|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
51-652 |
7.27e-69 |
|
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: 236.95 E-value: 7.27e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 51 VTRSFFGDFLYVAKLALPTVWCKEFAGMTVFIILFLVKSILHVAQSNANGQILKAIASDTPENRVQNFFRVLLLRAAVSM 130
Cdd:TIGR00954 71 VNGVFLGKLDFLLKILIPRVFCKETGLLILIAFLLVSRTYLSVYVATLDGQIESSIVRRSPRNFAWILFKWFLIAPPASF 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 131 MAAVcsgsIEHLRTLLIACYRERLSRYLQRRFYSHLLYYQATVLDGRLETADTVIATYCGEFAEHFAELPYYFLLPMFGC 210
Cdd:TIGR00954 151 INSA----IKYLLKELKLRFRVRLTRYLYSKYLSGFTFYKVSNLDSRIQNPDQLLTQDVEKFCDSVVELYSNLTKPILDV 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 211 MTSMVVLTRNVGAKAAGLACGAVAISVLILQKISPAFGRIHASLLAREEDYRRMLTNSLNNVEYIAMHNGGSYTRQKLER 290
Cdd:TIGR00954 227 ILYSFKLLTALGSVGPAGLFAYLFATGVVLTKLRPPIGKLTVEEQALEGEYRYVHSRLIMNSEEIAFYQGNKVEKETVMS 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 291 QLGKLKRALDHFALAKGHFDFLEISFSALLQAISSLVIFRGAHQMKTKSMNDIYVEIQCMQDLIEN----------VKSF 360
Cdd:TIGR00954 307 SFYRLVEHLNLIIKFRFSYGFLDNIVAKYTWSAVGLVAVSIPIFDKTHPAFLEMSEEELMQEFYNNgrlllkaadaLGRL 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 361 VVNFREVSHLSTFTVKLAEFDSTLTSIAEGCFIRSSGASPKSdcnsdfPVSYTHVNYIVRPKGK--KDFTLFAFSNLKLM 438
Cdd:TIGR00954 387 MLAGRDMTRLAGFTARVDTLLQVLDDVKSGNFKRPRVEEIES------GREGGRNSNLVPGRGIveYQDNGIKFENIPLV 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 439 TPAGQLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSMERGIKLLFAPQHSYMVPQcTLIEQVLFPI 518
Cdd:TIGR00954 461 TPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQRPYMTLG-TLRDQIIYPD 539
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 519 VSNT-----LGAKELDSFKEAIRLsgsHSVIDVLGGFDSpyvgadprtaddTYDW-DSLSGGQKQRITMARVFYNiltmd 592
Cdd:TIGR00954 540 SSEDmkrrgLSDKDLEQILDNVQL---THILEREGGWSA------------VQDWmDVLSGGEKQRIAMARLFYH----- 599
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 70886980 593 rseQTPVVLLDESTSMMD-ETEQAVLLNLRKLQVRMISVTHREEVITHHTHALRILPGGNW 652
Cdd:TIGR00954 600 ---KPQFAILDECTSAVSvDVEGYMYRLCREFGITLFSVSHRKSLWKYHEYLLYMDGRGGY 657
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
53-657 |
3.52e-41 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 158.05 E-value: 3.52e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 53 RSFFGDFLYVAKL-----ALPTVWckefaGMTVFIILF-LVKSILHVAQSNANGQILKAIasdtpENR-VQNFFRVLLLR 125
Cdd:COG4178 1 RSLLRQFWRLARPywrseEKWKAW-----GLLALLLLLtLASVGLNVLLNFWNRDFYDAL-----QARdAAAFWQQLGVF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 126 AAVSMMAAVCSGSIEHLRTLLIACYRERLSRYLQRRFYSHLLYYQATVLDGRLETADTVIAtycgEFAEHFAELPYYFLL 205
Cdd:COG4178 71 ALLAAISILLAVYQTYLRQRLQIRWREWLTERLLDRWLSNRAYYRLQLSGGEIDNPDQRIA----EDIRLFTETTLSLSL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 206 PMFGCMTSMV-----------VLTRNVGAKAAGLACGAVAISVL-------ILQKISPAFGRIHASLLAREEDYRRMLTN 267
Cdd:COG4178 147 GLLSSVVTLIsfigilwslsgSLTFTLGGYSITIPGYMVWAALIyaiigtlLTHLIGRPLIRLNFEQQRREADFRFALVR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 268 SLNNVEYIAMHNGGSYTRQKLERQLGKLKRALDHFALAKGHFDFLEISFSALLQAISSLVI----FRGahQMKTKSMndi 343
Cdd:COG4178 227 VRENAESIALYRGEAAERRRLRRRFDAVIANWRRLIRRQRNLTFFTTGYGQLAVIFPILVAapryFAG--EITLGGL--- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 344 yveiqcMQ------DLIENVKSFVVNFREVSHLSTFTVKLAEFDSTLTSIAEgcfiRSSGASPksdcnsdfpvsythvny 417
Cdd:COG4178 302 ------MQaasafgQVQGALSWFVDNYQSLAEWRATVDRLAGFEEALEAADA----LPEAASR----------------- 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 418 IVRPKGkkdfTLFAFSNLKLMTPAGQLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSMERGIKLLF 497
Cdd:COG4178 355 IETSED----GALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVLF 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 498 APQHSYMvPQCTLIEQVLFPIVSNTLGAKELdsfKEAIRLSGSHSVIDVLggfdspyvgadprtaDDTYDWDS-LSGGQK 576
Cdd:COG4178 431 LPQRPYL-PLGTLREALLYPATAEAFSDAEL---REALEAVGLGHLAERL---------------DEEADWDQvLSLGEQ 491
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 577 QRITMARVFYNiltmdrseQTPVVLLDESTSMMDETEQAVLLNL---RKLQVRMISVTHREEVITHHTHALRILPGGNWT 653
Cdd:COG4178 492 QRLAFARLLLH--------KPDWLFLDEATSALDEENEAALYQLlreELPGTTVISVGHRSTLAAFHDRVLELTGDGSWQ 563
|
....
gi 70886980 654 ATPV 657
Cdd:COG4178 564 LLPA 567
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
430-652 |
2.29e-40 |
|
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: 144.99 E-value: 2.29e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 430 FAFSNLKLMTPAGQLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSMERGIKLLFAPQHSYMvPQCT 509
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQRPYL-PLGT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 510 LIEQVLFPivsntlgakeldsfkeairlsgshsvidvlggfdspyvgadprtaddtydWDS-LSGGQKQRITMARVFYNi 588
Cdd:cd03223 80 LREQLIYP--------------------------------------------------WDDvLSGGEQQRLAFARLLLH- 108
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 70886980 589 ltmdrseQTPVVLLDESTSMMD-ETEQAVLLNLRKLQVRMISVTHREEVITHHTHALRILPGGNW 652
Cdd:cd03223 109 -------KPKFVFLDEATSALDeESEDRLYQLLKELGITVISVGHRPSLWKFHDRVLDLDGEGGW 166
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
130-639 |
9.21e-27 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 116.09 E-value: 9.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 130 MMAAVCSGSIEHLRTLLIACYRERLSRYLQRRFYSHLL------YYQATVLD--GRLETADTVIATYCGEFAEHFAELPy 201
Cdd:COG2274 203 LLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLrlplsfFESRSVGDlaSRFRDVESIREFLTGSLLTALLDLL- 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 202 yFLLpmfgcmTSMVVLTRnVGAKAAGLACGAVAISVLILQKISPAFGRIHASLLAREEDYRRMLTNSLNNVEYIAMHNGG 281
Cdd:COG2274 282 -FVL------IFLIVLFF-YSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAE 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 282 SYTRQKLERQLGKLKRAldhfALAKGHFDFLEISFSALLQAISS-LVIFRGAHQMKTKSMN-------DIYVE--IQCMQ 351
Cdd:COG2274 354 SRFRRRWENLLAKYLNA----RFKLRRLSNLLSTLSGLLQQLATvALLWLGAYLVIDGQLTlgqliafNILSGrfLAPVA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 352 DLIenvkSFVVNFREV-SHLStftvKLAEFDSTLTSIAEGcfirssgaspksdcnsdfpvsythVNYIVRPKGKKDFTL- 429
Cdd:COG2274 430 QLI----GLLQRFQDAkIALE----RLDDILDLPPEREEG------------------------RSKLSLPRLKGDIELe 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 430 ---FAFSnlklmtPAGQLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSMErGIKLLFAPQHSY--- 503
Cdd:COG2274 478 nvsFRYP------GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILID-GIDLRQIDPASLrrq 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 504 --MVPQctliEQVLFP--IVSN-TLGAKELDSFK--EAIRLSGSHSVIDVL-GGFDSPyVGADPRtaddtydwdSLSGGQ 575
Cdd:COG2274 551 igVVLQ----DVFLFSgtIRENiTLGDPDATDEEiiEAARLAGLHDFIEALpMGYDTV-VGEGGS---------NLSGGQ 616
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 70886980 576 KQRITMARVFYNiltmdrseQTPVVLLDESTSMMD-ETEQAVLLNLRKLQVR--MISVTHREEVITH 639
Cdd:COG2274 617 RQRLAIARALLR--------NPRILILDEATSALDaETEAIILENLRRLLKGrtVIIIAHRLSTIRL 675
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
440-647 |
3.70e-22 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 93.99 E-value: 3.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 440 PAGQLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSMeRGIKLLFAPQHSYMvPQCTLIEQ--VLFP 517
Cdd:cd03228 12 GRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILI-DGVDLRDLDLESLR-KNIAYVPQdpFLFS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 518 ivsntlgakelDSFKEAIrlsgshsvidvlggfdspyvgadprtaddtydwdsLSGGQKQRITMARVFYNiltmdrseQT 597
Cdd:cd03228 90 -----------GTIRENI-----------------------------------LSGGQRQRIAIARALLR--------DP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 70886980 598 PVVLLDESTSMMD-ETEQAVLLNLRKLQVR--MISVTHREEVIthhTHALRIL 647
Cdd:cd03228 116 PILILDEATSALDpETEALILEALRALAKGktVIVIAHRLSTI---RDADRII 165
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
432-639 |
3.92e-22 |
|
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: 100.60 E-value: 3.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 432 FSNLKLMTPAGQLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSMErGIKLLFAPQHSYMvPQCTLI 511
Cdd:COG4988 339 LEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILIN-GVDLSDLDPASWR-RQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 512 EQ--VLFP--IVSN-TLGAKELDS--FKEAIRLSGSHSVIDVL-GGFDSPyVGADPRTaddtydwdsLSGGQKQRITMAR 583
Cdd:COG4988 417 PQnpYLFAgtIRENlRLGRPDASDeeLEAALEAAGLDEFVAALpDGLDTP-LGEGGRG---------LSGGQAQRLALAR 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 70886980 584 VFYNiltmdrseQTPVVLLDESTSMMD-ETEQAVLLNLRKL--QVRMISVTHREEVITH 639
Cdd:COG4988 487 ALLR--------DAPLLLLDEPTAHLDaETEAEILQALRRLakGRTVILITHRLALLAQ 537
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
78-633 |
5.19e-21 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 97.16 E-value: 5.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 78 MTVFIILFLVKSILHVAQSNANGQILKAIASDTPenrVQNFFRVLLLRAAVSMMAAVCSgsieHLRTLLIACYRERLSRY 157
Cdd:COG1132 23 LILALLLLLLSALLELLLPLLLGRIIDALLAGGD---LSALLLLLLLLLGLALLRALLS----YLQRYLLARLAQRVVAD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 158 LQRRFYSHLL-----YYQ-------ATVLDGRLETADTVIATYCGEFAehfaelpyYFLLPMFGCMTSMVVLtrnvGAKA 225
Cdd:COG1132 96 LRRDLFEHLLrlplsFFDrrrtgdlLSRLTNDVDAVEQFLAHGLPQLV--------RSVVTLIGALVVLFVI----DWRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 226 AGLACGAVAISVLILQKISPAFGRIHASLLAREEDYRRMLTNSLNNVEYIAMHNGGSYTRQKLERQLGKLKRALDHFAla 305
Cdd:COG1132 164 ALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAA-- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 306 kghfdFLEISFSALLQAISSL----VIFRGAHQMKTKSMN--DIYVEIQCMQDLIENVKSFVVNFREVSHLSTFTVKLAE 379
Cdd:COG1132 242 -----RLSALFFPLMELLGNLglalVLLVGGLLVLSGSLTvgDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 380 FDSTLTSIAEGcfirsSGASPKSDCNSDfpVSYTHVNyivrpkgkkdftlFAFsnlklmtPAGQLLFNDLDLEIKSDQDW 459
Cdd:COG1132 317 LLDEPPEIPDP-----PGAVPLPPVRGE--IEFENVS-------------FSY-------PGDRPVLKDISLTIPPGETV 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 460 VILGENGCGKTSLLRMISGLWRPTEGSysmergIKL-------LfaPQHSY-----MVPQctliEQVLF--PIVSN-TLG 524
Cdd:COG1132 370 ALVGPSGSGKSTLVNLLLRFYDPTSGR------ILIdgvdirdL--TLESLrrqigVVPQ----DTFLFsgTIRENiRYG 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 525 AKE--LDSFKEAIRLSGSHSVIDVL-GGFDSPyVGADPRTaddtydwdsLSGGQKQRITMARVFYNiltmdrseQTPVVL 601
Cdd:COG1132 438 RPDatDEEVEEAAKAAQAHEFIEALpDGYDTV-VGERGVN---------LSGGQRQRIAIARALLK--------DPPILI 499
|
570 580 590
....*....|....*....|....*....|....*
gi 70886980 602 LDESTSMMD-ETEQAVLLNLRKLQVR--MISVTHR 633
Cdd:COG1132 500 LDEATSALDtETEALIQEALERLMKGrtTIVIAHR 534
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
420-638 |
1.34e-20 |
|
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: 95.82 E-value: 1.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 420 RPKGKKDFTLFAFSNLKLMTPAGQLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSMErGIKL---- 495
Cdd:TIGR02857 312 APVTAAPASSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVN-GVPLadad 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 496 --------LFAPQHSYMVPQcTLIEQVLFpivsNTLGAKELDSfKEAIRLSGSHSVIDVLG-GFDSPyVGADPRtaddty 566
Cdd:TIGR02857 391 adswrdqiAWVPQHPFLFAG-TIAENIRL----ARPDASDAEI-REALERAGLDEFVAALPqGLDTP-IGEGGA------ 457
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 70886980 567 dwdSLSGGQKQRITMARVFYNiltmdrseQTPVVLLDESTSMMD-ETEQAVLLNLRKL-QVR-MISVTHREEVIT 638
Cdd:TIGR02857 458 ---GLSGGQAQRLALARAFLR--------DAPLLLLDEPTAHLDaETEAEVLEALRALaQGRtVLLVTHRLALAA 521
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
446-607 |
6.84e-20 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 86.55 E-value: 6.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 446 FNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSMErGIKLLFAPQHSY-----MVPQctliEQVLFP--- 517
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLD-GQDLTDDERKSLrkeigYVFQ----DPQLFPrlt 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 518 IVSNTLGAKELDSFKEAIRLSGSHSVIDVLGGFDSPYVGADPRTAddtydwdSLSGGQKQRITMARVFYNiltmdrseQT 597
Cdd:pfam00005 76 VRENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGERPG-------TLSGGQRQRVAIARALLT--------KP 140
|
170
....*....|
gi 70886980 598 PVVLLDESTS 607
Cdd:pfam00005 141 KLLLLDEPTA 150
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
441-638 |
4.82e-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: 86.03 E-value: 4.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 441 AGQLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSM-----------ERGIKLLFapQHSYMVPQCT 509
Cdd:cd03259 11 GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIdgrdvtgvppeRRNIGMVF--QDYALFPHLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 510 LIEQVLFPIVSNTLGAKEL-DSFKEAIRLSGshsvidvlggfDSPYVGADPRTaddtydwdsLSGGQKQRITMARvfyni 588
Cdd:cd03259 89 VAENIAFGLKLRGVPKAEIrARVRELLELVG-----------LEGLLNRYPHE---------LSGGQQQRVALAR----- 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 70886980 589 lTMDRseQTPVVLLDESTSMMD-ETEQAVLLNLRKLQVR----MISVTH-REEVIT 638
Cdd:cd03259 144 -ALAR--EPSLLLLDEPLSALDaKLREELREELKELQRElgitTIYVTHdQEEALA 196
|
|
| ABC_membrane_2 |
pfam06472 |
ABC transporter transmembrane region 2; This domain covers the transmembrane of a small family ... |
63-329 |
6.06e-19 |
|
ABC transporter transmembrane region 2; This domain covers the transmembrane of a small family of ABC transporters and shares sequence similarity with pfam00664. Mutations in this domain in Swiss:P28288 are believed responsible for Zellweger Syndrome-2; mutations in Swiss:P33897 are responsible for recessive X-linked adrenoleukodystrophy. A Saccharomyces cerevisiae homolog is involved in the import of long-chain fatty acids.
Pssm-ID: 399466 Cd Length: 269 Bit Score: 87.28 E-value: 6.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 63 AKLALPTVWCKEFAGMTVFIILFLVKSILHVAQSNANGQILKAIAsdtpENRVQNFFRVLLLRAAVSMMAAVCSGSIEHL 142
Cdd:pfam06472 2 LKILFPRWFSKEAGLLLALAALLVLRTFLSVLVAQLDGQIVKALV----AKNGRGFIRLLLKWALLAVPASFVNSALKYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 143 RTLLIACYRERLSRYLQRRFYSHLLYYQATVLDGRLETADTVIATYCGEFAEHFAELpyyfLLPMFGCMTSMVV----LT 218
Cdd:pfam06472 78 TQRLALRFRTRLTRHLHDEYLKGRTYYKMSNLDGRIDNPDQRITQDVEKFCSSLSDL----YSNLLKPILDIILftfrLW 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 219 RNVGAKAAGLACGAVAISVLILQKISPAFGRIHASLLAREEDYRRMLTNSLNNVEYIAMHNGGSYTRQKLERQLGKLKRA 298
Cdd:pfam06472 154 RLSGWRGPAILFLYVLLSAVILRRLSPPFGKLVAEEQKLEGEFRYLHSRLITNAEEIAFYRGEKREKKQLQRSFKSLIDH 233
|
250 260 270
....*....|....*....|....*....|....*.
gi 70886980 299 LDHFALAKGHFDFLEISF-----SALLQAISSLVIF 329
Cdd:pfam06472 234 MRRILRRRLWYGFIEDFVlkytwSILGYVLVALPIF 269
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
443-637 |
8.01e-19 |
|
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: 85.21 E-value: 8.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 443 QLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSME----RGIKLLFAPQHSYMVPQ--------CTL 510
Cdd:cd03225 14 RPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDgkdlTKLSLKELRRKVGLVFQnpddqffgPTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 511 IEQVLFPIVSNTLGAKELdsfKEAIRlsgshSVIDVLGgfDSPYVGADPRTaddtydwdsLSGGQKQRITMArvfyNILT 590
Cdd:cd03225 94 EEEVAFGLENLGLPEEEI---EERVE-----EALELVG--LEGLRDRSPFT---------LSGGQKQRVAIA----GVLA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 70886980 591 MDrseqTPVVLLDESTSMMDE--TEQ--AVLLNLRKLQVRMISVTHREEVI 637
Cdd:cd03225 151 MD----PDILLLDEPTAGLDPagRREllELLKKLKAEGKTIIIVTHDLDLL 197
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
442-638 |
1.59e-18 |
|
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: 84.98 E-value: 1.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 442 GQLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSM-----------ERGIKLLFapQHSYMVPQCTL 510
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLdgkditnlpphKRPVNTVF--QNYALFPHLTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 511 IEQVLFPIVSNTLGAKELDS-FKEAIRLSGshsvidvLGGFDSPYVgadprtaddtydwDSLSGGQKQRITMARVFYNil 589
Cdd:cd03300 90 FENIAFGLRLKKLPKAEIKErVAEALDLVQ-------LEGYANRKP-------------SQLSGGQQQRVAIARALVN-- 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 70886980 590 tmdrseQTPVVLLDESTSMMD-ETEQAVLLNLRKLQVRM----ISVTH-REEVIT 638
Cdd:cd03300 148 ------EPKVLLLDEPLGALDlKLRKDMQLELKRLQKELgitfVFVTHdQEEALT 196
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
448-633 |
3.36e-18 |
|
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: 83.79 E-value: 3.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 448 DLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSME----RGIKLLFAPQHSYMVPQctliEQVLF--PIVSN 521
Cdd:cd03245 22 NVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDgtdiRQLDPADLRRNIGYVPQ----DVTLFygTLRDN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 522 -TLGAKELDSFK--EAIRLSGSHSVIDVLG-GFDSPyVGADPRtaddtydwdSLSGGQKQRITMARVFYNiltmdrseQT 597
Cdd:cd03245 98 iTLGAPLADDERilRAAELAGVTDFVNKHPnGLDLQ-IGERGR---------GLSGGQRQAVALARALLN--------DP 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 70886980 598 PVVLLDESTSMMD-ETEQAVLLNLRKL--QVRMISVTHR 633
Cdd:cd03245 160 PILLLDEPTSAMDmNSEERLKERLRQLlgDKTLIIITHR 198
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
442-640 |
4.90e-18 |
|
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: 81.52 E-value: 4.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 442 GQLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSysmergIKLLFAPqhsymvpqctlIEQVLFPIVSN 521
Cdd:cd00267 11 GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGE------ILIDGKD-----------IAKLPLEELRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 522 TLGakeldsfkeairlsgshsvidvlggfdspYVgadprtaddtydwDSLSGGQKQRITMARVFYNiltmdrseQTPVVL 601
Cdd:cd00267 74 RIG-----------------------------YV-------------PQLSGGQRQRVALARALLL--------NPDLLL 103
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 70886980 602 LDESTSMMD-ETEQAVLLNLRKLQVR---MISVTHREEVITHH 640
Cdd:cd00267 104 LDEPTSGLDpASRERLLELLRELAEEgrtVIIVTHDPELAELA 146
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
433-638 |
2.88e-17 |
|
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: 79.95 E-value: 2.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 433 SNLKLMTP-AGQLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGS-----------YSMERGikllfapQ 500
Cdd:cd03246 4 ENVSFRYPgAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRvrldgadisqwDPNELG-------D 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 501 HSYMVPQctliEQVLFPivsntlgakelDSFKEAIrlsgshsvidvlggfdspyvgadprtaddtydwdsLSGGQKQRIT 580
Cdd:cd03246 77 HVGYLPQ----DDELFS-----------GSIAENI-----------------------------------LSGGQRQRLG 106
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 70886980 581 MARVFYniltmdrseQTP-VVLLDESTSMMD-ETEQAVLLNLRKLQVRM---ISVTHREEVIT 638
Cdd:cd03246 107 LARALY---------GNPrILVLDEPNSHLDvEGERALNQAIAALKAAGatrIVIAHRPETLA 160
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
442-620 |
5.79e-17 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 79.83 E-value: 5.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 442 GQLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSME-RGIK---------LLFAPQHSYMVPQCTLI 511
Cdd:COG4133 14 ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNgEPIRdaredyrrrLAYLGHADGLKPELTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 512 EQVLFpiVSNTLGAK-ELDSFKEAIRLSGSHSVIDVLGGFdspyvgadprtaddtydwdsLSGGQKQRITMARVFyniLT 590
Cdd:COG4133 94 ENLRF--WAALYGLRaDREAIDEALEAVGLAGLADLPVRQ--------------------LSAGQKRRVALARLL---LS 148
|
170 180 190
....*....|....*....|....*....|
gi 70886980 591 mdrseQTPVVLLDESTSMMDETEQAVLLNL 620
Cdd:COG4133 149 -----PAPLWLLDEPFTALDAAGVALLAEL 173
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
442-632 |
1.34e-16 |
|
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: 78.25 E-value: 1.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 442 GQLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGS-YSMERGIKLL----FAPQHSYmVPQCtlIEQVlf 516
Cdd:cd03214 11 GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEiLLDGKDLASLspkeLARKIAY-VPQA--LELL-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 517 pivsntlgakELDSFKEaiRlsgshsvidvlggfdspyvgadprtaddtyDWDSLSGGQKQRITMARVFYNiltmdrseQ 596
Cdd:cd03214 86 ----------GLAHLAD--R------------------------------PFNELSGGERQRVLLARALAQ--------E 115
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 70886980 597 TPVVLLDESTSMMDETEQAVLLNL-----RKLQVRMISVTH 632
Cdd:cd03214 116 PPILLLDEPTSHLDIAHQIELLELlrrlaRERGKTVVMVLH 156
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
446-632 |
1.36e-16 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 79.05 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 446 FNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSM------ERGIKLLFAPQHSYMVPQCTLIEQVLFPIV 519
Cdd:cd03293 20 LEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVdgepvtGPGPDRGYVFQQDALLPWLTVLDNVALGLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 520 SNTLGAKELDS-FKEAIRLSGshsvidvLGGFDSPYvgadPRTaddtydwdsLSGGQKQRITMARVFYNiltmdrseQTP 598
Cdd:cd03293 100 LQGVPKAEARErAEELLELVG-------LSGFENAY----PHQ---------LSGGMRQRVALARALAV--------DPD 151
|
170 180 190
....*....|....*....|....*....|....*....
gi 70886980 599 VVLLDESTSMMD----ETEQAVLLNL-RKLQVRMISVTH 632
Cdd:cd03293 152 VLLLDEPFSALDaltrEQLQEELLDIwRETGKTVLLVTH 190
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
461-647 |
1.82e-16 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 82.64 E-value: 1.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 461 ILGENGCGKTSLLRMISGLWRPTEGSYSME----------------RGIKLLF-APQHSyMVPQCTLIEQVLFPIVSNTL 523
Cdd:COG1123 296 LVGESGSGKSTLARLLLGLLRPTSGSILFDgkdltklsrrslrelrRRVQMVFqDPYSS-LNPRMTVGDIIAEPLRLHGL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 524 GAKEldsfkEAIRLsgshsVIDVLG--GFDSPYVGADPRtaddtydwdSLSGGQKQRITMARvfynILTMDRSeqtpVVL 601
Cdd:COG1123 375 LSRA-----ERRER-----VAELLErvGLPPDLADRYPH---------ELSGGQRQRVAIAR----ALALEPK----LLI 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 70886980 602 LDESTSMMDETEQAVLLNL-RKLQVR----MISVTHREEVITHHTHalRIL 647
Cdd:COG1123 428 LDEPTSALDVSVQAQILNLlRDLQRElgltYLFISHDLAVVRYIAD--RVA 476
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
445-646 |
1.86e-16 |
|
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: 78.28 E-value: 1.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 445 LFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSMERGIklLFAPQHSYMVPQcTLIEQVLFpivsntlg 524
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSI--AYVSQEPWIQNG-TIRENILF-------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 525 AKELDS--FKEAIRLSGSHSVIDVLGGFDSPYVGADPRTaddtydwdsLSGGQKQRITMARVFYNiltmdrseQTPVVLL 602
Cdd:cd03250 89 GKPFDEerYEKVIKACALEPDLEILPDGDLTEIGEKGIN---------LSGGQKQRISLARAVYS--------DADIYLL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 70886980 603 DESTSMMD-ET-----EQAVLLNLRKLQVRmISVTHREEVITHHTHALRI 646
Cdd:cd03250 152 DDPLSAVDaHVgrhifENCILGLLLNNKTR-ILVTHQLQLLPHADQIVVL 200
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
442-651 |
2.75e-16 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 77.93 E-value: 2.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 442 GQLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSysmergIKLLFAPQHSYMVP----QCTLIEQ--VL 515
Cdd:COG4619 12 GKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGE------IYLDGKPLSAMPPPewrrQVAYVPQepAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 516 FPivsNTLGakelDSFKEAIRLSGSHS----VIDVLggfdsPYVGADPrtadDTYDWD--SLSGGQKQRITMARVfyniL 589
Cdd:COG4619 86 WG---GTVR----DNLPFPFQLRERKFdrerALELL-----ERLGLPP----DILDKPveRLSGGERQRLALIRA----L 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 70886980 590 TMDRSeqtpVVLLDESTSMMDET-----EQAVLLNLRKLQVRMISVTHREEVITHHTHALRILPGGN 651
Cdd:COG4619 146 LLQPD----VLLLDEPTSALDPEntrrvEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGR 208
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
442-606 |
3.02e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 82.03 E-value: 3.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 442 GQLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSMERGIKLLFAPQHSYMVPQCTLIEQVL--FPIV 519
Cdd:COG0488 10 GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDLTVLDTVLdgDAEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 520 S------NTLGAKELDSFKEAIRLSGSHSVIDVLGGFDspyvgADPRTAD-------DTYDWD----SLSGGQKQRITMA 582
Cdd:COG0488 90 RaleaelEELEAKLAEPDEDLERLAELQEEFEALGGWE-----AEARAEEilsglgfPEEDLDrpvsELSGGWRRRVALA 164
|
170 180
....*....|....*....|....
gi 70886980 583 RVFyniltMDRSEqtpVVLLDEST 606
Cdd:COG0488 165 RAL-----LSEPD---LLLLDEPT 180
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
442-649 |
7.19e-16 |
|
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: 77.82 E-value: 7.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 442 GQLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYsmergIKLLfapqhsymvpQCTLIEQVLFPI--- 518
Cdd:COG1119 15 GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGND-----VRLF----------GERRGGEDVWELrkr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 519 ---VSNTLGAkeldsfkeaiRLSGSHSVIDVL--GGFDS-----PYVGADPRTADDTYD-----------WDSLSGGQKQ 577
Cdd:COG1119 80 iglVSPALQL----------RFPRDETVLDVVlsGFFDSiglyrEPTDEQRERARELLEllglahladrpFGTLSQGEQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 70886980 578 RITMARVFYNiltmdrseQTPVVLLDESTSMMDETEQAVLLN-LRKL----QVRMISVTHR-EEVITHHTHALRILPG 649
Cdd:COG1119 150 RVLIARALVK--------DPELLILDEPTAGLDLGARELLLAlLDKLaaegAPTLVLVTHHvEEIPPGITHVLLLKDG 219
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
433-638 |
7.54e-16 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 80.85 E-value: 7.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 433 SNLKLMTPAGQL-LFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGS-----YSMERGIKLLFAPQHSYMvP 506
Cdd:TIGR01842 320 ENVTIVPPGGKKpTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSvrldgADLKQWDRETFGKHIGYL-P 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 507 QCtlIEqvLFPivsNTLGA------KELDSFK--EAIRLSGSHSVIDVL-GGFDSpYVGADPRTaddtydwdsLSGGQKQ 577
Cdd:TIGR01842 399 QD--VE--LFP---GTVAEniarfgENADPEKiiEAAKLAGVHELILRLpDGYDT-VIGPGGAT---------LSGGQRQ 461
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 70886980 578 RITMARVFYNILTMdrseqtpvVLLDESTSMMD-ETEQAVLLNLRKLQVRMISV---THREEVIT 638
Cdd:TIGR01842 462 RIALARALYGDPKL--------VVLDEPNSNLDeEGEQALANAIKALKARGITVvviTHRPSLLG 518
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
442-645 |
7.85e-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: 77.78 E-value: 7.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 442 GQLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEG----------SYS-MERGIKLLFAPQHSYMVPQCTL 510
Cdd:COG1120 13 GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGevlldgrdlaSLSrRELARRIAYVPQEPPAPFGLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 511 IEQVL---FPIVS--NTLGAKELDSFKEAIRLSGshsvidvLGGFdspyvgADpRtaddtyDWDSLSGGQKQRITMARVF 585
Cdd:COG1120 93 RELVAlgrYPHLGlfGRPSAEDREAVEEALERTG-------LEHL------AD-R------PVDELSGGERQRVLIARAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 70886980 586 yniltmdrSEQTPVVLLDESTSMMDETEQAVLLNL-RKLqvrmisvtHREE-----VITHH-THALR 645
Cdd:COG1120 153 --------AQEPPLLLLDEPTSHLDLAHQLEVLELlRRL--------ARERgrtvvMVLHDlNLAAR 203
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
447-637 |
1.82e-15 |
|
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: 76.08 E-value: 1.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 447 NDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSME-------RGIKLLFAPQHSYMVPQC-------TLIE 512
Cdd:cd03258 22 KDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDgtdltllSGKELRKARRRIGMIFQHfnllssrTVFE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 513 QVLFPIvsntlgakELDSFKEAIRLSGSHSVIDVLGGFDSpyvgADPRTAddtydwdSLSGGQKQRITMARVfyniLTMD 592
Cdd:cd03258 102 NVALPL--------EIAGVPKAEIEERVLELLELVGLEDK----ADAYPA-------QLSGGQKQRVGIARA----LANN 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 70886980 593 rseqtPVVLL-DESTSMMD-ETEQAVLLNLRKLQVR----MISVTHREEVI 637
Cdd:cd03258 159 -----PKVLLcDEATSALDpETTQSILALLRDINRElgltIVLITHEMEVV 204
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
447-632 |
3.53e-15 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 75.23 E-value: 3.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 447 NDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSME--------------RGIKLLFAPQHSY--MVPQCTL 510
Cdd:cd03257 22 DDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDgkdllklsrrlrkiRRKEIQMVFQDPMssLNPRMTI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 511 IEQVLFPIVSNTLGAKElDSFKEAIRLsgshsvIDVLGGFDSPYVGADPRtaddtydwdSLSGGQKQRITMARVFynILt 590
Cdd:cd03257 102 GEQIAEPLRIHGKLSKK-EARKEAVLL------LLVGVGLPEEVLNRYPH---------ELSGGQRQRVAIARAL--AL- 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 70886980 591 mdrseQTPVVLLDESTSMMDETEQAVLLNL-RKLQVR----MISVTH 632
Cdd:cd03257 163 -----NPKLLIADEPTSALDVSVQAQILDLlKKLQEElgltLLFITH 204
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
448-640 |
4.35e-15 |
|
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: 74.95 E-value: 4.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 448 DLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSMErGIKLLFAPQHSY-----MVPQctliEQVLFP----- 517
Cdd:cd03254 21 DINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILID-GIDIRDISRKSLrsmigVVLQ----DTFLFSgtime 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 518 -IVSNTLGAKElDSFKEAIRLSGSHSVIDVL-GGFDSpYVGadPRTADdtydwdsLSGGQKQRITMARVFyniltmdrSE 595
Cdd:cd03254 96 nIRLGRPNATD-EEVIEAAKEAGAHDFIMKLpNGYDT-VLG--ENGGN-------LSQGERQLLAIARAM--------LR 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 70886980 596 QTPVVLLDESTSMMD-ETEQAVLLNLRKLQVRMISVthreeVITHH 640
Cdd:cd03254 157 DPKILILDEATSNIDtETEKLIQEALEKLMKGRTSI-----IIAHR 197
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
432-633 |
4.84e-15 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 74.88 E-value: 4.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 432 FSNLKLMTPA--GQLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSY----SMERGIKLLFAPQHSYMV 505
Cdd:cd03249 3 FKNVSFRYPSrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEIlldgVDIRDLNLRWLRSQIGLV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 506 PQctliEQVLFP--IVSN-TLGAKE--LDSFKEAIRLSGSHSVIDVL-GGFDSPyVGadPRTAddtydwdSLSGGQKQRI 579
Cdd:cd03249 83 SQ----EPVLFDgtIAENiRYGKPDatDEEVEEAAKKANIHDFIMSLpDGYDTL-VG--ERGS-------QLSGGQKQRI 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 70886980 580 TMARVFYniltmdrsEQTPVVLLDESTSMMD-ETEQAVLLNLRKLQV-RM-ISVTHR 633
Cdd:cd03249 149 AIARALL--------RNPKILLLDEATSALDaESEKLVQEALDRAMKgRTtIVIAHR 197
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
440-632 |
9.13e-15 |
|
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: 73.91 E-value: 9.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 440 PAGQLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSMErGIKLLFAPQHSY-----MVPQctlieqv 514
Cdd:COG1122 11 PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVD-GKDITKKNLRELrrkvgLVFQ------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 515 lFP---IVSNTLgAKELdSF--------KEAIRlsgsHSVIDVLGgfdspYVGADPRTADDTYDwdsLSGGQKQRITMAR 583
Cdd:COG1122 83 -NPddqLFAPTV-EEDV-AFgpenlglpREEIR----ERVEEALE-----LVGLEHLADRPPHE---LSGGQKQRVAIAG 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 70886980 584 VfyniLTMdrseQTPVVLLDESTSMMDETEQ----AVLLNLRKLQVRMISVTH 632
Cdd:COG1122 148 V----LAM----EPEVLVLDEPTAGLDPRGRrellELLKRLNKEGKTVIIVTH 192
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
447-636 |
1.53e-14 |
|
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: 73.29 E-value: 1.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 447 NDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSME---------------RGIKLLFAPQHSYMVPQCTLI 511
Cdd:cd03255 21 KGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDgtdisklsekelaafRRRHIGFVFQSFNLLPDLTAL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 512 EQVLFP-IVSNTLGAKELDSFKEAIRLSGshsvidvLGGFDSPYVGadprtaddtydwdSLSGGQKQRITMARVFYNilt 590
Cdd:cd03255 101 ENVELPlLLAGVPKKERRERAEELLERVG-------LGDRLNHYPS-------------ELSGGQQQRVAIARALAN--- 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 70886980 591 mdrseQTPVVLLDESTSMMD-ETEQAVLLNLRKLQ----VRMISVTHREEV 636
Cdd:cd03255 158 -----DPKIILADEPTGNLDsETGKEVMELLRELNkeagTTIVVVTHDPEL 203
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
431-639 |
1.90e-14 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 73.42 E-value: 1.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 431 AFSNLKLMTPAGQLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSME----RGIKLLFAPQHSYMVP 506
Cdd:cd03253 2 EFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDgqdiREVTLDSLRRAIGVVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 507 QCTlieqVLF--PIVSN----TLGAKELDSFkEAIRLSGSHSVIDVL-GGFDSpYVGAdpRTAddtydwdSLSGGQKQRI 579
Cdd:cd03253 82 QDT----VLFndTIGYNirygRPDATDEEVI-EAAKAAQIHDKIMRFpDGYDT-IVGE--RGL-------KLSGGEKQRV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 70886980 580 TMARVFYniltmdrsEQTPVVLLDESTSMMD-ETEQAVLLNLRKLQVR--MISVTHREEVITH 639
Cdd:cd03253 147 AIARAIL--------KNPPILLLDEATSALDtHTEREIQAALRDVSKGrtTIVIAHRLSTIVN 201
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
447-632 |
3.03e-14 |
|
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: 72.29 E-value: 3.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 447 NDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGS-----------YSMERGIKLLFapQHSYMVPQCTLIEQVL 515
Cdd:cd03301 17 DDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRiyiggrdvtdlPPKDRDIAMVF--QNYALYPHMTVYDNIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 516 FPIVSNTLGAKELDsfkeairlSGSHSVIDVLGgfDSPYVGADPRTaddtydwdsLSGGQKQRITMARvfynilTMDRSE 595
Cdd:cd03301 95 FGLKLRKVPKDEID--------ERVREVAELLQ--IEHLLDRKPKQ---------LSGGQRQRVALGR------AIVREP 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 70886980 596 QtpVVLLDESTSMMD----ETEQAVLLNL-RKLQVRMISVTH 632
Cdd:cd03301 150 K--VFLMDEPLSNLDaklrVQMRAELKRLqQRLGTTTIYVTH 189
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
447-632 |
4.53e-14 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 73.99 E-value: 4.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 447 NDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEG-----------SYSMERGIKLLFapqHSY-MVPQCTLIEQV 514
Cdd:PRK11432 23 DNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGqifidgedvthRSIQQRDICMVF---QSYaLFPHMSLGENV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 515 LFPIVSNTLGAKEL-DSFKEAIRLsgshsvIDvLGGFDSPYVgadprtaddtydwDSLSGGQKQRITMARVFynILtmdr 593
Cdd:PRK11432 100 GYGLKMLGVPKEERkQRVKEALEL------VD-LAGFEDRYV-------------DQISGGQQQRVALARAL--IL---- 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 70886980 594 seqTPVVLL-DESTSMMDET-EQAVLLNLRKLQVRM----ISVTH 632
Cdd:PRK11432 154 ---KPKVLLfDEPLSNLDANlRRSMREKIRELQQQFnitsLYVTH 195
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
447-638 |
4.54e-14 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 74.21 E-value: 4.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 447 NDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSME-----------RGIKLLFapQHSYMVPQCTLIEQVL 515
Cdd:PRK09452 31 SNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDgqdithvpaenRHVNTVF--QSYALFPHMTVFENVA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 516 FPIVSNTLGAKELDS-FKEAIRLsgshsvidV-LGGFdspyvgADPRTADdtydwdsLSGGQKQRITMARVFYNiltmdr 593
Cdd:PRK09452 109 FGLRMQKTPAAEITPrVMEALRM--------VqLEEF------AQRKPHQ-------LSGGQQQRVAIARAVVN------ 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 70886980 594 seQTPVVLLDESTSMMD----ETEQAVLLNL-RKLQVRMISVTH-REEVIT 638
Cdd:PRK09452 162 --KPKVLLLDESLSALDyklrKQMQNELKALqRKLGITFVFVTHdQEEALT 210
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
447-632 |
7.47e-14 |
|
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: 72.29 E-value: 7.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 447 NDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSME---------------RGIKLLFAPQHSYMVPQCTLI 511
Cdd:cd03294 41 NDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDgqdiaamsrkelrelRRKKISMVFQSFALLPHRTVL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 512 EQVLFPIvsntlgakELDSFKEAIRLSGSHSVIDV--LGGFDSPYVgadprtaddtydwDSLSGGQKQRITMARVfyniL 589
Cdd:cd03294 121 ENVAFGL--------EVQGVPRAEREERAAEALELvgLEGWEHKYP-------------DELSGGMQQRVGLARA----L 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 70886980 590 TMDrseqTPVVLLDESTSMMD---ETE-QAVLLNL-RKLQVRMISVTH 632
Cdd:cd03294 176 AVD----PDILLMDEAFSALDpliRREmQDELLRLqAELQKTIVFITH 219
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
422-650 |
1.09e-13 |
|
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: 70.96 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 422 KGKKDF--TLFAFSNlklmTPAGQLLfNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSMERgiKLLFAP 499
Cdd:cd03248 9 KGIVKFqnVTFAYPT----RPDTLVL-QDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDG--KPISQY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 500 QHSYMVPQCTLIEQ--VLF--PIVSNT---LGAKELDSFKEAIRLSGSHSVIDVLGgfDSPYVGADPRTAddtydwdSLS 572
Cdd:cd03248 82 EHKYLHSKVSLVGQepVLFarSLQDNIaygLQSCSFECVKEAAQKAHAHSFISELA--SGYDTEVGEKGS-------QLS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 573 GGQKQRITMARVFYniltmdrsEQTPVVLLDESTSMMD-ETEQAVLLNLRK-LQVRMISV-THREEVItHHTHALRILPG 649
Cdd:cd03248 153 GGQKQRVAIARALI--------RNPQVLILDEATSALDaESEQQVQQALYDwPERRTVLViAHRLSTV-ERADQILVLDG 223
|
.
gi 70886980 650 G 650
Cdd:cd03248 224 G 224
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
442-638 |
1.44e-13 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 69.98 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 442 GQLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSME-RGIKLLFAPQHSYMVPQcTLIEQVLFPIVS 520
Cdd:cd03226 12 GTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNgKPIKAKERRKSIGYVMQ-DVDYQLFTDSVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 521 N--TLGAKELDSFKEAIRlsgshsviDVLGGFD-SPYVGADPRtaddtydwdSLSGGQKQRITMARVFYNiltmdrseQT 597
Cdd:cd03226 91 EelLLGLKELDAGNEQAE--------TVLKDLDlYALKERHPL---------SLSGGQKQRLAIAAALLS--------GK 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 70886980 598 PVVLLDESTSMMD-ETEQAVLLNLRKLQ---VRMISVTHREEVIT 638
Cdd:cd03226 146 DLLIFDEPTSGLDyKNMERVGELIRELAaqgKAVIVITHDYEFLA 190
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
442-620 |
1.59e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 69.90 E-value: 1.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 442 GQLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSMERG--IKLLFAPQHSY------MVPQCTLIEQ 513
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGdiDDPDVAEACHYlghrnaMKPALTVAEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 514 VLFpiVSNTLGAKELDsFKEAIRLSGSHSVIDVLGGFdspyvgadprtaddtydwdsLSGGQKQRITMAR--VFYniltm 591
Cdd:PRK13539 94 LEF--WAAFLGGEELD-IAAALEAVGLAPLAHLPFGY--------------------LSAGQKRRVALARllVSN----- 145
|
170 180
....*....|....*....|....*....
gi 70886980 592 drseqTPVVLLDESTSMMDETEQAVLLNL 620
Cdd:PRK13539 146 -----RPIWILDEPTAALDAAAVALFAEL 169
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
420-646 |
1.65e-13 |
|
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: 73.63 E-value: 1.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 420 RPKGKkdftlFAFSNLKLMTP-AGQLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGS----------YS 488
Cdd:COG4618 326 RPKGR-----LSVENLTVVPPgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSvrldgadlsqWD 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 489 MERgikllFAPQHSYMvPQctlieQV-LFP--IVSNTLGAKELDSFK--EAIRLSGSHSVIDVL-GGFDSPyVGADPRTa 562
Cdd:COG4618 401 REE-----LGRHIGYL-PQ-----DVeLFDgtIAENIARFGDADPEKvvAAAKLAGVHEMILRLpDGYDTR-IGEGGAR- 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 563 ddtydwdsLSGGQKQRITMARVFYNiltmdrseqTPV-VLLDESTSMMDET-EQAVLLNLRKLQVRMISVThreeVITHH 640
Cdd:COG4618 468 --------LSGGQRQRIGLARALYG---------DPRlVVLDEPNSNLDDEgEAALAAAIRALKARGATVV----VITHR 526
|
....*.
gi 70886980 641 THALRI 646
Cdd:COG4618 527 PSLLAA 532
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
442-644 |
2.92e-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: 69.10 E-value: 2.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 442 GQLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSysmergIKLLFAPQH------SYmVPQCTLIEQvL 515
Cdd:cd03235 11 GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGS------IRVFGKPLEkerkriGY-VPQRRSIDR-D 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 516 FPIvsntlgakeldsfkeairlsgshSVIDVLG-------GFDSPYVGADPRTADDTYD-----------WDSLSGGQKQ 577
Cdd:cd03235 83 FPI-----------------------SVRDVVLmglyghkGLFRRLSKADKAKVDEALErvglseladrqIGELSGGQQQ 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 70886980 578 RITMARvfynILTMDRSeqtpVVLLDESTSMMD-ETEQAVLLNLRKLQVR---MISVTH-REEVITHHTHAL 644
Cdd:cd03235 140 RVLLAR----ALVQDPD----LLLLDEPFAGVDpKTQEDIYELLRELRREgmtILVVTHdLGLVLEYFDRVL 203
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
439-639 |
3.25e-13 |
|
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: 69.57 E-value: 3.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 439 TPAGQLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSME----RGIKLLFAPQHSYMVPQCTLI--E 512
Cdd:cd03251 11 PGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDghdvRDYTLASLRRQIGLVSQDVFLfnD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 513 QVLFPIVSNTLGAKElDSFKEAIRLSGSHSVIDVL-GGFDSPyVGAdpRTAddtydwdSLSGGQKQRITMARVFYNiltm 591
Cdd:cd03251 91 TVAENIAYGRPGATR-EEVEEAARAANAHEFIMELpEGYDTV-IGE--RGV-------KLSGGQRQRIAIARALLK---- 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 70886980 592 drseQTPVVLLDESTSMMD-ETEQAVLLNLRKLQVR--MISVTHREEVITH 639
Cdd:cd03251 156 ----DPPILILDEATSALDtESERLVQAALERLMKNrtTFVIAHRLSTIEN 202
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
447-635 |
4.32e-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: 70.90 E-value: 4.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 447 NDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSM-----------ERGIKLLFapQhSYMV-PQCTLIEQV 514
Cdd:COG3842 22 DDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLdgrdvtglppeKRNVGMVF--Q-DYALfPHLTVAENV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 515 LFPIVSNTLGAKELDS-FKEAIRLSGshsvidvLGGFDSPYVgadprtaddtydwDSLSGGQKQRITMAR--VFyniltm 591
Cdd:COG3842 99 AFGLRMRGVPKAEIRArVAELLELVG-------LEGLADRYP-------------HQLSGGQQQRVALARalAP------ 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 70886980 592 drseQTPVVLLDESTSMMD-ETEQAVLLNLRKLQVR----MISVTH-REE 635
Cdd:COG3842 153 ----EPRVLLLDEPLSALDaKLREEMREELRRLQRElgitFIYVTHdQEE 198
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
447-635 |
1.35e-12 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 67.75 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 447 NDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSM-----------ERGIKLLFapQHSYMVPQCTLIEQVL 515
Cdd:cd03296 19 DDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFggedatdvpvqERNVGFVF--QHYALFRHMTVFDNVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 516 F-----PIVSNTLGAKELDSFKEAIRLSGshsvidvLGGFDSPYvgadPrtaddtydwDSLSGGQKQRITMARVfyniLT 590
Cdd:cd03296 97 FglrvkPRSERPPEAEIRAKVHELLKLVQ-------LDWLADRY----P---------AQLSGGQRQRVALARA----LA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 70886980 591 MDRSeqtpVVLLDESTSMMDETEQAVLLN-LRKLQVRM----ISVTHREE 635
Cdd:cd03296 153 VEPK----VLLLDEPFGALDAKVRKELRRwLRRLHDELhvttVFVTHDQE 198
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
432-632 |
1.60e-12 |
|
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: 67.71 E-value: 1.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 432 FSNLKLMTPAGQLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSMErGI------------KLLFAP 499
Cdd:cd03295 3 FENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFID-GEdireqdpvelrrKIGYVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 500 QHSYMVPQCTLIEQV-LFPIVSNTLGAKELDSFKEAIRLsgshsvidvlggfdspyVGADPRTADDTYDWDsLSGGQKQR 578
Cdd:cd03295 82 QQIGLFPHMTVEENIaLVPKLLKWPKEKIRERADELLAL-----------------VGLDPAEFADRYPHE-LSGGQQQR 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 70886980 579 ITMARVfyniLTMDrseqTPVVLLDESTSMMD----ETEQAVLLNL-RKLQVRMISVTH 632
Cdd:cd03295 144 VGVARA----LAAD----PPLLLMDEPFGALDpitrDQLQEEFKRLqQELGKTIVFVTH 194
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
447-637 |
2.02e-12 |
|
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: 65.88 E-value: 2.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 447 NDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSysmergIKLLFapqhsymvpqctlieqvlFPIVSNTLGAK 526
Cdd:cd03230 17 DDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGE------IKVLG------------------KDIKKEPEEVK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 527 ELdsfkeairlsgshsvIDVLGGFDSPYVGAdprTADDTYDwdsLSGGQKQRITMARVFyniltmdrSEQTPVVLLDEST 606
Cdd:cd03230 73 RR---------------IGYLPEEPSLYENL---TVRENLK---LSGGMKQRLALAQAL--------LHDPELLILDEPT 123
|
170 180 190
....*....|....*....|....*....|....*
gi 70886980 607 SMMDETEQAVLLN-LRKLQVRMISV---THREEVI 637
Cdd:cd03230 124 SGLDPESRREFWElLRELKKEGKTIllsSHILEEA 158
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
447-632 |
2.05e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 67.73 E-value: 2.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 447 NDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSM-----------ERGIKLLFAPQHsYMVPQ----CTLI 511
Cdd:PRK11231 19 NDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLgdkpismlssrQLARRLALLPQH-HLTPEgitvRELV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 512 EQVLFPIVS--NTLGAKELDSFKEAIRLSGshsvIDVLggfdspyvgADPRTADdtydwdsLSGGQKQRitmarVFyniL 589
Cdd:PRK11231 98 AYGRSPWLSlwGRLSAEDNARVNQAMEQTR----INHL---------ADRRLTD-------LSGGQRQR-----AF---L 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 70886980 590 TMDRSEQTPVVLLDESTSMMDETEQAVLLNL-RKLQVR---MISVTH 632
Cdd:PRK11231 150 AMVLAQDTPVVLLDEPTTYLDINHQVELMRLmRELNTQgktVVTVLH 196
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
440-633 |
3.03e-12 |
|
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: 66.74 E-value: 3.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 440 PAGQLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEG-----SYSMERGIKLLFAPQHSYMVPQCTLIEQV 514
Cdd:cd03252 12 PDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGrvlvdGHDLALADPAWLRRQVGVVLQENVLFNRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 515 LFPIVSNTLGAKELDSFKEAIRLSGSHSVIDVLG-GFDSpYVGAdpRTAddtydwdSLSGGQKQRITMARVFYNiltmdr 593
Cdd:cd03252 92 IRDNIALADPGMSMERVIEAAKLAGAHDFISELPeGYDT-IVGE--QGA-------GLSGGQRQRIAIARALIH------ 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 70886980 594 seQTPVVLLDESTSMMD-ETEQAVLLNLRKLQV--RMISVTHR 633
Cdd:cd03252 156 --NPRILIFDEATSALDyESEHAIMRNMHDICAgrTVIIIAHR 196
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
447-632 |
3.95e-12 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 68.18 E-value: 3.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 447 NDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSM-----------ERGIKLLFapQhSYMV-PQCTLIEQV 514
Cdd:COG3839 20 KDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIggrdvtdlppkDRNIAMVF--Q-SYALyPHMTVYENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 515 LFPIVSNTLGAKELDsfkEAIRlsgshSVIDVLGgfDSPYVGADPRTaddtydwdsLSGGQKQRITMARvfynilTMDRs 594
Cdd:COG3839 97 AFPLKLRKVPKAEID---RRVR-----EAAELLG--LEDLLDRKPKQ---------LSGGQRQRVALGR------ALVR- 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 70886980 595 eQTPVVLLDESTSMMDeteqAVL-----LNLRKLQVR----MISVTH 632
Cdd:COG3839 151 -EPKVFLLDEPLSNLD----AKLrvemrAEIKRLHRRlgttTIYVTH 192
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
447-649 |
4.35e-12 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 66.22 E-value: 4.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 447 NDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSME---------------RGIKLLFAPQHSYMVPQCTLI 511
Cdd:COG1136 25 RGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDgqdisslserelarlRRRHIGFVFQFFNLLPELTAL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 512 EQVLFPIVSNTLGAKELDS-FKEAIRLSGshsvidvLGGFdspyvgADPRTADdtydwdsLSGGQKQRITMARVFYNilt 590
Cdd:COG1136 105 ENVALPLLLAGVSRKERRErARELLERVG-------LGDR------LDHRPSQ-------LSGGQQQRVAIARALVN--- 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 70886980 591 mdrseQTPVVLLDESTSMMD-ETEQAVLLNLRKLQVRM----ISVTHREEVITHHTHALRILPG 649
Cdd:COG1136 162 -----RPKLILADEPTGNLDsKTGEEVLELLRELNRELgttiVMVTHDPELAARADRVIRLRDG 220
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
447-637 |
6.18e-12 |
|
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: 63.99 E-value: 6.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 447 NDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSMErGIKLLFA-PQHS-----YMVPQctlieqvlfpivs 520
Cdd:cd03216 17 DGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVD-GKEVSFAsPRDArragiAMVYQ------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 521 ntlgakeldsfkeairlsgshsvidvlggfdspyvgadprtaddtydwdsLSGGQKQRITMARVFYNiltmdrseQTPVV 600
Cdd:cd03216 83 --------------------------------------------------LSVGERQMVEIARALAR--------NARLL 104
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 70886980 601 LLDESTSMMDETEQAVLLN-LRKLQ---VRMISVTHR-EEVI 637
Cdd:cd03216 105 ILDEPTAALTPAEVERLFKvIRRLRaqgVAVIFISHRlDEVF 146
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
442-646 |
6.39e-12 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 65.88 E-value: 6.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 442 GQLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSysmergIKLLFAPQH------SYmVPQCTLIEQvL 515
Cdd:COG1121 18 GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGT------VRLFGKPPRrarrriGY-VPQRAEVDW-D 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 516 FPIvsntlgakeldsfkeairlsgshSVIDVLG-------GFDSPYVGADPRTADDTYD----WD-------SLSGGQKQ 577
Cdd:COG1121 90 FPI-----------------------TVRDVVLmgrygrrGLFRRPSRADREAVDEALErvglEDladrpigELSGGQQQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 70886980 578 RITMARVfyniLTMDRseqtPVVLLDESTSMMD-ETEQA---VLLNLRKLQVRMISVTH-REEVITHHTHALRI 646
Cdd:COG1121 147 RVLLARA----LAQDP----DLLLLDEPFAGVDaATEEAlyeLLRELRREGKTILVVTHdLGAVREYFDRVLLL 212
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
443-626 |
7.35e-12 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 66.37 E-value: 7.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 443 QLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYS----------------MERGIKLLFAPQHSYMVP 506
Cdd:TIGR02769 24 APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSfrgqdlyqldrkqrraFRRDVQLVFQDSPSAVNP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 507 QCTLIEQVLFPIvsntlgaKELDSFKEAIRLSGSHSVIDVLGgFDSPYVGADPRtaddtydwdSLSGGQKQRITMARVFy 586
Cdd:TIGR02769 104 RMTVRQIIGEPL-------RHLTSLDESEQKARIAELLDMVG-LRSEDADKLPR---------QLSGGQLQRINIARAL- 165
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 70886980 587 niltmdrSEQTPVVLLDESTSMMDETEQAVLLN-LRKLQVR 626
Cdd:TIGR02769 166 -------AVKPKLIVLDEAVSNLDMVLQAVILElLRKLQQA 199
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
442-632 |
1.10e-11 |
|
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: 62.85 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 442 GQLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSMERGIKLLFAPQhsymvpqctlieqvlfpivsn 521
Cdd:cd03221 12 GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ--------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 522 tlgakeldsfkeairlsgshsvidvlggfdspyvgadprtaddtydwdsLSGGQKQRITMARVFyniltmdrSEQTPVVL 601
Cdd:cd03221 71 -------------------------------------------------LSGGEKMRLALAKLL--------LENPNLLL 93
|
170 180 190
....*....|....*....|....*....|..
gi 70886980 602 LDESTSMMDETEQAVLLN-LRKLQVRMISVTH 632
Cdd:cd03221 94 LDEPTNHLDLESIEALEEaLKEYPGTVILVSH 125
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
441-632 |
1.20e-11 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 63.75 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 441 AGQLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSM---------------ERGIKLLFapQHSYMV 505
Cdd:cd03229 11 GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIdgedltdledelpplRRRIGMVF--QDFALF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 506 PQCTLIEQVLFPivsntlgakeldsfkeairlsgshsvidvlggfdspyvgadprtaddtydwdsLSGGQKQRITMARVf 585
Cdd:cd03229 89 PHLTVLENIALG-----------------------------------------------------LSGGQQQRVALARA- 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 70886980 586 yniLTMDrseqTPVVLLDESTSMMD-ETEQAVLLNLRKLQVR----MISVTH 632
Cdd:cd03229 115 ---LAMD----PDVLLLDEPTSALDpITRREVRALLKSLQAQlgitVVLVTH 159
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
430-640 |
1.30e-11 |
|
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: 63.49 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 430 FAFSNLKLMTP-AGQLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYsmergikllfapqhsymvpqc 508
Cdd:cd03247 1 LSINNVSFSYPeQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEI--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 509 tlieqvlfpivsnTLGAKELDSFKEAIRlsgshSVIDVLGgfDSPYVGADprTADDTYDwDSLSGGQKQRITMARvfynI 588
Cdd:cd03247 60 -------------TLDGVPVSDLEKALS-----SLISVLN--QRPYLFDT--TLRNNLG-RRFSGGERQRLALAR----I 112
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 70886980 589 LTMDrseqTPVVLLDESTSMMD-ETEQAvLLNLrklqvrMISVTHREEV--ITHH 640
Cdd:cd03247 113 LLQD----APIVLLDEPTVGLDpITERQ-LLSL------IFEVLKDKTLiwITHH 156
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
447-632 |
3.61e-11 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 63.32 E-value: 3.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 447 NDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSMErGIKLLFAPQHSY-------MV-------PQCTLIE 512
Cdd:cd03262 17 KGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIID-GLKLTDDKKNINelrqkvgMVfqqfnlfPHLTVLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 513 QVLFPIVsNTLGAKELDSFKEAIRLSGShsvidvlggfdspyVGADPRTadDTYDwDSLSGGQKQRITMARVfyniLTMD 592
Cdd:cd03262 96 NITLAPI-KVKGMSKAEAEERALELLEK--------------VGLADKA--DAYP-AQLSGGQQQRVAIARA----LAMN 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 70886980 593 rseqTPVVLLDESTSMMD-ETEQAVL---LNLRKLQVRMISVTH 632
Cdd:cd03262 154 ----PKVMLFDEPTSALDpELVGEVLdvmKDLAEEGMTMVVVTH 193
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
430-623 |
4.08e-11 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 63.36 E-value: 4.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 430 FAFSNLKLMTPAGQLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSME----------------RGI 493
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDgtdinklkgkalrqlrRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 494 KLLFapQHSYMVPQCTLIEQVLF------PIVSNTLGakeldSFKEAIRLSGSHSvIDVLGGFDSPYVGAdprtaddtyd 567
Cdd:cd03256 81 GMIF--QQFNLIERLSVLENVLSgrlgrrSTWRSLFG-----LFPKEEKQRALAA-LERVGLLDKAYQRA---------- 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 70886980 568 wDSLSGGQKQRITMARVFYniltmdrseQTPVVLL-DESTSMMD-ETEQAVLLNLRKL 623
Cdd:cd03256 143 -DQLSGGQQQRVAIARALM---------QQPKLILaDEPVASLDpASSRQVMDLLKRI 190
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
448-636 |
5.29e-11 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 65.92 E-value: 5.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 448 DLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSME----RGIKLLFAPQHSYMVPQctliEQVLF--PIVSN 521
Cdd:TIGR01193 492 DISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNgfslKDIDRHTLRQFINYLPQ----EPYIFsgSILEN 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 522 TL-GAKE---LDSFKEAIRLSGSHSVIDVLGgfdspyVGADPRTADDTYdwdSLSGGQKQRITMARVfynILTmdrseQT 597
Cdd:TIGR01193 568 LLlGAKEnvsQDEIWAACEIAEIKDDIENMP------LGYQTELSEEGS---SISGGQKQRIALARA---LLT-----DS 630
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 70886980 598 PVVLLDESTSMMDE-TEQAVLLNLRKLQVR-MISVTHREEV 636
Cdd:TIGR01193 631 KVLILDESTSNLDTiTEKKIVNNLLNLQDKtIIFVAHRLSV 671
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
442-632 |
5.77e-11 |
|
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: 62.70 E-value: 5.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 442 GQLLFNDLDLEIKSDQDWV-ILGENGCGKTSLLRMISGLWRPTEGSYSM-----------------ERGIKLLFapQHSY 503
Cdd:cd03297 8 KRLPDFTLKIDFDLNEEVTgIFGASGAGKSTLLRCIAGLEKPDGGTIVLngtvlfdsrkkinlppqQRKIGLVF--QQYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 504 MVPQCTLIEQVLFpivsntlGAKELDSFKEAIRLSgshSVIDVLGgfDSPYVGADPrtaddtydwDSLSGGQKQRITMAR 583
Cdd:cd03297 86 LFPHLNVRENLAF-------GLKRKRNREDRISVD---ELLDLLG--LDHLLNRYP---------AQLSGGEKQRVALAR 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 70886980 584 VFyniltmdrSEQTPVVLLDESTSMMDETEQAVLLN-LRK----LQVRMISVTH 632
Cdd:cd03297 145 AL--------AAQPELLLLDEPFSALDRALRLQLLPeLKQikknLNIPVIFVTH 190
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
447-632 |
6.23e-11 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 63.19 E-value: 6.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 447 NDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEG-----------SYSMERGIKL----LFapQHSYMVPQCTLI 511
Cdd:PRK09493 18 HNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGdlivdglkvndPKVDERLIRQeagmVF--QQFYLFPHLTAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 512 EQVLF-PIvsNTLGAKELDSFKEAIRLSGShsvidvlggfdspyVGADPRTadDTYDwDSLSGGQKQRITMARVFynilt 590
Cdd:PRK09493 96 ENVMFgPL--RVRGASKEEAEKQARELLAK--------------VGLAERA--HHYP-SELSGGQQQRVAIARAL----- 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 70886980 591 mdrSEQTPVVLLDESTSMMD-ETEQAVLLNLRKLQ---VRMISVTH 632
Cdd:PRK09493 152 ---AVKPKLMLFDEPTSALDpELRHEVLKVMQDLAeegMTMVIVTH 194
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
447-637 |
7.78e-11 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 63.22 E-value: 7.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 447 NDLDLEIKsDQDWV-ILGENGCGKTSLLRMISGLWRPTEGSYSMErGIKLLfAPQHSY-------MVPQ--------CTL 510
Cdd:TIGR04520 19 KNVSLSIE-KGEFVaIIGHNGSGKSTLAKLLNGLLLPTSGKVTVD-GLDTL-DEENLWeirkkvgMVFQnpdnqfvgATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 511 IEQVLF-------------PIVSNTLGAKELDSFKEAirlsgshsvidvlggfdSPYvgadprtaddtydwdSLSGGQKQ 577
Cdd:TIGR04520 96 EDDVAFglenlgvpreemrKRVDEALKLVGMEDFRDR-----------------EPH---------------LLSGGQKQ 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 70886980 578 RITMArvfyNILTMdrseQTPVVLLDESTSMMD-ETEQAVLLNLRKLQ----VRMISVTHR-EEVI 637
Cdd:TIGR04520 144 RVAIA----GVLAM----RPDIIILDEATSMLDpKGRKEVLETIRKLNkeegITVISITHDmEEAV 201
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
418-638 |
1.39e-10 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 63.70 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 418 IVRPKGKKDFTLFAFSNLKLMTPA--GQLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSME----- 490
Cdd:PRK11607 5 IPRPQAKTRKALTPLLEIRNLTKSfdGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDgvdls 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 491 ------RGIKLLFapQHSYMVPQCTLIEQVLFPIVSNTLGAKELDSFKEAIrLSGSHSvidvlggfdSPYVGADPRtadd 564
Cdd:PRK11607 85 hvppyqRPINMMF--QSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEM-LGLVHM---------QEFAKRKPH---- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 565 tydwdSLSGGQKQRITMARVFyniltmdrSEQTPVVLLDESTSMMDE-----TEQAVLLNLRKLQVRMISVTH-REEVIT 638
Cdd:PRK11607 149 -----QLSGGQRQRVALARSL--------AKRPKLLLLDEPMGALDKklrdrMQLEVVDILERVGVTCVMVTHdQEEAMT 215
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
441-652 |
1.52e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 61.65 E-value: 1.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 441 AGQLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGsysmergiKLLFAPQHSYMVPQCTLIEQVLFPIVS 520
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSG--------TLLFEGEDISTLKPEIYRQQVSYCAQT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 521 NTL-GAKELDSFKEAIRLSGSH----SVIDVLGGFDSPYVGADPRTADdtydwdsLSGGQKQRITMARvfyNILTMDRse 595
Cdd:PRK10247 90 PTLfGDTVYDNLIFPWQIRNQQpdpaIFLDDLERFALPDTILTKNIAE-------LSGGEKQRISLIR---NLQFMPK-- 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 70886980 596 qtpVVLLDESTSMMDETEQAVLLNL-----RKLQVRMISVTHREEVITHHTHALRILP-GGNW 652
Cdd:PRK10247 158 ---VLLLDEITSALDESNKHNVNEIihryvREQNIAVLWVTHDKDEINHADKVITLQPhAGEM 217
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
446-610 |
1.70e-10 |
|
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: 61.80 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 446 FNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSMErGI-----------KLLFAPQHSYMVPQCTLIEQV 514
Cdd:COG4555 17 LKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILID-GEdvrkeprearrQIGVLPDERGLYDRLTVRENI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 515 LFPIVSNTLGAKELDSFKEAIrlsgshsvIDVLGgfDSPYvgADPRtaddtydWDSLSGGQKQRITMARVFyniltmdrS 594
Cdd:COG4555 96 RYFAELYGLFDEELKKRIEEL--------IELLG--LEEF--LDRR-------VGELSTGMKKKVALARAL--------V 148
|
170
....*....|....*.
gi 70886980 595 EQTPVVLLDESTSMMD 610
Cdd:COG4555 149 HDPKVLLLDEPTNGLD 164
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
441-630 |
1.72e-10 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 62.06 E-value: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 441 AGQLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSME-RGIKLLFA----------PQHSYMVPQCT 509
Cdd:COG4559 12 GGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNgRPLAAWSPwelarrravlPQHSSLAFPFT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 510 LIEQVLFPIVSNTLGAKELDSF-KEAIRLSGshsvidvLGGFdspyvgadprtADDTYDwdSLSGGQKQRITMARVFYNI 588
Cdd:COG4559 92 VEEVVALGRAPHGSSAAQDRQIvREALALVG-------LAHL-----------AGRSYQ--TLSGGEQQRVQLARVLAQL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 70886980 589 LTmDRSEQTPVVLLDESTSMMDETEQAVLLNL-RKLQVRMISV 630
Cdd:COG4559 152 WE-PVDGGPRWLFLDEPTSALDLAHQHAVLRLaRQLARRGGGV 193
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
448-639 |
1.97e-10 |
|
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: 60.97 E-value: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 448 DLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSM-----------ERGIKLLFapQHSYMVPQCTLIEQVLF 516
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLIngvdvtaappaDRPVSMLF--QENNLFAHLTVEQNVGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 517 PIVSN-TLGAKELDSFKEAIRLSGshsvidvLGGFDSpyvgadpRTADdtydwdSLSGGQKQRITMARVfyniLTMDRse 595
Cdd:cd03298 94 GLSPGlKLTAEDRQAIEVALARVG-------LAGLEK-------RLPG------ELSGGERQRVALARV----LVRDK-- 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 70886980 596 qtPVVLLDESTSMMDETEQAVLLNL-----RKLQVRMISVTHREEVITH 639
Cdd:cd03298 148 --PVLLLDEPFAALDPALRAEMLDLvldlhAETKMTVLMVTHQPEDAKR 194
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
442-632 |
1.97e-10 |
|
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: 61.36 E-value: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 442 GQLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGS----------------YSMERGIKLLFapQHSYMV 505
Cdd:cd03261 12 GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEvlidgedisglseaelYRLRRRMGMLF--QSGALF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 506 PQCTLIEQVLFPIVSNT-LGAKELDSF-KEAIRLSGshsvidvLGGFDSPYVGadprtaddtydwdSLSGGQKQRITMAR 583
Cdd:cd03261 90 DSLTVFENVAFPLREHTrLSEEEIREIvLEKLEAVG-------LRGAEDLYPA-------------ELSGGMKKRVALAR 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 70886980 584 VfyniLTMDrseqTPVVLLDESTSMMDETEQAVLLNL-RKLQVRM----ISVTH 632
Cdd:cd03261 150 A----LALD----PELLLYDEPTAGLDPIASGVIDDLiRSLKKELgltsIMVTH 195
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
448-654 |
2.63e-10 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 62.44 E-value: 2.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 448 DLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSME-----RGIKLLFAPQH----SYMVPQCTLieqvlFP- 517
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNgrtlfDSRKGIFLPPEkrriGYVFQEARL-----FPh 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 518 --IVSNTL-GAKELDSFKEAIRLSgshSVIDVLGgfDSPYVGADPRTaddtydwdsLSGGQKQRITMARVfynILTMDRs 594
Cdd:TIGR02142 90 lsVRGNLRyGMKRARPSERRISFE---RVIELLG--IGHLLGRLPGR---------LSGGEKQRVAIGRA---LLSSPR- 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 70886980 595 eqtpVVLLDESTSMMDETEQAVLL----NLR-KLQVRMISVTHREEVITHHTHALRILPGGNWTA 654
Cdd:TIGR02142 152 ----LLLMDEPLAALDDPRKYEILpyleRLHaEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAA 212
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
446-632 |
3.56e-10 |
|
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: 60.66 E-value: 3.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 446 FNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLW-----RPTEGS---------------YSMERGIKLLFapQHSYMV 505
Cdd:cd03260 16 LKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEvlldgkdiydldvdvLELRRRVGMVF--QKPNPF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 506 PQcTLIEQVLFPI-VSNTLGAKELDSfkeairlsgshSVIDVLGGfdspyVGADPRTADDTyDWDSLSGGQKQRITMARV 584
Cdd:cd03260 94 PG-SIYDNVAYGLrLHGIKLKEELDE-----------RVEEALRK-----AALWDEVKDRL-HALGLSGGQQQRLCLARA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 70886980 585 fyniLTMDrseqtP-VVLLDESTSMMD-----ETEQAvLLNLRKlQVRMISVTH 632
Cdd:cd03260 156 ----LANE-----PeVLLLDEPTSALDpistaKIEEL-IAELKK-EYTIVIVTH 198
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
444-486 |
4.04e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 59.82 E-value: 4.04e-10
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 70886980 444 LLFNDLDLEIKSDqDWV-ILGENGCGKTSLLRMISGLWRPTEGS 486
Cdd:PRK13538 15 ILFSGLSFTLNAG-ELVqIEGPNGAGKTSLLRILAGLARPDAGE 57
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
442-606 |
4.52e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 62.39 E-value: 4.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 442 GQLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGsySMERGIKLLFA--PQH-SYMVPQCTLIEQVlfpi 518
Cdd:COG0488 327 DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSG--TVKLGETVKIGyfDQHqEELDPDKTVLDEL---- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 519 vsntlgAKELDSFKEAirlsgshSVIDVLGGF-------DSPyVGadprtaddtydwdSLSGGQKQRITMARVF---YNI 588
Cdd:COG0488 401 ------RDGAPGGTEQ-------EVRGYLGRFlfsgddaFKP-VG-------------VLSGGEKARLALAKLLlspPNV 453
|
170
....*....|....*...
gi 70886980 589 LtmdrseqtpvvLLDEST 606
Cdd:COG0488 454 L-----------LLDEPT 460
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
442-632 |
6.30e-10 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 60.15 E-value: 6.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 442 GQLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEG-------------SYSMERG-IKLL-----FAPQHS 502
Cdd:PRK11264 15 GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGtirvgditidtarSLSQQKGlIRQLrqhvgFVFQNF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 503 YMVPQCTLIEQVLFPIVSNTLGAKEldsfkEAIRLSGSHSVIDVLGGFDSPYvgadPRtaddtydwdSLSGGQKQRITMA 582
Cdd:PRK11264 95 NLFPHRTVLENIIEGPVIVKGEPKE-----EATARARELLAKVGLAGKETSY----PR---------RLSGGQQQRVAIA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 70886980 583 RVfyniLTMdrseQTPVVLLDESTSMMD-ETEQAVLLNLRKL---QVRMISVTH 632
Cdd:PRK11264 157 RA----LAM----RPEVILFDEPTSALDpELVGEVLNTIRQLaqeKRTMVIVTH 202
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
428-647 |
6.63e-10 |
|
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: 61.84 E-value: 6.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 428 TLFAFSNLKLMTPAGQL-LFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPT---EGSYSMErGIKLLFAPQHSY 503
Cdd:COG1123 3 PLLEVRDLSVRYPGGDVpAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLD-GRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 504 -----MVPQ--------CTLIEQVLFPIVSNTLgakeldSFKEAIRLsgshsVIDVLGgfdspYVGADPRTADDTydwDS 570
Cdd:COG1123 82 grrigMVFQdpmtqlnpVTVGDQIAEALENLGL------SRAEARAR-----VLELLE-----AVGLERRLDRYP---HQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 571 LSGGQKQRITMARVfyniLTMDrseqTPVVLLDESTSMMDETEQA-VLLNLRKLQVR----MISVTHREEVITHhtHALR 645
Cdd:COG1123 143 LSGGQRQRVAIAMA----LALD----PDLLIADEPTTALDVTTQAeILDLLRELQRErgttVLLITHDLGVVAE--IADR 212
|
..
gi 70886980 646 IL 647
Cdd:COG1123 213 VV 214
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
440-640 |
7.37e-10 |
|
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: 61.99 E-value: 7.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 440 PAGQLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSMErGIKLLFAPQHSYMVPQCTLIEQV-LF-P 517
Cdd:TIGR02868 345 PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLD-GVPVSSLDQDEVRRRVSVCAQDAhLFdT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 518 IVSNTL--GAKEL--DSFKEAIRLSGSHSVIDVL-GGFDSPyVGADPRtaddtydwdSLSGGQKQRITMARVfynILTmd 592
Cdd:TIGR02868 424 TVRENLrlARPDAtdEELWAALERVGLADWLRALpDGLDTV-LGEGGA---------RLSGGERQRLALARA---LLA-- 488
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 70886980 593 rseQTPVVLLDESTSMMD-ETEQAVLLNLRKLQVRMISVthreeVITHH 640
Cdd:TIGR02868 489 ---DAPILLLDEPTEHLDaETADELLEDLLAALSGRTVV-----LITHH 529
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
113-647 |
1.06e-09 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 61.25 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 113 NRVQNFFRVLLLRAAVSMMAAVCsgsiehlRTLLIACYRERLSRYLQRRFYSHLLY----YQATVLDG----RLETADTV 184
Cdd:TIGR02204 55 GLLNRYFAFLLVVALVLALGTAA-------RFYLVTWLGERVVADIRRAVFAHLISlspsFFDKNRSGevvsRLTTDTTL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 185 IATYCGEFAEhfaeLPYYFLLPMFGCMTSMVVltrnVGAKAAGLACGAVAISVLILQkispAFGRiHASLLAREEDYRRM 264
Cdd:TIGR02204 128 LQSVIGSSLS----MALRNALMCIGGLIMMFI----TSPKLTSLVLLAVPLVLLPIL----LFGR-RVRKLSRESQDRIA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 265 LTNSLNNVEYIAMHNGGSYTRQKLERQL--GKLKRALDhFALAKGHFDFLEISFSALLqAISS--LVIFRGAHQMKTKSM 340
Cdd:TIGR02204 195 DAGSYAGETLGAIRTVQAFGHEDAERSRfgGAVEKAYE-AARQRIRTRALLTAIVIVL-VFGAivGVLWVGAHDVIAGKM 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 341 NdiyveiqcmqdlienvksfvvnfreVSHLSTFTVKLAEFDSTLTSIAE--GCFIRSSGASPK----SDCNSDFPVSYTH 414
Cdd:TIGR02204 273 S-------------------------AGTLGQFVFYAVMVAGSIGTLSEvwGELQRAAGAAERlielLQAEPDIKAPAHP 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 415 VNYIVRPKGKkdftlFAFSNLKLMTPA--GQLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSMErG 492
Cdd:TIGR02204 328 KTLPVPLRGE-----IEFEQVNFAYPArpDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLD-G 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 493 IKLL-FAPQ----HSYMVPQctliEQVLFP------IVSNTLGAKElDSFKEAIRLSGSHSVIDVLG-GFDSpYVGADPR 560
Cdd:TIGR02204 402 VDLRqLDPAelraRMALVPQ----DPVLFAasvmenIRYGRPDATD-EEVEAAARAAHAHEFISALPeGYDT-YLGERGV 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 561 TaddtydwdsLSGGQKQRITMARVfynILtmdrsEQTPVVLLDESTSMMD-ETEQAVLLNLRKLqvrmisVTHREEVITH 639
Cdd:TIGR02204 476 T---------LSGGQRQRIAIARA---IL-----KDAPILLLDEATSALDaESEQLVQQALETL------MKGRTTLIIA 532
|
570
....*....|...
gi 70886980 640 H-----THALRIL 647
Cdd:TIGR02204 533 HrlatvLKADRIV 545
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
447-632 |
1.58e-09 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 60.04 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 447 NDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSY-----------SMERGIKLLFapqHSY-MVPQCTLIEQV 514
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLfigekrmndvpPAERGVGMVF---QSYaLYPHLSVAENM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 515 LFpivsntlGAKeLDSFKEAIRLSGSHSVIDVLggfdspYVGA--DPRTADdtydwdsLSGGQKQRITMARvfynilTMD 592
Cdd:PRK11000 97 SF-------GLK-LAGAKKEEINQRVNQVAEVL------QLAHllDRKPKA-------LSGGQRQRVAIGR------TLV 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 70886980 593 RseQTPVVLLDESTSMMDeteQAVLLNLR--------KLQVRMISVTH 632
Cdd:PRK11000 150 A--EPSVFLLDEPLSNLD---AALRVQMRieisrlhkRLGRTMIYVTH 192
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
440-633 |
1.59e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 60.99 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 440 PAGQLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSysmergIKLLFAPQHSYmvPQCTLIEQVLF--- 516
Cdd:PRK11160 350 DQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGE------ILLNGQPIADY--SEAALRQAISVvsq 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 517 --PIVSNTLG-----AKEL---DSFKEAIRLSGSHSVIDVLGGFDSpYVGADPRTaddtydwdsLSGGQKQRITMARVFY 586
Cdd:PRK11160 422 rvHLFSATLRdnlllAAPNasdEALIEVLQQVGLEKLLEDDKGLNA-WLGEGGRQ---------LSGGEQRRLGIARALL 491
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 70886980 587 NiltmdrseQTPVVLLDESTSMMD-ETEQAVLLNLRKL--QVRMISVTHR 633
Cdd:PRK11160 492 H--------DAPLLLLDEPTEGLDaETERQILELLAEHaqNKTVLMITHR 533
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
439-637 |
1.63e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 59.23 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 439 TPAGQLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSMErGIK-----LLFAPQHSYMVPQ------ 507
Cdd:PRK13632 18 PNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKID-GITiskenLKEIRKKIGIIFQnpdnqf 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 508 --CTLIEQVLFPIVSNTLGAKELDsfkeAIRLSGSHSVidvlgGFDSpYVGADPRtaddtydwdSLSGGQKQRITMARVf 585
Cdd:PRK13632 97 igATVEDDIAFGLENKKVPPKKMK----DIIDDLAKKV-----GMED-YLDKEPQ---------NLSGGQKQRVAIASV- 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 70886980 586 yniLTMDRSeqtpVVLLDESTSMMD----ETEQAVLLNLRKLQVR-MISVTH-REEVI 637
Cdd:PRK13632 157 ---LALNPE----IIIFDESTSMLDpkgkREIKKIMVDLRKTRKKtLISITHdMDEAI 207
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
441-620 |
1.76e-09 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 59.01 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 441 AGQLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSysmergIKLLFAPQHSY----------MVPQCTl 510
Cdd:PRK13548 13 GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGE------VRLNGRPLADWspaelarrraVLPQHS- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 511 ieQVLFP-----IVS-----NTLGAKELDS-FKEAIRLSGshsvidvLGGF-DSPYVgadprtaddtydwdSLSGGQKQR 578
Cdd:PRK13548 86 --SLSFPftveeVVAmgrapHGLSRAEDDAlVAAALAQVD-------LAHLaGRDYP--------------QLSGGEQQR 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 70886980 579 ITMARVfyniLTM--DRSEQTPVVLLDESTSMMDETEQAVLLNL 620
Cdd:PRK13548 143 VQLARV----LAQlwEPDGPPRWLLLDEPTSALDLAHQHHVLRL 182
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
448-632 |
2.18e-09 |
|
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: 58.50 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 448 DLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSME-----------RGIKllFAPQHSYMVPQCTLIEQVLF 516
Cdd:cd03299 17 NVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNgkditnlppekRDIS--YVPQNYALFPHMTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 517 PIVSNTLGAKELDsfKEAIRLSGSHSVIDVLggfdspyvGADPRTaddtydwdsLSGGQKQRITMARVfyniLTMDRSeq 596
Cdd:cd03299 95 GLKKRKVDKKEIE--RKVLEIAEMLGIDHLL--------NRKPET---------LSGGEQQRVAIARA----LVVNPK-- 149
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 70886980 597 tpVVLLDESTSMMDETEQAVLLNL-----RKLQVRMISVTH 632
Cdd:cd03299 150 --ILLLDEPFSALDVRTKEKLREElkkirKEFGVTVLHVTH 188
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
447-610 |
2.29e-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: 57.90 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 447 NDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGS-----YSMERGIKLL-----FAPQHSYMVPQCTLIEQVLF 516
Cdd:cd03263 19 DDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTayingYSIRTDRKAArqslgYCPQFDALFDELTVREHLRF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 517 pivsntlgAKELDSFKEAIRLSGSHSVIDVLGgfDSPYVGADPRTaddtydwdsLSGGQKQRITMArvfynILTMDRSeq 596
Cdd:cd03263 99 --------YARLKGLPKSEIKEEVELLLRVLG--LTDKANKRART---------LSGGMKRKLSLA-----IALIGGP-- 152
|
170
....*....|....
gi 70886980 597 tPVVLLDESTSMMD 610
Cdd:cd03263 153 -SVLLLDEPTSGLD 165
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
447-637 |
3.40e-09 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 59.04 E-value: 3.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 447 NDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSY----------------SMERGIKLLFapQHSYMVPQCTL 510
Cdd:PRK11153 22 NNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVlvdgqdltalsekelrKARRQIGMIF--QHFNLLSSRTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 511 IEQVLFPIvsntlgakELDSF-KEAIRlsgsHSVIDVLggfdsPYVG-ADPRtadDTYDwDSLSGGQKQRITMARVFYNi 588
Cdd:PRK11153 100 FDNVALPL--------ELAGTpKAEIK----ARVTELL-----ELVGlSDKA---DRYP-AQLSGGQKQRVAIARALAS- 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 70886980 589 ltmdrseqTPVVLL-DESTSMMD-ETEQAVLLNLRKLQVRM-ISV---THREEVI 637
Cdd:PRK11153 158 --------NPKVLLcDEATSALDpATTRSILELLKDINRELgLTIvliTHEMDVV 204
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
432-642 |
3.78e-09 |
|
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: 57.42 E-value: 3.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 432 FSNLKLMTPAGQLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYS----------------MERGIKL 495
Cdd:cd03292 3 FINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRvngqdvsdlrgraipyLRRKIGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 496 LFapQHSYMVPQCTLIEQVLFPIVSNTLGAKEL-DSFKEAIRLSGSHSVIDVLGgfdspyvgadprtaddtydwDSLSGG 574
Cdd:cd03292 83 VF--QDFRLLPDRNVYENVAFALEVTGVPPREIrKRVPAALELVGLSHKHRALP--------------------AELSGG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 70886980 575 QKQRITMARVFYNiltmdrseQTPVVLLDESTSMMDETEQAVLLNL----RKLQVRMISVTHREEVITHHTH 642
Cdd:cd03292 141 EQQRVAIARAIVN--------SPTILIADEPTGNLDPDTTWEIMNLlkkiNKAGTTVVVATHAKELVDTTRH 204
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
442-617 |
4.82e-09 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 56.60 E-value: 4.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 442 GQLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGsysmergiKLLFAPQHSYMVpQCTLIEQVLF----P 517
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSG--------EVRWNGTPLAEQ-RDEPHENILYlghlP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 518 IVSNTLGAKELDSFKEAIRLSGSHSVIDVLG--GFDspyvGADPRTAddtydwDSLSGGQKQRITMARVFyniLTmdrse 595
Cdd:TIGR01189 83 GLKPELSALENLHFWAAIHGGAQRTIEDALAavGLT----GFEDLPA------AQLSAGQQRRLALARLW---LS----- 144
|
170 180
....*....|....*....|..
gi 70886980 596 QTPVVLLDESTSMMDETEQAVL 617
Cdd:TIGR01189 145 RRPLWILDEPTTALDKAGVALL 166
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
447-583 |
4.86e-09 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 57.77 E-value: 4.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 447 NDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSY--------SMERGIKLLFapQHSYMVPQCTLIEQVlfpi 518
Cdd:PRK11247 29 NQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELlagtaplaEAREDTRLMF--QDARLLPWKKVIDNV---- 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 70886980 519 vsnTLGAKelDSFKEAirlsgSHSVIDVLGgfdspyvgadprTADDTYDWD-SLSGGQKQRITMAR 583
Cdd:PRK11247 103 ---GLGLK--GQWRDA-----ALQALAAVG------------LADRANEWPaALSGGQKQRVALAR 146
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
441-649 |
5.69e-09 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 57.40 E-value: 5.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 441 AGQLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSM----------ERGIklLFapQHSYMVPQCTL 510
Cdd:PRK11248 12 GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLdgkpvegpgaERGV--VF--QNEGLLPWRNV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 511 IEQVLFPIVSNTLG-AKELDSFKEAIRLSGshsvidvLGGFDSPYVgadprtaddtydWdSLSGGQKQRITMARVFynil 589
Cdd:PRK11248 88 QDNVAFGLQLAGVEkMQRLEIAHQMLKKVG-------LEGAEKRYI------------W-QLSGGQRQRVGIARAL---- 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 70886980 590 tmdrSEQTPVVLLDESTSMMD----ETEQAVLLNL----RKlQVRMIsvTHR-EEVITHHTHALRILPG 649
Cdd:PRK11248 144 ----AANPQLLLLDEPFGALDaftrEQMQTLLLKLwqetGK-QVLLI--THDiEEAVFMATELVLLSPG 205
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
445-637 |
5.74e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 56.89 E-value: 5.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 445 LFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSMErgikllFAPQHSYmvPQCTLIEQVLfpivsntlg 524
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD------VPDNQFG--REASLIDAIG--------- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 525 akELDSFKEAIRLsgSHSVidvlgGFDSPYVGADPrtaddtydWDSLSGGQKQRITMARVFyniltmdrSEQTPVVLLDE 604
Cdd:COG2401 108 --RKGDFKDAVEL--LNAV-----GLSDAVLWLRR--------FKELSTGQKFRFRLALLL--------AERPKLLVIDE 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 70886980 605 STSMMD-ETEQAVLLNLRKLQVR----MISVTHREEVI 637
Cdd:COG2401 163 FCSHLDrQTAKRVARNLQKLARRagitLVVATHHYDVI 200
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
432-610 |
6.49e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 59.60 E-value: 6.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 432 FS-NLKLMTPAgqllFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSMERGiKLLFAPQHSYMVpQCTL 510
Cdd:PLN03232 622 FSwDSKTSKPT----LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVIRG-SVAYVPQVSWIF-NATV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 511 IEQVLFpivsntlGAK-ELDSFKEAIRLSGSHSVIDVLGGFDSPYVGAdpRTADdtydwdsLSGGQKQRITMARVFYNil 589
Cdd:PLN03232 696 RENILF-------GSDfESERYWRAIDVTALQHDLDLLPGRDLTEIGE--RGVN-------ISGGQKQRVSMARAVYS-- 757
|
170 180
....*....|....*....|.
gi 70886980 590 tmdrseQTPVVLLDESTSMMD 610
Cdd:PLN03232 758 ------NSDIYIFDDPLSALD 772
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
442-632 |
6.68e-09 |
|
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: 56.91 E-value: 6.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 442 GQLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGS----------------YSMERGIKLLFapQH---- 501
Cdd:COG1127 17 DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEilvdgqditglsekelYELRRRIGMLF--QGgalf 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 502 SYMvpqcTLIEQVLFPIVSNT-LGAKELD---SFK-EAIRLSGShsvidvlggfdspyvgADPRTADdtydwdsLSGGQK 576
Cdd:COG1127 95 DSL----TVFENVAFPLREHTdLSEAEIRelvLEKlELVGLPGA----------------ADKMPSE-------LSGGMR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 70886980 577 QRITMARVfyniLTMDrseqtP-VVLLDESTS-----MMDETEQaVLLNLRK-LQVRMISVTH 632
Cdd:COG1127 148 KRVALARA----LALD-----PeILLYDEPTAgldpiTSAVIDE-LIRELRDeLGLTSVVVTH 200
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
442-610 |
6.71e-09 |
|
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: 56.35 E-value: 6.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 442 GQLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSMERGiklLFAPQHSYMVPQCTLIEQVlfPIVSN 521
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGG---PLDFQRDSIARGLLYLGHA--PGIKT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 522 TLGAKELDSFKEAIrlSGSHSVIDV-----LGGFDSPYVGadprtaddtydwdSLSGGQKQRITMARVFYNiltmdrseQ 596
Cdd:cd03231 87 TLSVLENLRFWHAD--HSDEQVEEAlarvgLNGFEDRPVA-------------QLSAGQQRRVALARLLLS--------G 143
|
170
....*....|....
gi 70886980 597 TPVVLLDESTSMMD 610
Cdd:cd03231 144 RPLWILDEPTTALD 157
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
458-632 |
1.05e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 56.95 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 458 DWV-ILGENGCGKTSLLRMISGLWRPTEGSYSMErGIKLlfAPQHSY-------MVPQ--------CTLIEQVLFPIVSN 521
Cdd:PRK13635 34 EWVaIVGHNGSGKSTLAKLLNGLLLPEAGTITVG-GMVL--SEETVWdvrrqvgMVFQnpdnqfvgATVQDDVAFGLENI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 522 TLGAKEL-DSFKEAIRLSGSHSVIDvlggfDSPYvgadprtaddtydwdSLSGGQKQRITMARVFyniltmdrSEQTPVV 600
Cdd:PRK13635 111 GVPREEMvERVDQALRQVGMEDFLN-----REPH---------------RLSGGQKQRVAIAGVL--------ALQPDII 162
|
170 180 190
....*....|....*....|....*....|....*..
gi 70886980 601 LLDESTSMMD-ETEQAVLLNLRKLQ----VRMISVTH 632
Cdd:PRK13635 163 ILDEATSMLDpRGRREVLETVRQLKeqkgITVLSITH 199
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
447-632 |
1.19e-08 |
|
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: 56.99 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 447 NDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRP---TEGSYSMeRGIKLLFAPQHSY---------MVPQ------- 507
Cdd:COG0444 22 DGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILF-DGEDLLKLSEKELrkirgreiqMIFQdpmtsln 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 508 --CTLIEQVLFPIVSNTLGAKeldsfKEAIRLsgshsVIDVLG--GFDSPyvgadPRTADDtYDWdSLSGGQKQRITMAR 583
Cdd:COG0444 101 pvMTVGDQIAEPLRIHGGLSK-----AEARER-----AIELLErvGLPDP-----ERRLDR-YPH-ELSGGMRQRVMIAR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 70886980 584 VfyniLTMDrseqtP-VVLLDESTSMMDETEQAVLLNL-RKLQVR----MISVTH 632
Cdd:COG0444 164 A----LALE-----PkLLIADEPTTALDVTIQAQILNLlKDLQRElglaILFITH 209
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
441-620 |
1.39e-08 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 57.54 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 441 AGQLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSME-RGIKLLFAPQHSYMV---PQCTLIeqvlf 516
Cdd:PRK09536 14 GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAgDDVEALSARAASRRVasvPQDTSL----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 517 pivsntlgakeldSFK---EAIRLSGSHSVIDVLGGFDSPYVGADPRTADDT-------YDWDSLSGGQKQRITMARVFy 586
Cdd:PRK09536 89 -------------SFEfdvRQVVEMGRTPHRSRFDTWTETDRAAVERAMERTgvaqfadRPVTSLSGGERQRVLLARAL- 154
|
170 180 190
....*....|....*....|....*....|....
gi 70886980 587 niltmdrSEQTPVVLLDESTSMMDETEQAVLLNL 620
Cdd:PRK09536 155 -------AQATPVLLLDEPTASLDINHQVRTLEL 181
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
448-639 |
1.48e-08 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 57.83 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 448 DLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSMErGIKLLFA-PQHSYMVPQCTLIEQVLF--PIVSNTLG 524
Cdd:TIGR01846 475 NLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVD-GVDLAIAdPAWLRRQMGVVLQENVLFsrSIRDNIAL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 525 AKELDSFKEAI---RLSGSHSVIDVL-GGFDSPYV--GAdprtaddtydwdSLSGGQKQRITMARVFYNiltmdrseQTP 598
Cdd:TIGR01846 554 CNPGAPFEHVIhaaKLAGAHDFISELpQGYNTEVGekGA------------NLSGGQRQRIAIARALVG--------NPR 613
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 70886980 599 VVLLDESTSMMD-ETEQAVLLNLRKL-QVR-MISVTHREEVITH 639
Cdd:TIGR01846 614 ILIFDEATSALDyESEALIMRNMREIcRGRtVIIIAHRLSTVRA 657
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
421-638 |
1.63e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 57.95 E-value: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 421 PKGKKDFTLFAFSNLKLMTPAGQLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSMERGIKLLFAPQ 500
Cdd:PLN03073 500 PDDRPGPPIISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQ 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 501 HSymVPQCTLIEQVLFPIVSNTLGAKEldsfkEAIRlsgSHsvidvLGGFdspyvGADPRTA-DDTYdwdSLSGGQKQRI 579
Cdd:PLN03073 580 HH--VDGLDLSSNPLLYMMRCFPGVPE-----QKLR---AH-----LGSF-----GVTGNLAlQPMY---TLSGGQKSRV 636
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 580 TMARVFYNiltmdrseQTPVVLLDESTSMMD-ETEQAVLLNLRKLQVRMISVTHREEVIT 638
Cdd:PLN03073 637 AFAKITFK--------KPHILLLDEPSNHLDlDAVEALIQGLVLFQGGVLMVSHDEHLIS 688
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
447-632 |
1.83e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 55.91 E-value: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 447 NDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGsysmergiKLLFAPQhsymvpqctlieqvlfPIVSNTLgaK 526
Cdd:PRK13648 26 KDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSG--------EIFYNNQ----------------AITDDNF--E 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 527 ELdsfKEAI---------RLSGSHSVIDVLGGFDSPYVGAD------PRTADDT-------YDWDSLSGGQKQRITMARV 584
Cdd:PRK13648 80 KL---RKHIgivfqnpdnQFVGSIVKYDVAFGLENHAVPYDemhrrvSEALKQVdmleradYEPNALSGGQKQRVAIAGV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 70886980 585 fyniLTMDRSeqtpVVLLDESTSMMDETEQAVLLNL-RKLQ----VRMISVTH 632
Cdd:PRK13648 157 ----LALNPS----VIILDEATSMLDPDARQNLLDLvRKVKsehnITIISITH 201
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
440-650 |
2.11e-08 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 55.85 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 440 PAGQLLfNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYS----------------MERGIKLLFAPQHSY 503
Cdd:PRK10419 23 QHQTVL-NNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSwrgeplaklnraqrkaFRRDIQMVFQDSISA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 504 MVPQCTLIEQVLFPIvsntlgaKELDSFKEAIRLSGSHSVIDVlggfdspyVGADPRTADDTYDwdSLSGGQKQRITMAR 583
Cdd:PRK10419 102 VNPRKTVREIIREPL-------RHLLSLDKAERLARASEMLRA--------VDLDDSVLDKRPP--QLSGGQLQRVCLAR 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 70886980 584 VFyniltmdrSEQTPVVLLDESTSMMDETEQAVLLN-LRKLQVRM----ISVTHREEVITHHTHALRILPGG 650
Cdd:PRK10419 165 AL--------AVEPKLLILDEAVSNLDLVLQAGVIRlLKKLQQQFgtacLFITHDLRLVERFCQRVMVMDNG 228
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
446-639 |
2.35e-08 |
|
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: 55.03 E-value: 2.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 446 FNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEG----------------SYSMERGiKLLFAPQHSYMVpQCT 509
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGkvhwsnknesepsfeaTRSRNRY-SVAYAAQKPWLL-NAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 510 LIEQVLFPIVSNTlgakelDSFKEAIRLSGSHSVIDVLGGFDSPYVGAdpRTADdtydwdsLSGGQKQRITMARVFYnil 589
Cdd:cd03290 95 VEENITFGSPFNK------QRYKAVTDACSLQPDIDLLPFGDQTEIGE--RGIN-------LSGGQRQRICVARALY--- 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 70886980 590 tmdrsEQTPVVLLDESTSMMD------ETEQAVLLNLRKLQVRMISVTHREEVITH 639
Cdd:cd03290 157 -----QNTNIVFLDDPFSALDihlsdhLMQEGILKFLQDDKRTLVLVTHKLQYLPH 207
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
460-636 |
3.92e-08 |
|
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: 55.88 E-value: 3.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 460 VILGENGCGKTSLLRMISGLWRPTEGS--------YSMERGIkllFAPQH----SYmVPQctliEQVLFP--IVSNTL-- 523
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGLERPDSGRirlggevlQDSARGI---FLPPHrrriGY-VFQ----EARLFPhlSVRGNLly 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 524 GAKELDSFKEAIRLsgsHSVIDVLGgfdspyVGA--DPRTAddtydwdSLSGGQKQRITMARVfynILTMDRseqtpVVL 601
Cdd:COG4148 101 GRKRAPRAERRISF---DEVVELLG------IGHllDRRPA-------TLSGGERQRVAIGRA---LLSSPR-----LLL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 70886980 602 LDESTSMMDETEQAVLLNL-----RKLQVRMISVTH-REEV 636
Cdd:COG4148 157 MDEPLAALDLARKAEILPYlerlrDELDIPILYVSHsLDEV 197
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
461-636 |
4.08e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 56.18 E-value: 4.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 461 ILGENGCGKTSLLRMISGLWRPTEGSYSMErGIKLLFA-PQHS-----YMVPQctliEQVLFP---IVSN-TLGakelds 530
Cdd:COG1129 35 LLGENGAGKSTLMKILSGVYQPDSGEILLD-GEPVRFRsPRDAqaagiAIIHQ----ELNLVPnlsVAENiFLG------ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 531 fkeaiRLSGSHSVID----------VLGGFDspyVGADPRT--ADdtydwdsLSGGQKQRITMARVFyniltmdrSEQTP 598
Cdd:COG1129 104 -----REPRRGGLIDwramrrrareLLARLG---LDIDPDTpvGD-------LSVAQQQLVEIARAL--------SRDAR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 70886980 599 VVLLDESTSMMDETEQAVLLNL-RKLQ---VRMISVTHR-EEV 636
Cdd:COG1129 161 VLILDEPTASLTEREVERLFRIiRRLKaqgVAIIYISHRlDEV 203
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
461-639 |
5.11e-08 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 54.59 E-value: 5.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 461 ILGENGCGKTSLLRMISGLWRPTEGSYSM-------------------ERGIKLL-----FAPQHSYMVPQCTLIEQVL- 515
Cdd:PRK10619 36 IIGSSGSGKSTFLRCINFLEKPSEGSIVVngqtinlvrdkdgqlkvadKNQLRLLrtrltMVFQHFNLWSHMTVLENVMe 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 516 FPIvsNTLGAKELDSFKEAIRLSGShsvidvlggfdspyVGADPRtADDTYDWDsLSGGQKQRITMARVfyniLTMdrse 595
Cdd:PRK10619 116 API--QVLGLSKQEARERAVKYLAK--------------VGIDER-AQGKYPVH-LSGGQQQRVSIARA----LAM---- 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 70886980 596 QTPVVLLDESTSMMD-ETEQAVLLNLRKLQVR---MISVTHREEVITH 639
Cdd:PRK10619 170 EPEVLLFDEPTSALDpELVGEVLRIMQQLAEEgktMVVVTHEMGFARH 217
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
443-633 |
5.33e-08 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 56.27 E-value: 5.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 443 QLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSMErGIKLlfaPQ--HSYMVPQCTLIEQ--VLF-- 516
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLD-GVPL---VQydHHYLHRQVALVGQepVLFsg 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 517 PIVSNT---LGAKELDSFKEAIRLSGSHSVIdvlGGFdspyvgadprtaDDTYDWD------SLSGGQKQRITMARVFYn 587
Cdd:TIGR00958 570 SVRENIaygLTDTPDEEIMAAAKAANAHDFI---MEF------------PNGYDTEvgekgsQLSGGQKQRIAIARALV- 633
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 70886980 588 iltmdrseQTPVVL-LDESTSMMDETEQAVLLNLRKLQVR-MISVTHR 633
Cdd:TIGR00958 634 --------RKPRVLiLDEATSALDAECEQLLQESRSRASRtVLLIAHR 673
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
442-620 |
8.27e-08 |
|
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: 53.35 E-value: 8.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 442 GQLLFNDLDLEIkSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSM------ERGIKLL----FAPQHSYMVPQCTLI 511
Cdd:cd03264 12 KKRALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIdgqdvlKQPQKLRrrigYLPQEFGVYPNFTVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 512 EQVLFPIVSNTLGAKELDS-FKEAIRLSGshsvidvLGGFDSPYVGadprtaddtydwdSLSGGQKQRITMARVFYNilt 590
Cdd:cd03264 91 EFLDYIAWLKGIPSKEVKArVDEVLELVN-------LGDRAKKKIG-------------SLSGGMRRRVGIAQALVG--- 147
|
170 180 190
....*....|....*....|....*....|
gi 70886980 591 mdrseQTPVVLLDESTSMMDETEQAVLLNL 620
Cdd:cd03264 148 -----DPSILIVDEPTAGLDPEERIRFRNL 172
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
461-627 |
8.69e-08 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 54.35 E-value: 8.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 461 ILGENGCGKTSLLRMISGLWRPTEGS----------------YSMERGIKLLFapQHSYMV--PQCTLIEQVLFPIVSNT 522
Cdd:COG4608 49 LVGESGCGKSTLGRLLLRLEEPTSGEilfdgqditglsgrelRPLRRRMQMVF--QDPYASlnPRMTVGDIIAEPLRIHG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 523 LGAKE--LDSFKEAIRLsgshsvidvlggfdspyVGADPRTADdTYDwDSLSGGQKQRITMARVfyniLTMDrseqtP-V 599
Cdd:COG4608 127 LASKAerRERVAELLEL-----------------VGLRPEHAD-RYP-HEFSGGQRQRIGIARA----LALN-----PkL 178
|
170 180
....*....|....*....|....*....
gi 70886980 600 VLLDESTSMMDETEQAVLLNL-RKLQVRM 627
Cdd:COG4608 179 IVCDEPVSALDVSIQAQVLNLlEDLQDEL 207
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
448-620 |
1.39e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 53.45 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 448 DLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEG-------------SYSMERGIKLLfaPQHSYMVPQCTLIE-- 512
Cdd:PRK10253 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGhvwldgehiqhyaSKEVARRIGLL--AQNATTPGDITVQElv 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 513 -------QVLFpivsnTLGAKE-LDSFKEAIRLSGSHSVIDvlggfdspyvgadprtaddtYDWDSLSGGQKQRITMARV 584
Cdd:PRK10253 103 argryphQPLF-----TRWRKEdEEAVTKAMQATGITHLAD--------------------QSVDTLSGGQRQRAWIAMV 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 70886980 585 FyniltmdrSEQTPVVLLDESTSMMDETEQAVLLNL 620
Cdd:PRK10253 158 L--------AQETAIMLLDEPTTWLDISHQIDLLEL 185
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
447-610 |
1.45e-07 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 52.76 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 447 NDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGS-----YSMERGIKLL-----FAPQHSYMVPQCTLIEQVLF 516
Cdd:COG1131 17 DGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEvrvlgEDVARDPAEVrrrigYVPQEPALYPDLTVRENLRF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 517 pivsntlgAKELDSFKEAIRLSGSHSVIDvlggfdspYVGADPRtADDTYdwDSLSGGQKQRITMARVFYNiltmdrseQ 596
Cdd:COG1131 97 --------FARLYGLPRKEARERIDELLE--------LFGLTDA-ADRKV--GTLSGGMKQRLGLALALLH--------D 149
|
170
....*....|....
gi 70886980 597 TPVVLLDESTSMMD 610
Cdd:COG1131 150 PELLILDEPTSGLD 163
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
446-486 |
1.71e-07 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 52.78 E-value: 1.71e-07
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 70886980 446 FNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGS 486
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGR 82
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
461-639 |
1.87e-07 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 52.92 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 461 ILGENGCGKTSLLRMISGLWRPTEGSYSMeRGIKLLFAP-----QHSYMV---PQCTL-----IEQVL-FPIVSNT-LGA 525
Cdd:COG4167 44 IIGENGSGKSTLAKMLAGIIEPTSGEILI-NGHKLEYGDykyrcKHIRMIfqdPNTSLnprlnIGQILeEPLRLNTdLTA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 526 KELdsfKEAIrlsgshsvIDVLGgfdspYVGADPRTADdtYDWDSLSGGQKQRITMARVFynILtmdrseQTPVVLLDES 605
Cdd:COG4167 123 EER---EERI--------FATLR-----LVGLLPEHAN--FYPHMLSSGQKQRVALARAL--IL------QPKIIIADEA 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 70886980 606 TSMMDETEQAVLLNLR-KLQVRM----ISVTHREEVITH 639
Cdd:COG4167 177 LAALDMSVRSQIINLMlELQEKLgisyIYVSQHLGIVKH 215
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
425-639 |
1.92e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 54.65 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 425 KDFTLFAFSNLKLM--TPAGQLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEG----------------- 485
Cdd:PTZ00265 378 KDIKKIQFKNVRFHydTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGdiiindshnlkdinlkw 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 486 ---------------SYSMERGIK--LLFAPQHSYMVPQ-----------------CTLIEQVLFPIVSNTLGAKELDSF 531
Cdd:PTZ00265 458 wrskigvvsqdpllfSNSIKNNIKysLYSLKDLEALSNYynedgndsqenknkrnsCRAKCAGDLNDMSNTTDSNELIEM 537
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 532 KEAIRLSGSHSVIDVLGG-FDSPYVGADPrtadDTYDW------DSLSGGQKQRITMARVFYniltmdrsEQTPVVLLDE 604
Cdd:PTZ00265 538 RKNYQTIKDSEVVDVSKKvLIHDFVSALP----DKYETlvgsnaSKLSGGQKQRISIARAII--------RNPKILILDE 605
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 70886980 605 STSMMDETE----QAVLLNLRKLQVRM-ISVTHREEVITH 639
Cdd:PTZ00265 606 ATSSLDNKSeylvQKTINNLKGNENRItIIIAHRLSTIRY 645
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
447-637 |
2.14e-07 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 53.16 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 447 NDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSME----------------RGIKLLFapQHSYMVPQCTL 510
Cdd:COG1135 22 DDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDgvdltalserelraarRKIGMIF--QHFNLLSSRTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 511 IEQVLFPIvsntlgakELDSF-KEAIRlsgsHSVIDVLggfdsPYVG----AD--PrtaddtydwDSLSGGQKQRITMAR 583
Cdd:COG1135 100 AENVALPL--------EIAGVpKAEIR----KRVAELL-----ELVGlsdkADayP---------SQLSGGQKQRVGIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 70886980 584 VfyniLTMDrseqtPVVLL-DESTSMMD-ETEQAVL-----LNlRKLQVRMISVTHREEVI 637
Cdd:COG1135 154 A----LANN-----PKVLLcDEATSALDpETTRSILdllkdIN-RELGLTIVLITHEMDVV 204
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
426-586 |
2.22e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 54.53 E-value: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 426 DFTLFaFSNLKLM-TPagqlLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGsySMERGIKLLFAPQHSYM 504
Cdd:TIGR01271 426 DDGLF-FSNFSLYvTP----VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEG--KIKHSGRISFSPQTSWI 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 505 VPQcTLIEQVLFPIVSNTLgakeldSFKEAIRLSGSHSVIDVLGGFDSPYVGADPRTaddtydwdsLSGGQKQRITMARV 584
Cdd:TIGR01271 499 MPG-TIKDNIIFGLSYDEY------RYTSVIKACQLEEDIALFPEKDKTVLGEGGIT---------LSGGQRARISLARA 562
|
..
gi 70886980 585 FY 586
Cdd:TIGR01271 563 VY 564
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
434-633 |
2.22e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 54.08 E-value: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 434 NLKLMTPAGQLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGlWRPTEGSYSMErGIKLLFAPQHSY---------- 503
Cdd:PRK11174 354 DLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLG-FLPYQGSLKIN-GIELRELDPESWrkhlswvgqn 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 504 -MVPQCTLIEQVLfpivsntLGAKELD--SFKEAIRLSGSHSVIDVLG-GFDSPyVGadPRTAddtydwdSLSGGQKQRI 579
Cdd:PRK11174 432 pQLPHGTLRDNVL-------LGNPDASdeQLQQALENAWVSEFLPLLPqGLDTP-IG--DQAA-------GLSVGQAQRL 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 70886980 580 TMARVFYNiltmdrseQTPVVLLDESTSMMD-ETEQAVL--LNLRKLQVRMISVTHR 633
Cdd:PRK11174 495 ALARALLQ--------PCQLLLLDEPTASLDaHSEQLVMqaLNAASRRQTTLMVTHQ 543
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
448-620 |
2.96e-07 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 52.48 E-value: 2.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 448 DLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEG--------------SYSMERgIKLLFAPQHSYMVPQcTLIEQ 513
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGelliddhplhfgdySYRSQR-IRMIFQDPSTSLNPR-QRISQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 514 VL-FPIVSNTlgakELDSFKEAIRlsgshsVIDVLggfdsPYVGADPRTAddTYDWDSLSGGQKQRITMARVFynILtmd 592
Cdd:PRK15112 109 ILdFPLRLNT----DLEPEQREKQ------IIETL-----RQVGLLPDHA--SYYPHMLAPGQKQRLGLARAL--IL--- 166
|
170 180
....*....|....*....|....*...
gi 70886980 593 rseQTPVVLLDESTSMMDETEQAVLLNL 620
Cdd:PRK15112 167 ---RPKVIIADEALASLDMSMRSQLINL 191
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
446-647 |
3.25e-07 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 51.76 E-value: 3.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 446 FNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSMERGIKLLFAPQHSyMVPQCTLIEQVLFPIVSNTLGA 525
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLGGG-FNPELTGRENIYLNGRLLGLSR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 526 KELDSFKEAI-RLSGshsvidvLGGF-DSPYVgadprtaddTYdwdslSGGQKQRITMArvfynILTMDRSEqtpVVLLD 603
Cdd:cd03220 117 KEIDEKIDEIiEFSE-------LGDFiDLPVK---------TY-----SSGMKARLAFA-----IATALEPD---ILLID 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 70886980 604 ESTSMMDETEQ----AVLLNLRKLQVRMISVTHREEVITHHTHALRIL 647
Cdd:cd03220 168 EVLAVGDAAFQekcqRRLRELLKQGKTVILVSHDPSSIKRLCDRALVL 215
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
426-586 |
3.69e-07 |
|
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: 52.17 E-value: 3.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 426 DFTLFaFSNLKLMtpaGQLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGsySMERGIKLLFAPQHSYMV 505
Cdd:cd03291 37 DNNLF-FSNLCLV---GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEG--KIKHSGRISFSSQFSWIM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 506 PQcTLIEQVLFPIVSNTLgakeldSFKEAIRLSGSHSVIDVLGGFDSPYVGADPRTaddtydwdsLSGGQKQRITMARVF 585
Cdd:cd03291 111 PG-TIKENIIFGVSYDEY------RYKSVVKACQLEEDITKFPEKDNTVLGEGGIT---------LSGGQRARISLARAV 174
|
.
gi 70886980 586 Y 586
Cdd:cd03291 175 Y 175
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
444-626 |
4.55e-07 |
|
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: 51.12 E-value: 4.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 444 LLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSY------SMERGIKLL-----FAPQHSYMVPQCTLIE 512
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTSgqilfnGQPRKPDQFqkcvaYVRQDDILLPGLTVRE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 513 QVLFpIVSNTLGAKELDSFKEAI--RLSGSHSVIDVLGGfdsPYVGadprtaddtydwdSLSGGQKQRITMARVFyniLT 590
Cdd:cd03234 101 TLTY-TAILRLPRKSSDAIRKKRveDVLLRDLALTRIGG---NLVK-------------GISGGERRRVSIAVQL---LW 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 70886980 591 MDRseqtpVVLLDESTSMMDE-TEQAVLLNLRKLQVR 626
Cdd:cd03234 161 DPK-----VLILDEPTSGLDSfTALNLVSTLSQLARR 192
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
446-610 |
4.71e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 53.41 E-value: 4.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 446 FNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSMERGIKllFAPQHSYmVPQCTLIEQVLFpivSNTLGA 525
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVA--YVPQQAW-IQNDSLRENILF---GKALNE 727
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 526 KELDSFKEAIRLSGShsvIDVLGGFDSPYVGADPRtaddtydwdSLSGGQKQRITMARVFYNiltmdrseQTPVVLLDES 605
Cdd:TIGR00957 728 KYYQQVLEACALLPD---LEILPSGDRTEIGEKGV---------NLSGGQKQRVSLARAVYS--------NADIYLFDDP 787
|
....*
gi 70886980 606 TSMMD 610
Cdd:TIGR00957 788 LSAVD 792
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
447-632 |
4.89e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 51.72 E-value: 4.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 447 NDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSM--ERGIKL--------------LFA-PQHSYMvpQCT 509
Cdd:PRK13640 24 NDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKitVDGITLtaktvwdirekvgiVFQnPDNQFV--GAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 510 LIEQVLFPIVSNTLGAKELdsfkeairLSGSHSVIDVLGGFDspYVGADPRtaddtydwdSLSGGQKQRITMArvfyNIL 589
Cdd:PRK13640 102 VGDDVAFGLENRAVPRPEM--------IKIVRDVLADVGMLD--YIDSEPA---------NLSGGQKQRVAIA----GIL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 70886980 590 TMdrseQTPVVLLDESTSMMDETEQAVLLNL-RKLQVR----MISVTH 632
Cdd:PRK13640 159 AV----EPKIIILDESTSMLDPAGKEQILKLiRKLKKKnnltVISITH 202
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
443-624 |
4.98e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 50.72 E-value: 4.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 443 QLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSMER-GIK---------LLFAPQHSYMVPQCTLIE 512
Cdd:PRK13540 14 QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERqSIKkdlctyqkqLCFVGHRSGINPYLTLRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 513 QVLFPIVSNTlGAKELDsfkEAIRLSGSHSVIDVLGGFdspyvgadprtaddtydwdsLSGGQKQRITMARvfyniLTMD 592
Cdd:PRK13540 94 NCLYDIHFSP-GAVGIT---ELCRLFSLEHLIDYPCGL--------------------LSSGQKRQVALLR-----LWMS 144
|
170 180 190
....*....|....*....|....*....|..
gi 70886980 593 RSEqtpVVLLDESTSMMDetEQAVLLNLRKLQ 624
Cdd:PRK13540 145 KAK---LWLLDEPLVALD--ELSLLTIITKIQ 171
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
458-632 |
5.20e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 51.63 E-value: 5.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 458 DWV-ILGENGCGKTSLLRMISGLWRPTEG-------------SYSMERGIKLLFA-PQHSYMvpQCTLIEQVLFPIVSNT 522
Cdd:PRK13642 34 EWVsIIGQNGSGKSTTARLIDGLFEEFEGkvkidgelltaenVWNLRRKIGMVFQnPDNQFV--GATVEDDVAFGMENQG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 523 LGAKELDSfkeaiRLSGSHSVIDVLggfdspyvgaDPRTADDTydwdSLSGGQKQRITMARVFyniltmdrSEQTPVVLL 602
Cdd:PRK13642 112 IPREEMIK-----RVDEALLAVNML----------DFKTREPA----RLSGGQKQRVAVAGII--------ALRPEIIIL 164
|
170 180 190
....*....|....*....|....*....|....*
gi 70886980 603 DESTSMMDETEQAVLLNL-----RKLQVRMISVTH 632
Cdd:PRK13642 165 DESTSMLDPTGRQEIMRViheikEKYQLTVLSITH 199
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
442-650 |
5.26e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 51.75 E-value: 5.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 442 GQLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISG-LWRPTEGSYSMERG-IKLLFAPQHSYMVPQCTLIEQVL---- 515
Cdd:PRK13547 13 HRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGGAPRGARVTGdVTLNGEPLAAIDAPRLARLRAVLpqaa 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 516 ---FPIVSNTLGAkeLDSFKEAIRlSGSHSVIDvlGGFDS---PYVGADPRTADDTydwDSLSGGQKQRITMARVFYNIL 589
Cdd:PRK13547 93 qpaFAFSAREIVL--LGRYPHARR-AGALTHRD--GEIAWqalALAGATALVGRDV---TTLSGGELARVQFARVLAQLW 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 70886980 590 TMDRSEQTP-VVLLDESTSMMDETEQAVLLNL-----RKLQVRMISVTHREEVITHHTHALRILPGG 650
Cdd:PRK13547 165 PPHDAAQPPrYLLLDEPTAALDLAHQHRLLDTvrrlaRDWNLGVLAIVHDPNLAARHADRIAMLADG 231
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
447-632 |
5.27e-07 |
|
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: 52.88 E-value: 5.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 447 NDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYS---------------MERGikllFAPQHSYMVPQctli 511
Cdd:TIGR03269 301 DNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdewvdmtkpgpDGRG----RAKRYIGILHQ---- 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 512 EQVLFP---IVSNTLGAKELDSFKEAIRLSGSHSVIDVlgGFDSPYVgadpRTADDTYDwDSLSGGQKQRITMARVFYni 588
Cdd:TIGR03269 373 EYDLYPhrtVLDNLTEAIGLELPDELARMKAVITLKMV--GFDEEKA----EEILDKYP-DELSEGERHRVALAQVLI-- 443
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 70886980 589 ltmdrsEQTPVVLLDESTSMMDE-TEQAV---LLNLRK-LQVRMISVTH 632
Cdd:TIGR03269 444 ------KEPRIVILDEPTGTMDPiTKVDVthsILKAREeMEQTFIIVSH 486
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
440-632 |
5.38e-07 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 52.15 E-value: 5.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 440 PAGQLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSM-----------ERGIKLLFapQHSYMVPQC 508
Cdd:PRK11650 14 DGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIggrvvnelepaDRDIAMVF--QNYALYPHM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 509 TLIEQVLFPIVSNTLGAKELDS-FKEAIRLSGshsvidvLGgfdsPYVGADPRtaddtydwdSLSGGQKQRITMARVfyn 587
Cdd:PRK11650 92 SVRENMAYGLKIRGMPKAEIEErVAEAARILE-------LE----PLLDRKPR---------ELSGGQRQRVAMGRA--- 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 70886980 588 iltMDRSEQtpVVLLDESTSMMDeteqAVL-----LNLRKLQVRM----ISVTH 632
Cdd:PRK11650 149 ---IVREPA--VFLFDEPLSNLD----AKLrvqmrLEIQRLHRRLkttsLYVTH 193
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
447-630 |
8.67e-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: 50.51 E-value: 8.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 447 NDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSMErGIKLLFAPQH-------SYmVPQctliEQVLFPiv 519
Cdd:cd03224 17 FGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFD-GRDITGLPPHeraragiGY-VPE----GRRIFP-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 520 sntlgakeldsfkeairlsgSHSVID--VLGGFDSPyvgadPRTADDTYDW----------------DSLSGGQKQRITM 581
Cdd:cd03224 89 --------------------ELTVEEnlLLGAYARR-----RAKRKARLERvyelfprlkerrkqlaGTLSGGEQQMLAI 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 70886980 582 ARVfyniLTMDRSeqtpVVLLDEST-----SMMDETEQAvLLNLRKLQVRMISV 630
Cdd:cd03224 144 ARA----LMSRPK----LLLLDEPSeglapKIVEEIFEA-IRELRDEGVTILLV 188
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
444-615 |
9.28e-07 |
|
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: 51.86 E-value: 9.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 444 LLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSMERGIKLLFAPQ-HSYMVPQCTLIEQVlfpivsnt 522
Cdd:TIGR03719 336 LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQsRDALDPNKTVWEEI-------- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 523 lgakeldsfkeairlSGSHSVIDVlGGFDSP---YVGA-DPRTADDTYDWDSLSGGQKQRITMARVFyniltmdrSEQTP 598
Cdd:TIGR03719 408 ---------------SGGLDIIKL-GKREIPsraYVGRfNFKGSDQQKKVGQLSGGERNRVHLAKTL--------KSGGN 463
|
170
....*....|....*...
gi 70886980 599 VVLLDESTSMMD-ETEQA 615
Cdd:TIGR03719 464 VLLLDEPTNDLDvETLRA 481
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
425-637 |
1.13e-06 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 50.13 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 425 KDFTLFAFSNLKLmtPAgqllFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGS---YSMERGIKLLFAP-- 499
Cdd:COG4778 12 KTFTLHLQGGKRL--PV----LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSilvRHDGGWVDLAQASpr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 500 --------------QHSYMVPQCTLIEQVLFPIVSntLGAKELDSFKEAIRLsgshsvidvLGGFDSPyvgadPRTaddt 565
Cdd:COG4778 86 eilalrrrtigyvsQFLRVIPRVSALDVVAEPLLE--RGVDREEARARAREL---------LARLNLP-----ERL---- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 566 ydWDS----LSGGQKQRITMARVFynILtmdrseQTPVVLLDESTSMMDETEQAVLLNL-RKLQVR---MISVTHREEVI 637
Cdd:COG4778 146 --WDLppatFSGGEQQRVNIARGF--IA------DPPLLLLDEPTASLDAANRAVVVELiEEAKARgtaIIGIFHDEEVR 215
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
447-632 |
1.18e-06 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 50.50 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 447 NDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSMERGIKLLFAPQHSYMVPQCTLIEQVLFPIVSNTLGAK 526
Cdd:PRK09544 21 SDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDTTLPLTVNRFLRLRPGTKKED 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 527 ELDSFKeaiRLSGSHSVidvlggfDSPYvgadprtaddtydwDSLSGGQKQRITMARVFYNiltmdrseQTPVVLLDEST 606
Cdd:PRK09544 101 ILPALK---RVQAGHLI-------DAPM--------------QKLSGGETQRVLLARALLN--------RPQLLVLDEPT 148
|
170 180 190
....*....|....*....|....*....|.
gi 70886980 607 SMMDETEQAVLLNL-----RKLQVRMISVTH 632
Cdd:PRK09544 149 QGVDVNGQVALYDLidqlrRELDCAVLMVSH 179
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
461-620 |
1.21e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 51.12 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 461 ILGENGCGKTSLLRMISGLWRPTEGSYSMErGIKLLFAPQHSY--------MV---PQCTL-----IEQVLF-PIVSNT- 522
Cdd:PRK11308 46 VVGESGCGKSTLARLLTMIETPTGGELYYQ-GQDLLKADPEAQkllrqkiqIVfqnPYGSLnprkkVGQILEePLLINTs 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 523 LGAKEldsfkeaiRLSGSHSVIDVlggfdspyVGADPRTADdTYDwDSLSGGQKQRITMARVFynILTMDrseqtpVVLL 602
Cdd:PRK11308 125 LSAAE--------RREKALAMMAK--------VGLRPEHYD-RYP-HMFSGGQRQRIAIARAL--MLDPD------VVVA 178
|
170
....*....|....*...
gi 70886980 603 DESTSMMDETEQAVLLNL 620
Cdd:PRK11308 179 DEPVSALDVSVQAQVLNL 196
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
442-485 |
1.28e-06 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 49.52 E-value: 1.28e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 70886980 442 GQLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEG 485
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSG 55
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
443-610 |
1.37e-06 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 50.57 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 443 QLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSM------ERG----IKLLFAPQHSYMVPQCTLIE 512
Cdd:PRK13537 20 KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLcgepvpSRArharQRVGVVPQFDNLDPDFTVRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 513 QVL-----FPIVSNTLGAKeLDSFKEAIRLSGShsvidvlggfdspyvgADPRTADdtydwdsLSGGQKQRITMARVFYN 587
Cdd:PRK13537 100 NLLvfgryFGLSAAAARAL-VPPLLEFAKLENK----------------ADAKVGE-------LSGGMKRRLTLARALVN 155
|
170 180
....*....|....*....|...
gi 70886980 588 iltmdrseQTPVVLLDESTSMMD 610
Cdd:PRK13537 156 --------DPDVLVLDEPTTGLD 170
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
448-636 |
1.66e-06 |
|
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: 49.29 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 448 DLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSME------------RGIKLLFAPQHSYmvPQCTLIEQVL 515
Cdd:cd03266 23 GVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDgfdvvkepaearRRLGFVSDSTGLY--DRLTARENLE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 516 FpivSNTLGAKELDSFKEAIRlsgshSVIDVLGGFDSpyvgADPRTADdtydwdsLSGGQKQRITMARVfyniLTMDrse 595
Cdd:cd03266 101 Y---FAGLYGLKGDELTARLE-----ELADRLGMEEL----LDRRVGG-------FSTGMRQKVAIARA----LVHD--- 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 70886980 596 qTPVVLLDESTSMMDETEQAVLLN----LRKLQVRMISVTHR-EEV 636
Cdd:cd03266 155 -PPVLLLDEPTTGLDVMATRALREfirqLRALGKCILFSTHImQEV 199
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
447-637 |
1.81e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 50.09 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 447 NDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGS--------------YSMERGIKLLFAPQHSYMVpqCTLIE 512
Cdd:PRK13633 27 DDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKvyvdgldtsdeenlWDIRNKAGMVFQNPDNQIV--ATIVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 513 Q-VLFpivsntlGAKELDSFKEAIRLSGSHSVIDVlGGFDspYVGADPRTaddtydwdsLSGGQKQRITMArvfyNILTM 591
Cdd:PRK13633 105 EdVAF-------GPENLGIPPEEIRERVDESLKKV-GMYE--YRRHAPHL---------LSGGQKQRVAIA----GILAM 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 70886980 592 drseQTPVVLLDESTSMMDETEQAVLLNL-----RKLQVRMISVTH-REEVI 637
Cdd:PRK13633 162 ----RPECIIFDEPTAMLDPSGRREVVNTikelnKKYGITIILITHyMEEAV 209
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
447-647 |
2.05e-06 |
|
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: 50.97 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 447 NDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSMErGIKLLFAPQHSY-----MVPQCTlieqVLFpivSN 521
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILID-GQDIRDVTQASLraaigIVPQDT----VLF---ND 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 522 TL---------GAKElDSFKEAIRLSGSHSVIDVL-GGFDSPyVGAdpRTAddtydwdSLSGGQKQRITMARVfynILtm 591
Cdd:COG5265 447 TIayniaygrpDASE-EEVEAAARAAQIHDFIESLpDGYDTR-VGE--RGL-------KLSGGEKQRVAIART---LL-- 510
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 70886980 592 drsEQTPVVLLDESTSMMD-ETEQAVLLNLRKLQVR--MISVTHREEVIthhTHALRIL 647
Cdd:COG5265 511 ---KNPPILIFDEATSALDsRTERAIQAALREVARGrtTLVIAHRLSTI---VDADEIL 563
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
447-635 |
2.45e-06 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 50.08 E-value: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 447 NDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSM-----------ERGIKLLFapQHSYMVPQCTLIEQVL 515
Cdd:PRK10851 19 NDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFhgtdvsrlharDRKVGFVF--QHYALFRHMTVFDNIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 516 FPIvsNTLGAKELDSfKEAIRlsgsHSVIDVLGGFDSPYVgADPRTAddtydwdSLSGGQKQRITMARVFyniltmdrSE 595
Cdd:PRK10851 97 FGL--TVLPRRERPN-AAAIK----AKVTQLLEMVQLAHL-ADRYPA-------QLSGGQKQRVALARAL--------AV 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 70886980 596 QTPVVLLDESTSMMDETEQAVLLN-LRKL--QVRMIS--VTHREE 635
Cdd:PRK10851 154 EPQILLLDEPFGALDAQVRKELRRwLRQLheELKFTSvfVTHDQE 198
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
442-650 |
2.54e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 50.66 E-value: 2.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 442 GQLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSMERGIKLLFAPQ-HSYMVPQctliEQVLFPIVS 520
Cdd:PRK15064 331 NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQdHAYDFEN----DLTLFDWMS 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 521 NTLGAKELDsfkEAIRlsgshsviDVLGgfdspyvgadpR---TADDT-YDWDSLSGGQKQRITMARvfyniLTMDRseq 596
Cdd:PRK15064 407 QWRQEGDDE---QAVR--------GTLG-----------RllfSQDDIkKSVKVLSGGEKGRMLFGK-----LMMQK--- 456
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 70886980 597 TPVVLLDESTSMMD-ETEQAVLLNLRKLQVRMISVTH-REEVITHHTHALRILPGG 650
Cdd:PRK15064 457 PNVLVMDEPTNHMDmESIESLNMALEKYEGTLIFVSHdREFVSSLATRIIEITPDG 512
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
435-635 |
2.70e-06 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 50.78 E-value: 2.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 435 LKLMTPAGQLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSY-----SMERGI-----KLLFAPQHSYM 504
Cdd:TIGR01257 935 VKIFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVlvggkDIETNLdavrqSLGMCPQHNIL 1014
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 505 VPQCTLIEQVLFpivSNTLGAKeldSFKEAiRLSGSHSVIDvlggfdspyVGADPRTADDTYDwdsLSGGQKQRITMARV 584
Cdd:TIGR01257 1015 FHHLTVAEHILF---YAQLKGR---SWEEA-QLEMEAMLED---------TGLHHKRNEEAQD---LSGGMQRKLSVAIA 1075
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 70886980 585 FYNiltmdrseQTPVVLLDESTSMMDETEQA----VLLNLRKLQVRMISVTHREE 635
Cdd:TIGR01257 1076 FVG--------DAKVVVLDEPTSGVDPYSRRsiwdLLLKYRSGRTIIMSTHHMDE 1122
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
433-610 |
3.49e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 50.51 E-value: 3.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 433 SNLKLMTPAGQLLfndldleiksdqdwVILGENGCGKTSLLRMISGLWRPTEGSYSMERGiKLLFAPQHSYMVpQCTLIE 512
Cdd:PLN03130 634 SNINLDVPVGSLV--------------AIVGSTGEGKTSLISAMLGELPPRSDASVVIRG-TVAYVPQVSWIF-NATVRD 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 513 QVLFpivsntlGAK-ELDSFKEAIRLSGSHSVIDVLGGFDSPYVGAdpRTADdtydwdsLSGGQKQRITMARVFYNiltm 591
Cdd:PLN03130 698 NILF-------GSPfDPERYERAIDVTALQHDLDLLPGGDLTEIGE--RGVN-------ISGGQKQRVSMARAVYS---- 757
|
170
....*....|....*....
gi 70886980 592 drseQTPVVLLDESTSMMD 610
Cdd:PLN03130 758 ----NSDVYIFDDPLSALD 772
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
452-617 |
3.51e-06 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 48.94 E-value: 3.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 452 EIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSMERgIKLLFAPQhsYMVP-QCTLIEQVLFPIVSNTLgakELDS 530
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIEL-DTVSYKPQ--YIKAdYEGTVRDLLSSITKDFY---THPY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 531 FKEAIrlsgshsvidvlggfdspyvgADPRTADDTYDWD--SLSGGQKQRITMArvfyniLTMdrSEQTPVVLLDESTSM 608
Cdd:cd03237 95 FKTEI---------------------AKPLQIEQILDREvpELSGGELQRVAIA------ACL--SKDADIYLLDEPSAY 145
|
....*....
gi 70886980 609 MDeTEQAVL 617
Cdd:cd03237 146 LD-VEQRLM 153
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
441-636 |
4.05e-06 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 48.47 E-value: 4.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 441 AGQLLFnDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSM------------ERGIKLLfaPQHSYMV--- 505
Cdd:PRK11124 14 AHQALF-DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIagnhfdfsktpsDKAIREL--RRNVGMVfqq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 506 ----PQCTLIEQVL-FPIvsNTLGAKELDSFKEAIRLsgshsvIDVLggfdspyvgadpRTADDTYDWD-SLSGGQKQRI 579
Cdd:PRK11124 91 ynlwPHLTVQQNLIeAPC--RVLGLSKDQALARAEKL------LERL------------RLKPYADRFPlHLSGGQQQRV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 70886980 580 TMARVfyniLTMdrseQTPVVLLDESTSMMDE--TEQAVLLnLRKLQVRMIS---VTHREEV 636
Cdd:PRK11124 151 AIARA----LMM----EPQVLLFDEPTAALDPeiTAQIVSI-IRELAETGITqviVTHEVEV 203
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
447-630 |
4.14e-06 |
|
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: 48.59 E-value: 4.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 447 NDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSME--------------RGIKLLFapQHSYMVPQCTLIE 512
Cdd:cd03219 17 DDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDgeditglppheiarLGIGRTF--QIPRLFPELTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 513 QVL----FPIVSNTLGAKELDSFKEAIRLsgSHSVIDvlggfdspYVGADPRtADDTYdwDSLSGGQKQRITMARVfyni 588
Cdd:cd03219 95 NVMvaaqARTGSGLLLARARREEREARER--AEELLE--------RVGLADL-ADRPA--GELSYGQQRRLEIARA---- 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 70886980 589 LTMDrseqtP-VVLLDESTSMMDETEQAVLLNL-RKLQVRMISV 630
Cdd:cd03219 158 LATD-----PkLLLLDEPAAGLNPEETEELAELiRELRERGITV 196
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
443-638 |
4.15e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 48.88 E-value: 4.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 443 QLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLwRPTEGSYSMERGIKLLFAPQHSYMVPQCTLIEQV--LFPiVS 520
Cdd:PRK14258 20 QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRM-NELESEVRVEGRVEFFNQNIYERRVNLNRLRRQVsmVHP-KP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 521 NTLGAKELDSFKEAIRLSGSHSVIDVLGGFDSPYVGADPrtaddtydWDS-----------LSGGQKQRITMARVFY--- 586
Cdd:PRK14258 98 NLFPMSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADL--------WDEikhkihksaldLSGGQQQRLCIARALAvkp 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 70886980 587 NILTMDRseqtPVVLLDESTSMMDETeqaVLLNLR-KLQVRMISVTHREEVIT 638
Cdd:PRK14258 170 KVLLMDE----PCFGLDPIASMKVES---LIQSLRlRSELTMVIVSHNLHQVS 215
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
461-636 |
5.33e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 49.25 E-value: 5.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 461 ILGENGCGKTSLLRMISGLWRPTEGsySME-RGIKLLFA-PQHSY-----MVPQ-CTLIEQvlFPIVSN-TLGAKELDSF 531
Cdd:COG3845 36 LLGENGAGKSTLMKILYGLYQPDSG--EILiDGKPVRIRsPRDAIalgigMVHQhFMLVPN--LTVAENiVLGLEPTKGG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 532 KeaIRLSGSHSVIDVLG---GFDspyvgADPrtadDTYDWDsLSGGQKQRITMARVFYNiltmdrseQTPVVLLDESTSM 608
Cdd:COG3845 112 R--LDRKAARARIRELSeryGLD-----VDP----DAKVED-LSVGEQQRVEILKALYR--------GARILILDEPTAV 171
|
170 180 190
....*....|....*....|....*....|...
gi 70886980 609 M--DETEQ--AVLLNLRKLQVRMISVTHR-EEV 636
Cdd:COG3845 172 LtpQEADElfEILRRLAAEGKSIIFITHKlREV 204
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
432-639 |
6.48e-06 |
|
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: 47.87 E-value: 6.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 432 FSNLKLM-TPAGQLLFNDLDLEIKSDQDWVILGENGCGKTS----LLRMISglwrPTEGSYSMErGIKLLFAPQHSY--- 503
Cdd:cd03244 5 FKNVSLRyRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLVE----LSSGSILID-GVDISKIGLHDLrsr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 504 --MVPQctliEQVLFpivSNTLgAKELDSFKE--------AIRLSGSHSVIDVLGGfdspyvGADPRTADDTydwDSLSG 573
Cdd:cd03244 80 isIIPQ----DPVLF---SGTI-RSNLDPFGEysdeelwqALERVGLKEFVESLPG------GLDTVVEEGG---ENLSV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 70886980 574 GQKQRITMARVfynILTmdrseQTPVVLLDESTSMMD-ETEQAVLLNLRKL--QVRMISVTHREEVITH 639
Cdd:cd03244 143 GQRQLLCLARA---LLR-----KSKILVLDEATASVDpETDALIQKTIREAfkDCTVLTIAHRLDTIID 203
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
441-651 |
6.92e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 48.19 E-value: 6.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 441 AGQLLFnDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEG----------SYSMERGIKllfaPQHS-----YMV 505
Cdd:PRK13643 18 ASRALF-DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGkvtvgdivvsSTSKQKEIK----PVRKkvgvvFQF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 506 PQCTLIEQVLFPIVSntLGAKELDSFKEAIRLSGSHSVIDVlgGFDSPYVGADPRtaddtydwdSLSGGQKQRITMArvf 585
Cdd:PRK13643 93 PESQLFEETVLKDVA--FGPQNFGIPKEKAEKIAAEKLEMV--GLADEFWEKSPF---------ELSGGQMRRVAIA--- 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 586 yNILTMdrseQTPVVLLDESTSMMDETEQAVLLNL----RKLQVRMISVTHREEVITHHTHALRILPGGN 651
Cdd:PRK13643 157 -GILAM----EPEVLVLDEPTAGLDPKARIEMMQLfesiHQSGQTVVLVTHLMDDVADYADYVYLLEKGH 221
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
439-640 |
8.44e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 48.08 E-value: 8.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 439 TPAGQLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLW-----RPTEGSYSMERGIK-------------LLFA-P 499
Cdd:PRK13645 20 TPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIisetgQTIVGDYAIPANLKkikevkrlrkeigLVFQfP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 500 QhsYMVPQCTLIEQVLF-PIvsnTLGAKELDSFKEAIRLsgshsvIDVLGgFDSPYVGADPRtaddtydwdSLSGGQKQR 578
Cdd:PRK13645 100 E--YQLFQETIEKDIAFgPV---NLGENKQEAYKKVPEL------LKLVQ-LPEDYVKRSPF---------ELSGGQKRR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 70886980 579 ITMArvfyNILTMDRSeqtpVVLLDESTSMMDETEQAVLLNL-----RKLQVRMISVTHR--------EEVITHH 640
Cdd:PRK13645 159 VALA----GIIAMDGN----TLVLDEPTGGLDPKGEEDFINLferlnKEYKKRIIMVTHNmdqvlriaDEVIVMH 225
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
555-647 |
1.32e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 48.16 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 555 VGADPRTaddTYDWDS-LSGGQKQRITMARVFynILtmdrseQTPVVLLDESTSMMDETEQAVLLN-LRKLQVRmisvtH 632
Cdd:PRK15134 412 VGLDPET---RHRYPAeFSGGQRQRIAIARAL--IL------KPSLIILDEPTSSLDKTVQAQILAlLKSLQQK-----H 475
|
90
....*....|....*..
gi 70886980 633 REE--VITHHTHALRIL 647
Cdd:PRK15134 476 QLAylFISHDLHVVRAL 492
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
570-624 |
1.46e-05 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 48.09 E-value: 1.46e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 70886980 570 SLSGGQKQRITMARVfyniLTMDrseqTPVVLLDESTSMMD-ETEQAVLLNLRKLQ 624
Cdd:PRK11176 480 LLSGGQRQRIAIARA----LLRD----SPILILDEATSALDtESERAIQAALDELQ 527
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
447-632 |
1.81e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 47.03 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 447 NDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGS-------------YSMERGIKLLFA-PQHSYMvpQCTLIE 512
Cdd:PRK13650 24 NDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQiiidgdllteenvWDIRHKIGMVFQnPDNQFV--GATVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 513 QVLFPIVSNTLGAKELDS-FKEAIRLSGShsvidvlggfdSPYVGADPRtaddtydwdSLSGGQKQRITMArvfyNILTM 591
Cdd:PRK13650 102 DVAFGLENKGIPHEEMKErVNEALELVGM-----------QDFKEREPA---------RLSGGQKQRVAIA----GAVAM 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 70886980 592 DRSeqtpVVLLDESTSMMD-ETEQAVLLNLRKL----QVRMISVTH 632
Cdd:PRK13650 158 RPK----IIILDEATSMLDpEGRLELIKTIKGIrddyQMTVISITH 199
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
450-632 |
2.28e-05 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 46.29 E-value: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 450 DLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSM-----------ERGIKLLFapqhsymvpQctliEQVLFP- 517
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWngqdltalppaERPVSMLF---------Q----ENNLFPh 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 518 --IVSN---------TLGAKELDSFKEAIRLSGshsvidvLGGFDSPYVGAdprtaddtydwdsLSGGQKQRITMARVfy 586
Cdd:COG3840 86 ltVAQNiglglrpglKLTAEQRAQVEQALERVG-------LAGLLDRLPGQ-------------LSGGQRQRVALARC-- 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 70886980 587 niLTMDRseqtPVVLLDESTSMMDETEQAVLLNL-----RKLQVRMISVTH 632
Cdd:COG3840 144 --LVRKR----PILLLDEPFSALDPALRQEMLDLvdelcRERGLTVLMVTH 188
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
461-645 |
2.64e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.47 E-value: 2.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 461 ILGENGCGKTSLLRMISGLWRPTEGSYSMERGIKLLFAPQHsymvpqctlieQVLFpivsntLGAKElDSFKEAIRLS-- 538
Cdd:PRK10636 343 LLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQH-----------QLEF------LRADE-SPLQHLARLApq 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 539 -GSHSVIDVLGGFDspYVGadPRTADDTydwDSLSGGQKQRITMARVFYniltmdrseQTP-VVLLDESTSMMDeteqav 616
Cdd:PRK10636 405 eLEQKLRDYLGGFG--FQG--DKVTEET---RRFSGGEKARLVLALIVW---------QRPnLLLLDEPTNHLD------ 462
|
170 180 190
....*....|....*....|....*....|
gi 70886980 617 lLNLRK-LQVRMISVTHREEVITHHTHALR 645
Cdd:PRK10636 463 -LDMRQaLTEALIDFEGALVVVSHDRHLLR 491
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
450-648 |
2.84e-05 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 45.73 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 450 DLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSME-----------RGIKLLFapQHSYMVPQCTLIEQV---L 515
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNgqdhtttppsrRPVSMLF--QENNLFSHLTVAQNIglgL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 516 FPivSNTLGAKELDSFKEAIRLSGSHSVIDVLGGfdspyvgadprtaddtydwdSLSGGQKQRITMARVFYniltmdrsE 595
Cdd:PRK10771 97 NP--GLKLNAAQREKLHAIARQMGIEDLLARLPG--------------------QLSGGQRQRVALARCLV--------R 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 70886980 596 QTPVVLLDESTSMMDETEQAVLLNL-----RKLQVRMISVTHREEvithhtHALRILP 648
Cdd:PRK10771 147 EQPILLLDEPFSALDPALRQEMLTLvsqvcQERQLTLLMVSHSLE------DAARIAP 198
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
446-497 |
3.79e-05 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 45.76 E-value: 3.79e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 70886980 446 FNDLDLEIKSDQDW-VILGENGCGKTSLLRMISGLWRPTEGSYSMERGIKLLF 497
Cdd:COG3950 14 FEDLEIDFDNPPRLtVLVGENGSGKTTLLEAIALALSGLLSRLDDVKFRKLLI 66
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
445-660 |
5.44e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 44.84 E-value: 5.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 445 LFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEG-----SYSMERGIKLLFAPQHSYMvpqctlieqvlfPIV 519
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGqiqidGKTATRGDRSRFMAYLGHL------------PGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 520 SNTLGAKELDSF------KEAIRLSGSHSVIDVLGGFDSPYVgadprtaddtydwDSLSGGQKQRITMARVFYNiltmdr 593
Cdd:PRK13543 94 KADLSTLENLHFlcglhgRRAKQMPGSALAIVGLAGYEDTLV-------------RQLSAGQKKRLALARLWLS------ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 70886980 594 seQTPVVLLDESTSMMDeTEQAVLLNlrklqvRMISVTHREE----VITHhthalrilpgGNWTATPVTTR 660
Cdd:PRK13543 155 --PAPLWLLDEPYANLD-LEGITLVN------RMISAHLRGGgaalVTTH----------GAYAAPPVRTR 206
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
440-647 |
7.37e-05 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 44.66 E-value: 7.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 440 PAGQLLFNDLDLEIKSDqDWVIL-GENGCGKTSLLRMISGLWRPTEGSYSME----------------RGI-------KL 495
Cdd:COG2884 12 PGGREALSDVSLEIEKG-EFVFLtGPSGAGKSTLLKLLYGEERPTSGQVLVNgqdlsrlkrreipylrRRIgvvfqdfRL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 496 LfapqhsymvPQCTLIEQVLFP-IVsntLGAKeldsfKEAIRlsgsHSVIDVLGgfdspYVG------ADPRTaddtydw 568
Cdd:COG2884 91 L---------PDRTVYENVALPlRV---TGKS-----RKEIR----RRVREVLD-----LVGlsdkakALPHE------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 569 dsLSGGQKQRITMARVFYNiltmdrseqTPVVL--------LDESTSM--MDeteqaVLLNLRKLQVRMISVTHREEVIT 638
Cdd:COG2884 138 --LSGGEQQRVAIARALVN---------RPELLladeptgnLDPETSWeiME-----LLEEINRRGTTVLIATHDLELVD 201
|
....*....
gi 70886980 639 HHTHalRIL 647
Cdd:COG2884 202 RMPK--RVL 208
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
570-632 |
1.07e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 44.38 E-value: 1.07e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 70886980 570 SLSGGQKQRITMARVFyniltmdrSEQTPVVLLDESTSMMDETE----QAVLLNLRKlQVRMISVTH 632
Cdd:PRK14239 148 GLSGGQQQRVCIARVL--------ATSPKIILLDEPTSALDPISagkiEETLLGLKD-DYTMLLVTR 205
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
448-486 |
1.11e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 45.16 E-value: 1.11e-04
10 20 30
....*....|....*....|....*....|....*....
gi 70886980 448 DLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGS 486
Cdd:PRK09700 23 SVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGT 61
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
569-638 |
1.54e-04 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 44.71 E-value: 1.54e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 70886980 569 DSLSGGQKQRITMARVFYniltmdrseQTPVVL-LDESTSMMDE-TEQAVLLNLRKL--QVRMISVTHREEVIT 638
Cdd:PRK10790 475 NNLSVGQKQLLALARVLV---------QTPQILiLDEATANIDSgTEQAIQQALAAVreHTTLVVIAHRLSTIV 539
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
571-626 |
1.85e-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: 1.85e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 70886980 571 LSGGQKQRITMARVfyniLTMDrseqtP-VVLLDESTSMMDETEQAVLLNL-RKLQVR 626
Cdd:COG4172 426 FSGGQRQRIAIARA----LILE-----PkLLVLDEPTSALDVSVQAQILDLlRDLQRE 474
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
447-485 |
1.91e-04 |
|
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: 43.04 E-value: 1.91e-04
10 20 30
....*....|....*....|....*....|....*....
gi 70886980 447 NDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEG 485
Cdd:cd03269 17 DDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSG 55
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
569-648 |
2.40e-04 |
|
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: 41.96 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 569 DSLSGGQKQRITMArvfyNILTMDRSEQTPVVLLDESTSMMDETEQAVLLN----LRKLQVRMISVTHREEVITHHTHAL 644
Cdd:cd03227 76 LQLSGGEKELSALA----LILALASLKPRPLYILDEIDRGLDPRDGQALAEaileHLVKGAQVIVITHLPELAELADKLI 151
|
....
gi 70886980 645 RILP 648
Cdd:cd03227 152 HIKK 155
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
429-636 |
2.54e-04 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 44.33 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 429 LFAFSNLKLMTPAGQ---LLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSME-RGIKLL-------- 496
Cdd:PRK10535 4 LLELKDIRRSYPSGEeqvEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAgQDVATLdadalaql 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 497 ------FAPQHSYMVPQCTLIEQVLFPIVSNTLGAKEldsfkeaiRLSGSHSVIDVLGGFDSPYvgadprtaddtYDWDS 570
Cdd:PRK10535 84 rrehfgFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQ--------RLLRAQELLQRLGLEDRVE-----------YQPSQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 571 LSGGQKQRITMARVFYNiltmdrseQTPVVLLDESTSMMD----ETEQAVLLNLRKLQVRMISVTHREEV 636
Cdd:PRK10535 145 LSGGQQQRVSIARALMN--------GGQVILADEPTGALDshsgEEVMAILHQLRDRGHTVIIVTHDPQV 206
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
461-632 |
3.33e-04 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 42.99 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 461 ILGENGCGKTSLLRMISGLWRPTEGS--YSMERGI------------KLL------FAPQHSymvpqctliEQVLFPIVS 520
Cdd:PRK11701 37 IVGESGSGKTTLLNALSARLAPDAGEvhYRMRDGQlrdlyalseaerRRLlrtewgFVHQHP---------RDGLRMQVS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 521 ---N------TLGAKELdsfkEAIRLSGSHSVIDVlgGFDSPYVGADPRTaddtydwdsLSGGQKQRITMARvfyNILTM 591
Cdd:PRK11701 108 aggNigerlmAVGARHY----GDIRATAGDWLERV--EIDAARIDDLPTT---------FSGGMQQRLQIAR---NLVTH 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 70886980 592 DRseqtpVVLLDESTSMMDETEQAVLLNL-----RKLQVRMISVTH 632
Cdd:PRK11701 170 PR-----LVFMDEPTGGLDVSVQARLLDLlrglvRELGLAVVIVTH 210
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
447-486 |
3.94e-04 |
|
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: 42.36 E-value: 3.94e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 70886980 447 NDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGS 486
Cdd:cd03265 17 RGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGR 56
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
448-486 |
4.21e-04 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 42.32 E-value: 4.21e-04
10 20 30
....*....|....*....|....*....|....*....
gi 70886980 448 DLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGS 486
Cdd:cd03267 39 GISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGE 77
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
428-486 |
4.45e-04 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 42.67 E-value: 4.45e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 70886980 428 TLFAFSNLKlMTPAGQLLFNDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGS 486
Cdd:PRK11300 4 PLLSVSGLM-MRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGT 61
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
447-486 |
4.63e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 42.79 E-value: 4.63e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 70886980 447 NDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGS 486
Cdd:COG4152 18 DDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGE 57
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
439-632 |
6.38e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 42.04 E-value: 6.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 439 TP-AGQLLFnDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEG----------SYSMERGIK-------LLFAPQ 500
Cdd:PRK13649 16 TPfEGRALF-DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGsvrvddtlitSTSKNKDIKqirkkvgLVFQFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 501 HSYMVPQcTLIEQVLFPIVSNTLGAKELDSF-KEAIRLSG-SHSVIDvlggfDSPYvgadprtaddtydwdSLSGGQKQR 578
Cdd:PRK13649 95 ESQLFEE-TVLKDVAFGPQNFGVSQEEAEALaREKLALVGiSESLFE-----KNPF---------------ELSGGQMRR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 70886980 579 ITMArvfyNILTMdrseQTPVVLLDESTSMMDETEQAVLL----NLRKLQVRMISVTH 632
Cdd:PRK13649 154 VAIA----GILAM----EPKILVLDEPTAGLDPKGRKELMtlfkKLHQSGMTIVLVTH 203
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
461-485 |
6.94e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 41.40 E-value: 6.94e-04
10 20
....*....|....*....|....*
gi 70886980 461 ILGENGCGKTSLLRMISGLWRPTEG 485
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMQPSSG 55
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
449-486 |
8.23e-04 |
|
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: 42.48 E-value: 8.23e-04
10 20 30
....*....|....*....|....*....|....*...
gi 70886980 449 LDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGS 486
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGE 388
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
571-622 |
1.03e-03 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 42.01 E-value: 1.03e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 70886980 571 LSGGQKQRITMARVfyniLTMDrseqTPVVLLDESTSMMD-ETEQAVLLNLRK 622
Cdd:PRK10789 452 LSGGQKQRISIARA----LLLN----AEILILDDALSAVDgRTEHQILHNLRQ 496
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
448-611 |
1.24e-03 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 41.56 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 448 DLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSME---------------RGIKLLFAPQHSYMVPQCTLIE 512
Cdd:PRK10070 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDgvdiakisdaelrevRRKKIAMVFQSFALMPHMTVLD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 513 QVLFPI-VSNTLGAKELDSFKEAIRLSGSHSvidvlggfdspYVGADPrtaddtydwDSLSGGQKQRITMARVFY---NI 588
Cdd:PRK10070 126 NTAFGMeLAGINAEERREKALDALRQVGLEN-----------YAHSYP---------DELSGGMRQRVGLARALAinpDI 185
|
170 180
....*....|....*....|....*
gi 70886980 589 LTMDR--SEQTPVVlldeSTSMMDE 611
Cdd:PRK10070 186 LLMDEafSALDPLI----RTEMQDE 206
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
452-501 |
1.31e-03 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 40.25 E-value: 1.31e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 70886980 452 EIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGSYSMERgIKLLFAPQH 501
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDG-ITPVYKPQY 69
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
570-647 |
1.64e-03 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 41.49 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 570 SLSGGQKQRITMARVfynILtmdrsEQTPVVLLDESTSMMD-ETE---QAVLLNLRKLQVRMIsVTHREEVIthhTHALR 645
Cdd:PRK13657 471 QLSGGERQRLAIARA---LL-----KDPPILILDEATSALDvETEakvKAALDELMKGRTTFI-IAHRLSTV---RNADR 538
|
..
gi 70886980 646 IL 647
Cdd:PRK13657 539 IL 540
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
447-478 |
3.11e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 40.38 E-value: 3.11e-03
10 20 30
....*....|....*....|....*....|..
gi 70886980 447 NDLDLEIKSDQDWVILGENGCGKTSLLRMISG 478
Cdd:PRK10938 277 HNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG 308
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
570-633 |
3.11e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 40.78 E-value: 3.11e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 70886980 570 SLSGGQKQRITMARVFYniltmdrsEQTPVVLLDESTSMMDETEQAV----LLNLR-KLQVRMISVTHR 633
Cdd:PTZ00265 1358 SLSGGQKQRIAIARALL--------REPKILLLDEATSSLDSNSEKLiektIVDIKdKADKTIITIAHR 1418
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
461-524 |
3.72e-03 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 40.54 E-value: 3.72e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 70886980 461 ILGENGCGKTSLLRMISGLWRPTEGsySMERGIKLLFAPQhsYMVP-QCTLIEQVLFPIVSNTLG 524
Cdd:COG1245 371 IVGPNGIGKTTFAKILAGVLKPDEG--EVDEDLKISYKPQ--YISPdYDGTVEEFLRSANTDDFG 431
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
442-592 |
7.62e-03 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 39.09 E-value: 7.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 442 GQLLFnDLDLEIKSDQDWVILGENGCGKTSLLRMISGLWRPTEGS--------YSMERGIKLlfaPQHS----YmVPQct 509
Cdd:PRK11144 11 GDLCL-TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRivlngrvlFDAEKGICL---PPEKrrigY-VFQ-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70886980 510 liEQVLFP--IVSNTL--GAKELDS--FKEAIRLSGSHSVIDVLggfdspyvgadPRTaddtydwdsLSGGQKQRITMAR 583
Cdd:PRK11144 84 --DARLFPhyKVRGNLryGMAKSMVaqFDKIVALLGIEPLLDRY-----------PGS---------LSGGEKQRVAIGR 141
|
170
....*....|..
gi 70886980 584 VFY---NILTMD 592
Cdd:PRK11144 142 ALLtapELLLMD 153
|
|
| |
