEYLERADVVLLMEAGQLVRTGPPSEI 812
Cdd:PRK09452 170 ESLSALDYklrkQMQNELkaLQR-KLGI----TFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPREI 232
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
625-812 |
1.84e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 60.25 E-value: 1.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 625 KKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAV--------------------------SELSKGFGLATQEPWIQC 678
Cdd:PRK13631 50 EKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknnhelitnpyskkiknfKELRRRVSMVFQFPEYQL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 679 --ATIRDNILFG-------KTFDAQLYREVLEACALNDD-LSILPAGdqtevgekgvtLSGGQRARIALARAVYQEKALY 748
Cdd:PRK13631 130 fkDTIEKDIMFGpvalgvkKSEAKKLAKFYLNKMGLDDSyLERSPFG-----------LSGGQKRRVAIAGILAIQPEIL 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039753390 749 LLDDPLAAVDADvANHLLHRCILGV-LSHTTRLLCTHRTEY-LERADVVLLMEAGQLVRTGPPSEI 812
Cdd:PRK13631 199 IFDEPTAGLDPK-GEHEMMQLILDAkANNKTVFVITHTMEHvLEVADEVIVMDKGKILKTGTPYEI 263
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
622-812 |
2.63e-09 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 60.43 E-value: 2.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAI-------TGELhrLCGWVAVSEL---SKGFGLATQE----PWIQCAtirDNILF 687
Cdd:PRK11000 24 LDIHEGEFVVFVGPSGCGKSTLLRMIagleditSGDL--FIGEKRMNDVppaERGVGMVFQSyalyPHLSVA---ENMSF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 688 G----KTFDAQLYREVLEACAlnddlsILPAGDQTEVGEKgvTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVAN 763
Cdd:PRK11000 99 GlklaGAKKEEINQRVNQVAE------VLQLAHLLDRKPK--ALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRV 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039753390 764 HL------LHRCIlgvlsHTTRLLCTH-RTEYLERADVVLLMEAGQLVRTGPPSEI 812
Cdd:PRK11000 171 QMrieisrLHKRL-----GRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
621-810 |
3.21e-09 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 60.59 E-value: 3.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 621 HLQVKKGMLVGIVGKVGCGKSSLLAAI-------TGELHRLCGWVAVselskgfgLATQEPWIQCATIRDNILFGKT--- 690
Cdd:COG4178 383 SLSLKPGERLLITGPSGSGKSTLLRAIaglwpygSGRIARPAGARVL--------FLPQRPYLPLGTLREALLYPATaea 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 691 FDAQLYREVLEACALnDDLsilpAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHRcI 770
Cdd:COG4178 455 FSDAELREALEAVGL-GHL----AERLDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQL-L 528
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1039753390 771 LGVLSHTTRLLCTHRTEYLERADVVLLMEAGQLVRTGPPS 810
Cdd:COG4178 529 REELPGTTVISVGHRSTLAAFHDRVLELTGDGSWQLLPAE 568
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
622-798 |
4.40e-09 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 57.24 E-value: 4.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVSeLSKGFGLATQ---EPWIQCATIRDNILFGKTFDAQLYR- 697
Cdd:NF040873 13 LTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRA-GGARVAYVPQrseVPDSLPLTVRDLVAMGRWARRGLWRr 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 698 ----------EVLEACALnDDLSILPAGdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLlh 767
Cdd:NF040873 92 ltrddraavdDALERVGL-ADLAGRQLG----------ELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERI-- 158
|
170 180 190
....*....|....*....|....*....|...
gi 1039753390 768 RCILGVLSHTTR--LLCTHRTEYLERADVVLLM 798
Cdd:NF040873 159 IALLAEEHARGAtvVVVTHDLELVRRADPCVLL 191
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
622-812 |
5.35e-09 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 57.51 E-value: 5.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVSelskGFGLATQEPWIQ-----CAtiRDNILFGK------- 689
Cdd:cd03263 23 LNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYIN----GYSIRTDRKAARqslgyCP--QFDALFDEltvrehl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 690 TFDAQLYREVLEACALNDDLsILPAGDQTEVGEKGV-TLSGGQRARIALARAVYQEKALYLLDDPLAAVDAdVANHLLHR 768
Cdd:cd03263 97 RFYARLKGLPKSEIKEEVEL-LLRVLGLTDKANKRArTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDP-ASRRAIWD 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1039753390 769 CILGVLSHTTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEI 812
Cdd:cd03263 175 LILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
622-811 |
5.52e-09 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 57.37 E-value: 5.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELH------RLCGwVAVSELSKG--------FGLATQEPW-IQCATIRDNIL 686
Cdd:COG2884 23 LEIEKGEFVFLTGPSGAGKSTLLKLLYGEERptsgqvLVNG-QDLSRLKRReipylrrrIGVVFQDFRlLPDRTVYENVA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 687 F-----GKTfDAQLYREVLEACALnddlsilpagdqteVG--EKG----VTLSGGQRARIALARAVYQEKALYLLDDPLA 755
Cdd:COG2884 102 LplrvtGKS-RKEIRRRVREVLDL--------------VGlsDKAkalpHELSGGEQQRVAIARALVNRPELLLADEPTG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039753390 756 AVDADVAN---HLLHR-CILGvlshTTRLLCTHRTEYLERADV-VLLMEAGQLVRTGPPSE 811
Cdd:COG2884 167 NLDPETSWeimELLEEiNRRG----TTVLIATHDLELVDRMPKrVLELEDGRLVRDEARGV 223
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
622-812 |
6.09e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 58.52 E-value: 6.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAV------------SELSKGFGLATQEPWIQC--ATIRDNILF 687
Cdd:PRK13637 28 IEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIdgvditdkkvklSDIRKKVGLVFQYPEYQLfeETIEKDIAF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 688 GKT----FDAQLYREVLEACALnddlsilpAG-DQTEVGEKG-VTLSGGQRARIALARAVYQEKALYLLDDPLAAVDA-- 759
Cdd:PRK13637 108 GPInlglSEEEIENRVKRAMNI--------VGlDYEDYKDKSpFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPkg 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039753390 760 --DVANHL--LHRcilgvLSHTTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEI 812
Cdd:PRK13637 180 rdEILNKIkeLHK-----EYNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPREV 232
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
622-765 |
6.14e-09 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 59.69 E-value: 6.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVselSKGFGLA--TQEPWI-QCATIRDNILFGKTFDAQL--- 695
Cdd:COG0488 19 LSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI---PKGLRIGylPQEPPLdDDLTVLDTVLDGDAELRALeae 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 696 YREVLEACALNDDLSILPAGDQTEVGEKGV--------------------------TLSGGQRARIALARAVYQEKALYL 749
Cdd:COG0488 96 LEELEAKLAEPDEDLERLAELQEEFEALGGweaearaeeilsglgfpeedldrpvsELSGGWRRRVALARALLSEPDLLL 175
|
170
....*....|....*.
gi 1039753390 750 LDDPlaavdadvANHL 765
Cdd:COG0488 176 LDEP--------TNHL 183
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
622-812 |
6.48e-09 |
|
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: 59.82 E-value: 6.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGE----------LHRL-----CGWVAVSELSK------GFGLATQEP--WIQC 678
Cdd:TIGR03269 21 FTIEEGEVLGILGRSGAGKSVLMHVLRGMdqyeptsgriIYHValcekCGYVERPSKVGepcpvcGGTLEPEEVdfWNLS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 679 ATIRDN------ILFGKTFdaQLYRE--VLEAC--ALND-----DLSILPAGD---QTEVGEK----GVTLSGGQRARIA 736
Cdd:TIGR03269 101 DKLRRRirkriaIMLQRTF--ALYGDdtVLDNVleALEEigyegKEAVGRAVDlieMVQLSHRithiARDLSGGEKQRVV 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039753390 737 LARAVYQEKALYLLDDPLAAVDADVANhLLHRCIL-GVL-SHTTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEI 812
Cdd:TIGR03269 179 LARQLAKEPFLFLADEPTGTLDPQTAK-LVHNALEeAVKaSGISMVLTSHWPEVIEDlSDKAIWLENGEIKEEGTPDEV 256
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
622-807 |
6.57e-09 |
|
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: 57.16 E-value: 6.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELH-------RLCGWVAVSELSKGFGLAtqepwiqcATIRDNILFG------ 688
Cdd:cd03220 43 FEVPRGERIGLIGRNGAGKSTLLRLLAGIYPpdsgtvtVRGRVSSLLGLGGGFNPE--------LTGRENIYLNgrllgl 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 689 -KTFDAQLYREVLEACALNDDLSiLPAGdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAVDA-------D 760
Cdd:cd03220 115 sRKEIDEKIDEIIEFSELGDFID-LPVK----------TYSSGMKARLAFAIATALEPDILLIDEVLAVGDAafqekcqR 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1039753390 761 VANHLLHRC-ILGVLSH---TTRLLCthrteyleraDVVLLMEAGQLVRTG 807
Cdd:cd03220 184 RLRELLKQGkTVILVSHdpsSIKRLC----------DRALVLEKGKIRFDG 224
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
622-813 |
7.50e-09 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 57.41 E-value: 7.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAI-------TGEL-----HRLCGWVAVSELSKGFGLATQE----PWIqcaTIRDNI 685
Cdd:PRK09493 22 LNIDQGEVVVIIGPSGSGKSTLLRCInkleeitSGDLivdglKVNDPKVDERLIRQEAGMVFQQfylfPHL---TALENV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 686 LFG-------KTFDA-QLYREVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAV 757
Cdd:PRK09493 99 MFGplrvrgaSKEEAeKQARELLAKVGLAERAHHYPS-----------ELSGGQQQRVAIARALAVKPKLMLFDEPTSAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039753390 758 DADvanhLLHRcILGVLSH-----TTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEIL 813
Cdd:PRK09493 168 DPE----LRHE-VLKVMQDlaeegMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLI 224
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
612-807 |
1.36e-08 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 56.56 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 612 GASQKTFISHLQVKKGMLVGIVGKVGCGKSSLLAAI-------TGELH---------RLCGWVAVSELSKGFGLATQE-- 673
Cdd:PRK11124 13 GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLnllemprSGTLNiagnhfdfsKTPSDKAIRELRRNVGMVFQQyn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 674 --PWIqcaTIRDNIL--------FGKTFDAQLYREVLEACALNDDLSILPagdqtevgekgVTLSGGQRARIALARAVYQ 743
Cdd:PRK11124 93 lwPHL---TVQQNLIeapcrvlgLSKDQALARAEKLLERLRLKPYADRFP-----------LHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039753390 744 EKALYLLDDPLAAVDADVANHLLHrcILGVLSHT--TRLLCTHRTEYLER-ADVVLLMEAGQLVRTG 807
Cdd:PRK11124 159 EPQVLLFDEPTAALDPEITAQIVS--IIRELAETgiTQVIVTHEVEVARKtASRVVYMENGHIVEQG 223
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
622-759 |
1.40e-08 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 56.79 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELH------RLCGwVAVSELSKGFGLATQE----PWIqcaTIRDNILFGKTF 691
Cdd:COG4525 28 LTIESGEFVVALGASGCGKTTLLNLIAGFLApssgeiTLDG-VPVTGPGADRGVVFQKdallPWL---NVLDNVAFGLRL 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039753390 692 D----AQLYREVLEACALnddlsilpagdqteVGEKGV------TLSGGQRARIALARAVYQEKALYLLDDPLAAVDA 759
Cdd:COG4525 104 RgvpkAERRARAEELLAL--------------VGLADFarrriwQLSGGMRQRVGIARALAADPRFLLMDEPFGALDA 167
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
622-813 |
1.48e-08 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 56.68 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGEL-----------HRLCGWvAVSELSK-GFGLATQEPWI-QCATIRDNILFG 688
Cdd:cd03219 21 FSVRPGEIHGLIGPNGAGKTTLFNLISGFLrptsgsvlfdgEDITGL-PPHEIARlGIGRTFQIPRLfPELTVLENVMVA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 689 KTFDAQLY-----------------REVLEACALnDDLSILPAGdqtevgekgvTLSGGQRARIALARAVYQEKALYLLD 751
Cdd:cd03219 100 AQARTGSGlllararreereareraEELLERVGL-ADLADRPAG----------ELSYGQQRRLEIARALATDPKLLLLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039753390 752 DPLAAVDADVANHLLHRcILGV-LSHTTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEIL 813
Cdd:cd03219 169 EPAAGLNPEETEELAEL-IRELrERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVR 231
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
622-819 |
1.53e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 57.02 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVSELS-----------KGFGLATQEPWIQ-CATI-RDNILFG 688
Cdd:PRK13633 31 LEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDtsdeenlwdirNKAGMVFQNPDNQiVATIvEEDVAFG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 689 KtfdaqlyrevleacalnDDLSILPAGDQTEVGE--KGVT-----------LSGGQRARIALARAVYQEKALYLLDDPLA 755
Cdd:PRK13633 111 P-----------------ENLGIPPEEIRERVDEslKKVGmyeyrrhaphlLSGGQKQRVAIAGILAMRPECIIFDEPTA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039753390 756 AVDA----DVANHLLHrciLGVLSHTTRLLCTHRTEYLERADVVLLMEAGQLVRTGPPSEILPLVQAV 819
Cdd:PRK13633 174 MLDPsgrrEVVNTIKE---LNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKEVEMM 238
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
616-762 |
1.68e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 56.94 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 616 KTFISH-------LQVKKGMLVGIVGKVGCGKSSLLAAITG--------ELH------------RLCGWVAVSELSKGFg 668
Cdd:PRK09984 12 KTFNQHqalhavdLNIHHGEMVALLGPSGSGKSTLLRHLSGlitgdksaGSHiellgrtvqregRLARDIRKSRANTGY- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 669 LATQEPWIQCATIRDNILFGKTFDAQLYREVLEACALNDDLSILPAgdQTEVG------EKGVTLSGGQRARIALARAVY 742
Cdd:PRK09984 91 IFQQFNLVNRLSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQA--LTRVGmvhfahQRVSTLSGGQQQRVAIARALM 168
|
170 180
....*....|....*....|
gi 1039753390 743 QEKALYLLDDPLAAVDADVA 762
Cdd:PRK09984 169 QQAKVILADEPIASLDPESA 188
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
621-813 |
2.19e-08 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 56.13 E-value: 2.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 621 HLQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCG--WVA-------------VSELSKGFGLATQepwiqcATIRDNI 685
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGslTLNgqdhtttppsrrpVSMLFQENNLFSH------LTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 686 LFG-----KTFDAQlyREVLEACA----LNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAA 756
Cdd:PRK10771 93 GLGlnpglKLNAAQ--REKLHAIArqmgIEDLLARLPG-----------QLSGGQRQRVALARCLVREQPILLLDEPFSA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039753390 757 VDADVANHllhrcILGVLS------HTTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEIL 813
Cdd:PRK10771 160 LDPALRQE-----MLTLVSqvcqerQLTLLMVSHSLEDAARiAPRSLVVADGRIAWDGPTDELL 218
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
621-815 |
2.20e-08 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 55.23 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 621 HLQVKKGMLVGIVGKVGCGKSSLLAAITG-------ELHRLCGWVAVSELS------KGFGLATQEPW-IQCATIRDnil 686
Cdd:cd03217 20 NLTIKKGEVHALMGPNGSGKSTLAKTIMGhpkyevtEGEILFKGEDITDLPpeerarLGIFLAFQYPPeIPGVKNAD--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 687 fgktfdaqLYREVleacalnddlsilpagdqtevgekGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVD-------A 759
Cdd:cd03217 97 --------FLRYV------------------------NEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDidalrlvA 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039753390 760 DVANHLL--HRCILgVLSHTTRLLcthrtEYLeRADVVLLMEAGQLVRTGPPSEILPL 815
Cdd:cd03217 145 EVINKLReeGKSVL-IITHYQRLL-----DYI-KPDRVHVLYDGRIVKSGDKELALEI 195
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
615-813 |
2.77e-08 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 55.93 E-value: 2.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 615 QKTFISH--LQVKKGMLVGIVGKVGCGKSSLLAAITGELH------RLCG-----WvAVSELSKGFGLATQE-----PWi 676
Cdd:PRK13548 14 GRTLLDDvsLTLRPGEVVAILGPNGAGKSTLLRALSGELSpdsgevRLNGrpladW-SPAELARRRAVLPQHsslsfPF- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 677 qcaTIRDNILFG-------KTFDAQLYREVLEACALnDDLSilpagdqtevGEKGVTLSGGQRARIALARAVYQ------ 743
Cdd:PRK13548 92 ---TVEEVVAMGraphglsRAEDDALVAAALAQVDL-AHLA----------GRDYPQLSGGEQQRVQLARVLAQlwepdg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 744 EKALYLLDDPLAAVD-------ADVANHLLHRCILGVLS--H----TTRllcthrteYlerADVVLLMEAGQLVRTGPPS 810
Cdd:PRK13548 158 PPRWLLLDEPTSALDlahqhhvLRLARQLAHERGLAVIVvlHdlnlAAR--------Y---ADRIVLLHQGRLVADGTPA 226
|
...
gi 1039753390 811 EIL 813
Cdd:PRK13548 227 EVL 229
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
623-789 |
3.40e-08 |
|
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: 57.45 E-value: 3.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 623 QVKKGMLVGIVGKVGCGKSSLLAaITGELHRLCGWV-AVSELSKGFGLAtQEPWIQCATIRDNILFGKTFDAQLYR---- 697
Cdd:TIGR00954 474 EVPSGNNLLICGPNGCGKSSLFR-ILGELWPVYGGRlTKPAKGKLFYVP-QRPYMTLGTLRDQIIYPDSSEDMKRRglsd 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 698 EVLEACALNDDLS-ILpagdQTEVGEKGV-----TLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHRC-- 769
Cdd:TIGR00954 552 KDLEQILDNVQLThIL----EREGGWSAVqdwmdVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCre 627
|
170 180
....*....|....*....|...
gi 1039753390 770 ---ILGVLSHTTRLLCTHrtEYL 789
Cdd:TIGR00954 628 fgiTLFSVSHRKSLWKYH--EYL 648
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
621-765 |
3.58e-08 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 53.22 E-value: 3.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 621 HLQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVSELSKgFGLATQepwiqcatirdnilfgktfdaqlyrevl 700
Cdd:cd03221 20 SLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVK-IGYFEQ---------------------------- 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039753390 701 eacalnddlsilpagdqtevgekgvtLSGGQRARIALARAVYQEKALYLLDDPLaavdadvaNHL 765
Cdd:cd03221 71 --------------------------LSGGEKMRLALAKLLLENPNLLLLDEPT--------NHL 101
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
622-813 |
5.51e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 55.23 E-value: 5.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLL------------AAITGELhRLCGWVAVS------ELSKGFGLATQEP-WIQCATIR 682
Cdd:PRK14267 25 LKIPQNGVFALMGPSGCGKSTLLrtfnrllelneeARVEGEV-RLFGRNIYSpdvdpiEVRREVGMVFQYPnPFPHLTIY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 683 DNILFGKTFDA---------QLYREVLEACALNDDLsilpagdQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDP 753
Cdd:PRK14267 104 DNVAIGVKLNGlvkskkeldERVEWALKKAALWDEV-------KDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEP 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039753390 754 LAAVDAdVANHLLHRCILGVLSHTTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEIL 813
Cdd:PRK14267 177 TANIDP-VGTAKIEELLFELKKEYTIVLVTHSPAQAARvSDYVAFLYLGKLIEVGPTRKVF 236
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
622-812 |
6.28e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 55.14 E-value: 6.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVSELS--------------KGFGLATQEPWIQC--ATIRDNI 685
Cdd:PRK13649 28 LTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLitstsknkdikqirKKVGLVFQFPESQLfeETVLKDV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 686 LFG-------KTFDAQLYREVLEACALNDDLsilpagdqteVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVD 758
Cdd:PRK13649 108 AFGpqnfgvsQEEAEALAREKLALVGISESL----------FEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039753390 759 ADVANHL------LHRcilgvlSHTTRLLCTHRTEYL-ERADVVLLMEAGQLVRTGPPSEI 812
Cdd:PRK13649 178 PKGRKELmtlfkkLHQ------SGMTIVLVTHLMDDVaNYADFVYVLEKGKLVLSGKPKDI 232
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
622-790 |
7.10e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 54.19 E-value: 7.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRL--CGWVAVSELskgfglatqePWIQCATIRDNILFGKTFDAQLyrEV 699
Cdd:COG2401 51 LEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTpvAGCVDVPDN----------QFGREASLIDAIGRKGDFKDAV--EL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 700 LEACALNDDLSILpagdqTEVGEkgvtLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHrcILGVLSH--- 776
Cdd:COG2401 119 LNAVGLSDAVLWL-----RRFKE----LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVAR--NLQKLARrag 187
|
170
....*....|....
gi 1039753390 777 TTRLLCTHRTEYLE 790
Cdd:COG2401 188 ITLVVATHHYDVID 201
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
622-819 |
7.14e-08 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 54.65 E-value: 7.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVA-----VSELS------KGFGLATQEPWI-QCATIRDNIL--- 686
Cdd:COG1137 24 LEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFldgedITHLPmhkrarLGIGYLPQEASIfRKLTVEDNILavl 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 687 --FGKTFDAQlyREVLEAcaLNDDLSILPAGDQtevgeKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVD----AD 760
Cdd:COG1137 104 elRKLSKKER--EERLEE--LLEEFGITHLRKS-----KAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDpiavAD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039753390 761 VAN---HLLHRCIlGVL--SHTTRllcthrtEYLERADVVLLMEAGQLVRTGPPSEIL--PLVQAV 819
Cdd:COG1137 175 IQKiirHLKERGI-GVLitDHNVR-------ETLGICDRAYIISEGKVLAEGTPEEILnnPLVRKV 232
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
623-812 |
7.39e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 55.22 E-value: 7.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 623 QVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVS--------------ELSKGFGLATQEPWIQC--ATIRDNIL 686
Cdd:PRK13641 29 ELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAgyhitpetgnknlkKLRKKVSLVFQFPEAQLfeNTVLKDVE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 687 FG-KTFDAQlyrevlEACALNDDLS-ILPAGDQTEVGEKG-VTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVAN 763
Cdd:PRK13641 109 FGpKNFGFS------EDEAKEKALKwLKKVGLSEDLISKSpFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRK 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1039753390 764 HLLHRCILGVLSHTTRLLCTHRTEYL-ERADVVLLMEAGQLVRTGPPSEI 812
Cdd:PRK13641 183 EMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKEI 232
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
622-812 |
1.13e-07 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 55.11 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVSelskgfGLATQEPWIQ----C-----------ATIRDNIL 686
Cdd:PRK11432 27 LTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFID------GEDVTHRSIQqrdiCmvfqsyalfphMSLGENVG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 687 FG----KTFDAQLYREVLEACALNDdlsilPAG------DQtevgekgvtLSGGQRARIALARA-VYQEKALyLLDDPLA 755
Cdd:PRK11432 101 YGlkmlGVPKEERKQRVKEALELVD-----LAGfedryvDQ---------ISGGQQQRVALARAlILKPKVL-LFDEPLS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039753390 756 AVDADvanhlLHRCI----------LGVlshtTRLLCTH-RTEYLERADVVLLMEAGQLVRTGPPSEI 812
Cdd:PRK11432 166 NLDAN-----LRRSMrekirelqqqFNI----TSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
622-813 |
1.24e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 54.63 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVSE---------------LSKGFGLATQEPWIQC--ATIRDN 684
Cdd:PRK13645 32 LTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlkkikevkrLRKEIGLVFQFPEYQLfqETIEKD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 685 ILFGKTFDAQLYREVLEACALNDDLSILPagdQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDA----D 760
Cdd:PRK13645 112 IAFGPVNLGENKQEAYKKVPELLKLVQLP---EDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPkgeeD 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1039753390 761 VANHLLHrciLGVLSHTTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEIL 813
Cdd:PRK13645 189 FINLFER---LNKEYKKRIIMVTHNMDQVLRiADEVIVMHEGKVISIGSPFEIF 239
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
622-813 |
1.34e-07 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 53.97 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELH------RLCGwVAVSELSKGfGLATQE-----------PWiqcaTIRDN 684
Cdd:COG4559 22 LTLRPGELTAIIGPNGAGKSTLLKLLTGELTpssgevRLNG-RPLAAWSPW-ELARRRavlpqhsslafPF----TVEEV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 685 ILFG-------KTFDAQLYREVLEACalndDLSILPAGDQTevgekgvTLSGGQRARIALARAVYQ--------EKALyL 749
Cdd:COG4559 96 VALGraphgssAAQDRQIVREALALV----GLAHLAGRSYQ-------TLSGGEQQRVQLARVLAQlwepvdggPRWL-F 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039753390 750 LDDPLAAVD-------ADVANHLLHR-----CILGVLSHTTRllcthrteYlerADVVLLMEAGQLVRTGPPSEIL 813
Cdd:COG4559 164 LDEPTSALDlahqhavLRLARQLARRgggvvAVLHDLNLAAQ--------Y---ADRILLLHQGRLVAQGTPEEVL 228
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
632-812 |
1.97e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 53.24 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 632 IVGKVGCGKSSLLAAI------------TGEL----HRLCG-WVAVSELSKGFGLATQEPWIQCATIRDNILFGKTFDAQ 694
Cdd:PRK14239 36 LIGPSGSGKSTLLRSInrmndlnpevtiTGSIvyngHNIYSpRTDTVDLRKEIGMVFQQPNPFPMSIYENVVYGLRLKGI 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 695 LYREVLEACALNddlSILPAGDQTEVGEK----GVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDAdVANHLLHRCI 770
Cdd:PRK14239 116 KDKQVLDEAVEK---SLKGASIWDEVKDRlhdsALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDP-ISAGKIEETL 191
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1039753390 771 LGVLSHTTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEI 812
Cdd:PRK14239 192 LGLKDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYNDTKQM 234
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
622-818 |
2.00e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 53.87 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVS----------ELSKGFGLATQEPWIQC--ATIRDNILFGk 689
Cdd:PRK13635 28 FSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGgmvlseetvwDVRRQVGMVFQNPDNQFvgATVQDDVAFG- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 690 tfdaqlyrevLEACALNDDLSIlPAGDQ--TEVG------EKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDA-- 759
Cdd:PRK13635 107 ----------LENIGVPREEMV-ERVDQalRQVGmedflnREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPrg 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039753390 760 -----DVANHLLHRCILGVLShttrllCTHRTEYLERADVVLLMEAGQLVRTGPPSEILPLVQA 818
Cdd:PRK13635 176 rrevlETVRQLKEQKGITVLS------ITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSGHM 233
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
622-812 |
2.26e-07 |
|
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: 52.76 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSS-------LLAAITGELHrLCGWVAVSE---LSKGFGLATQEPWIQCA-TIRDNI-LFGK 689
Cdd:cd03265 21 FRVRRGEIFGLLGPNGAGKTTtikmlttLLKPTSGRAT-VAGHDVVREpreVRRRIGIVFQDLSVDDElTGWENLyIHAR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 690 TFD------AQLYREVLEACALnddlsilpagdqTEVGEKGV-TLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVA 762
Cdd:cd03265 100 LYGvpgaerRERIDELLDFVGL------------LEAADRLVkTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1039753390 763 NHLLHRCILGVLSH-TTRLLCTHrteYLERA----DVVLLMEAGQLVRTGPPSEI 812
Cdd:cd03265 168 AHVWEYIEKLKEEFgMTILLTTH---YMEEAeqlcDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
622-807 |
3.61e-07 |
|
ATP-binding cassette domain of the Na+ transporter; 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 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 a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 51.98 E-value: 3.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELH------RLCGWVAVSE----------LSKGFGLAtqePWIqcaTIRDNI 685
Cdd:cd03266 26 FTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEpdagfaTVDGFDVVKEpaearrrlgfVSDSTGLY---DRL---TARENL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 686 LFgktFdAQLY---REVLEAcALNDDLSILPAGDQTEVGEKGvtLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVA 762
Cdd:cd03266 100 EY---F-AGLYglkGDELTA-RLEELADRLGMEELLDRRVGG--FSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMAT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1039753390 763 NHLL----HRCILGvlshTTRLLCTHRTEYLER-ADVVLLMEAGQLVRTG 807
Cdd:cd03266 173 RALRefirQLRALG----KCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
622-758 |
3.86e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 52.48 E-value: 3.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLL------------AAITGEL----HRL-CGWVAVSELSKGFGLATQEPWIQCATIRDN 684
Cdd:PRK14243 31 LDIPKNQITAFIGPSGCGKSTILrcfnrlndlipgFRVEGKVtfhgKNLyAPDVDPVEVRRRIGMVFQKPNPFPKSIYDN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 685 ILFGKTFDA------QLYREVLEACALNDDLsilpagdQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVD 758
Cdd:PRK14243 111 IAYGARINGykgdmdELVERSLRQAALWDEV-------KDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALD 183
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
562-803 |
3.93e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 53.82 E-value: 3.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 562 LLESKVSLDRIQRFlDLPSYSPEAyysPDPPAEPS-TALELHEALFSWDPIGASQKTFisHLQVKKGMLVGIVGKVGCGK 640
Cdd:PRK10522 289 LLSAQVAFNKLNKL-ALAPYKAEF---PRPQAFPDwQTLELRNVTFAYQDNGFSVGPI--NLTIKRGELLFLIGGNGSGK 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 641 SSLLAAITGELHRLCGWVAVSelSKGFGLATQEPWIQ--CATIRDNILFGKTFDAQlyREVLEACALNDDLSILPAGDQT 718
Cdd:PRK10522 363 STLAMLLTGLYQPQSGEILLD--GKPVTAEQPEDYRKlfSAVFTDFHLFDQLLGPE--GKPANPALVEKWLERLKMAHKL 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 719 EVGEKGVT---LSGGQRARIALARAVYQEKALYLLDDplAAVDAD-VANHLLHRCILGVLSHT--TRLLCTHRTEYLERA 792
Cdd:PRK10522 439 ELEDGRISnlkLSKGQKKRLALLLALAEERDILLLDE--WAADQDpHFRREFYQVLLPLLQEMgkTIFAISHDDHYFIHA 516
|
250
....*....|.
gi 1039753390 793 DVVLLMEAGQL 803
Cdd:PRK10522 517 DRLLEMRNGQL 527
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
622-813 |
5.29e-07 |
|
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: 51.67 E-value: 5.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELH------RLCGwVAVSELS------KGFGLATQEPWI-QCATIRDNILFG 688
Cdd:cd03224 21 LTVPEGEIVALLGRNGAGKTTLLKTIMGLLPprsgsiRFDG-RDITGLPpherarAGIGYVPEGRRIfPELTVEENLLLG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 689 ktfdAQLYREVLEACALNDDLSILPAGDQTEvGEKGVTLSGGQRARIALARAVYQEKALYLLDDP---LA-AVDADVANH 764
Cdd:cd03224 100 ----AYARRRAKRKARLERVYELFPRLKERR-KQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPsegLApKIVEEIFEA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1039753390 765 LLHRCILGVlshtTRLLCTHR-TEYLERADVVLLMEAGQLVRTGPPSEIL 813
Cdd:cd03224 175 IRELRDEGV----TILLVEQNaRFALEIADRAYVLERGRVVLEGTAAELL 220
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
622-813 |
5.37e-07 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 52.06 E-value: 5.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVSELS--KGFGLATQEPWIQcaTIRDNILF-GKTFDAQLYRE 698
Cdd:PRK11264 24 LEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITidTARSLSQQKGLIR--QLRQHVGFvFQNFNLFPHRT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 699 VLE----------------ACALNDDL--SILPAGDQTEVGEKgvtLSGGQRARIALARAVYQEKALYLLDDPLAAVDAD 760
Cdd:PRK11264 102 VLEniiegpvivkgepkeeATARARELlaKVGLAGKETSYPRR---LSGGQQQRVAIARALAMRPEVILFDEPTSALDPE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1039753390 761 VANHLLHRCILGVLSHTTRLLCTHRTEYL-ERADVVLLMEAGQLVRTGPPSEIL 813
Cdd:PRK11264 179 LVGEVLNTIRQLAQEKRTMVIVTHEMSFArDVADRAIFMDQGRIVEQGPAKALF 232
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
589-765 |
6.55e-07 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 53.14 E-value: 6.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 589 PDPPAEPSTALELHEALFSWDpigasQKTFISH--LQVKKGMLVGIVGKVGCGKSSLLAAITGELhrlcgwvavsELSKG 666
Cdd:COG0488 306 PPPERLGKKVLELEGLSKSYG-----DKTLLDDlsLRIDRGDRIGLIGPNGAGKSTLLKLLAGEL----------EPDSG 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 667 fglatqepwiqcaTIRdnilFGKT-----FDaQLYREvleacaLNDDLSIL-------PAGDQTEV----------GEK- 723
Cdd:COG0488 371 -------------TVK----LGETvkigyFD-QHQEE------LDPDKTVLdelrdgaPGGTEQEVrgylgrflfsGDDa 426
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1039753390 724 ----GVtLSGGQRARIALARAVYQEKALYLLDDPlaavdadvANHL 765
Cdd:COG0488 427 fkpvGV-LSGGEKARLALAKLLLSPPNVLLLDEP--------TNHL 463
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
622-791 |
6.76e-07 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 51.25 E-value: 6.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWV-------------AVSELSKGFGLATQE-PWIQCATIRDNILF 687
Cdd:cd03292 22 ISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIrvngqdvsdlrgrAIPYLRRKIGVVFQDfRLLPDRNVYENVAF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 688 GKTFDAQLYRE-------VLEACALNDDLSILPAGdqtevgekgvtLSGGQRARIALARAVYQEKALYLLDDPLAAVDAD 760
Cdd:cd03292 102 ALEVTGVPPREirkrvpaALELVGLSHKHRALPAE-----------LSGGEQQRVAIARAIVNSPTILIADEPTGNLDPD 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 1039753390 761 VANHllhrcILGVLSH-----TTRLLCTHRTEYLER 791
Cdd:cd03292 171 TTWE-----IMNLLKKinkagTTVVVATHAKELVDT 201
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
622-803 |
6.77e-07 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 50.99 E-value: 6.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAI-------TGELhRLCGWV------AVSELSKGFGLATQE----PWIqcaTIRDN 684
Cdd:cd03262 21 LTVKKGEVVVIIGPSGSGKSTLLRCInlleepdSGTI-IIDGLKltddkkNINELRQKVGMVFQQfnlfPHL---TVLEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 685 ILFGKTF-------DAQ-LYREVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAA 756
Cdd:cd03262 97 ITLAPIKvkgmskaEAEeRALELLEKVGLADKADAYPA-----------QLSGGQQQRVAIARALAMNPKVMLFDEPTSA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1039753390 757 VDADVANHllhrcILGVL-----SHTTRLLCTHRTEY-LERADVVLLMEAGQL 803
Cdd:cd03262 166 LDPELVGE-----VLDVMkdlaeEGMTMVVVTHEMGFaREVADRVIFMDDGRI 213
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
716-813 |
6.91e-07 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 51.89 E-value: 6.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 716 DQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHrcILGVLSH--TTRLLCTHRTEYLER-A 792
Cdd:PRK10619 142 DERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLR--IMQQLAEegKTMVVVTHEMGFARHvS 219
|
90 100
....*....|....*....|.
gi 1039753390 793 DVVLLMEAGQLVRTGPPSEIL 813
Cdd:PRK10619 220 SHVIFLHQGKIEEEGAPEQLF 240
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
624-804 |
1.16e-06 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 50.24 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 624 VKKGMLVGIVGKVGCGKSSLLAAITGEL--HRLCGWVAVSelskgfGLATQEPWIQCATI---RDNILFGktfdaQL-YR 697
Cdd:cd03213 32 AKPGELTAIMGPSGAGKSTLLNALAGRRtgLGVSGEVLIN------GRPLDKRSFRKIIGyvpQDDILHP-----TLtVR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 698 EVLE-ACALnddlsilpagdqtevgeKGvtLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHrcILGVLSH 776
Cdd:cd03213 101 ETLMfAAKL-----------------RG--LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMS--LLRRLAD 159
|
170 180 190
....*....|....*....|....*....|..
gi 1039753390 777 TTR-LLCT-H--RTEYLERADVVLLMEAGQLV 804
Cdd:cd03213 160 TGRtIICSiHqpSSEIFELFDKLLLLSQGRVI 191
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
632-812 |
1.52e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 51.41 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 632 IVGKVGCGKSSLLAAITGELHRLCGWVAVSE-----LSKGFGLATQEPWI----QCA------TIRDNILFG-KTFDAQL 695
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdAEKGICLPPEKRRIgyvfQDArlfphyKVRGNLRYGmAKSMVAQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 696 YREVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHrcILGVLS 775
Cdd:PRK11144 109 FDKIVALLGIEPLLDRYPG-----------SLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLP--YLERLA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1039753390 776 HTTR---LLCTHR-TEYLERADVVLLMEAGQLVRTGPPSEI 812
Cdd:PRK11144 176 REINipiLYVSHSlDEILRLADRVVVLEQGKVKAFGPLEEV 216
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
622-813 |
1.96e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 50.30 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLL------------AAITGELHrLCGW----VAVSELSKGFGLATQEP-WIQCATIRDN 684
Cdd:PRK14247 24 LEIPDNTITALMGPSGSGKSTLLrvfnrlielypeARVSGEVY-LDGQdifkMDVIELRRRVQMVFQIPnPIPNLSIFEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 685 ILFGKTFD---------AQLYREVLEACALNDDLsilpagdQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLA 755
Cdd:PRK14247 103 VALGLKLNrlvkskkelQERVRWALEKAQLWDEV-------KDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039753390 756 AVDAdVANHLLHRCILGVLSHTTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEIL 813
Cdd:PRK14247 176 NLDP-ENTAKIESLFLELKKDMTIVLVTHFPQQAARiSDYVAFLYKGQIVEWGPTREVF 233
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
630-812 |
2.77e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 50.19 E-value: 2.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 630 VGIVGKVGCGKSSLLAAITGELHRLCGWVAV----------SELSKGFGLATQEP--WIQCATIRDNILFGKT---FD-- 692
Cdd:PRK13652 33 IAVIGPNGAGKSTLFRHFNGILKPTSGSVLIrgepitkeniREVRKFVGLVFQNPddQIFSPTVEQDIAFGPInlgLDee 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 693 --AQLYREVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHrcI 770
Cdd:PRK13652 113 tvAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELID--F 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1039753390 771 LGVLSHT---TRLLCTHRTEYL-ERADVVLLMEAGQLVRTGPPSEI 812
Cdd:PRK13652 180 LNDLPETygmTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
622-806 |
2.93e-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: 48.19 E-value: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRlcgwvavselSKGfglatqepwiqcatirdNILF-GKTFDAQLYREVL 700
Cdd:cd03216 21 LSVRRGEVHALLGENGAGKSTLMKILSGLYKP----------DSG-----------------EILVdGKEVSFASPRDAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 701 EAcalnddlsilpagdqtevgekGVT----LSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHrcILGVL-- 774
Cdd:cd03216 74 RA---------------------GIAmvyqLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFK--VIRRLra 130
|
170 180 190
....*....|....*....|....*....|...
gi 1039753390 775 SHTTRLLCTHR-TEYLERADVVLLMEAGQLVRT 806
Cdd:cd03216 131 QGVAVIFISHRlDEVFEIADRVTVLRDGRVVGT 163
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
622-813 |
3.07e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 49.66 E-value: 3.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVS----------------ELSKGFGLATQEP-WIQCATIRDN 684
Cdd:PRK14246 31 IKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDgkvlyfgkdifqidaiKLRKEVGMVFQQPnPFPHLSIYDN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 685 ILFG-KTFDAQLYREVLEACalndDLSILPAGDQTEVGEK----GVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDA 759
Cdd:PRK14246 111 IAYPlKSHGIKEKREIKKIV----EECLRKVGLWKEVYDRlnspASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDI 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1039753390 760 dVANHLLHRCILGVLSHTTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEIL 813
Cdd:PRK14246 187 -VNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIF 240
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
621-769 |
3.14e-06 |
|
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: 48.30 E-value: 3.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 621 HLQVKKGMLVGIVGKVGCGKSSLLAAI-------TGELHRLCGwvavselSKGFGLAtQEPWIQCATIRDNIlfgktfda 693
Cdd:cd03223 21 SFEIKPGDRLLITGPSGTGKSSLFRALaglwpwgSGRIGMPEG-------EDLLFLP-QRPYLPLGTLREQL-------- 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039753390 694 qlyrevleacalnddlsILPAGDqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHRC 769
Cdd:cd03223 85 -----------------IYPWDD---------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL 134
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
622-759 |
3.15e-06 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 49.70 E-value: 3.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELH------RLCGwVAVSELSKGFGLATQE----PWiqcATIRDNILFGKTF 691
Cdd:PRK11248 22 LTLESGELLVVLGPSGCGKTTLLNLIAGFVPyqhgsiTLDG-KPVEGPGAERGVVFQNegllPW---RNVQDNVAFGLQL 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039753390 692 dAQLYREVLEACALnddlSILPAGDQTEVGEKGV-TLSGGQRARIALARAVYQEKALYLLDDPLAAVDA 759
Cdd:PRK11248 98 -AGVEKMQRLEIAH----QMLKKVGLEGAEKRYIwQLSGGQRQRVGIARALAANPQLLLLDEPFGALDA 161
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
523-804 |
3.54e-06 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 50.95 E-value: 3.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 523 FITYVLMGHQLTATKVFTALALVRM-LILPLNNFPWVINGLLESKVSLDRIQRF-LDLPSYSPEAYYSPDPPAEPS-TAL 599
Cdd:COG4615 249 LILFLLPALGWADPAVLSGFVLVLLfLRGPLSQLVGALPTLSRANVALRKIEELeLALAAAEPAAADAAAPPAPADfQTL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 600 ELHEALFSWDPIGASqKTF----IShLQVKKGMLVGIVGKVGCGKSSLLAAITGeLHR------LCGWVAVSElskgfgl 669
Cdd:COG4615 329 ELRGVTYRYPGEDGD-EGFtlgpID-LTIRRGELVFIVGGNGSGKSTLAKLLTG-LYRpesgeiLLDGQPVTA------- 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 670 ATQEPWIQ--CATIRDNILF------GKTFDAQLYREVLEACALNDDLSIlpagdqtevgEKG----VTLSGGQRARIAL 737
Cdd:COG4615 399 DNREAYRQlfSAVFSDFHLFdrllglDGEADPARARELLERLELDHKVSV----------EDGrfstTDLSQGQRKRLAL 468
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039753390 738 ARAVYQEKALYLLDDpLAAvDADVAN-HLLHRCILGVL----------SHTTRllcthrteYLERADVVLLMEAGQLV 804
Cdd:COG4615 469 LVALLEDRPILVFDE-WAA-DQDPEFrRVFYTELLPELkargktviaiSHDDR--------YFDLADRVLKMDYGKLV 536
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
623-822 |
3.92e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 49.62 E-value: 3.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 623 QVKKGM--------LVGIVGKVGCGKSSLLAAITGELHRLCGWV-----AVSELSKGF-----GLAT--QEPWIQC--AT 680
Cdd:PRK13638 15 PVLKGLnldfslspVTGLVGANGCGKSTLFMNLSGLLRPQKGAVlwqgkPLDYSKRGLlalrqQVATvfQDPEQQIfyTD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 681 IRDNILFG----KTFDAQLYREVLEACALNDDLSILPAGDQTevgekgvtLSGGQRARIALARAVYQEKALYLLDDPLAA 756
Cdd:PRK13638 95 IDSDIAFSlrnlGVPEAEITRRVDEALTLVDAQHFRHQPIQC--------LSHGQKKRVAIAGALVLQARYLLLDEPTAG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039753390 757 VDADVANHLLH--RCILGVLSHTtrLLCTHRTEYL-ERADVVLLMEAGQLVRTGPPSEILPLVQAVPTA 822
Cdd:PRK13638 167 LDPAGRTQMIAiiRRIVAQGNHV--IISSHDIDLIyEISDAVYVLRQGQILTHGAPGEVFACTEAMEQA 233
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
630-812 |
4.75e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 50.93 E-value: 4.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 630 VGIVGKVGCGKSSLLAAIT-------GELH---RLCGWVAVSELSKGFGLATQEPWIQCATIRDNI-LFGKTFDAQLYRe 698
Cdd:PTZ00243 1339 VGIVGRTGSGKSTLLLTFMrmvevcgGEIRvngREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVdPFLEASSAEVWA- 1417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 699 VLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQE-KALYLLDDPLAAVDadvanHLLHRCI----LGV 773
Cdd:PTZ00243 1418 ALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKgSGFILMDEATANID-----PALDRQIqatvMSA 1492
|
170 180 190
....*....|....*....|....*....|....*....
gi 1039753390 774 LSHTTRLLCTHRTEYLERADVVLLMEAGQLVRTGPPSEI 812
Cdd:PTZ00243 1493 FSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPREL 1531
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
622-807 |
4.75e-06 |
|
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: 48.73 E-value: 4.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLvGIVGKVGCGKSSLLAAITGELHRLCGWVAV---------SELSKGFGLATQEP-WIQCATIRD-----NIL 686
Cdd:cd03264 21 LTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIdgqdvlkqpQKLRRRIGYLPQEFgVYPNFTVREfldyiAWL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 687 FG---KTFDAQLyREVLEACALNDdlsilpagdqtEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVdaDVAN 763
Cdd:cd03264 100 KGipsKEVKARV-DEVLELVNLGD-----------RAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGL--DPEE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1039753390 764 HLLHRCILGVLSHT-TRLLCTHRTEYLER-ADVVLLMEAGQLVRTG 807
Cdd:cd03264 166 RIRFRNLLSELGEDrIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
615-813 |
5.02e-06 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 49.42 E-value: 5.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 615 QKTFISHL--QVKKGMLVGIVGKVGCGKSSLLAAITGELH------RLCGWVAVSELSKG---FGLATQ----EPWIqca 679
Cdd:PRK13537 19 DKLVVDGLsfHVQRGECFGLLGPNGAGKTTTLRMLLGLTHpdagsiSLCGEPVPSRARHArqrVGVVPQfdnlDPDF--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 680 TIRDNIL-FGKTF--DAQLYREVLEACAlndDLSILPAGDQTEVGEkgvtLSGGQRARIALARAVYQEKALYLLDDPLAA 756
Cdd:PRK13537 96 TVRENLLvFGRYFglSAAAARALVPPLL---EFAKLENKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEPTTG 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039753390 757 VDADvANHLLHRCILGVLSH-TTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEIL 813
Cdd:PRK13537 169 LDPQ-ARHLMWERLRSLLARgKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALI 226
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
623-812 |
5.79e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 49.34 E-value: 5.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 623 QVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVS----------ELSKGFGLATQEPWIQC--ATIRDNILFG-- 688
Cdd:PRK13650 29 HVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDgdllteenvwDIRHKIGMVFQNPDNQFvgATVEDDVAFGle 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 689 -KTFDAQLYRE-VLEACALnddlsilpAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLL 766
Cdd:PRK13650 109 nKGIPHEEMKErVNEALEL--------VGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELI 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1039753390 767 hRCILGVLS--HTTRLLCTHRTEYLERADVVLLMEAGQLVRTGPPSEI 812
Cdd:PRK13650 181 -KTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
588-813 |
6.96e-06 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 49.44 E-value: 6.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 588 SPDPPAEPSTALELHEALFSW-DPIGASQKTFishlQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAV------ 660
Cdd:PRK13536 31 ASIPGSMSTVAIDLAGVSKSYgDKAVVNGLSF----TVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVlgvpvp 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 661 --SELSK-GFGLATQ-EPWIQCATIRDNIL-FGKTFDAQLyREVLEACALNDDLSILPAGDQTEVGEkgvtLSGGQRARI 735
Cdd:PRK13536 107 arARLARaRIGVVPQfDNLDLEFTVRENLLvFGRYFGMST-REIEAVIPSLLEFARLESKADARVSD----LSGGMKRRL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 736 ALARAVYQEKALYLLDDPLAAVDADvANHLLHRCILGVLSH-TTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEIL 813
Cdd:PRK13536 182 TLARALINDPQLLILDEPTTGLDPH-ARHLIWERLRSLLARgKTILLTTHFMEEAERlCDRLCVLEAGRKIAEGRPHALI 260
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
622-759 |
7.65e-06 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 47.87 E-value: 7.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVavseLSKGFGLATQEPWIQCA--------------TIRDNILF 687
Cdd:cd03231 21 FTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRV----LLNGGPLDFQRDSIARGllylghapgikttlSVLENLRF 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039753390 688 gktfdaqlyrevleACALNDDLSILPAGDQteVGEKGV------TLSGGQRARIALARAVYQEKALYLLDDPLAAVDA 759
Cdd:cd03231 97 --------------WHADHSDEQVEEALAR--VGLNGFedrpvaQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
621-784 |
7.71e-06 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 47.74 E-value: 7.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 621 HLQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVSelSKGFGLATQEPWIQCA------------TIRDNILFG 688
Cdd:TIGR01189 20 SFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWN--GTPLAEQRDEPHENILylghlpglkpelSALENLHFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 689 KTFDAQLYREVLEACALN--DDLSILPAGdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLL 766
Cdd:TIGR01189 98 AAIHGGAQRTIEDALAAVglTGFEDLPAA----------QLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLA 167
|
170 180
....*....|....*....|..
gi 1039753390 767 HRcilgVLSHTTR----LLCTH 784
Cdd:TIGR01189 168 GL----LRAHLARggivLLTTH 185
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
622-810 |
8.15e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 48.58 E-value: 8.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAV----------SELSKGFGLATQEPWIQ--CATIRDNILFG- 688
Cdd:PRK13647 26 LSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVmgrevnaeneKWVRSKVGLVFQDPDDQvfSSTVWDDVAFGp 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 689 ---KTFDAQLYREVLEAcalnddlsiLPAGDQTEVGEKG-VTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANH 764
Cdd:PRK13647 106 vnmGLDKDEVERRVEEA---------LKAVRMWDFRDKPpYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQET 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1039753390 765 LlhRCILGVLSH--TTRLLCTHRTEY-LERADVVLLMEAGQLVRTGPPS 810
Cdd:PRK13647 177 L--MEILDRLHNqgKTVIVATHDVDLaAEWADQVIVLKEGRVLAEGDKS 223
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
727-813 |
9.18e-06 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 48.07 E-value: 9.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 727 LSGGQRARIALARAVYQEKALYLLDDPLAAVD----ADVanhllhrciLGVL-----SHTTRLLCTH-----RteylERA 792
Cdd:COG1126 137 LSGGQQQRVAIARALAMEPKVMLFDEPTSALDpelvGEV---------LDVMrdlakEGMTMVVVTHemgfaR----EVA 203
|
90 100
....*....|....*....|.
gi 1039753390 793 DVVLLMEAGQLVRTGPPSEIL 813
Cdd:COG1126 204 DRVVFMDGGRIVEEGPPEEFF 224
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
621-812 |
1.10e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 48.24 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 621 HLQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVSELS--------------KGFGLATQEPWIQC--ATIRDN 684
Cdd:PRK13646 27 NTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITithktkdkyirpvrKRIGMVFQFPESQLfeDTVERE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 685 ILFG-KTFDAQL-------YREVLEACALNDDLSILPagdqtevgekgVTLSGGQRARIALARAVYQEKALYLLDDPLAA 756
Cdd:PRK13646 107 IIFGpKNFKMNLdevknyaHRLLMDLGFSRDVMSQSP-----------FQMSGGQMRKIAIVSILAMNPDIIVLDEPTAG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039753390 757 VDADvANHLLHRCI--LGVLSHTTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEI 812
Cdd:PRK13646 176 LDPQ-SKRQVMRLLksLQTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKEL 233
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
632-768 |
1.13e-05 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 47.79 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 632 IVGKVGCGKSSLLAAITGELHRLCGWV-----AVSELS-----KGFGLATQEPWIQCATIRDNILfgktFDAQLYREVLE 701
Cdd:PRK10247 38 ITGPSGCGKSTLLKIVASLISPTSGTLlfegeDISTLKpeiyrQQVSYCAQTPTLFGDTVYDNLI----FPWQIRNQQPD 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039753390 702 ACALNDDLSI--LPagdqTEVGEKGVT-LSGGQRARIALARAV-YQEKALyLLDDPLAAVDAD---VANHLLHR 768
Cdd:PRK10247 114 PAIFLDDLERfaLP----DTILTKNIAeLSGGEKQRISLIRNLqFMPKVL-LLDEITSALDESnkhNVNEIIHR 182
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
622-758 |
1.23e-05 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 47.96 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVSELSKGFGL----------ATQEPWIQCATIRDNILFGKTF 691
Cdd:PRK15056 28 FTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALqknlvayvpqSEEVDWSFPVLVEDVVMMGRYG 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039753390 692 DAQLYRE--------VLEACALNDDLSIlpagDQTEVGEkgvtLSGGQRARIALARAVYQEKALYLLDDPLAAVD 758
Cdd:PRK15056 108 HMGWLRRakkrdrqiVTAALARVDMVEF----RHRQIGE----LSGGQKKRVFLARAIAQQGQVILLDEPFTGVD 174
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
598-813 |
1.33e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 48.11 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 598 ALELHEALFSWDpigaSQKTFIS-HLQVKKGMLVGIVGKVGCGKSSLLAAITgELHRLCGWVAVSELSKGFGLATQEPWI 676
Cdd:PRK14258 7 AIKVNNLSFYYD----TQKILEGvSMEIYQSKVTAIIGPSGCGKSTFLKCLN-RMNELESEVRVEGRVEFFNQNIYERRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 677 QCATIRDNI--LFGKT--FDAQLYREVLEACALN--------DDL--SILPAGD-----QTEVGEKGVTLSGGQRARIAL 737
Cdd:PRK14258 82 NLNRLRRQVsmVHPKPnlFPMSVYDNVAYGVKIVgwrpkleiDDIveSALKDADlwdeiKHKIHKSALDLSGGQQQRLCI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 738 ARAVYQEKALYLLDDPLAAVDADVA---NHLLHRciLGVLSHTTRLLCTHRTEYLER-ADVVLLMEA-----GQLVRTGP 808
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDPIASmkvESLIQS--LRLRSELTMVIVSHNLHQVSRlSDFTAFFKGnenriGQLVEFGL 239
|
....*
gi 1039753390 809 PSEIL 813
Cdd:PRK14258 240 TKKIF 244
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
609-813 |
1.50e-05 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 48.49 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 609 DPIGASQKTFISHLQVKKGMLVGIVGKVGCGKSSLLAAitgeLHRLCGWVAVSELSKGFGLATqepwIQCATIRD----- 683
Cdd:PRK10070 36 EKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRL----LNRLIEPTRGQVLIDGVDIAK----ISDAELREvrrkk 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 684 -NILFgKTFDAQLYREVLEACALNDDLSILPAGDQTE--------VGEKGVT------LSGGQRARIALARAVYQEKALY 748
Cdd:PRK10070 108 iAMVF-QSFALMPHMTVLDNTAFGMELAGINAEERREkaldalrqVGLENYAhsypdeLSGGMRQRVGLARALAINPDIL 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039753390 749 LLDDPLAAVDADVANHLLHRCI-LGVLSHTTRLLCTHR-TEYLERADVVLLMEAGQLVRTGPPSEIL 813
Cdd:PRK10070 187 LMDEAFSALDPLIRTEMQDELVkLQAKHQRTIVFISHDlDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
627-781 |
1.64e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.01 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 627 GMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAvseLSKGFGL------------ATQEPWIQCATIRDNILfgktfdAQ 694
Cdd:PRK10636 338 GSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIG---LAKGIKLgyfaqhqleflrADESPLQHLARLAPQEL------EQ 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 695 LYREVLEACALNddlsilpaGDQteVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHRCI---- 770
Cdd:PRK10636 409 KLRDYLGGFGFQ--------GDK--VTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIdfeg 478
|
170
....*....|..
gi 1039753390 771 -LGVLSHTTRLL 781
Cdd:PRK10636 479 aLVVVSHDRHLL 490
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
622-807 |
2.34e-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: 46.50 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVseLSKGFGLATQEPW---------IQCATIRDNILFGktfd 692
Cdd:cd03269 21 FSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLF--DGKPLDIAARNRIgylpeerglYPKMKVIDQLVYL---- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 693 AQLyREVLEACALNDDLSILPAGDQTEVGEKGV-TLSGGQRARIALARAVYQEKALYLLDDPLAAVDAdVANHLLHRCIL 771
Cdd:cd03269 95 AQL-KGLKKEEARRRIDEWLERLELSEYANKRVeELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP-VNVELLKDVIR 172
|
170 180 190
....*....|....*....|....*....|....*...
gi 1039753390 772 GVLSH-TTRLLCTHRTEYLER-ADVVLLMEAGQLVRTG 807
Cdd:cd03269 173 ELARAgKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
625-815 |
2.74e-05 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 48.12 E-value: 2.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 625 KKGMLVGIVGKVGCGKSSLLAAITG----------------------ELHRLCGWVAVSELSKGfGLATQEPWIQCATIR 682
Cdd:TIGR00955 49 KPGELLAVMGSSGAGKTTLMNALAFrspkgvkgsgsvllngmpidakEMRAISAYVQQDDLFIP-TLTVREHLMFQAHLR 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 683 DNILFGKTFDAQLYREVLEacalndDLSILPAGDqTEVGEKGVT--LSGGQRARIALARAVYQEKALYLLDDPLAAVDAD 760
Cdd:TIGR00955 128 MPRRVTKKEKRERVDEVLQ------ALGLRKCAN-TRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSF 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039753390 761 VANHLLHrcILGVLSHTTR-LLCT-HR--TEYLERADVVLLMEAGQLVRTGPPSEILPL 815
Cdd:TIGR00955 201 MAYSVVQ--VLKGLAQKGKtIICTiHQpsSELFELFDKIILMAEGRVAYLGSPDQAVPF 257
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
622-812 |
3.00e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 46.99 E-value: 3.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVS------------ELSKGFGLATQEPWIQ--CATIRDNILF 687
Cdd:PRK13639 23 FKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKgepikydkksllEVRKTVGIVFQNPDDQlfAPTVEEDVAF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 688 G----KTFDAQLYREVLEACAlnddlsilpagdqtEVGEKGVT------LSGGQRARIALARAVYQEKALYLLDDPLAAV 757
Cdd:PRK13639 103 GplnlGLSKEEVEKRVKEALK--------------AVGMEGFEnkpphhLSGGQKKRVAIAGILAMKPEIIVLDEPTSGL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039753390 758 DADVANHLLHrcILGVLSH--TTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEI 812
Cdd:PRK13639 169 DPMGASQIMK--LLYDLNKegITIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPKEV 224
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
705-798 |
3.54e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.10 E-value: 3.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 705 LNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDaDVANHLLHRCILGVLSHTTR--LLC 782
Cdd:PTZ00265 558 IHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD-NKSEYLVQKTINNLKGNENRitIII 636
|
90
....*....|....*.
gi 1039753390 783 THRTEYLERADVVLLM 798
Cdd:PTZ00265 637 AHRLSTIRYANTIFVL 652
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
621-769 |
7.20e-05 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 44.79 E-value: 7.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 621 HLQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVavseLSKGFGLATQepwiqcatirdnilfgktfDAQLYREVL 700
Cdd:PRK13538 21 SFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEV----LWQGEPIRRQ-------------------RDEYHQDLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 701 ---EACALNDDLSILP--------AGDQTE---------VGEKGV------TLSGGQRARIALARAVYQEKALYLLDDPL 754
Cdd:PRK13538 78 ylgHQPGIKTELTALEnlrfyqrlHGPGDDealwealaqVGLAGFedvpvrQLSAGQQRRVALARLWLTRAPLWILDEPF 157
|
170
....*....|....*....
gi 1039753390 755 AAVD----ADVANHLLHRC 769
Cdd:PRK13538 158 TAIDkqgvARLEALLAQHA 176
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
727-803 |
9.86e-05 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 44.81 E-value: 9.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 727 LSGGQRARIALARAVYQEKALYLLDDPLAAVD---ADVANHLLHRciLGVLSHTTRLLCTHRTEYLERADVVLLMEAGQL 803
Cdd:PRK11629 146 LSGGERQRVAIARALVNNPRLVLADEPTGNLDarnADSIFQLLGE--LNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRL 223
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
624-760 |
1.34e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 44.09 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 624 VKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVAVselsKGFGLATQEPWIQCA------------TIRDNILFGKTF 691
Cdd:PRK13539 25 LAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKL----DGGDIDDPDVAEACHylghrnamkpalTVAENLEFWAAF 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039753390 692 DAQLYREVLEA-CALN-DDLSILPAGDqtevgekgvtLSGGQRARIALARAVYQEKALYLLDDPLAAVDAD 760
Cdd:PRK13539 101 LGGEELDIAAAlEAVGlAPLAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTAALDAA 161
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
621-813 |
1.37e-04 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 44.68 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 621 HLQVKKGMLVGIVGKVGCGKSSL---LAAITGELHRLCGW--VAVSELSKGFGLATQEPwIQCA------------TIRD 683
Cdd:PRK10419 32 SLSLKSGETVALLGRSGCGKSTLarlLVGLESPSQGNVSWrgEPLAKLNRAQRKAFRRD-IQMVfqdsisavnprkTVRE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 684 NI------LFGKTFDAQLYR--EVLEACALND-DLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPL 754
Cdd:PRK10419 111 IIreplrhLLSLDKAERLARasEMLRAVDLDDsVLDKRPP-----------QLSGGQLQRVCLARALAVEPKLLILDEAV 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039753390 755 AAVDAdvanhLLHRCILGVL------SHTTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEIL 813
Cdd:PRK10419 180 SNLDL-----VLQAGVIRLLkklqqqFGTACLFITHDLRLVERfCQRVMVMDNGQIVETQPVGDKL 240
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
622-813 |
1.71e-04 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 44.43 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELH--------RLCGWVAVSelskGFGLATQEP---------WIQCA----- 679
Cdd:PRK13547 22 LRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggaprgaRVTGDVTLN----GEPLAAIDAprlarlravLPQAAqpafa 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 680 -TIRDNILFGKTFDAQLYREVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQ--------EKALY-L 749
Cdd:PRK13547 98 fSAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphdaaQPPRYlL 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039753390 750 LDDPLAAVDADVANHLLH--RCI-----LGVLS--HTTRLLCTHrteylerADVVLLMEAGQLVRTGPPSEIL 813
Cdd:PRK13547 178 LDEPTAALDLAHQHRLLDtvRRLardwnLGVLAivHDPNLAARH-------ADRIAMLADGAIVAHGAPADVL 243
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
624-814 |
1.73e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 44.79 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 624 VKKGMLVGIVGKVGCGKSSLLAAITG-----------------ELHRLCGWvavsELSKGFGLATQEPWIQC--ATIRDN 684
Cdd:PRK13640 30 IPRGSWTALIGHNGSGKSTISKLINGlllpddnpnskitvdgiTLTAKTVW----DIREKVGIVFQNPDNQFvgATVGDD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 685 ILFGKTFDA-------QLYREVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAV 757
Cdd:PRK13640 106 VAFGLENRAvprpemiKIVRDVLADVGMLDYIDSEPA-----------NLSGGQKQRVAIAGILAVEPKIIILDESTSML 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039753390 758 DA-------DVANHLLHRCILGVLShttrllCTHRTEYLERADVVLLMEAGQLVRTGPPSEILP 814
Cdd:PRK13640 175 DPagkeqilKLIRKLKKKNNLTVIS------ITHDIDEANMADQVLVLDDGKLLAQGSPVEIFS 232
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
622-812 |
2.62e-04 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 43.92 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGEL----HRLCGWV-------AVSELsKGFGLAT--QEPwiQCA-----TIRD 683
Cdd:PRK10418 24 LTLQRGRVLALVGGSGSGKSLTCAAALGILpagvRQTAGRVlldgkpvAPCAL-RGRKIATimQNP--RSAfnplhTMHT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 684 NIL-----FGKTFDAQLYREVLEACALNDDLSILPAgdqtevgeKGVTLSGG--QRARIALAraVYQEKALYLLDDPLAA 756
Cdd:PRK10418 101 HARetclaLGKPADDATLTAALEAVGLENAARVLKL--------YPFEMSGGmlQRMMIALA--LLCEAPFIIADEPTTD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039753390 757 VDADVANHllhrcILGVLSHTTR------LLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEI 812
Cdd:PRK10418 171 LDVVAQAR-----ILDLLESIVQkralgmLLVTHDMGVVARlADDVAVMSHGRIVEQGDVETL 228
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
728-837 |
2.80e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 44.19 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 728 SGGQRARIALARAVYQEKALYLLDDPLAAVD----ADVAN---------HLLHRCI---LGVLSHTtrllcthrteyler 791
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDvsvqAQVLNlmmdlqqelGLSYVFIshdLSVVEHI-------------- 221
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039753390 792 ADVVLLMEAGQLVRTGPPSEIL--P-------LVQAVPTAWAE--KEQVATSGQSPS 837
Cdd:PRK11308 222 ADEVMVMYLGRCVEKGTKEQIFnnPrhpytqaLLSATPRLNPDdrRERIKLTGELPS 278
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
627-819 |
3.00e-04 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 44.87 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 627 GMLVGIVGKVGCGKSSLLAAITGELHRLC--GWVAVS------ELSKGFGLATQepwiqcatirDNILFGKTfdaqLYRE 698
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANnrkptkQILKRTGFVTQ----------DDILYPHL----TVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 699 VLEACALNDDLSILPAGDQTEVGEK-----GVT--------------LSGGQRARIALARAVYQEKALYLLDDPLAAVDA 759
Cdd:PLN03211 160 TLVFCSLLRLPKSLTKQEKILVAESviselGLTkcentiignsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDA 239
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039753390 760 DVANHLLHrcILGVLSHTTRLLCTHRTEYLERA----DVVLLMEAGQLVRTGPPSEILPLVQAV 819
Cdd:PLN03211 240 TAAYRLVL--TLGSLAQKGKTIVTSMHQPSSRVyqmfDSVLVLSEGRCLFFGKGSDAMAYFESV 301
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
622-820 |
3.16e-04 |
|
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: 44.68 E-value: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAI------TGELhRLCGwVAVSELSKG------------F---------------- 667
Cdd:COG4172 307 LTLRRGETLGLVGESGSGKSTLGLALlrlipsEGEI-RFDG-QDLDGLSRRalrplrrrmqvvFqdpfgslsprmtvgqi 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 668 ---GLATQEPWIQCATIRDNIlfgktfdaqlyREVLEacalnddlsilpagdqtEVGEKGVTL-------SGGQRARIAL 737
Cdd:COG4172 385 iaeGLRVHGPGLSAAERRARV-----------AEALE-----------------EVGLDPAARhryphefSGGQRQRIAI 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 738 ARAVYQEKALYLLDDPLAAVDADVANHllhrcILGVLShttRLLCTHRTEYL----------ERADVVLLMEAGQLVRTG 807
Cdd:COG4172 437 ARALILEPKLLVLDEPTSALDVSVQAQ-----ILDLLR---DLQREHGLAYLfishdlavvrALAHRVMVMKDGKVVEQG 508
|
250 260
....*....|....*....|..
gi 1039753390 808 PPSEIL--P-------LVQAVP 820
Cdd:COG4172 509 PTEQVFdaPqhpytraLLAAAP 530
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
622-812 |
3.63e-04 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 44.02 E-value: 3.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGeLHR------LCGWVAVSELSKG---------------FGLATQEpwiqcaT 680
Cdd:PRK11153 26 LHIPAGEIFGVIGASGAGKSTLIRCINL-LERptsgrvLVDGQDLTALSEKelrkarrqigmifqhFNLLSSR------T 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 681 IRDNILF----GKTFDAQLYR---EVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDP 753
Cdd:PRK11153 99 VFDNVALplelAGTPKAEIKArvtELLELVGLSDKADRYPA-----------QLSGGQKQRVAIARALASNPKVLLCDEA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039753390 754 LAAVDADVAnhllhRCILGVLS------HTTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEI 812
Cdd:PRK11153 168 TSALDPATT-----RSILELLKdinrelGLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGTVSEV 228
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
619-758 |
4.16e-04 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 44.24 E-value: 4.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 619 IShLQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLCGWVA---------------------VSELSKGFGLatqepwIQ 677
Cdd:COG1129 271 VS-FSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRldgkpvrirsprdairagiayVPEDRKGEGL------VL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 678 CATIRDNI---LFGKTFDAQLY---REVLEACALNDDLSILPAGDQTEVGekgvTLSGGQRARIALARAVYQEKALYLLD 751
Cdd:COG1129 344 DLSIRENItlaSLDRLSRGGLLdrrRERALAEEYIKRLRIKTPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLILD 419
|
....*..
gi 1039753390 752 DPLAAVD 758
Cdd:COG1129 420 EPTRGID 426
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
727-813 |
4.70e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 43.54 E-value: 4.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 727 LSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHrcILGVL--SHTTRLLCTHRTEY-LERADVVLLMEAGQL 803
Cdd:PRK13651 166 LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILE--IFDNLnkQGKTIILVTHDLDNvLEWTKRTIFFKDGKI 243
|
90
....*....|
gi 1039753390 804 VRTGPPSEIL 813
Cdd:PRK13651 244 IKDGDTYDIL 253
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
622-837 |
4.87e-04 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 43.50 E-value: 4.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGeLHRLCGWVA---------VSELS---------KGFGLATQEP-------Wi 676
Cdd:COG0444 26 FDVRRGETLGLVGESGSGKSTLARAILG-LLPPPGITSgeilfdgedLLKLSekelrkirgREIQMIFQDPmtslnpvM- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 677 qcaTIRDNI-----LFGKTFDAQLY---REVLEACALNDDLSIL---PagdqtevGEkgvtLSGGQRARIALARAVYQEK 745
Cdd:COG0444 104 ---TVGDQIaeplrIHGGLSKAEAReraIELLERVGLPDPERRLdryP-------HE----LSGGMRQRVMIARALALEP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 746 ALYLLDDPLAAVD----ADVANHLLHRC---------I---LGVLSHTtrllcthrteylerADVVLLMEAGQLVRTGPP 809
Cdd:COG0444 170 KLLIADEPTTALDvtiqAQILNLLKDLQrelglailfIthdLGVVAEI--------------ADRVAVMYAGRIVEEGPV 235
|
250 260 270
....*....|....*....|....*....|....*...
gi 1039753390 810 SEIL-----P----LVQAVPTAWAEKEQVAT-SGQSPS 837
Cdd:COG0444 236 EELFenprhPytraLLSSIPRLDPDGRRLIPiPGEPPS 273
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
611-822 |
7.73e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 42.78 E-value: 7.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 611 IGASQKTFIShlQVKKGM----LVGIVGKVGCGKSSLLAAITGELHRLCGWVA----------------VSELSKGFGLA 670
Cdd:PRK14271 29 LGFAGKTVLD--QVSMGFparaVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYsgdvllggrsifnyrdVLEFRRRVGML 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 671 TQEPWIQCATIRDNILFG----KTFDAQLYREVLEAC--------ALNDDLSILPagdqtevgekgVTLSGGQRARIALA 738
Cdd:PRK14271 107 FQRPNPFPMSIMDNVLAGvrahKLVPRKEFRGVAQARltevglwdAVKDRLSDSP-----------FRLSGGQQQLLCLA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 739 RAVYQEKALYLLDDPLAAVDADVANHlLHRCILGVLSHTTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEILPLVQ 817
Cdd:PRK14271 176 RTLAVNPEVLLLDEPTSALDPTTTEK-IEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFSSPK 254
|
....*
gi 1039753390 818 AVPTA 822
Cdd:PRK14271 255 HAETA 259
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
623-813 |
7.82e-04 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 42.23 E-value: 7.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 623 QVKKGMLVGIVGKVGCGKSSLLAAI------TGELH----RLCGWVAvSELSKGFG-LATQE------PWIQCATIRDNI 685
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLARMagllpgSGSIQfagqPLEAWSA-AELARHRAyLSQQQtppfamPVFQYLTLHQPD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 686 LFGKTFDAQLYREVLEACALNDDLSilpagdqTEVGekgvTLSGGQRARIALARAVYQ-------EKALYLLDDPLAAVD 758
Cdd:PRK03695 97 KTRTEAVASALNEVAEALGLDDKLG-------RSVN----QLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039753390 759 -ADVA--NHLLHR-CILGVlshtTRLLCTH---RTeyLERADVVLLMEAGQLVRTGPPSEIL 813
Cdd:PRK03695 166 vAQQAalDRLLSElCQQGI----AVVMSSHdlnHT--LRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
728-795 |
9.28e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 43.16 E-value: 9.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 728 SGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLL---------HRCILGVLSH---TTRLLCtHRTEYLERADVV 795
Cdd:PRK15134 427 SGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILallkslqqkHQLAYLFISHdlhVVRALC-HQVIVLRQGEVV 505
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
630-765 |
1.01e-03 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 43.00 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 630 VGIVGKVGCGKSSLL---AAI----TGElhrlcgwvAVSELSKGFGLATQEPWI-QCATIRDNILFG------------- 688
Cdd:TIGR03719 34 IGVLGLNGAGKSTLLrimAGVdkdfNGE--------ARPQPGIKVGYLPQEPQLdPTKTVRENVEEGvaeikdaldrfne 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 689 ---------KTFDAQLYR-----EVLEACA---LNDDLSI------LPAGDQtevgeKGVTLSGGQRARIALARAVYQEK 745
Cdd:TIGR03719 106 isakyaepdADFDKLAAEqaelqEIIDAADawdLDSQLEIamdalrCPPWDA-----DVTKLSGGERRRVALCRLLLSKP 180
|
170 180
....*....|....*....|....
gi 1039753390 746 ALYLLDDPLAAVDAD-VA---NHL 765
Cdd:TIGR03719 181 DMLLLDEPTNHLDAEsVAwleRHL 204
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
630-781 |
1.09e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.92 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 630 VGIVGKVGCGKSSLLAAITGELHRLCGWV--------AVSELSKGFGL-ATQEPWIQCATIRDNILfgktfdAQLYREVL 700
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGTVfrsakvrmAVFSQHHVDGLdLSSNPLLYMMRCFPGVP------EQKLRAHL 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 701 EACALNDDLSILPAgdqtevgekgVTLSGGQRARIALARAVYQEKALYLLDDPLAAVDADVANHLLHRCIL---GVL--S 775
Cdd:PLN03073 612 GSFGVTGNLALQPM----------YTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLfqgGVLmvS 681
|
....*.
gi 1039753390 776 HTTRLL 781
Cdd:PLN03073 682 HDEHLI 687
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
726-767 |
1.33e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.54 E-value: 1.33e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1039753390 726 TLSGGQRARIALARAVYQEKALYLLDDPlaavdadvANHL-LH 767
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEP--------TNHLdLH 378
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
883-994 |
2.35e-03 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350043 [Multi-domain] Cd Length: 313 Bit Score: 41.39 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 883 GSGLAAAILVSLLLMQATRNGADWWLAHWLSQlKAGRNGSREDPASCSPGSTalfsprlllfspgnlytpllstplhkaa 962
Cdd:cd18599 1 GYVVFLFVLLLFILSVGSTVFSDWWLSYWLKQ-GSGNTTNNVDNSTVDSGNI---------------------------- 51
|
90 100 110
....*....|....*....|....*....|..
gi 1039753390 963 sNGTADVHFYLIVYATIAGVNSLCTLLRAVLF 994
Cdd:cd18599 52 -SDNPDLNFYQLVYGGSILVILLLSLIRGFVF 82
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
725-796 |
3.23e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 39.27 E-value: 3.23e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039753390 725 VTLSGGQRARIALARAV----YQEKALYLLDDPLAAVDADVANHLLhRCILGVLSHTTRLLC-THRTEYLERADVVL 796
Cdd:cd03227 76 LQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALA-EAILEHLVKGAQVIViTHLPELAELADKLI 151
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
622-802 |
3.57e-03 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 39.61 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITGELHRLcgwVAVSELSKGFglatqepwiqcatiRDNILFGKtfdaQLYRevle 701
Cdd:cd03238 16 VSIPLNVLVVVTGVSGSGKSTLVNEGLYASGKA---RLISFLPKFS--------------RNKLIFID----QLQF---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 702 acALNDDLSILPagdqteVGEKGVTLSGGQRARIALARAVYQE--KALYLLDDPLAAVDADVANHLLhRCI--LGVLSHT 777
Cdd:cd03238 71 --LIDVGLGYLT------LGQKLSTLSGGELQRVKLASELFSEppGTLFILDEPSTGLHQQDINQLL-EVIkgLIDLGNT 141
|
170 180
....*....|....*....|....*
gi 1039753390 778 TrLLCTHRTEYLERADVVLLMEAGQ 802
Cdd:cd03238 142 V-ILIEHNLDVLSSADWIIDFGPGS 165
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
622-803 |
3.74e-03 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 40.15 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITG--------------ELHRLCGWVAVSELSKGFGLATQE-PWIQCATIRDNI- 685
Cdd:PRK10584 31 LVVKRGETIALIGESGSGKSTLLAILAGlddgssgevslvgqPLHQMDEEARAKLRAKHVGFVFQSfMLIPTLNALENVe 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 686 ----LFGKTfDAQLY---REVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKALYLLDDPLAAVD 758
Cdd:PRK10584 111 lpalLRGES-SRQSRngaKALLEQLGLGKRLDHLPA-----------QLSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1039753390 759 ADVANHLLHrcILGVLSH---TTRLLCTHRTEYLERADVVLLMEAGQL 803
Cdd:PRK10584 179 RQTGDKIAD--LLFSLNRehgTTLILVTHDLQLAARCDRRLRLVNGQL 224
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
627-813 |
5.33e-03 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 39.77 E-value: 5.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 627 GMLVGIVGKVGCGKSSLL-------AAITGELhRLCGWVAVSELSKGFG-----LATQEPWIQCATIRDNILFGK----- 689
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLkmlgrhqPPSEGEI-LLDAQPLESWSSKAFArkvayLPQQLPAAEGMTVRELVAIGRypwhg 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 690 ---TFDAQLYREVLEACALnddlsilpagdqteVGEKGV------TLSGGQRARIALARAVYQEKALYLLDDPLAAVD-- 758
Cdd:PRK10575 116 algRFGAADREKVEEAISL--------------VGLKPLahrlvdSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDia 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039753390 759 --ADVANhLLHRcilgvLSHT---TRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEIL 813
Cdd:PRK10575 182 hqVDVLA-LVHR-----LSQErglTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAELM 236
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
622-813 |
6.32e-03 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 40.06 E-value: 6.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 622 LQVKKGMLVGIVGKVGCGKSSLLAAITG--------------ELHRLCGwvavSELSK----------GFGLATQepwiq 677
Cdd:COG1135 26 LTIEKGEIFGIIGYSGAGKSTLIRCINLlerptsgsvlvdgvDLTALSE----RELRAarrkigmifqHFNLLSS----- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753390 678 cATIRDNILF-----GKTFDAQLYR--EVLEACALNDDLSILPAgdQtevgekgvtLSGGQRARIALARAVYQEKALYLL 750
Cdd:COG1135 97 -RTVAENVALpleiaGVPKAEIRKRvaELLELVGLSDKADAYPS--Q---------LSGGQKQRVGIARALANNPKVLLC 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039753390 751 DDPLAAVD----ADVANhLLHRcI---LGVlshtTRLLCTHRTEYLER-ADVVLLMEAGQLVRTGPPSEIL 813
Cdd:COG1135 165 DEATSALDpettRSILD-LLKD-InreLGL----TIVLITHEMDVVRRiCDRVAVLENGRIVEQGPVLDVF 229
|
|
| |
