|
Name |
Accession |
Description |
Interval |
E-value |
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
17-698 |
0e+00 |
|
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: 721.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 17 RRKVPQVLQTEAAECGLASLAMVCGYYGMHIDMLSMRQKFDISARGATLSSLIAIAENLNLKTRALSLSLDEIHQVKRPC 96
Cdd:COG2274 1 RRKVPFVLQMEAADCGLACLAMIARYYGRPVSLEELREALGVSRDGLSLLGLLRAARRLGLRARGVRLDLEELAELPLPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 97 ILHWDMNHFVVLVNIRGGRITLHDPAFGRRVIGLQEFSLHFTGIALEVWPSSEFTPVVQKnRLHFRKLLSNVTGLKSALV 176
Cdd:COG2274 81 ILHWDGNHFVVLEGVDGDKVTIADPATGRRKLSLEEFAESWTGVALLLEPTPEFDKRGEK-PFGLRWFLRLLRRYRRLLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 177 KIFALSLVIEAVNLLMPVGTQLVMDHVIQAGDHNLLVIICVGLLFFILFRTCVSMFRSWISIVMGALIDIQWKSGLFDHL 256
Cdd:COG2274 160 QVLLASLLINLLALATPLFTQVVIDRVLPNQDLSTLWVLAIGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 257 MKLPLAYFEKRKLGDIQSRFGSLDAIRTTFTTSIVSSIIDGIMSVGVFIMMFMYGGWLVWVASGFTVLYVLLRLSTYRYY 336
Cdd:COG2274 240 LRLPLSFFESRSVGDLASRFRDVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 337 RQASEEQLVKSAKASSHFMETLYSIATLKSLGLAGTRSQFWLNLNIDTANANIRVTKLDMFFGGVNAFLAACDQIVILWL 416
Cdd:COG2274 320 RRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 417 GASLVIDSQMTLGMFVAFNAYRGQFSDRASNLIDMVIRLRMLNLHNERLADIVLSTTEEEKPYRKICNPNEAVTFEVRDL 496
Cdd:COG2274 400 GAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPPEREEGRSKLSLPRLKGDIELENV 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 497 LYQYDSLSRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINNYRECIACVLQEDK 576
Cdd:COG2274 480 SFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVF 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 577 LLAGSIAENICSFDAHPDTEFIVECAKHCNIHDDIMKMPMGYETLVGELGGSLSGGQKQRVLIARALYRRPSILFMDEAT 656
Cdd:COG2274 560 LFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEAT 639
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 727181609 657 SHLDLDNEKRVNEAISSLK--MTRVIIAHRPSTIASADRVITLQ 698
Cdd:COG2274 640 SALDAETEAIILENLRRLLkgRTVIIIAHRLSTIRLADRIIVLD 683
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
172-465 |
8.49e-137 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 403.77 E-value: 8.49e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 172 KSALVKIFALSLVIEAVNLLMPVGTQLVMDHVIQAGDHNLLVIICVGLLFFILFRTCVSMFRSWISIVMGALIDIQWKSG 251
Cdd:cd18567 1 KRALLQILLLSLALELFALASPLYLQLVIDEVIVSGDRDLLTVLAIGFGLLLLLQALLSALRSWLVLYLSTSLNLQWTSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 252 LFDHLMKLPLAYFEKRKLGDIQSRFGSLDAIRTTFTTSIVSSIIDGIMSVGVFIMMFMYGGWLVWVASGFTVLYVLLRLS 331
Cdd:cd18567 81 LFRHLLRLPLSYFEKRHLGDIVSRFGSLDEIQQTLTTGFVEALLDGLMAILTLVMMFLYSPKLALIVLAAVALYALLRLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 332 TYRYYRQASEEQLVKSAKASSHFMETLYSIATLKSLGLAGTRSQFWLNLNIDTANANIRVTKLDMFFGGVNAFLAACDQI 411
Cdd:cd18567 161 LYPPLRRATEEQIVASAKEQSHFLETIRGIQTIKLFGREAEREARWLNLLVDAINADIRLQRLQILFSAANGLLFGLENI 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 727181609 412 VILWLGASLVIDSQMTLGMFVAFNAYRGQFSDRASNLIDMVIRLRMLNLHNERL 465
Cdd:cd18567 241 LVIYLGALLVLDGEFTVGMLFAFLAYKDQFSSRASSLIDKLFELRMLRLHLERL 294
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
19-698 |
5.74e-133 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 408.56 E-value: 5.74e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 19 KVPQVLQTEAAECGLASLAMVCGYYGMHIDMLSMRQKFDISARGATLSSLIAIAENLNLKTRALSLSLDEIHQVKRPCIL 98
Cdd:TIGR03796 1 RTPTVLQMEAVECGAASLAMILAYYGRYVPLEELREECGVSRDGSKASNLLKAARSYGLEAKGFRKELDALAELPLPYIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 99 HWDMNHFVVLVNIRGGRITLHDPAFGRRVIGLQEFSLHFTGIALEVWPSSEFTPVVQKNRLhFRKLLSNVTGLKSALVKI 178
Cdd:TIGR03796 81 FWNFNHFVVVEGFRGGRVYLNDPALGPRTVSLEEFDESFTGVVLTFEPGPEFQKGGRKPSL-LRALWRRLRGSRGALLYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 179 FALSLVIEAVNLLMPVGTQLVMDHVIQAGDHNLLVIICVGLLFFILFRTCVSMFRSwisivmGALIDIQWK------SGL 252
Cdd:TIGR03796 160 LLAGLLLVLPGLVIPAFSQIFVDEILVQGRQDWLRPLLLGMGLTALLQGVLTWLQL------YYLRRLEIKlavgmsARF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 253 FDHLMKLPLAYFEKRKLGDIQSRFGSLDAIRTTFTTSIVSSIIDGIMSVGVFIMMFMYGGWLVWVASGFTVLYVL-LRLS 331
Cdd:TIGR03796 234 LWHILRLPVRFFAQRHAGDIASRVQLNDQVAEFLSGQLATTALDAVMLVFYALLMLLYDPVLTLIGIAFAAINVLaLQLV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 332 TYRyyRQASEEQLVK-SAKASSHFMETLYSIATLKSlglAGTRSQF---WLNLNIDTANANIRVTKLDMFFGGVNAFLAA 407
Cdd:TIGR03796 314 SRR--RVDANRRLQQdAGKLTGVAISGLQSIETLKA---SGLESDFfsrWAGYQAKLLNAQQELGVLTQILGVLPTLLTS 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 408 CDQIVILWLGASLVIDSQMTLGMFVAFNAYRGQFSDRASNLIDMVIRLRMLNLHNERLADIVlstTEEEKPYRKICNPNE 487
Cdd:TIGR03796 389 LNSALILVVGGLRVMEGQLTIGMLVAFQSLMSSFLEPVNNLVGFGGTLQELEGDLNRLDDVL---RNPVDPLLEEPEGSA 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 488 AVT---------FEVRDLLYQYDSLSRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHD 558
Cdd:TIGR03796 466 ATSepprrlsgyVELRNITFGYSPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREE 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 559 IGINNYRECIACVLQEDKLLAGSIAENICSFDAHPDTEFIVECAKHCNIHDDIMKMPMGYETLVGELGGSLSGGQKQRVL 638
Cdd:TIGR03796 546 IPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPTIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLE 625
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 639 IARALYRRPSILFMDEATSHLDLDNEKRVNEAISSLKMTRVIIAHRPSTIASADRVITLQ 698
Cdd:TIGR03796 626 IARALVRNPSILILDEATSALDPETEKIIDDNLRRRGCTCIIVAHRLSTIRDCDEIIVLE 685
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
161-698 |
5.56e-121 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 373.35 E-value: 5.56e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 161 FRKLLSNVTGLKSALVKIFALSLVIEAVNLLMPVGTQLVMDHVIQAGDHNLLVIICVGLLFFILFRTCVSMFRSWISIVM 240
Cdd:COG1132 9 LRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLLARL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 241 GALI--DIQWKsgLFDHLMKLPLAYFEKRKLGDIQSRFGS-LDAIRTTFTTSIVSSIIDGIMSVGVFIMMFMYGGWLVWV 317
Cdd:COG1132 89 AQRVvaDLRRD--LFEHLLRLPLSFFDRRRTGDLLSRLTNdVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 318 ASGFTVLYVLLRLSTYRYYRQASEEQLVKSAKASSHFMETLYSIATLKSLGLAGTRSQFWLNLNIDTANANIRVTKLDMF 397
Cdd:COG1132 167 VLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSAL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 398 FGGVNAFLAACDQIVILWLGASLVIDSQMTLGMFVAFNAYRGQFSDRASNLIDMVIRLRMLNLHNERLADIVLSTTEEEK 477
Cdd:COG1132 247 FFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIPD 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 478 PYRKICNPNEAVTFEVRDLLYQYDSlSRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIH 557
Cdd:COG1132 327 PPGAVPLPPVRGEIEFENVSFSYPG-DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIR 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 558 DIGINNYRECIACVLQEDKLLAGSIAENICSFDAHPDTEFIVECAKHCNIHDDIMKMPMGYETLVGELGGSLSGGQKQRV 637
Cdd:COG1132 406 DLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRI 485
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 727181609 638 LIARALYRRPSILFMDEATSHLDLDNEKRVNEAISSL--KMTRVIIAHRPSTIASADRVITLQ 698
Cdd:COG1132 486 AIARALLKDPPILILDEATSALDTETEALIQEALERLmkGRTTIVIAHRLSTIRNADRILVLD 548
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
32-698 |
1.12e-90 |
|
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: 297.42 E-value: 1.12e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 32 GLASLAMVCGYYGMHIDMLSMRQKFDISARGATLSSLIAIAENLNLKTRALSLSLDEIHQVKRPCILhWDMNHFVVLVNI 111
Cdd:TIGR01846 1 GLEALSLLAQVHNIAVTPSQLRHMLGHAGASLDDLEILLAAKQLGLKAKAVKVSIGRLNKLPLPALI-DGEGGWFVLGKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 112 RGGRITLHDPAFGR-RVIGLQEFSLHFTGialEVWPSSEFTPVVQKNRLHFRKLLSNVTGLKSALVKIFALSLVIEAVNL 190
Cdd:TIGR01846 80 TANGVTIYDPPGDApEVLSREVLEALWSG---TVILLATRSVAGKALKFGFSWFIPAIIRYRKQFREVLLISLALQLFAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 191 LMPVGTQLVMDHVIQAGDHNLLVIICVGLLFFILFRTCVSMFRSWISIVMGALIDIQWKSGLFDHLMKLPLAYFEKRKLG 270
Cdd:TIGR01846 157 VTPLLFQVVIDKVLVHRGLSTLSVLALAMLAVAIFEPALGGLRTYLFAHLTSRIDVELGARLYRHLLGLPLGYFESRRVG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 271 DIQSRFGSLDAIRTTFTTSIVSSIIDGIMSVGVFIMMFMYGGWLVWVASGFTVLYVLLRLSTYRYYRQASEEQLVKSAKA 350
Cdd:TIGR01846 237 DTVARVRELEQIRNFLTGSALTVVLDLLFVVVFLAVMFFYSPTLTGVVIGSLVCYALLSVFVGPILRKRVEDKFERSAAA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 351 SSHFMETLYSIATLKSLGLAGTRSQFWLNLNIDTANANIRVTKLDMFFGGVNAFLAACDQIVILWLGASLVIDSQMTLGM 430
Cdd:TIGR01846 317 TSFLVESVTGIETIKATATEPQFQNRWDRQLAAYVAASFRVTNLGNIAGQAIELIQKLTFAILLWFGAHLVIGGALSPGQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 431 FVAFNAYRGQFSDRASNLIDMVIRLRMLNLHNERLADIvLSTTEEEKPYRKICNPNEAVTFEVRDLLYQYDSLSRPVIPG 510
Cdd:TIGR01846 397 LVAFNMLAGRVTQPVLRLAQLWQDFQQTGIALERLGDI-LNSPTEPRSAGLAALPELRGAITFENIRFRYAPDSPEVLSN 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 511 LSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINNYRECIACVLQEDKLLAGSIAENICSFD 590
Cdd:TIGR01846 476 LNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCN 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 591 AHPDTEFIVECAKHCNIHDDIMKMPMGYETLVGELGGSLSGGQKQRVLIARALYRRPSILFMDEATSHLDLDNEKRVNEA 670
Cdd:TIGR01846 556 PGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRN 635
|
650 660 670
....*....|....*....|....*....|
gi 727181609 671 ISSLKMTR--VIIAHRPSTIASADRVITLQ 698
Cdd:TIGR01846 636 MREICRGRtvIIIAHRLSTVRACDRIIVLE 665
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
25-698 |
4.51e-88 |
|
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: 290.87 E-value: 4.51e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 25 QTEAAECGLASLAMVCGYYGMHIDMLSMRQKFDISARGATLSSLIAIAENLNLKTRAL--SLSLDEIHQVKRPCILHWDM 102
Cdd:TIGR01193 1 QVDEKDCGIAALSMILKKYGTEYSLAKLRQLAKTDLEGTTVLGLVKAAEYLNFEAKAIqaDMSLFEDKNLPLPFIAHVIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 103 N----HFVVLVNIRGGRITLHDP--AFGRRVIGLQEFSLHFTGIALEVWPSSEFTPVVQKNRlHFRKLLSNVTGLKSALV 176
Cdd:TIGR01193 81 NgklpHYYVVYGVTKNHLIIADPdpTVGITKISKEDFYEEWTGIAIFISPTPEYKPIKEKEN-SLLKFIPLITRQKKLIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 177 KIFALSLVIEAVNLLMPVGTQLVMDHVIQAGDHNLLVIICVGLLFFILFRTCVSMFRSWISIVMGALIDIQWKSGLFDHL 256
Cdd:TIGR01193 160 NIVIAAIIVTLISIAGSYYLQKIIDTYIPHKMMGTLGIISIGLIIAYIIQQILSYIQIFLLNVLGQRLSIDIILSYIKHL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 257 MKLPLAYFEKRKLGDIQSRFGSLDAIRTTFTTSIVSSIIDGIMSVGVFIMMFMYGGWLVWVASGFTVLYVLLRLSTYRYY 336
Cdd:TIGR01193 240 FELPMSFFSTRRTGEIVSRFTDASSIIDALASTILSLFLDMWILVIVGLFLVRQNMLLFLLSLLSIPVYAVIIILFKRTF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 337 RQASEEQLVKSAKASSHFMETLYSIATLKSLGLAGTRSQFWLNLNIDTANANIRVTKLDMFFGGVNAFLAACDQIVILWL 416
Cdd:TIGR01193 320 NKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAERYSKIDSEFGDYLNKSFKYQKADQGQQAIKAVTKLILNVVILWT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 417 GASLVIDSQMTLGMFVAFNAYRGQFSDRASNLIDMVIRLRMLNLHNERLADIVLSTTEEEKPYRKICNPNEAVTFEVRDL 496
Cdd:TIGR01193 400 GAYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEVYLVDSEFINKKKRTELNNLNGDIVINDV 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 497 LYQYdSLSRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINNYRECIACVLQEDK 576
Cdd:TIGR01193 480 SYSY-GYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPY 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 577 LLAGSIAENICsFDAHPDT--EFIVECAKHCNIHDDIMKMPMGYETLVGELGGSLSGGQKQRVLIARALYRRPSILFMDE 654
Cdd:TIGR01193 559 IFSGSILENLL-LGAKENVsqDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDE 637
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 727181609 655 ATSHLDLDNEKRVNEAISSLK-MTRVIIAHRPSTIASADRVITLQ 698
Cdd:TIGR01193 638 STSNLDTITEKKIVNNLLNLQdKTIIFVAHRLSVAKQSDKIIVLD 682
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
172-465 |
3.46e-78 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) 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. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 252.05 E-value: 3.46e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 172 KSALVKIFALSLVIEAVNLLMPVGTQLVMDHVIQAGDHNLLVIICVGLLFFILFRTCVSMFRSWISIVMGALIDIQWKSG 251
Cdd:cd18555 1 KKLLISILLLSLLLQLLTLLIPILTQYVIDNVIVPGNLNLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 252 LFDHLMKLPLAYFEKRKLGDIQSRFGSLDAIRTTFTTSIVSSIIDGIMSVGVFIMMFMYGGWLVWVASGFTVLYVLLRLS 331
Cdd:cd18555 81 FFEHLLKLPYSFFENRSSGDLLFRANSNVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 332 TYRYYRQASEEQLVKSAKASSHFMETLYSIATLKSLGLAGTRSQFWLNLNIDTANANIRVTKLDMFFGGVNAFLAACDQI 411
Cdd:cd18555 161 TRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNILNSISSSIQFIAPL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 727181609 412 VILWLGASLVIDSQMTLGMFVAFNAYRGQFSDRASNLIDMVIRLRMLNLHNERL 465
Cdd:cd18555 241 LILWIGAYLVINGELTLGELIAFSSLAGSFLTPIVSLINSYNQFILLKSYLERL 294
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
106-698 |
1.13e-76 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 259.89 E-value: 1.13e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 106 VVLVNIRGGRITLHDPAFGRRVIGLQEFSLHFTGIALEVWPsseftPVVQKnRLHFRKLLS-NVTGLKSALVKIFALSLV 184
Cdd:TIGR03797 74 VALLPVSRGGYEIFDPATGTRRRVDAAMAATLAPEAYMFYR-----PLPDK-ALGLRDLLRfALRGARRDLLAILAMGLL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 185 IEAVNLLMPVGTQLVMDHVIQAGDHNLLVIICVGLLFFILFRTCVSMFRSWISIVMGALIDIQWKSGLFDHLMKLPLAYF 264
Cdd:TIGR03797 148 GTLLGMLVPIATGILIGTAIPDADRSLLVQIALALLAAAVGAAAFQLAQSLAVLRLETRMDASLQAAVWDRLLRLPVSFF 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 265 EKRKLGDIQSRFGSLDAIRTTFTTSIVSSIIDGIMSVGVFIMMFMYGGWLVWVASGFTVLYVLLRL-STY---RYYRQAS 340
Cdd:TIGR03797 228 RQYSTGDLASRAMGISQIRRILSGSTLTTLLSGIFALLNLGLMFYYSWKLALVAVALALVAIAVTLvLGLlqvRKERRLL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 341 EEQlvksAKASSHFMETLYSIATLKslgLAGTRSQ---FWLNLNIDTANANIRVTKLDMFFGGVNAFLAACDQIVILWLG 417
Cdd:TIGR03797 308 ELS----GKISGLTVQLINGISKLR---VAGAENRafaRWAKLFSRQRKLELSAQRIENLLTVFNAVLPVLTSAALFAAA 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 418 ASLVIDSQMTLGMFVAFNAYRGQFSDRASNLIDMVIRLRMLNLHNERLADIVLSTTE--EEKPyrkicNPNE-AVTFEVR 494
Cdd:TIGR03797 381 ISLLGGAGLSLGSFLAFNTAFGSFSGAVTQLSNTLISILAVIPLWERAKPILEALPEvdEAKT-----DPGKlSGAIEVD 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 495 DLLYQYDSLSRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINNYRECIACVLQE 574
Cdd:TIGR03797 456 RVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQN 535
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 575 DKLLAGSIAENICSfdAHPDT-EFIVECAKHCNIHDDIMKMPMGYETLVGELGGSLSGGQKQRVLIARALYRRPSILFMD 653
Cdd:TIGR03797 536 GRLMSGSIFENIAG--GAPLTlDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFD 613
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 727181609 654 EATSHLDLDNEKRVNEAISSLKMTRVIIAHRPSTIASADRVITLQ 698
Cdd:TIGR03797 614 EATSALDNRTQAIVSESLERLKVTRIVIAHRLSTIRNADRIYVLD 658
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
171-698 |
6.15e-73 |
|
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: 246.58 E-value: 6.15e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 171 LKSALVKIFALSLVIeavNLLMPVGT----QlVMDHVIQAGDHNLLVIICVGLLFFILFRTCVSMFRSWISIVMGALIDI 246
Cdd:COG4618 18 CRRAFLSVGLFSFFI---NLLMLTPPlymlQ-VYDRVLTSRSVDTLLMLTLLALGLYAVMGLLDAVRSRILVRVGARLDR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 247 QWKSGLFDHLMKLPLayfeKRKLGDIQSRFGSLDAIRTTFTTSIVSSIIDGIMSVgVFI-MMFMYGGWLVWVASGFTVLY 325
Cdd:COG4618 94 RLGPRVFDAAFRAAL----RGGGGAAAQALRDLDTLRQFLTGPGLFALFDLPWAP-IFLaVLFLFHPLLGLLALVGALVL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 326 VLLRLSTYRYYRQASEEQLVKSAKASSHFMETLYSIATLKSLGLAGTRSQFWLNLNIDTANANIRVTKLDMFFGGVNAFL 405
Cdd:COG4618 169 VALALLNERLTRKPLKEANEAAIRANAFAEAALRNAEVIEAMGMLPALRRRWQRANARALALQARASDRAGGFSALSKFL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 406 AACDQIVILWLGASLVIDSQMTLGMFVAfnayrgqfsdrASNL-------IDMVIRL-RMLN---LHNERLADIvLSTTE 474
Cdd:COG4618 249 RLLLQSAVLGLGAYLVIQGEITPGAMIA-----------ASILmgralapIEQAIGGwKQFVsarQAYRRLNEL-LAAVP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 475 EEKPYRKICNPNEAVTfeVRDLLYQYDSLSRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGI 554
Cdd:COG4618 317 AEPERMPLPRPKGRLS--VENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGA 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 555 NIHDIGINNYRECIACVLQEDKLLAGSIAENICSFDAhPDTEFIVECAKHCNIHDDIMKMPMGYETLVGELGGSLSGGQK 634
Cdd:COG4618 395 DLSQWDREELGRHIGYLPQDVELFDGTIAENIARFGD-ADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQR 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 727181609 635 QRVLIARALYRRPSILFMDEATSHLDLDNEKRVNEAISSLK---MTRVIIAHRPSTIASADRVITLQ 698
Cdd:COG4618 474 QRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKargATVVVITHRPSLLAAVDKLLVLR 540
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
491-698 |
1.12e-68 |
|
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: 222.48 E-value: 1.12e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 491 FEVRDLLYQYDSLSRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINNYRECIAC 570
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 571 VLQEDKLLAGSIAENICSfdahpdtefivecakhcnihddimkmpmgyetlvgelggslsGGQKQRVLIARALYRRPSIL 650
Cdd:cd03246 81 LPQDDELFSGSIAENILS------------------------------------------GGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 727181609 651 FMDEATSHLDLDNEKRVNEAISSLKM---TRVIIAHRPSTIASADRVITLQ 698
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAALKAagaTRIVIAHRPETLASADRILVLE 169
|
|
| Peptidase_C39C |
cd02419 |
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
20-146 |
3.37e-68 |
|
A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family.
Pssm-ID: 239100 [Multi-domain] Cd Length: 127 Bit Score: 219.43 E-value: 3.37e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 20 VPQVLQTEAAECGLASLAMVCGYYGMHIDMLSMRQKFDISARGATLSSLIAIAENLNLKTRALSLSLDEIHQVKRPCILH 99
Cdd:cd02419 1 LPVILQTEAAECGLACLAMIASYHGHHVDLASLRQRFPVSLKGATLADLIDIAQQLGLSTRALRLDLEELGQLKLPCILH 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 727181609 100 WDMNHFVVLVNIRGGRITLHDPAFGRRVIGLQEFSLHFTGIALEVWP 146
Cdd:cd02419 81 WDMNHFVVLKKVSRRRIVIHDPALGKRKLSLEEASRHFTGVALELWP 127
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
162-698 |
1.16e-61 |
|
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: 216.16 E-value: 1.16e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 162 RKLLSNVTGLKSALVKIFALSLVIEAVNLLMPVGTQLVMDHVI--QAGDHNLLVIIcVGLLFFILFRTCVSMFRSWISIV 239
Cdd:COG4988 6 KRLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIigGAPLSALLPLL-GLLLAVLLLRALLAWLRERAAFR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 240 MGALIDIQWKSGLFDHLMKLPLAYFEKRKLGDIQSRFG-SLDAIRTTFTTSIVSSIIDGIMSVGVFIMMFmyggWLVWVa 318
Cdd:COG4988 85 AAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTeGVEALDGYFARYLPQLFLAALVPLLILVAVF----PLDWL- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 319 SGFTVL---------YVLLRLSTyryyRQASEEQLVKSAKASSHFMETLYSIATLKSLGLAGTRSQfwlnlNIDTAN--- 386
Cdd:COG4988 160 SGLILLvtapliplfMILVGKGA----AKASRRQWRALARLSGHFLDRLRGLTTLKLFGRAKAEAE-----RIAEASedf 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 387 --ANIRVTK--------LDMFfggvnAFLAACdqIVILWLGASLvIDSQMTL--GMFVafnayrgqfsdrasnLI---DM 451
Cdd:COG4988 231 rkRTMKVLRvaflssavLEFF-----ASLSIA--LVAVYIGFRL-LGGSLTLfaALFV---------------LLlapEF 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 452 VIRLRMLNLHN----------ERLADIvLSTTEEEKPYR-KICNPNEAVTFEVRDLLYQYDSlSRPVIPGLSLQIAAGES 520
Cdd:COG4988 288 FLPLRDLGSFYharangiaaaEKIFAL-LDAPEPAAPAGtAPLPAAGPPSIELEDVSFSYPG-GRPALDGLSLTIPPGER 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 521 VAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINNYRECIACVLQEDKLLAGSIAENICSFDAHPDTEFIVE 600
Cdd:COG4988 366 VALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEA 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 601 CAKHCNIHDDIMKMPMGYETLVGELGGSLSGGQKQRVLIARALYRRPSILFMDEATSHLDLDNEKRVNEAISSLKMTR-- 678
Cdd:COG4988 446 ALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRtv 525
|
570 580
....*....|....*....|
gi 727181609 679 VIIAHRPSTIASADRVITLQ 698
Cdd:COG4988 526 ILITHRLALLAQADRILVLD 545
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
492-697 |
3.29e-60 |
|
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: 202.07 E-value: 3.29e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDLLYQYDSlSRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINNYRECIACV 571
Cdd:cd03254 4 EFENVNFSYDE-KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 572 LQEDKLLAGSIAENICSFDAHPDTEFIVECAKHCNIHDDIMKMPMGYETLVGELGGSLSGGQKQRVLIARALYRRPSILF 651
Cdd:cd03254 83 LQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILI 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 727181609 652 MDEATSHLDLDNEKRVNEAISSLKMTR--VIIAHRPSTIASADRVITL 697
Cdd:cd03254 163 LDEATSNIDTETEKLIQEALEKLMKGRtsIIIAHRLSTIKNADKILVL 210
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
492-698 |
9.44e-59 |
|
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: 198.15 E-value: 9.44e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDLLYQYDSlsRP---VIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINNYRECI 568
Cdd:cd03249 2 EFKNVSFRYPS--RPdvpILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 569 ACVLQEDKLLAGSIAENICSFDAHPDTEFIVECAKHCNIHDDIMKMPMGYETLVGELGGSLSGGQKQRVLIARALYRRPS 648
Cdd:cd03249 80 GLVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 727181609 649 ILFMDEATSHLDLDNEKRVNEAISSLKMTR--VIIAHRPSTIASADRVITLQ 698
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEALDRAMKGRttIVIAHRLSTIRNADLIAVLQ 211
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
172-465 |
4.08e-58 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) 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. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 350052 [Multi-domain] Cd Length: 294 Bit Score: 198.54 E-value: 4.08e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 172 KSALVKIFALSLVIEAVNLLMPVGTQLVMDHVIQAGDHNLLVIICVGLLFFILFRTCVSMFRSWISIVMGALIDIQWKSG 251
Cdd:cd18779 1 PGLLGQILLASLLLQLLGLALPLLTGVLVDRVIPRGDRDLLGVLGLGLAALVLTQLLAGLLRSHLLLRLRTRLDTQLTLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 252 LFDHLMKLPLAYFEKRKLGDIQSRFGSLDAIRTTFTTSIVSSIIDGIMSVGVFIMMFMYGGWLVWVASGFTVLYVLLRLS 331
Cdd:cd18779 81 FLEHLLRLPYRFFQQRSTGDLLMRLSSNATIRELLTSQTLSALLDGTLVLGYLALLFAQSPLLGLVVLGLAALQVALLLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 332 TYRYYRQASEEQLVKSAKASSHFMETLYSIATLKSLGLAGTRSQFWLNLNIDTANANIRVTKLDMFFGGVNAFLAACDQI 411
Cdd:cd18779 161 TRRRVRELMARELAAQAEAQSYLVEALSGIETLKASGAEDRALDRWSNLFVDQLNASLRRGRLDALVDALLATLRLAAPL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 727181609 412 VILWLGASLVIDSQMTLGMFVAFNAYRGQFSDRASNLIDMVIRLRMLNLHNERL 465
Cdd:cd18779 241 VLLWVGAWQVLDGQLSLGTMLALNALAGAFLAPLASLVGTAQQLQLLGSHLERL 294
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
172-451 |
1.58e-57 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 197.01 E-value: 1.58e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 172 KSALVKIFALSLVIEAVNLLMPVGTQLVMDHVIQAGDHNLLVIICVGLLFFILFRTCVSMFRSWISIVMGALIDIQWKSG 251
Cdd:cd18568 1 RKLLAEILLASLLLQLLGLALPLFTQIILDRVLVHKNISLLNLILIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 252 LFDHLMKLPLAYFEKRKLGDIQSRFGSLDAIRTTFTTSIVSSIIDGIMSVGVFIMMFMYGGWLVWVASGFTVLYVLLRLS 331
Cdd:cd18568 81 FYKHLLSLPLSFFASRKVGDIITRFQENQKIRRFLTRSALTTILDLLMVFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 332 TYRYYRQASEEQLVKSAKASSHFMETLYSIATLKSLGLAGTRSQFWLNLNIDTANANIRVTKLDMFFGGVNAFLAACDQI 411
Cdd:cd18568 161 SSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERPIRWRWENKFAKALNTRFRGQKLSIVLQLISSLINHLGTI 240
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 727181609 412 VILWLGASLVIDSQMTLGMFVAFNAYRGQFSDRASNLIDM 451
Cdd:cd18568 241 AVLWYGAYLVISGQLTIGQLVAFNMLFGSVINPLLALVGL 280
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
492-697 |
2.19e-57 |
|
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: 192.21 E-value: 2.19e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDLLYQYDSLSRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINNYRECIACV 571
Cdd:cd03228 2 EFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAYV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 572 LQEDKLLAGSIAENICSfdahpdtefivecakhcnihddimkmpmgyetlvgelggslsGGQKQRVLIARALYRRPSILF 651
Cdd:cd03228 82 PQDPFLFSGTIRENILS------------------------------------------GGQRQRIAIARALLRDPPILI 119
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 727181609 652 MDEATSHLDLDNEKRVNEAISSL--KMTRVIIAHRPSTIASADRVITL 697
Cdd:cd03228 120 LDEATSALDPETEALILEALRALakGKTVIVIAHRLSTIRDADRIIVL 167
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
492-697 |
1.36e-55 |
|
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: 189.75 E-value: 1.36e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDLLYQYDSLSRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINNYRECIACV 571
Cdd:cd03251 2 EFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 572 LQEDKLLAGSIAENICSFDAHPDTEFIVECAKHCNIHDDIMKMPMGYETLVGELGGSLSGGQKQRVLIARALYRRPSILF 651
Cdd:cd03251 82 SQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILI 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 727181609 652 MDEATSHLDLDNEKRVNEAISSLKMTR--VIIAHRPSTIASADRVITL 697
Cdd:cd03251 162 LDEATSALDTESERLVQAALERLMKNRttFVIAHRLSTIENADRIVVL 209
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
172-465 |
1.53e-55 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 191.51 E-value: 1.53e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 172 KSALVKIFALSLVIEAVNLLMPVGTQLVMDHVIQAGDHNLLVIICVGLLFFILFRTCVSMFRSWISIVMGALIDIQWKSG 251
Cdd:cd18570 1 KKLLILILLLSLLITLLGIAGSFFFQILIDDIIPSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 252 LFDHLMKLPLAYFEKRKLGDIQSRFGSLDAIRTTFTTSIVSSIIDGIMSVGVFIMMFMYGGWLVWVASGFTVLYVLLRLS 331
Cdd:cd18570 81 YFKHLLKLPLSFFETRKTGEIISRFNDANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLYILIILL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 332 TYRYYRQASEEQLVKSAKASSHFMETLYSIATLKSLGLagtRSQFWLNLN---IDTANANIRVTKLDMFFGGVNAFLAAC 408
Cdd:cd18570 161 FNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNA---EEQFLKKIEkkfSKLLKKSFKLGKLSNLQSSIKGLISLI 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 727181609 409 DQIVILWLGASLVIDSQMTLGMFVAFNAYRGQFSDRASNLIDMVIRLRMLNLHNERL 465
Cdd:cd18570 238 GSLLILWIGSYLVIKGQLSLGQLIAFNALLGYFLGPIENLINLQPKIQEAKVAADRL 294
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
160-697 |
2.07e-54 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 196.48 E-value: 2.07e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 160 HFRKLLSNVTGLKSALVKIFALSLVIEAVNLLMPVGTQLVMDHVIQAGDHNLLVIICVGLLFFILFRTCVS----MFRSW 235
Cdd:TIGR02203 1 TFRRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLDDGFGGRDRSVLWWVPLVVIGLAVLRGICSfvstYLLSW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 236 IS--IVMGALIDiqwksgLFDHLMKLPLAYFEKRKLGDIQSRFGSLDAIRTTFTTSIVSSII-DGIMSVGVFIMMFmygg 312
Cdd:TIGR02203 81 VSnkVVRDIRVR------MFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVrETLTVIGLFIVLL---- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 313 WLVW-----VASGFTVLYVLLRLSTYRYYRQASEEQlVKSAKASSHFMETLYSIATLKSLG---LAGTRSQFWLNLNIDT 384
Cdd:TIGR02203 151 YYSWqltliVVVMLPVLSILMRRVSKRLRRISKEIQ-NSMGQVTTVAEETLQGYRVVKLFGgqaYETRRFDAVSNRNRRL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 385 AnanIRVTKLDMFFGGVNAFLAACDQIVILWLGASLVIDSQMTLGMFVAFNAYRGQFSDRASNLIDMVIRLRMLNLHNER 464
Cdd:TIGR02203 230 A---MKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAES 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 465 LADIVLSTTEEEKPYRKIcnpnEAVT--FEVRDLLYQYDSLSRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLL 542
Cdd:TIGR02203 307 LFTLLDSPPEKDTGTRAI----ERARgdVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFY 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 543 EPTEGRLFINGINIHDIGINNYRECIACVLQEDKLLAGSIAENICSFD-AHPDTEFIVECAKHCNIHDDIMKMPMGYETL 621
Cdd:TIGR02203 383 EPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRtEQADRAEIERALAAAYAQDFVDKLPLGLDTP 462
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 727181609 622 VGELGGSLSGGQKQRVLIARALYRRPSILFMDEATSHLDLDNEKRVNEAISSLKMTR--VIIAHRPSTIASADRVITL 697
Cdd:TIGR02203 463 IGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRttLVIAHRLSTIEKADRIVVM 540
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
492-698 |
8.91e-54 |
|
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: 184.74 E-value: 8.91e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDLLYQYDSlSRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINNYRECIACV 571
Cdd:cd03253 2 EFENVTFAYDP-GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 572 LQEDKLLAGSIAENICSFDAHPDTEFIVECAKHCNIHDDIMKMPMGYETLVGELGGSLSGGQKQRVLIARALYRRPSILF 651
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 727181609 652 MDEATSHLDLDNEKRVNEAISSL--KMTRVIIAHRPSTIASADRVITLQ 698
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVskGRTTIVIAHRLSTIVNADKIIVLK 209
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
242-698 |
5.15e-53 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 194.94 E-value: 5.15e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 242 ALIDIQWKSGLFDHLMKLPLAYFEKRKLGDIQSRFGSlDAIRTTFTTSIVSSII--DGIMSVGVFIMMFmyggWLVWVAS 319
Cdd:TIGR00958 230 ARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSS-DTQTMSRSLSLNVNVLlrNLVMLLGLLGFML----WLSPRLT 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 320 GFTVLYV-LLRLSTYRY---YRQASEEQLVKSAKASSHFMETLYSIATLKSLGLAGTRSQ-FWLNLNiDTANANIRVTKL 394
Cdd:TIGR00958 305 MVTLINLpLVFLAEKVFgkrYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASrFKEALE-ETLQLNKRKALA 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 395 DMFFGGVNAFLAACDQIVILWLGASLVIDSQMTLGMFVAFNAYRGQFSDRASNLIDMVIRLrmlnLHNERLADIVLSTTE 474
Cdd:TIGR00958 384 YAGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGM----MQAVGASEKVFEYLD 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 475 eekpyRKICNPNEA----------VTFevRDLLYQYDSL-SRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLE 543
Cdd:TIGR00958 460 -----RKPNIPLTGtlaplnleglIEF--QDVSFSYPNRpDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQ 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 544 PTEGRLFINGINIHDIGINNYRECIACVLQEDKLLAGSIAENICSFDAHPDTEFIVECAKHCNIHDDIMKMPMGYETLVG 623
Cdd:TIGR00958 533 PTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVG 612
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 727181609 624 ELGGSLSGGQKQRVLIARALYRRPSILFMDEATSHLDLDNEKRVNEAISSLKMTRVIIAHRPSTIASADRVITLQ 698
Cdd:TIGR00958 613 EKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAHRLSTVERADQILVLK 687
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
252-697 |
2.14e-52 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 190.75 E-value: 2.14e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 252 LFDHLMKLPLAYFEKRKLGDIQSRFGS-LDAIRTTFTTSIVSSIIDGIMSVGVFIMMFMYGGWL-VWVASGFTVLYVLLR 329
Cdd:COG4987 94 LYRRLEPLAPAGLARLRSGDLLNRLVAdVDALDNLYLRVLLPLLVALLVILAAVAFLAFFSPALaLVLALGLLLAGLLLP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 330 LSTYRYYRQASEEQLVKSAKASSHFMETLYSIATLKSLGLAGTRSQfwlnlNIDTANANIRV--TKLDMFFGGVNAFLAA 407
Cdd:COG4987 174 LLAARLGRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALA-----RLDAAEARLAAaqRRLARLSALAQALLQL 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 408 CDQ---IVILWLGASLVIDSQMT---LGMFV-----AFNAyrgqfsdrASNLIDMVIRLRMLNLHNERLADIVLSTTEEE 476
Cdd:COG4987 249 AAGlavVAVLWLAAPLVAAGALSgplLALLVlaalaLFEA--------LAPLPAAAQHLGRVRAAARRLNELLDAPPAVT 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 477 KPYRKICNPnEAVTFEVRDLLYQYDSLSRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINI 556
Cdd:COG4987 321 EPAEPAPAP-GGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDL 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 557 HDIGINNYRECIACVLQEDKLLAGSIAENICSFDAHPDTEFIVECAKHCNIHDDIMKMPMGYETLVGELGGSLSGGQKQR 636
Cdd:COG4987 400 RDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRR 479
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 727181609 637 VLIARALYRRPSILFMDEATSHLDLDNEKRVNEAISSLKMTR--VIIAHRPSTIASADRVITL 697
Cdd:COG4987 480 LALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRtvLLITHRLAGLERMDRILVL 542
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
172-451 |
2.27e-52 |
|
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) 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. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).
Pssm-ID: 350032 [Multi-domain] Cd Length: 294 Bit Score: 183.08 E-value: 2.27e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 172 KSALVKIFALSLVIEAVNLLMPVGTQLVMDHVIqaGDHNL--LVIICVGLLFFILFRTCVSMFRSWISIVMGALIDIQWK 249
Cdd:cd18588 1 KKLLGEVLLASLFLQLFALVTPLFFQVIIDKVL--VHRSLstLDVLAIGLLVVALFEAVLSGLRTYLFSHTTNRIDAELG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 250 SGLFDHLMKLPLAYFEKRKLGDIQSRFGSLDAIRTTFTTSIVSSIIDGIMSVGVFIMMFMYGGWLVWVASGFTVLYVLLR 329
Cdd:cd18588 79 ARLFRHLLRLPLSYFESRQVGDTVARVRELESIRQFLTGSALTLVLDLVFSVVFLAVMFYYSPTLTLIVLASLPLYALLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 330 LSTYRYYRQASEEQLVKSAKASSHFMETLYSIATLKSLGLAGTRSQFWLNLNIDTANANIRVTKLDMFFGGVNAFLAACD 409
Cdd:cd18588 159 LLVTPILRRRLEEKFQRGAENQSFLVETVTGIETVKSLAVEPQFQRRWEELLARYVKASFKTANLSNLASQIVQLIQKLT 238
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 727181609 410 QIVILWLGASLVIDSQMTLGMFVAFNAYRGQFSDRASNLIDM 451
Cdd:cd18588 239 TLAILWFGAYLVMDGELTIGQLIAFNMLAGQVSQPVLRLVQL 280
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
146-698 |
5.68e-52 |
|
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: 190.03 E-value: 5.68e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 146 PSSEFTPVVQKNRLHFRKLLSNVTGLKSALVKIFALSLVIEAVNLLMPVGTQLVMDHVIQAGDHNLLVIICVGLLF-FIL 224
Cdd:COG5265 7 MSAPAAPPRLDLLLRLLLLLLLPPYLRRRRRALAALLLLLLAAALALVVPPLLKDAIDALLSGAAALLVVPVGLLLaYGL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 225 FRTCVSMFRSWISIVMGALI-DIQWKSGL--FDHLMKLPLAYFEKRKLG----DIqSRfgSLDAIRT--TFTT-SIVSSI 294
Cdd:COG5265 87 LRLLSVLFGELRDALFARVTqRAVRRLALevFRHLHALSLRFHLERQTGglsrDI-ER--GTKGIEFllRFLLfNILPTL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 295 IDGIMSVGVFImmFMYGGWLVWVASGFTVLYVL--LRLSTYR--YYRQASEEQlvksAKASSHFMETLYSIATLKSLG-- 368
Cdd:COG5265 164 LEIALVAGILL--VKYDWWFALITLVTVVLYIAftVVVTEWRtkFRREMNEAD----SEANTRAVDSLLNYETVKYFGne 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 369 --LAGTRSQFWLNLnidtANANIRVTKLDMFFGGVNAFLAACDQIVILWLGASLVIDSQMTLGMFVAFNAYRGQFSdRAS 446
Cdd:COG5265 238 arEARRYDEALARY----ERAAVKSQTSLALLNFGQALIIALGLTAMMLMAAQGVVAGTMTVGDFVLVNAYLIQLY-IPL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 447 NLIDMV---IRLRMLNLhnERLADIvLSTTEE--EKPYRKICNPNEA-VTFEvrDLLYQYDSlSRPVIPGLSLQIAAGES 520
Cdd:COG5265 313 NFLGFVyreIRQALADM--ERMFDL-LDQPPEvaDAPDAPPLVVGGGeVRFE--NVSFGYDP-ERPILKGVSFEVPAGKT 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 521 VAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINNYRECIACVLQEDKLLAGSIAENICSFDAHPDTEFIVE 600
Cdd:COG5265 387 VAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEA 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 601 CAKHCNIHDDIMKMPMGYETLVGELGGSLSGGQKQRVLIARALYRRPSILFMDEATSHLDLDNEKRVNEAISSLKMTR-- 678
Cdd:COG5265 467 AARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRtt 546
|
570 580
....*....|....*....|
gi 727181609 679 VIIAHRPSTIASADRVITLQ 698
Cdd:COG5265 547 LVIAHRLSTIVDADEILVLE 566
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
489-698 |
1.12e-49 |
|
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: 173.83 E-value: 1.12e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 489 VTFEVRDLLYQYDSlsRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINNYRECI 568
Cdd:cd03252 1 ITFEHVRFRYKPDG--PVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 569 ACVLQEDKLLAGSIAENICSFDAHPDTEFIVECAKHCNIHDDIMKMPMGYETLVGELGGSLSGGQKQRVLIARALYRRPS 648
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 727181609 649 ILFMDEATSHLDLDNEKRVNEAISSLKMTR--VIIAHRPSTIASADRVITLQ 698
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICAGRtvIIIAHRLSTVKNADRIIVME 210
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
491-698 |
7.99e-49 |
|
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: 170.85 E-value: 7.99e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 491 FEVRDLLYQYDSLSRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINNYRECIAC 570
Cdd:cd03245 3 IEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 571 VLQEDKLLAGSIAENICSFDAHPDTEFIVECAKHCNIHDDIMKMPMGYETLVGELGGSLSGGQKQRVLIARALYRRPSIL 650
Cdd:cd03245 83 VPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPIL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 727181609 651 FMDEATSHLDLDNEKRVNEAISSLKMTR--VIIAHRPSTIASADRVITLQ 698
Cdd:cd03245 163 LLDEPTSAMDMNSEERLKERLRQLLGDKtlIIITHRPSLLDLVDRIIVMD 212
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
253-697 |
1.47e-44 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 168.60 E-value: 1.47e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 253 FDHLMKLPLAYFEKRKLGD--------IQSRFGS-LDAIRTTFTTsivssiidgIMSVGVFIMMFMYGGW-----LVWVA 318
Cdd:PRK13657 96 FERIIQLPLAWHSQRGSGRalhtllrgTDALFGLwLEFMREHLAT---------LVALVVLLPLALFMNWrlslvLVVLG 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 319 SGFTVLYVLLRLSTYryYRQASEEQlvKSAKASSHFMETLYSIATLKSLGLAGTRSQFWLNLNIDTANANIRVTKLDMFF 398
Cdd:PRK13657 167 IVYTLITTLVMRKTK--DGQAAVEE--HYHDLFAHVSDAIGNVSVVQSYNRIEAETQALRDIADNLLAAQMPVLSWWALA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 399 GGVNAFLAACDQIVILWLGASLVIDSQMTLG---MFVAFNAYRGQFSDRASNLIDMVIRLRmlnlhnERLADI--VLSTT 473
Cdd:PRK13657 243 SVLNRAASTITMLAILVLGAALVQKGQLRVGevvAFVGFATLLIGRLDQVVAFINQVFMAA------PKLEEFfeVEDAV 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 474 E--EEKP-YRKICNPNEAVTFEvrDLLYQYDSlSRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLF 550
Cdd:PRK13657 317 PdvRDPPgAIDLGRVKGAVEFD--DVSFSYDN-SRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRIL 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 551 INGINIHDIGINNYRECIACVLQEDKLLAGSIAENICSFDAHPDTEFIVECAKHCNIHDDIMKMPMGYETLVGELGGSLS 630
Cdd:PRK13657 394 IDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLS 473
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 727181609 631 GGQKQRVLIARALYRRPSILFMDEATSHLDLDNEKRVNEAISSLKMTRV--IIAHRPSTIASADRVITL 697
Cdd:PRK13657 474 GGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTtfIIAHRLSTVRNADRILVF 542
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
172-435 |
1.76e-44 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 161.22 E-value: 1.76e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 172 KSALVKIFALSLVIEAVNLLMPVGTQLVMDHVIQAGDHNLLVIICVGLLFFILFRTCVSMFRSWISIVMGALIDIQWKSG 251
Cdd:cd18782 1 RRALIEVLALSFVVQLLGLANPLLFQVIIDKVLVQQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 252 LFDHLMKLPLAYFEKRKLGDIQSRFGSLDAIRTTFTTSIVSSIIDGIMSVGVFIMMFMYGGWLVWVASGFTVLYVLLRLS 331
Cdd:cd18782 81 IIDHLLRLPLGFFDKRPVGELSTRISELDTIRGFLTGTALTTLLDVLFSVIYIAVLFSYSPLLTLVVLATVPLQLLLTFL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 332 TYRYYRQASEEQLVKSAKASSHFMETLYSIATLKSLGLAGTRSQFWLNLNIDTANANIRVTKLDMFFGGVNAFLAACDQI 411
Cdd:cd18782 161 FGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELKARWRWQNRYARSLGEGFKLTVLGTTSGSLSQFLNKLSSL 240
|
250 260
....*....|....*....|....
gi 727181609 412 VILWLGASLVIDSQMTLGMFVAFN 435
Cdd:cd18782 241 LVLWVGAYLVLRGELTLGQLIAFR 264
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
175-442 |
2.96e-43 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 157.42 E-value: 2.96e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 175 LVKIFALSLVIEAVNLLMPVGTQLVMDHVIQAGDHN--LLVIICVGLLFFILFRTCVSMFRSWISIVMGALIDIQWKSGL 252
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPEtqALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 253 FDHLMKLPLAYFEKRKLGDIQSRFGS-LDAIRTTFTTSIVSSIIDGIMSVGVFIMMFMYGGWLVWVASGFTVLYVLLRLS 331
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNdTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 332 TYRYYRQASEEQLVKSAKASSHFMETLYSIATLKSLGLAGTRSQFWLNLNIDTANANIRVTKLDMFFGGVNAFLAACDQI 411
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
|
250 260 270
....*....|....*....|....*....|.
gi 727181609 412 VILWLGASLVIDSQMTLGMFVAFNAYRGQFS 442
Cdd:pfam00664 241 LALWFGAYLVISGELSVGDLVAFLSLFAQLF 271
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
492-697 |
7.90e-43 |
|
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: 154.19 E-value: 7.90e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDLLYQYDSLSRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINNYRECIACV 571
Cdd:cd03244 4 EFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISII 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 572 LQEDKLLAGSIAENICSFDAHPDTEfIVECAKHCNIHDDIMKMPMGYETLVGELGGSLSGGQKQRVLIARALYRRPSILF 651
Cdd:cd03244 84 PQDPVLFSGTIRSNLDPFGEYSDEE-LWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILV 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 727181609 652 MDEATSHLDLDNEKRVNEAISS-LKMTRVI-IAHRPSTIASADRVITL 697
Cdd:cd03244 163 LDEATASVDPETDALIQKTIREaFKDCTVLtIAHRLDTIIDSDRILVL 210
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
175-455 |
2.62e-42 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 155.02 E-value: 2.62e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 175 LVKIFALSLVIEAVNLLMPVGTQLVMDHVIQAGDHNLLVIICVGLLFFILFRTCVSMFRSWISIVMGALIDIQWKSGLFD 254
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 255 HLMKLPLAYFEKRKLGDIQSRFGS-LDAIRTTFTTSIVSSIIDGIMSVGVFIMMFMYGGWLVWVASGFTVLYVLLRLSTY 333
Cdd:cd07346 81 HLQRLSLSFFDRNRTGDLMSRLTSdVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 334 RYYRQASEEQLVKSAKASSHFMETLYSIATLKSLGLAGTRSQFWLNLNIDTANANIRVTKLDMFFGGVNAFLAACDQIVI 413
Cdd:cd07346 161 RRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 727181609 414 LWLGASLVIDSQMTLGMFVAFNAYRGQFSDRASNLIDMVIRL 455
Cdd:cd07346 241 LLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQL 282
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
199-697 |
1.02e-40 |
|
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: 156.68 E-value: 1.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 199 VMDHVIQAGDHNL-LVIICVGLLFFILFRTCVSMFRSWISIVMGALIDIQWKSGLFDHLMKLPLAYFEKRKLGDIQS--- 274
Cdd:TIGR02857 29 VVDGLISAGEPLAeLLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLRERLLEAVAALGPRWLQGRPSGELATlal 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 275 -RFGSLDAIRTTFTTSIVSS-IIDGIMSVGVFimmfmyggWLVWVASGFTVLYVLL----RLSTYRYYRQASEEQLVKSA 348
Cdd:TIGR02857 109 eGVEALDGYFARYLPQLVLAvIVPLAILAAVF--------PQDWISGLILLLTAPLipifMILIGWAAQAAARKQWAALS 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 349 KASSHFMETLYSIATLKSLGLAGTRSQFWLNLNIDTANANIRVTKLDMFFGGVNAFLAACD-QIVILWLGASLViDSQMT 427
Cdd:TIGR02857 181 RLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEYRERTMRVLRIAFLSSAVLELFATLSvALVAVYIGFRLL-AGDLD 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 428 L--GMFV------AFNAYR---GQFSDRAS--NLIDMVIRlrmlnlhnerladiVLSTTEEEKPYRKICNPNEAVTFEVR 494
Cdd:TIGR02857 260 LatGLFVlllapeFYLPLRqlgAQYHARADgvAAAEALFA--------------VLDAAPRPLAGKAPVTAAPASSLEFS 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 495 DLLYQYDSlSRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINNYRECIACVLQE 574
Cdd:TIGR02857 326 GVSVAYPG-RRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQH 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 575 DKLLAGSIAENICSFDAHPDTEFIVECAKHCNIHDDIMKMPMGYETLVGELGGSLSGGQKQRVLIARALYRRPSILFMDE 654
Cdd:TIGR02857 405 PFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDE 484
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 727181609 655 ATSHLDLDNEKRVNEAISSLKMTR--VIIAHRPSTIASADRVITL 697
Cdd:TIGR02857 485 PTAHLDAETEAEVLEALRALAQGRtvLLVTHRLALAALADRIVVL 529
|
|
| Peptidase_C39 |
pfam03412 |
Peptidase C39 family; Lantibiotic and non-lantibiotic bacteriocins are synthesized as ... |
19-149 |
1.15e-39 |
|
Peptidase C39 family; Lantibiotic and non-lantibiotic bacteriocins are synthesized as precursor peptides containing N-terminal extensions (leader peptides) which are cleaved off during maturation. Most non-lantibiotics and also some lantibiotics have leader peptides of the so-called double-glycine type. These leader peptides share consensus sequences and also a common processing site with two conserved glycine residues in positions -1 and -2. The double- glycine-type leader peptides are unrelated to the N-terminal signal sequences which direct proteins across the cytoplasmic membrane via the sec pathway. Their processing sites are also different from typical signal peptidase cleavage sites, suggesting that a different processing enzyme is involved. Peptide bacteriocins are exported across the cytoplasmic membrane by a dedicated ATP-binding cassette (ABC) transporter. The ABC transporter is the maturation protease and its proteolytic domain resides in the N-terminal part of the protein. This peptidase domain is found in a wide range of ABC transporters, however the presumed catalytic cysteine and histidine are not conserved in all members of this family.
Pssm-ID: 367483 [Multi-domain] Cd Length: 133 Bit Score: 142.36 E-value: 1.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 19 KVPQVLQTEAAECGLASLAMVCGYYGMHIDMLSMRQKFDISARGATLSSLIAIAENLNLKTRALSLSLDEIHQVKRPCIL 98
Cdd:pfam03412 1 KYKIVLQVDENDCGLACLAMILKYYGSNVSLEELRELAGTPAEGTSLLGLKKAAEKLGFKAKAIKADLSELKELPLPFIA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 727181609 99 HWDMN--HFVVLVNIRGGRITLHDPAFGRRVIGLQEFSLHFTGIALEVWPSSE 149
Cdd:pfam03412 81 HWDGNggHFVVVYGIKKNKVLIADPAVGKIKLSREEFEKEWTGVALLVAPKPS 133
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
492-698 |
2.05e-39 |
|
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: 144.92 E-value: 2.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDLLYQYDSLS-RPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINNYRECIAC 570
Cdd:cd03248 13 KFQNVTFAYPTRPdTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 571 VLQEDKLLAGSIAENICSFDAHPDTEFIVECAKHCNIHDDIMKMPMGYETLVGELGGSLSGGQKQRVLIARALYRRPSIL 650
Cdd:cd03248 93 VGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 727181609 651 FMDEATSHLDLDNEKRVNEAIS-SLKMTRV-IIAHRPSTIASADRVITLQ 698
Cdd:cd03248 173 ILDEATSALDAESEQQVQQALYdWPERRTVlVIAHRLSTVERADQILVLD 222
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
161-695 |
6.45e-39 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 152.10 E-value: 6.45e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 161 FRKLLSNVTGLKSALVkIFALSLVIEAV------NLLMPVgtqlvMDHVIQAGDHNLLVIICVGLLFFILFRTcVSMFRS 234
Cdd:PRK11176 13 FRRLWPTIAPFKAGLI-VAGVALILNAAsdtfmlSLLKPL-----LDDGFGKADRSVLKWMPLVVIGLMILRG-ITSFIS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 235 -----WIS--IVMgalidiQWKSGLFDHLMKLPLAYFEKRKLGDIQSRFgSLDAIRTTFTTS--IVSSIIDGIMSVGVFI 305
Cdd:PRK11176 86 sycisWVSgkVVM------TMRRRLFGHMMGMPVSFFDKQSTGTLLSRI-TYDSEQVASSSSgaLITVVREGASIIGLFI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 306 MMFmYGGW-----LVWVASgftVLYVLLRLSTYRYYR------------QASEEQLVKSAKasshfmETLysiatlkSLG 368
Cdd:PRK11176 159 MMF-YYSWqlsliLIVIAP---IVSIAIRVVSKRFRNisknmqntmgqvTTSAEQMLKGHK------EVL-------IFG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 369 LAGTRSQFWLNLNIDTANANIRVTKLDMFFGGVNAFLAACDQIVILWLGASLVIDSQMTLGMF-VAFnayrgqfsdraSN 447
Cdd:PRK11176 222 GQEVETKRFDKVSNRMRQQGMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMDTLTAGTItVVF-----------SS 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 448 LIDMVIRLRML---NLHNER-------LADIVLSTTEEEKPYRKICNPNEAVTFevRDLLYQYDSLSRPVIPGLSLQIAA 517
Cdd:PRK11176 291 MIALMRPLKSLtnvNAQFQRgmaacqtLFAILDLEQEKDEGKRVIERAKGDIEF--RNVTFTYPGKEVPALRNINFKIPA 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 518 GESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINNYRECIACVLQEDKLLAGSIAENIC-SFDAHPDTE 596
Cdd:PRK11176 369 GKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAyARTEQYSRE 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 597 FIVECAKHCNIHDDIMKMPMGYETLVGELGGSLSGGQKQRVLIARALYRRPSILFMDEATSHLDLDNEKRVNEAISSLKM 676
Cdd:PRK11176 449 QIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQK 528
|
570 580
....*....|....*....|.
gi 727181609 677 TR--VIIAHRPSTIASADRVI 695
Cdd:PRK11176 529 NRtsLVIAHRLSTIEKADEIL 549
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
172-435 |
2.63e-37 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350056 [Multi-domain] Cd Length: 294 Bit Score: 141.11 E-value: 2.63e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 172 KSALVKIFALSLVIEAVNLLMPVGTQLVMDHVIQAGDHNLLVIICVGLLFFILFRTCVSMFRSWISIVMGALIDIQWKSG 251
Cdd:cd18783 1 KRLFRDVAIASLILHVLALAPPIFFQIVIDKVLVHQSYSTLYVLTIGVVIALLFEGILGYLRRYLLLVATTRIDARLALR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 252 LFDHLMKLPLAYFEKRKLGDIQSRFGSLDAIRTTFTTSIVSSIIDGIMSVGVFIMMFMYGGWLVWVASGFTVLYVLLRLS 331
Cdd:cd18783 81 TFDRLLSLPIDFFERTPAGVLTKHMQQIERIRQFLTGQLFGTLLDATSLLVFLPVLFFYSPTLALVVLAFSALIALIILA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 332 TYRYYRQASEEQLVKSAKASSHFMETLYSIATLKSLGLAGTRSQFWLNLNIDTANANIRVTKLDMFFGGVNAFLAACDQI 411
Cdd:cd18783 161 FLPPFRRRLQALYRAEGERQAFLVETVHGIRTVKSLALEPRQRREWDERVARAIRARFAVGRLSNWPQTLTGPLEKLMTV 240
|
250 260
....*....|....*....|....
gi 727181609 412 VILWLGASLVIDSQMTLGMFVAFN 435
Cdd:cd18783 241 GVIWVGAYLVFAGSLTVGALIAFN 264
|
|
| ABC_6TM_NHLM_bacteriocin |
cd18569 |
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ... |
172-465 |
8.52e-36 |
|
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; This group includes the six-transmembrane helical domain (6-TMD) of the ABC subunit of NHLM (Nitrile Hydratase Leader Microcin) bacteriocin system, which contains ABC transporter (permease/ATP-binding fused protein) with a peptidase domain. ABC-transporter proteins in this group are predicted to be a subunit of a bacteriocin processing and export system, and they carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350013 [Multi-domain] Cd Length: 294 Bit Score: 136.84 E-value: 8.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 172 KSALVKIFALSLVIEAVNLLMPVGTQLVMDHVIQAGDHNLLVIICVGLLFFILFRTCVSMFRSWISIVMGALIDIQWKSG 251
Cdd:cd18569 1 RSALLFVVLAGLLLVIPGLVIPVFSRIFIDDILVGGLPDWLRPLLLGMALTALLQGLLTWLQQYYLLRLETKLALSSSSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 252 LFDHLMKLPLAYFEKRKLGDIQSRFGSLDAIRTTFTTSIVSSIIDGIMSVGVFIMMFMYGGWLVWVASGFTVLYVLLRLS 331
Cdd:cd18569 81 FFWHVLRLPVEFFSQRYAGDIASRVQSNDRVANLLSGQLATTVLNLVMAVFYALLMLQYDVPLTLIGIAIALLNLLVLRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 332 TYRYYRQASEEQLVKSAKASSHFMETLYSIATLKSlglAGTRSQF---WLNLNIDTANANIRVTKLDMFFGGVNAFLAAC 408
Cdd:cd18569 161 VSRKRVDLNRRLLQDSGKLTGTTMSGLQMIETLKA---SGAESDFfsrWAGYQAKVLNAQQELGRTNQLLGALPTLLSAL 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 727181609 409 DQIVILWLGASLVIDSQMTLGMFVAFNAYRGQFSDRASNLIDMVIRLRMLNLHNERL 465
Cdd:cd18569 238 TNAAILGLGGLLVMDGALTIGMLVAFQSLMASFLAPVNSLVGLGGTLQEMRGDMERL 294
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
491-699 |
9.35e-36 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 134.17 E-value: 9.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 491 FEVRDLLYQYDSlsRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINNYRECIAC 570
Cdd:COG4619 1 LELEGLSFRVGG--KPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 571 VLQEDKLLAGSIAENI----CSFDAHPDTEFIVECAKHCNIHDDIMKMPM-----GyetlvgelggslsggQKQRVLIAR 641
Cdd:COG4619 79 VPQEPALWGGTVRDNLpfpfQLRERKFDRERALELLERLGLPPDILDKPVerlsgG---------------ERQRLALIR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 727181609 642 ALYRRPSILFMDEATSHLDLDNEKRVNEAISSLK----MTRVIIAHRPSTIAS-ADRVITLQP 699
Cdd:COG4619 144 ALLLQPDVLLLDEPTSALDPENTRRVEELLREYLaeegRAVLWVSHDPEQIERvADRVLTLEA 206
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
492-697 |
4.57e-34 |
|
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: 129.51 E-value: 4.57e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDLLYQYDSLSRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINNYRECIACV 571
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 572 LQ--EDKLLAGSIAENIC------SFDAHPDTEFIVECAKHCNI----HDDIMKMPMGyetlvgelggslsggQKQRVLI 639
Cdd:cd03225 81 FQnpDDQFFGPTVEEEVAfglenlGLPEEEIEERVEEALELVGLeglrDRSPFTLSGG---------------QKQRVAI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 727181609 640 ARALYRRPSILFMDEATSHLDLDNEKRVNEAISSLK---MTRVIIAHRPSTIAS-ADRVITL 697
Cdd:cd03225 146 AGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKaegKTIIIVTHDLDLLLElADRVIVL 207
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
178-436 |
3.76e-33 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 129.24 E-value: 3.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 178 IFALSLVIEAVNLLMPVGTQLVMDHVIQAGDHNLLVIICVGLLFFILFRTCVSMFRSWISIVMGALIDIQWKSGLFDHLM 257
Cdd:cd18566 7 VLLASLFINILALATPLFILQVYDRVIPNESIPTLQVLVIGVVIAILLESLLRLLRSYILAWIGARFDHRLSNAAFEHLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 258 KLPLAYFEKRKLGDIQSRFGSLDAIRTTFTTSIVSSIIDGIMSVGVFIMMFMYGGWLVWVASGFTVLYVLLRLSTYRYYR 337
Cdd:cd18566 87 SLPLSFFEREPSGAHLERLNSLEQIREFLTGQALLALLDLPFVLIFLGLIWYLGGKLVLVPLVLLGLFVLVAILLGPILR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 338 QASEEQLVKSAKASSHFMETLYSIATLKSLGLagtRSQF---WLNLNIDTANANIRVTKLDMFFGGVNAFLAACDQIVIL 414
Cdd:cd18566 167 RALKERSRADERRQNFLIETLTGIHTIKAMAM---EPQMlrrYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSMVAVV 243
|
250 260
....*....|....*....|..
gi 727181609 415 WLGASLVIDSQMTLGMFVAFNA 436
Cdd:cd18566 244 AFGALLVINGDLTVGALIACTM 265
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
492-697 |
8.53e-33 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 125.60 E-value: 8.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDLLYQYDSLSRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINNYRECIACV 571
Cdd:cd03369 8 EVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTII 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 572 LQEDKLLAGSIAENICSFDAHPDTEFivecakhcnihddimkmpmgYETL-VGELGGSLSGGQKQRVLIARALYRRPSIL 650
Cdd:cd03369 88 PQDPTLFSGTIRSNLDPFDEYSDEEI--------------------YGALrVSEGGLNLSQGQRQLLCLARALLKRPRVL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 727181609 651 FMDEATSHLDLDNEKRVNEAISSL--KMTRVIIAHRPSTIASADRVITL 697
Cdd:cd03369 148 VLDEATASIDYATDALIQKTIREEftNSTILTIAHRLRTIIDYDKILVM 196
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
492-698 |
1.20e-32 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 125.93 E-value: 1.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDL--LYQYDSLSRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGIN---NYR- 565
Cdd:COG1136 6 ELRNLtkSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERelaRLRr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 566 ECIACVLQEDKLLAG-SIAENIC------SFDAHPDTEFIVECAKHCNIHDDIMKMPM----GyetlvgelggslsggQK 634
Cdd:COG1136 86 RHIGFVFQFFNLLPElTALENVAlplllaGVSRKERRERARELLERVGLGDRLDHRPSqlsgG---------------QQ 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 727181609 635 QRVLIARALYRRPSILFMDEATSHLDLDNEKRVNEAISSL----KMTRVIIAHRPSTIASADRVITLQ 698
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELnrelGTTIVMVTHDPELAARADRVIRLR 218
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
492-697 |
1.29e-32 |
|
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: 123.51 E-value: 1.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDLLYQYDSlsRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINNYRECIACV 571
Cdd:cd00267 1 EIENLSFRYGG--RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 572 LQedkLLAGsiaenicsfdahpdtefivecakhcnihddimkmpmgyetlvgelggslsggQKQRVLIARALYRRPSILF 651
Cdd:cd00267 79 PQ---LSGG----------------------------------------------------QRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 727181609 652 MDEATSHLDLDNEKRVNEAISSL---KMTRVIIAHRPSTIA-SADRVITL 697
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELaeeGRTVIIVTHDPELAElAADRVIVL 153
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
492-698 |
2.09e-31 |
|
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: 121.83 E-value: 2.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDLLYQY--DSLSRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINN----YR 565
Cdd:cd03255 2 ELKNLSKTYggGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKElaafRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 566 ECIACVLQEDKLLAG-SIAENI---CSFDAHPDTEfIVECAKHC----NIHDDIMKMPM----GyetlvgelggslsggQ 633
Cdd:cd03255 82 RHIGFVFQSFNLLPDlTALENVelpLLLAGVPKKE-RRERAEELlervGLGDRLNHYPSelsgG---------------Q 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 727181609 634 KQRVLIARALYRRPSILFMDEATSHLDLDNEKRVNEAISSLK----MTRVIIAHRPSTIASADRVITLQ 698
Cdd:cd03255 146 QQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNkeagTTIVVVTHDPELAEYADRIIELR 214
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
262-698 |
2.65e-31 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 129.45 E-value: 2.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 262 AYFEKRKLGDIQSRfGSLDAIRTTFTT-----SIVSSIIdgiMSVGVFIMMFMYGGWLVwvasgfTVLYVL----LRLST 332
Cdd:PRK10789 85 EFYLRHRTGDLMAR-ATNDVDRVVFAAgegvlTLVDSLV---MGCAVLIVMSTQISWQL------TLLALLpmpvMAIMI 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 333 YRYYRQAseEQLVKSAKA--SS---HFMETLYSIATLKSLGLAGTRSQFWLNLNIDTANANIRVTKLDMFFG-------G 400
Cdd:PRK10789 155 KRYGDQL--HERFKLAQAafSSlndRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDptiyiaiG 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 401 VNAFLAACDqivilwlGASLVIDSQMTLGMFVAFNAYRGQFsdrasnLIDMVIRLRMLNLhNER--LADIVLSTTEEEKP 478
Cdd:PRK10789 233 MANLLAIGG-------GSWMVVNGSLTLGQLTSFVMYLGLM------IWPMLALAWMFNI-VERgsAAYSRIRAMLAEAP 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 479 YRK---ICNPNEAVTFEVRDLLYQYDSLSRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGIN 555
Cdd:PRK10789 299 VVKdgsEPVPEGRGELDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIP 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 556 IHDIGINNYRECIACVLQEDKLLAGSIAENICSfdAHPDT--EFIVECAKHCNIHDDIMKMPMGYETLVGELGGSLSGGQ 633
Cdd:PRK10789 379 LTKLQLDSWRSRLAVVSQTPFLFSDTVANNIAL--GRPDAtqQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQ 456
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 727181609 634 KQRVLIARALYRRPSILFMDEATSHLDLDNEKRVNEAISSLKMTRVII--AHRPSTIASADRVITLQ 698
Cdd:PRK10789 457 KQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIisAHRLSALTEASEILVMQ 523
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
484-698 |
2.02e-30 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 126.88 E-value: 2.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 484 NPNEAVTFEVRDL-LYQYDS--LSRPvipgLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLePTEGRLFINGINIHDIG 560
Cdd:PRK11174 343 ASNDPVTIEAEDLeILSPDGktLAGP----LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELD 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 561 INNYRECIACVLQEDKLLAGSIAENICSFDAHPDTEFIVECAKHCNIHDDIMKMPMGYETLVGELGGSLSGGQKQRVLIA 640
Cdd:PRK11174 418 PESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALA 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 641 RALYRRPSILFMDEATSHLDLDNEKRVNEAIS--SLKMTRVIIAHRPSTIASADRVITLQ 698
Cdd:PRK11174 498 RALLQPCQLLLLDEPTASLDAHSEQLVMQALNaaSRRQTTLMVTHQLEDLAQWDQIWVMQ 557
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
491-697 |
2.27e-30 |
|
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: 119.36 E-value: 2.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 491 FEVRDLLYQYDSlSRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINNYRECIAC 570
Cdd:COG1122 1 IELENLSFSYPG-GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 571 VLQ--EDKLLAGSIAENIcSF----------DAHpdtEFIVECAKHCNIHD----DIMKMPMGyetlvgelggslsggQK 634
Cdd:COG1122 80 VFQnpDDQLFAPTVEEDV-AFgpenlglpreEIR---ERVEEALELVGLEHladrPPHELSGG---------------QK 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 727181609 635 QRVLIARALYRRPSILFMDEATSHLDLDNEKRVNEAISSLK---MTRVIIAHRPSTIAS-ADRVITL 697
Cdd:COG1122 141 QRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNkegKTVIIVTHDLDLVAElADRVIVL 207
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
252-685 |
4.63e-30 |
|
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: 125.17 E-value: 4.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 252 LFDHLMKLPLAYFEKRKLGDIQSRFGS-LDAIRTTfttsIVSSIIDGIMSVGVFIMMFMYGGWLVWVASGFTVLYVLLR- 329
Cdd:TIGR02868 92 VYERLARQALAGRRRLRRGDLLGRLGAdVDALQDL----YVRVIVPAGVALVVGAAAVAAIAVLSVPAALILAAGLLLAg 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 330 ----LSTYRYYRQAseEQLVKSAKA--SSHFMETLYSIATLKSLG-LAGTRSQF------WLNLNIDTANANIRVTKLDM 396
Cdd:TIGR02868 168 fvapLVSLRAARAA--EQALARLRGelAAQLTDALDGAAELVASGaLPAALAQVeeadreLTRAERRAAAATALGAALTL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 397 FFGGVNAFLAacdqiviLWLGASLVIDSQM---TLGMFV-----AFNAYrGQFSDRASNLIDMVIRLRMLN--LHNERLA 466
Cdd:TIGR02868 246 LAAGLAVLGA-------LWAGGPAVADGRLapvTLAVLVllplaAFEAF-AALPAAAQQLTRVRAAAERIVevLDAAGPV 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 467 DIVlsTTEEEKPYrkicnPNEAVTFEVRDLLYQYDSlSRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTE 546
Cdd:TIGR02868 318 AEG--SAPAAGAV-----GLGKPTLELRDLSAGYPG-APPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQ 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 547 GRLFINGINIHDIGINNYRECIACVLQEDKLLAGSIAENICSfdAHPDT--EFIVECAKHCNIHDDIMKMPMGYETLVGE 624
Cdd:TIGR02868 390 GEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRL--ARPDAtdEELWAALERVGLADWLRALPDGLDTVLGE 467
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 727181609 625 LGGSLSGGQKQRVLIARALYRRPSILFMDEATSHLDLDNEKRVNEAISSL--KMTRVIIAHRP 685
Cdd:TIGR02868 468 GGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAAlsGRTVVLITHHL 530
|
|
| Peptidase_C39D |
cd02420 |
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
20-143 |
4.74e-29 |
|
A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family.
Pssm-ID: 239101 [Multi-domain] Cd Length: 125 Bit Score: 112.14 E-value: 4.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 20 VPQVLQTEAAECGLASLAMVCGYYGMHIDMLSMRQKFDISARGATLSSLIAIAENLNLKTRALSLSLDEIHQVKRPCILH 99
Cdd:cd02420 1 TPTVLQMEATECGAASLAIILAYYGRYVPLSELRIACGVSRDGSNASNLLKAAREYGLTAKGYKKDLEALREVSLPAIVF 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 727181609 100 WDMNHFVVLVNIRGGRITLHDPAFGRRVIGLQEFSLHFTGIALE 143
Cdd:cd02420 81 WNFNHFLVVEGFDKRKVFLNDPATGRRTVSLEEFDQSFTGVVLT 124
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
174-451 |
9.21e-29 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 116.80 E-value: 9.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 174 ALVKIFALSLVIEAVNLLMPVGTQLVMDHVIQAGDHNLLVIICVGLLFFILFRTCVSMFRSWISIVMG--ALIDIqwKSG 251
Cdd:cd18545 1 KLLLALLLMLLSTAASLAGPYLIKIAIDEYIPNGDLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGqrILYDL--RQD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 252 LFDHLMKLPLAYFEKRKLGDIQSRF-GSLDAIRTTFTTSIVSSIIDGIMSVGVFIMMFMYGGWLVWVAsgFTVLYVLLRL 330
Cdd:cd18545 79 LFSHLQKLSFSFFDSRPVGKILSRViNDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVT--LAVLPLLVLV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 331 STY--RYYRQASEEQLVKSAKASSHFMETLYSIATLKSLGLAGTRSQFWLNLNIDTANANIRVTKLDMFFGGVNAFLAAC 408
Cdd:cd18545 157 VFLlrRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVELISAL 236
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 727181609 409 DQIVILWLGASLVIDSQMTLGMFVAFNAYRGQFSDRASNLIDM 451
Cdd:cd18545 237 GTALVYWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNF 279
|
|
| ABC_6TM_peptidase_like |
cd18571 |
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and ... |
172-465 |
9.30e-29 |
|
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and similar proteins; This group includes the 6-TMD of an uncharacterized peptidase-containing ABC transporter of T1SS (type 1 secretion systems), similar to heterocyst differentiation protein HetC. HetC is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350015 [Multi-domain] Cd Length: 294 Bit Score: 116.77 E-value: 9.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 172 KSALVKIFALSLVIEAVNLLMPVGTQLVMDHVIQAGDHNLLVIICVGLLFFILFRTCVSMFRSWISIVMGALIDIQWKSG 251
Cdd:cd18571 1 KKLILQLLLGLLLGSLLQLIFPFLTQSIVDKGINNKDLNFIYLILIAQLVLFLGSTSIEFIRSWILLHISSRINISIISD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 252 LFDHLMKLPLAYFEKRKLGDIQSRFGSLDAIRTTFTTSIVSSIIDgIMSVGVF-IMMFMYGGWLVWVASGFTVLYVL--- 327
Cdd:cd18571 81 FLIKLMRLPISFFDTKMTGDILQRINDHSRIESFLTSSSLSILFS-LLNLIVFsIVLAYYNLTIFLIFLIGSVLYILwil 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 328 -----LRLSTYRYYRQASEEQlvksakasSHFMETLYSIATLKSLGLAGTRSQFWLNLNIDTANANIRVTKLDMFFGGVN 402
Cdd:cd18571 160 lflkkRKKLDYKRFDLSSENQ--------SKLIELINGMQEIKLNNSERQKRWEWERIQAKLFKINIKSLKLDQYQQIGA 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 727181609 403 AFLAACDQIVILWLGASLVIDSQMTLGMFVAFNAYRGQFSDRASNLIDMVIRLRMLNLHNERL 465
Cdd:cd18571 232 LFINQLKNILITFLAAKLVIDGEITLGMMLAIQYIIGQLNSPIEQLIGFIQSLQDAKISLERL 294
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
175-455 |
1.48e-28 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 116.07 E-value: 1.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 175 LVKIFALSLVIEAVNLLMPVGTQLVMDHVI----QAGDHNLLVIICVGLLFFILFRTCVSMFRSWISIVMGALI--DIqw 248
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPYLTKILIDDVLiqlgPGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERItaDL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 249 KSGLFDHLMKLPLAYFEKRKLGDIQSRFGS-LDAIRTTFTTSIVSSIIDGIMSVGVFIMMFMYGGWLVWVASGFTVLYVL 327
Cdd:cd18563 79 RRDLYEHLQRLSLSFFDKRQTGSLMSRVTSdTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVW 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 328 LRLSTYRYYRQASEEQLVKSAKASSHFMETLYSIATLKSLGLAGTRSQFWLNLNIDTANANIRVTKLDMFFGGVNAFLAA 407
Cdd:cd18563 159 GSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFLTS 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 727181609 408 CDQIVILWLGASLVIDSQMTLGMFVAFNAYRGQFSDRASNLIDMVIRL 455
Cdd:cd18563 239 LGTLIVWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWI 286
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
492-698 |
7.91e-28 |
|
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: 110.60 E-value: 7.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDLLYQYDSlsRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINNYRECIACV 571
Cdd:cd03214 1 EVENLSVGYGG--RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 572 LQedkllagsiaenicsfdahpdtefiveCAKHCNIHDDIMKmpmGYETLvgelggslSGGQKQRVLIARALYRRPSILF 651
Cdd:cd03214 79 PQ---------------------------ALELLGLAHLADR---PFNEL--------SGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 727181609 652 MDEATSHLDLDNEKRVNEAISSLK----MTRVIIAHRPSTIAS-ADRVITLQ 698
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRRLArergKTVVMVLHDLNLAARyADRVILLK 172
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
492-695 |
9.56e-28 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 112.08 E-value: 9.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDLLYQYDSlsRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGInNYRECIACV 571
Cdd:COG1131 2 EVRGLTKRYGD--KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPA-EVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 572 LQEDKLLAG-SIAEN------ICSFDAHPDTEFIVECAKHCNIHDD----IMKMPMGyetlvgelggslsggQKQRVLIA 640
Cdd:COG1131 79 PQEPALYPDlTVRENlrffarLYGLPRKEARERIDELLELFGLTDAadrkVGTLSGG---------------MKQRLGLA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 641 RALYRRPSILFMDEATSHLDLDNEKRVNEAISSLK---MTrVIIA-HRPSTIAS-ADRVI 695
Cdd:COG1131 144 LALLHDPELLILDEPTSGLDPEARRELWELLRELAaegKT-VLLStHYLEEAERlCDRVA 202
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
491-699 |
1.19e-27 |
|
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: 110.65 E-value: 1.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 491 FEVRDLLYQYDSlsRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGiNNYRECIAC 570
Cdd:COG4133 3 LEAENLSCRRGE--RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR-EDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 571 VLQEDKLLAG-SIAENI---CSFD-AHPDTEFIVECAKHCNIhDDIMKMPMGYetlvgelggslsggQKQRVLIARALYR 645
Cdd:COG4133 80 LGHADGLKPElTVRENLrfwAALYgLRADREAIDEALEAVGL-AGLADLPVRQls----------agQKRRVALARLLLS 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 727181609 646 RPSILFMDEATSHLDLDNEKRVNEAISSLKMTR--VIIA-HRPSTIAsADRVITLQP 699
Cdd:COG4133 149 PAPLWLLDEPFTALDAAGVALLAELIAAHLARGgaVLLTtHQPLELA-AARVLDLGD 204
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
492-697 |
2.43e-27 |
|
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: 108.64 E-value: 2.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDLLYQYDSlsRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGInNYRECIACV 571
Cdd:cd03230 2 EVRNLSKRYGK--KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPE-EVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 572 LQEDKLLAG-SIAENIcsfdahpdtefivecakhcnihddimKMPMGyetlvgelggslsggQKQRVLIARALYRRPSIL 650
Cdd:cd03230 79 PEEPSLYENlTVRENL--------------------------KLSGG---------------MKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 727181609 651 FMDEATSHLDLDNEKRVNEAISSLK---MTRVIIAHRPSTIAS-ADRVITL 697
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLRELKkegKTILLSSHILEEAERlCDRVAIL 168
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
252-698 |
3.02e-27 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 118.54 E-value: 3.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 252 LFDHLMKLPLAYFEKRKLGDIQSRFGSldairttfttsivsSIIDGIMSVGVFIMMFMYGGW-------LVWVASGFTVL 324
Cdd:PLN03232 989 MLNSILRAPMLFFHTNPTGRVINRFSK--------------DIGDIDRNVANLMNMFMNQLWqllstfaLIGTVSTISLW 1054
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 325 YVL----LRLSTYRYYRQASEE----QLVKSAKASSHFMETLYSIATLKSLglagtRSQFWLN-LNIDTANANIRVTKLD 395
Cdd:PLN03232 1055 AIMplliLFYAAYLYYQSTSREvrrlDSVTRSPIYAQFGEALNGLSSIRAY-----KAYDRMAkINGKSMDNNIRFTLAN 1129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 396 MFFGGVNAFLAACDQIVILWLGASLVIDSQMTLGMFVAFNAYRGQFSDRASNLIDM---VIRL--RMLNLHN--ERLA-- 466
Cdd:PLN03232 1130 TSSNRWLTIRLETLGGVMIWLTATFAVLRNGNAENQAGFASTMGLLLSYTLNITTLlsgVLRQasKAENSLNsvERVGny 1209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 467 -DIVLSTTEEEKPYRKICNPNEAVTFEVRDLLYQYDSLSRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPT 545
Cdd:PLN03232 1210 iDLPSEATAIIENNRPVSGWPSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELE 1289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 546 EGRLFINGINIHDIGINNYRECIACVLQEDKLLAGSIAENICSFDAHPDTEfIVECAKHCNIHDDIMKMPMGYETLVGEL 625
Cdd:PLN03232 1290 KGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDAD-LWEALERAHIKDVIDRNPFGLDAEVSEG 1368
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 727181609 626 GGSLSGGQKQRVLIARALYRRPSILFMDEATSHLDLDN----EKRVNEAISSLKMtrVIIAHRPSTIASADRVITLQ 698
Cdd:PLN03232 1369 GENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTdsliQRTIREEFKSCTM--LVIAHRLNTIIDCDKILVLS 1443
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
491-698 |
3.80e-27 |
|
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: 110.90 E-value: 3.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 491 FEVRDLLYQYDSlsRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINNYRECIAC 570
Cdd:COG1120 2 LEAENLSVGYGG--RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 571 VLQEdkllaGSIAENICSFDA-----HP-----------DTEFIVECAKHCNIHDDIMKMpmgYETLvgelggslsggQK 634
Cdd:COG1120 80 VPQE-----PPAPFGLTVRELvalgrYPhlglfgrpsaeDREAVEEALERTGLEHLADRP---VDELsg--------gER 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 635 QRVLIARALYRRPSILFMDEATSHLDLDNEKRVNEAISSLKMTR---VIIA-HRPsTIAS--ADRVITLQ 698
Cdd:COG1120 144 QRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERgrtVVMVlHDL-NLAAryADRLVLLK 212
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
510-657 |
4.46e-27 |
|
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: 107.35 E-value: 4.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 510 GLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINNYRECIACVLQEDKLLAG-SIAENI-- 586
Cdd:pfam00005 3 NVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENLrl 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 727181609 587 -CSFDAHPDTEFIVEcakhcnIHDDIMKMPMGY--ETLVGELGGSLSGGQKQRVLIARALYRRPSILFMDEATS 657
Cdd:pfam00005 83 gLLLKGLSKREKDAR------AEEALEKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| Peptidase_C39B |
cd02418 |
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
21-149 |
5.08e-27 |
|
A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family.
Pssm-ID: 239099 [Multi-domain] Cd Length: 136 Bit Score: 106.52 E-value: 5.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 21 PQVLQTEAAECGLASLAMVCGYYGMHIDMLSMRQKFDISARGATLSSLIAIAENLNLKTRAL--SLSLDEIHQVKRPCIL 98
Cdd:cd02418 2 PYVLQVDEMDCGAACLAMIAKYYGKNYSLAKLRELAGTDREGTSLLGLVKAAEKLGFETRAVkaDMDLFELKDIPLPFIA 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 727181609 99 H----WDMNHFVVLVNIRGGRITLHDPAFGRRVIGLQEFSLHFTGIALEVWPSSE 149
Cdd:cd02418 82 HvikeWKLNHYVVVYKIKKKKILIADPAVGITKISKEEFEKEWTGVALFLEPTPN 136
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
492-697 |
7.22e-27 |
|
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: 110.60 E-value: 7.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDLLYQYDSLSRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGI------NIHDIginnyR 565
Cdd:TIGR04520 2 EVENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLdtldeeNLWEI-----R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 566 ECIACVLQedkllagsiaenicsfdaHPDTEFI---VEcakhcnihDDI------MKMP--------------MGYETLV 622
Cdd:TIGR04520 77 KKVGMVFQ------------------NPDNQFVgatVE--------DDVafglenLGVPreemrkrvdealklVGMEDFR 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 727181609 623 GELGGSLSGGQKQRVLIARALYRRPSILFMDEATSHLDLDNEKRVNEAISSLK----MTRVIIAHRPSTIASADRVITL 697
Cdd:TIGR04520 131 DREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNkeegITVISITHDMEEAVLADRVIVM 209
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
187-434 |
7.45e-27 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 111.04 E-value: 7.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 187 AVNLLMPVGTQLVMDHVIQAGDHNLLVIICVGLLFFILFRTCVSMFRSWISIVMG--ALIDIqwKSGLFDHLMKLPLAYF 264
Cdd:cd18576 10 AIGLVFPLLAGQLIDAALGGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGerVVADL--RKDLYRHLQRLPLSFF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 265 EKRKLGDIQSRFGS-LDAIRTTFTTSIVSSIIDGIMSVG-VFIMMFMYGGWLVWVASGFTVLYVLLRLSTyRYYRQASEE 342
Cdd:cd18576 88 HERRVGELTSRLSNdVTQIQDTLTTTLAEFLRQILTLIGgVVLLFFISWKLTLLMLATVPVVVLVAVLFG-RRIRKLSKK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 343 QLVKSAKASSHFMETLYSIATLKSLglagTRSQFWLN----LNIDTANANIRVTKLDMFFGGVNAFLAACDQIVILWLGA 418
Cdd:cd18576 167 VQDELAEANTIVEETLQGIRVVKAF----TREDYEIEryrkALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWYGG 242
|
250
....*....|....*.
gi 727181609 419 SLVIDSQMTLGMFVAF 434
Cdd:cd18576 243 RLVLAGELTAGDLVAF 258
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
492-697 |
1.06e-26 |
|
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: 109.13 E-value: 1.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDLLYQYDSlsRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINNYREC---I 568
Cdd:cd03261 2 ELRGLTKSFGG--RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLrrrM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 569 ACVLQEDKLLAG-SIAENIC-------SFDAHPDTEFIVECAKHCNIHDDIMKMP------MgyetlvgelggslsggqK 634
Cdd:cd03261 80 GMLFQSGALFDSlTVFENVAfplrehtRLSEEEIREIVLEKLEAVGLRGAEDLYPaelsggM-----------------K 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 727181609 635 QRVLIARALYRRPSILFMDEATSHLDLDNEKRVNEAISSLK----MTRVIIAHRPSTIAS-ADRVITL 697
Cdd:cd03261 143 KRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKkelgLTSIMVTHDLDTAFAiADRIAVL 210
|
|
| ABC_6TM_PrtD_like |
cd18586 |
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ... |
172-435 |
1.10e-26 |
|
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS metalloprotease secretion system, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) such as PrtD, which is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) 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. The Aquifex aeolicus PrtDEF of T1SS is composed of an inner-membrane ABC transporter (PrtD), a periplasmic membrane-fusion protein (PrtE), and an outer-membrane porin (PrtF). These three components assemble into complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides
Pssm-ID: 350030 [Multi-domain] Cd Length: 291 Bit Score: 110.39 E-value: 1.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 172 KSALVKIFALSLVIeavNLLM---PVGTQLVMDHVIQAGDHNLLVIICVGLLFFILFRTCVSMFRSWISIVMGALIDIQW 248
Cdd:cd18586 1 RRVFVEVGLFSFFI---NLLAlapPIFMLQVYDRVLPSGSLSTLLGLTLGMVVLLAFDGLLRQVRSRILQRVGLRLDVEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 249 KSGLFDHLMKLPLayfEKRKLGDIQSRFGSLDAIRTTFTTSIVSSIIDGIMSVGVFIMMFMYGGWLVWVASGFTVLYVLL 328
Cdd:cd18586 78 GRRVFRAVLELPL---ESRPSGYWQQLLRDLDTLRNFLTGPSLFAFFDLPWAPLFLAVIFLIHPPLGWVALVGAPVLVGL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 329 RLSTYRYYRQASEEQLVKSAKASSHFMETLYSIATLKSLGLAGTRSQFWLNLNIDTANANIRVTKLDMFFGGVNAFLAAC 408
Cdd:cd18586 155 AWLNHRATRKPLGEANEAQAARDALAAETLRNAETIKALGMLGNLRRRWEARHAETLELQIRASDLAGAISAIGKTLRMA 234
|
250 260
....*....|....*....|....*..
gi 727181609 409 DQIVILWLGASLVIDSQMTLGMFVAFN 435
Cdd:cd18586 235 LQSLILGVGAYLVIDGELTIGALIAAS 261
|
|
| Peptidase_C39F |
cd02425 |
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
20-144 |
1.94e-26 |
|
A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family.
Pssm-ID: 239105 [Multi-domain] Cd Length: 126 Bit Score: 104.65 E-value: 1.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 20 VPQVLQTEAAECGLASLAMVCGYYGMHIDMLSMRQKFDISARGATLSSLIAIAENLNLKTRALSLSLDE-IHQVKRPCIL 98
Cdd:cd02425 1 VKPILQNNQTECGLACYAMILNYFGYKVSLNELREKYELGRDGLSLSYLKQLLEEYGFKCKVYKISFKKnLYPLKLPVII 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 727181609 99 HWDMNHFVVLVNIRGGRITLHDPAFGRRVIGLQEFSLHFTGIALEV 144
Cdd:cd02425 81 FWNNNHFVVLEKIKKNKVTIVDPAIGRIKISIDEFLENFSGYILTF 126
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
491-695 |
2.44e-26 |
|
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: 107.65 E-value: 2.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 491 FEVRDLLYQYDSLSrpVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLE-----PTEGRLFINGINIHDIGIN--N 563
Cdd:cd03260 1 IELRDLNVYYGDKH--ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDvlE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 564 YRECIACVLQEDKLLAGSIAENI--------CSFDAHPDTefIVE-CAKHCNIHDDIMKMPMGYEtlvgelggsLSGGQK 634
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVayglrlhgIKLKEELDE--RVEeALRKAALWDEVKDRLHALG---------LSGGQQ 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 727181609 635 QRVLIARALYRRPSILFMDEATSHLDLDNEKRVNEAISSLK--MTRVIIAHRPSTIAS-ADRVI 695
Cdd:cd03260 148 QRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKkeYTIVIVTHNMQQAARvADRTA 211
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
252-697 |
5.11e-26 |
|
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: 114.66 E-value: 5.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 252 LFDHLMKLPLAYFEKRKLGDIQSRFG-SLDAIrttftTSIVSSIIDGIMS-----VGVFIMMFMYGGWLVWVASGFTVLY 325
Cdd:TIGR00957 1044 LLHNKLRSPMSFFERTPSGNLVNRFSkELDTV-----DSMIPPVIKMFMGslfnvIGALIVILLATPIAAVIIPPLGLLY 1118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 326 VLLRlstyRYY----RQASEEQLVKSAKASSHFMETLYSIATLKslglAGTRSQFWLNLNIDTANANIRVTKLDMFfggV 401
Cdd:TIGR00957 1119 FFVQ----RFYvassRQLKRLESVSRSPVYSHFNETLLGVSVIR----AFEEQERFIHQSDLKVDENQKAYYPSIV---A 1187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 402 NAFLAACDQIV---ILWLGASLVIDSQMTL--GMFVAFNAYRGQFSDRASNLIDMVIRLRMLNLHNERLADivLSTTEEE 476
Cdd:TIGR00957 1188 NRWLAVRLECVgncIVLFAALFAVISRHSLsaGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKE--YSETEKE 1265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 477 KPYR-KICNPNEAV----TFEVRDLLYQYDSLSRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFI 551
Cdd:TIGR00957 1266 APWQiQETAPPSGWpprgRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIII 1345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 552 NGINIHDIGINNYRECIACVLQEDKLLAGSIAENICSFDAHPDTEfIVECAKHCNIHDDIMKMPMGYETLVGELGGSLSG 631
Cdd:TIGR00957 1346 DGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEE-VWWALELAHLKTFVSALPDKLDHECAEGGENLSV 1424
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 727181609 632 GQKQRVLIARALYRRPSILFMDEATSHLDLDNEKRVNEAISSL--KMTRVIIAHRPSTIASADRVITL 697
Cdd:TIGR00957 1425 GQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQfeDCTVLTIAHRLNTIMDYTRVIVL 1492
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
179-437 |
3.39e-25 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 106.34 E-value: 3.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 179 FALSLVIEAVNLLMPVGTQLVMDHVIQAG-DHNLLVIICVGLLFFILFRTCVSMFRSWISIVMGALIDIQWKSGLFDHLM 257
Cdd:cd18541 5 ILFLILVDLLQLLIPRIIGRAIDALTAGTlTASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFAHLL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 258 KLPLAYFEKRKLGDIQSRFGS-LDAIRTTFTTSIVSsIIDGI-MSVGVFIMMFMYGGWLVWVASGFTVL--YVLLRLST- 332
Cdd:cd18541 85 TLSPSFYQKNRTGDLMARATNdLNAVRMALGPGILY-LVDALfLGVLVLVMMFTISPKLTLIALLPLPLlaLLVYRLGKk 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 333 -YRYYRQASEEQlvksAKASSHFMETLYSIATLKSLGLAGTRSQFWLNLNIDTANANIRVTKLDMFFGGVNAFLAACDQI 411
Cdd:cd18541 164 iHKRFRKVQEAF----SDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFL 239
|
250 260
....*....|....*....|....*.
gi 727181609 412 VILWLGASLVIDSQMTLGMFVAFNAY 437
Cdd:cd18541 240 IVLWYGGRLVIRGTITLGDLVAFNSY 265
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
492-697 |
3.43e-25 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 112.04 E-value: 3.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDLLYQYDSLSR-PVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFIN-GINIHDIGINNYRECIA 569
Cdd:PTZ00265 384 QFKNVRFHYDTRKDvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdSHNLKDINLKWWRSKIG 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 570 CVLQEDKLLAGSIAENI-------------------------------------CSFDAH-------------------- 592
Cdd:PTZ00265 464 VVSQDPLLFSNSIKNNIkyslyslkdlealsnyynedgndsqenknkrnscrakCAGDLNdmsnttdsneliemrknyqt 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 593 -PDTEfIVECAKHCNIHDDIMKMPMGYETLVGELGGSLSGGQKQRVLIARALYRRPSILFMDEATSHLDLDNEKRVNEAI 671
Cdd:PTZ00265 544 iKDSE-VVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
|
250 260 270
....*....|....*....|....*....|
gi 727181609 672 SSLKMTR----VIIAHRPSTIASADRVITL 697
Cdd:PTZ00265 623 NNLKGNEnritIIIAHRLSTIRYANTIFVL 652
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
179-437 |
3.70e-25 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 105.98 E-value: 3.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 179 FALSLVIEAVNLLMPVGTQLVMDHVIQAGDHNLLVIICVGLLFFILFRTCVSMFRSWISIVMG--ALIDIqwKSGLFDHL 256
Cdd:cd18542 5 ILALLLATALNLLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASqkVAYDL--RNDLYDHL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 257 MKLPLAYFEKRKLGDIQSRFGS-LDAIRTTFTTSIVSSIIDGIMSVGVFIMMFMYGGWLVWVASGFT--VLYVLLRLST- 332
Cdd:cd18542 83 QRLSFSFHDKARTGDLMSRCTSdVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIpfIALFSYVFFKk 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 333 -YRYYRQASEEQlvksAKASSHFMETLYSIATLKSLGlagtRSQF----WLNLNIDTANANIRVTKLDMFFGGVNAFLAA 407
Cdd:cd18542 163 vRPAFEEIREQE----GELNTVLQENLTGVRVVKAFA----REDYeiekFDKENEEYRDLNIKLAKLLAKYWPLMDFLSG 234
|
250 260 270
....*....|....*....|....*....|
gi 727181609 408 CDQIVILWLGASLVIDSQMTLGMFVAFNAY 437
Cdd:cd18542 235 LQIVLVLWVGGYLVINGEITLGELVAFISY 264
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
484-695 |
4.67e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 105.46 E-value: 4.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 484 NPNEAVTFEVRDLLYQYDSLSRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINN 563
Cdd:PRK13632 1 IKNKSVMIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 564 YRECIACVLQE-DKLLAGS-----IA---ENICsFDAHPDTEFIVECAKHCNIHDDIMKMPmgyetlvgelgGSLSGGQK 634
Cdd:PRK13632 81 IRKKIGIIFQNpDNQFIGAtveddIAfglENKK-VPPKKMKDIIDDLAKKVGMEDYLDKEP-----------QNLSGGQK 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 727181609 635 QRVLIARALYRRPSILFMDEATSHLDLDNEKRVNEAISSLKMTR---VI-IAHRPSTIASADRVI 695
Cdd:PRK13632 149 QRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkktLIsITHDMDEAILADKVI 213
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
492-697 |
6.36e-25 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 104.02 E-value: 6.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDLLYQYDSlsRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDiginnYRECIACV 571
Cdd:COG1121 8 ELENLTVSYGG--RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR-----ARRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 572 LQ------------EDKLLAGSIAE-NICSFDAHPDTEFIVECAKHCNIhDDIMKMPM-----GyetlvgelggslsggQ 633
Cdd:COG1121 81 PQraevdwdfpitvRDVVLMGRYGRrGLFRRPSRADREAVDEALERVGL-EDLADRPIgelsgG---------------Q 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 727181609 634 KQRVLIARALYRRPSILFMDEATSHLDLDNEKRVNEAISSLK---MTRVIIAHRPSTIAS-ADRVITL 697
Cdd:COG1121 145 QQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRregKTILVVTHDLGAVREyFDRVLLL 212
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
492-697 |
6.82e-25 |
|
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: 103.00 E-value: 6.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDLLYQYDSlsRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIginnyRECIACV 571
Cdd:cd03235 1 EVEDLTVSYGG--HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 572 LQE---DKLLAGSIAENICS-FDAHPDTEFIVECAKHCNIhDDIMKMpMGYETLVGELGGSLSGGQKQRVLIARALYRRP 647
Cdd:cd03235 74 PQRrsiDRDFPISVRDVVLMgLYGHKGLFRRLSKADKAKV-DEALER-VGLSELADRQIGELSGGQQQRVLLARALVQDP 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 727181609 648 SILFMDEATSHLDLDNEKRVNEAISSLK---MTRVIIAHRPSTI-ASADRVITL 697
Cdd:cd03235 152 DLLLLDEPFAGVDPKTQEDIYELLRELRregMTILVVTHDLGLVlEYFDRVLLL 205
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
506-695 |
1.04e-24 |
|
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: 102.60 E-value: 1.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 506 PVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGInnYRECIACVLQEDKL---LagSI 582
Cdd:cd03259 14 RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPP--ERRNIGMVFQDYALfphL--TV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 583 AENIcsfdAHPDTEFIVECAKHCNIHDDIMKMpMGYETLVGELGGSLSGGQKQRVLIARALYRRPSILFMDEATSHLD-- 660
Cdd:cd03259 90 AENI----AFGLKLRGVPKAEIRARVRELLEL-VGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDak 164
|
170 180 190
....*....|....*....|....*....|....*...
gi 727181609 661 LDNEKR--VNEAISSLKMTRVIIAHRPSTIAS-ADRVI 695
Cdd:cd03259 165 LREELReeLKELQRELGITTIYVTHDQEEALAlADRIA 202
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
251-697 |
2.94e-24 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 109.06 E-value: 2.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 251 GLFDHLMKLPLAYFEKRKLGDIQSRF----GSLDairttfttsivssiidgiMSVGVFIMMFMyGGWLVWVASGFTVLYV 326
Cdd:PLN03130 991 AMLGSILRAPMSFFHTNPLGRIINRFakdlGDID------------------RNVAVFVNMFL-GQIFQLLSTFVLIGIV 1051
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 327 ------------LLRLSTYRYYRQASEEqlVK---SAKAS---SHFMETLYSIATLKSLglagtRSQFWL-NLNIDTANA 387
Cdd:PLN03130 1052 stislwaimpllVLFYGAYLYYQSTARE--VKrldSITRSpvyAQFGEALNGLSTIRAY-----KAYDRMaEINGRSMDN 1124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 388 NIRVTKLDMffgGVNAFLAACDQIV---ILWLGASLVI------------DSQMTLGMFVAFNAyrgqfsdraSNLIDMV 452
Cdd:PLN03130 1125 NIRFTLVNM---SSNRWLAIRLETLgglMIWLTASFAVmqngraenqaafASTMGLLLSYALNI---------TSLLTAV 1192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 453 IRLrmlnlhnERLADIVLSTTEEEKPYRKIcnPNEAVT----------------FEVRDLLYQYDSLSRPVIPGLSLQIA 516
Cdd:PLN03130 1193 LRL-------ASLAENSLNAVERVGTYIDL--PSEAPLviennrpppgwpssgsIKFEDVVLRYRPELPPVLHGLSFEIS 1263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 517 AGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINNYRECIACVLQEDKLLAGSIAENICSFDAHPDTE 596
Cdd:PLN03130 1264 PSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDAD 1343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 597 fIVECAKHCNIHDDIMKMPMGYETLVGELGGSLSGGQKQRVLIARALYRRPSILFMDEATSHLDLDN----EKRVNEAIS 672
Cdd:PLN03130 1344 -LWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTdaliQKTIREEFK 1422
|
490 500
....*....|....*....|....*
gi 727181609 673 SLKMtrVIIAHRPSTIASADRVITL 697
Cdd:PLN03130 1423 SCTM--LIIAHRLNTIIDCDRILVL 1445
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
492-698 |
6.03e-24 |
|
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: 106.14 E-value: 6.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDLLYQYDSLSRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPT---EGRLFINGINIHDIGINNYRECI 568
Cdd:COG1123 6 EVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRRI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 569 ACVLQE--DKLLAGSIAENICsfdahpdteFIVE--CAKHCNIHDDIMKM--PMGYETLVGELGGSLSGGQKQRVLIARA 642
Cdd:COG1123 86 GMVFQDpmTQLNPVTVGDQIA---------EALEnlGLSRAEARARVLELleAVGLERRLDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 727181609 643 LYRRPSILFMDEATSHLDLDNEKRVNEAISSLK----MTRVIIAHRPSTIAS-ADRVITLQ 698
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELQrergTTVLLITHDLGVVAEiADRVVVMD 217
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
492-697 |
7.52e-24 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 102.02 E-value: 7.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDLLYQYDSLSRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINNYRECIACV 571
Cdd:PRK13635 7 RVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGMV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 572 LQE-DKLLAGSIAENICSFDAH----PDTEfIVEcakhcNIHDDIMKMPMgyETLVGELGGSLSGGQKQRVLIARALYRR 646
Cdd:PRK13635 87 FQNpDNQFVGATVQDDVAFGLEnigvPREE-MVE-----RVDQALRQVGM--EDFLNREPHRLSGGQKQRVAIAGVLALQ 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 727181609 647 PSILFMDEATSHLDLDNEKRVNEAISSLK----MTRVIIAHRPSTIASADRVITL 697
Cdd:PRK13635 159 PDIIILDEATSMLDPRGRREVLETVRQLKeqkgITVLSITHDLDEAAQADRVIVM 213
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
505-698 |
7.71e-24 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 100.51 E-value: 7.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 505 RPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDI---GINNYRECIACVLQEDKLLAG- 580
Cdd:COG2884 15 REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrrEIPYLRRRIGVVFQDFRLLPDr 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 581 SIAENIcsfdahpdtEFIVECA--KHCNIHDDIM-------------KMPM---GYEtlvgelggslsggqKQRVLIARA 642
Cdd:COG2884 95 TVYENV---------ALPLRVTgkSRKEIRRRVRevldlvglsdkakALPHelsGGE--------------QQRVAIARA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 727181609 643 LYRRPSILFMDEATSHLDLDNEKRVN---EAISSLKMTrVIIA-HRPSTIASAD-RVITLQ 698
Cdd:COG2884 152 LVNRPELLLADEPTGNLDPETSWEIMellEEINRRGTT-VLIAtHDLELVDRMPkRVLELE 211
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
491-698 |
2.06e-23 |
|
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: 97.64 E-value: 2.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 491 FEVRDLLYQYDSlsRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINN--YRECI 568
Cdd:cd03229 1 LELKNVSKRYGQ--KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 569 ACVLQEDKLLAG-SIAENIcsfdAHPdtefivecakhcnihddimkMPMGyetlvgelggslsggQKQRVLIARALYRRP 647
Cdd:cd03229 79 GMVFQDFALFPHlTVLENI----ALG--------------------LSGG---------------QQQRVALARALAMDP 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 727181609 648 SILFMDEATSHLDLDNEKRVNEAISSLK----MTRVIIAHRPS-TIASADRVITLQ 698
Cdd:cd03229 120 DVLLLDEPTSALDPITRREVRALLKSLQaqlgITVVLVTHDLDeAARLADRVVVLR 175
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
492-698 |
2.50e-23 |
|
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: 99.55 E-value: 2.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDLLYQYDSlsRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHdIGINNYRECIACV 571
Cdd:COG4555 3 EVENLSKKYGK--VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVR-KEPREARRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 572 LQEDKLLAG-SIAENICSF---------DAHPDTEFIVECAKHCNIHDD-IMKMPMGyetlvgelggslsggQKQRVLIA 640
Cdd:COG4555 80 PDERGLYDRlTVRENIRYFaelyglfdeELKKRIEELIELLGLEEFLDRrVGELSTG---------------MKKKVALA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 727181609 641 RALYRRPSILFMDEATSHLDLDNEKRVNEAISSLKMTRVII---AHRPSTIAS-ADRVITLQ 698
Cdd:COG4555 145 RALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVlfsSHIMQEVEAlCDRVVILH 206
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
492-695 |
3.12e-23 |
|
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: 99.28 E-value: 3.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDLLYQYDSlsRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIG---INNYRECI 568
Cdd:COG1127 7 EVRNLTKSFGD--RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 569 ACVLQEDKLLAG-SIAENIcsfdAHPDTEF----------IV-ECAKHCNIHDDIMKMP------Mgyetlvgelggsls 630
Cdd:COG1127 85 GMLFQGGALFDSlTVFENV----AFPLREHtdlseaeireLVlEKLELVGLPGAADKMPselsggM-------------- 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 631 ggQKqRVLIARALYRRPSILFMDEATSHLDLDNEKRVNEAI----SSLKMTRVIIAHR-PSTIASADRVI 695
Cdd:COG1127 147 --RK-RVALARALALDPEILLYDEPTAGLDPITSAVIDELIrelrDELGLTSVVVTHDlDSAFAIADRVA 213
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
179-434 |
3.92e-23 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 100.19 E-value: 3.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 179 FALSLVIEAVNLLMPVGTQLVMDHVIQAGDHNLLVIICVGLLFFILFRTCVSMFRSWI--SIVMGALIDIQwkSGLFDHL 256
Cdd:cd18552 5 ILGMILVAATTAALAWLLKPLLDDIFVEKDLEALLLVPLAIIGLFLLRGLASYLQTYLmaYVGQRVVRDLR--NDLFDKL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 257 MKLPLAYFEKRKLGDIQSRFGS-LDAIRTTFTTSIVSSIIDGIMSVGVFIMMFmyggWLVWVASGFTVL------YVLLR 329
Cdd:cd18552 83 LRLPLSFFDRNSSGDLISRITNdVNQVQNALTSALTVLVRDPLTVIGLLGVLF----YLDWKLTLIALVvlplaaLPIRR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 330 LStyRYYRQASEEQLVKSAKASSHFMETLYSIATLKSLGLAGTRSQFWLNLNIDTANANIRVTKLDMFFGGVNAFLAACD 409
Cdd:cd18552 159 IG--KRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGAIA 236
|
250 260
....*....|....*....|....*
gi 727181609 410 QIVILWLGASLVIDSQMTLGMFVAF 434
Cdd:cd18552 237 IALVLWYGGYQVISGELTPGEFISF 261
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
492-699 |
4.39e-23 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 98.25 E-value: 4.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDLLYQYDSlsRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINNYRECIACV 571
Cdd:PRK10247 9 QLQNVGYLAGD--AKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 572 LQEDKLLAGSIAENICsF-----DAHPDTEFIVecakhcnihDDIMKMPMGyETLVGELGGSLSGGQKQRVLIARALYRR 646
Cdd:PRK10247 87 AQTPTLFGDTVYDNLI-FpwqirNQQPDPAIFL---------DDLERFALP-DTILTKNIAELSGGEKQRISLIRNLQFM 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 727181609 647 PSILFMDEATSHLDLDNEKRVNEAISSLKMTRVI----IAHRPSTIASADRVITLQP 699
Cdd:PRK10247 156 PKVLLLDEITSALDESNKHNVNEIIHRYVREQNIavlwVTHDKDEINHADKVITLQP 212
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
510-698 |
5.53e-23 |
|
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: 97.48 E-value: 5.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 510 GLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINI---HDIGINNYRECIACVLQEDKLLAG-SIAEN 585
Cdd:cd03292 19 GINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsdlRGRAIPYLRRKIGVVFQDFRLLPDrNVYEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 586 ICsfdahpdteFIVECAKHCniHDDIMK-MPMGYETLVGELGGSLSGGQ-----KQRVLIARALYRRPSILFMDEATSHL 659
Cdd:cd03292 99 VA---------FALEVTGVP--PREIRKrVPAALELVGLSHKHRALPAElsggeQQRVAIARAIVNSPTILIADEPTGNL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 727181609 660 DLDNEKRVNEAISSLKM--TRVIIAHRPSTIASA--DRVITLQ 698
Cdd:cd03292 168 DPDTTWEIMNLLKKINKagTTVVVATHAKELVDTtrHRVIALE 210
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
492-660 |
5.90e-23 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 99.01 E-value: 5.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDLLYQYDSL--SRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINnyrecIA 569
Cdd:COG1116 9 ELRGVSKRFPTGggGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD-----RG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 570 CVLQEDKLLA-GSIAENIcsfdahpdtEFIVECAK--HCNIHDDIMKM-------------P----MGyetlvgelggsl 629
Cdd:COG1116 84 VVFQEPALLPwLTVLDNV---------ALGLELRGvpKAERRERARELlelvglagfedayPhqlsGG------------ 142
|
170 180 190
....*....|....*....|....*....|.
gi 727181609 630 sggQKQRVLIARALYRRPSILFMDEATSHLD 660
Cdd:COG1116 143 ---MRQRVAIARALANDPEVLLMDEPFGALD 170
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
492-698 |
6.25e-23 |
|
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: 97.96 E-value: 6.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDLLYQY--DSLSRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIG---INNYRE 566
Cdd:cd03257 3 EVKNLSVSFptGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 567 CIACVLQE-----DKLLagSIAENIC-----SFDAHPDTEF---IVECAKHCNIHDDIMKM-PM----Gyetlvgelggs 628
Cdd:cd03257 83 EIQMVFQDpmsslNPRM--TIGEQIAeplriHGKLSKKEARkeaVLLLLVGVGLPEEVLNRyPHelsgG----------- 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 727181609 629 lsggQKQRVLIARALYRRPSILFMDEATSHLDLDNEKRVNEAISSLK----MTRVIIAHRPSTIAS-ADRVITLQ 698
Cdd:cd03257 150 ----QRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQeelgLTLLFITHDLGVVAKiADRVAVMY 220
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
179-450 |
9.80e-23 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 98.79 E-value: 9.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 179 FALSLVIEAVNLLMPVGTQLVMDHVIQAGDHNLLVIICVGLLFFILFRTCVSMFRSWISIVMGALIDIQWKSGLFDHLMK 258
Cdd:cd18557 2 LLFLLISSAAQLLLPYLIGRLIDTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 259 LPLAYFEKRKLGDIQSRFGS-LDAIRTTFTTSIVSSIIDGIMSVGVFIMMFmyggWLVWVASGFTVLYVLLRLSTY---- 333
Cdd:cd18557 82 QEIAFFDKHKTGELTSRLSSdTSVLQSAVTDNLSQLLRNILQVIGGLIILF----ILSWKLTLVLLLVIPLLLIASkiyg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 334 RYYRQASEEQLVKSAKASSHFMETLYSIATLKSLGLAGTRSQFWLNLNIDTANANIRVTKLDMFFGGVNAFLAACDQIVI 413
Cdd:cd18557 158 RYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLV 237
|
250 260 270
....*....|....*....|....*....|....*..
gi 727181609 414 LWLGASLVIDSQMTLGMFVAFNAYRGQFSDRASNLID 450
Cdd:cd18557 238 LWYGGYLVLSGQLTVGELTSFILYTIMVASSVGGLSS 274
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
178-699 |
1.17e-22 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 102.58 E-value: 1.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 178 IFALSLVIEAVNLLMPVGTQLVMDhVIQAGDH----NLLVIICVGLLFFILfrtcVSMFRSWISivmgALIDIQWKSGLF 253
Cdd:COG4178 30 LLLLTLASVGLNVLLNFWNRDFYD-ALQARDAaafwQQLGVFALLAAISIL----LAVYQTYLR----QRLQIRWREWLT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 254 DHLMKlplAYFEKRKLGDIQSRFGSLD--------AIR--TTFTTSIVSSIIDGIMSVGVFI---------MMFMYGGW- 313
Cdd:COG4178 101 ERLLD---RWLSNRAYYRLQLSGGEIDnpdqriaeDIRlfTETTLSLSLGLLSSVVTLISFIgilwslsgsLTFTLGGYs 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 314 ------LVWVAsgftVLYVLL-------------RLS--------TYRY----YRQASEeqlvksakasshfmetlySIA 362
Cdd:COG4178 178 itipgyMVWAA----LIYAIIgtllthligrpliRLNfeqqrreaDFRFalvrVRENAE------------------SIA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 363 TLKslGLAGTRSQFWLNLN--IDTANANIRVTKLDMFFGGVNAFLAacdQIVILWLGASLVIDSQMTLGMFV----AFNA 436
Cdd:COG4178 236 LYR--GEAAERRRLRRRFDavIANWRRLIRRQRNLTFFTTGYGQLA---VIFPILVAAPRYFAGEITLGGLMqaasAFGQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 437 YRGQFS------DRASNLIDMVIRLRMLNLHNERLAdivlsttEEEKPYRKICnPNEAVTFEVRDL-LYQYDSlsRPVIP 509
Cdd:COG4178 311 VQGALSwfvdnyQSLAEWRATVDRLAGFEEALEAAD-------ALPEAASRIE-TSEDGALALEDLtLRTPDG--RPLLE 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 510 GLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLfinginihdiginnYRECIACVL---QEDKLLAGSIAENI 586
Cdd:COG4178 381 DLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRI--------------ARPAGARVLflpQRPYLPLGTLREAL 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 587 C---SFDAHPDTEfIVECAKHCNIHDDI----------MKMPMGyetlvgelggslsggQKQRVLIARALYRRPSILFMD 653
Cdd:COG4178 447 LypaTAEAFSDAE-LREALEAVGLGHLAerldeeadwdQVLSLG---------------EQQRLAFARLLLHKPDWLFLD 510
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 727181609 654 EATSHLDLDNEKRVNEAI-SSLKMTRVI-IAHRPSTIASADRVITLQP 699
Cdd:COG4178 511 EATSALDEENEAALYQLLrEELPGTTVIsVGHRSTLAAFHDRVLELTG 558
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
492-697 |
1.95e-22 |
|
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: 95.79 E-value: 1.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDLLYQYDSLSRpVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDigiNNYRECIACV 571
Cdd:cd03226 1 RIENISFSYKKGTE-ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA---KERRKSIGYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 572 LQE--DKLLAGSIAENI-CSFDAHPDTEFIVECakhcnihddIMKMpMGYETLVGELGGSLSGGQKQRVLIARALYRRPS 648
Cdd:cd03226 77 MQDvdYQLFTDSVREELlLGLKELDAGNEQAET---------VLKD-LDLYALKERHPLSLSGGQKQRLAIAAALLSGKD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 727181609 649 ILFMDEATSHLDLDNEKRVNEAISSL---KMTRVIIAHRPSTIAS-ADRVITL 697
Cdd:cd03226 147 LLIFDEPTSGLDYKNMERVGELIRELaaqGKAVIVITHDYEFLAKvCDRVLLL 199
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
491-698 |
2.36e-22 |
|
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: 95.61 E-value: 2.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 491 FEVRDLLYQYDS---LSRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGinihdiginnyreC 567
Cdd:cd03250 1 ISVEDASFTWDSgeqETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 568 IACVLQEDKLLAGSIAENICsFDAHPDTEFIVECAKHCNIHDDIMKMPMGYETLVGELGGSLSGGQKQRVLIARALYRRP 647
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENIL-FGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 727181609 648 SILFMDEATSHLDLDNEKRV-NEAISSLKM---TRVIIAHRPSTIASADRVITLQ 698
Cdd:cd03250 147 DIYLLDDPLSAVDAHVGRHIfENCILGLLLnnkTRILVTHQLQLLPHADQIVVLD 201
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
504-699 |
2.73e-22 |
|
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: 94.14 E-value: 2.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 504 SRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRlfingINIHDiginnyRECIACVLQEDKLLAGSIA 583
Cdd:cd03223 13 GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGR-----IGMPE------GEDLLFLPQRPYLPLGTLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 584 ENICsfdaHP-DTEFivecakhcnihddimkmpmgyetlvgelggslSGGQKQRVLIARALYRRPSILFMDEATSHLDLD 662
Cdd:cd03223 82 EQLI----YPwDDVL--------------------------------SGGEQQRLAFARLLLHKPKFVFLDEATSALDEE 125
|
170 180 190
....*....|....*....|....*....|....*..
gi 727181609 663 NEKRVNEAISSLKMTRVIIAHRPSTIASADRVITLQP 699
Cdd:cd03223 126 SEDRLYQLLKELGITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
492-698 |
5.09e-22 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 95.64 E-value: 5.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDL--LYQYDSLSRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINNYRECIA 569
Cdd:COG1124 3 EVRNLsvSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 570 CVLQeD--------KLLAGSIAE--NICSFDAHPDTefIVECAKHCNIHDDIMKMPM-----GyetlvgelggslsggQK 634
Cdd:COG1124 83 MVFQ-DpyaslhprHTVDRILAEplRIHGLPDREER--IAELLEQVGLPPSFLDRYPhqlsgG---------------QR 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 727181609 635 QRVLIARALYRRPSILFMDEATSHLDLDNEKRVNEAISSLK----MTRVIIAHRPSTIAS-ADRVITLQ 698
Cdd:COG1124 145 QRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLReergLTYLFVSHDLAVVAHlCDRVAVMQ 213
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
510-697 |
6.50e-22 |
|
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: 92.88 E-value: 6.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 510 GLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHdigINNYREC----IACVLQedkllagsiaen 585
Cdd:cd03216 18 GVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS---FASPRDArragIAMVYQ------------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 586 icsfdahpdtefivecakhcnihddimkMPMGyetlvgelggslsggQKQRVLIARALYRRPSILFMDEATSHLDLDNEK 665
Cdd:cd03216 83 ----------------------------LSVG---------------ERQMVEIARALARNARLLILDEPTAALTPAEVE 119
|
170 180 190
....*....|....*....|....*....|....*.
gi 727181609 666 RVNEAISSLK---MTRVIIAHRPSTIAS-ADRVITL 697
Cdd:cd03216 120 RLFKVIRRLRaqgVAVIFISHRLDEVFEiADRVTVL 155
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
492-698 |
1.12e-21 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 94.98 E-value: 1.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDLLYQYDSLSRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINNYRECIACV 571
Cdd:cd03288 21 KIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSII 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 572 LQEDKLLAGSIAENI-----CSFDAhpdtefIVECAKHCNIHDDIMKMPMGYETLVGELGGSLSGGQKQRVLIARALYRR 646
Cdd:cd03288 101 LQDPILFSGSIRFNLdpeckCTDDR------LWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRK 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 727181609 647 PSILFMDEATSHLDLDNEKRVNEAISSLKMTR--VIIAHRPSTIASADRVITLQ 698
Cdd:cd03288 175 SSILIMDEATASIDMATENILQKVVMTAFADRtvVTIAHRVSTILDADLVLVLS 228
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
179-441 |
1.26e-21 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 95.63 E-value: 1.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 179 FALSLVIEAVNLLMPVGTQLVMDHVIQAGDHNLLVIICVGLLFFILFRTCVSMFRSWISIVMGALIDIQWKSGLFDHLMK 258
Cdd:cd18546 5 LLLVVVDTAASLAGPLLVRYGIDSGVRAGDLGVLLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 259 LPLAYFEKRKLGDIQSRFGS-LDAIRTTFTTSIVSSIIDGIMSVGVFIMMFMYGGWL-VWVASGFTVLYVLL----RLST 332
Cdd:cd18546 85 LSLDFHERETSGRIMTRMTSdIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLaLVALAALPPLALATrwfrRRSS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 333 yRYYRQASEEqlvkSAKASSHFMETLYSIATLKSLGL-AGTRSQFwLNLNIDTANANIRVTKL-DMFFGGVNaFLAACDQ 410
Cdd:cd18546 165 -RAYRRARER----IAAVNADLQETLAGIRVVQAFRReRRNAERF-AELSDDYRDARLRAQRLvAIYFPGVE-LLGNLAT 237
|
250 260 270
....*....|....*....|....*....|.
gi 727181609 411 IVILWLGASLVIDSQMTLGMFVAFNAYRGQF 441
Cdd:cd18546 238 AAVLLVGAWRVAAGTLTVGVLVAFLLYLRRF 268
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
175-441 |
1.29e-21 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 96.04 E-value: 1.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 175 LVKIFALSLVIEAVNLLMPVGTQLVMDHVIQAGDHNLLVIICVGLLFFILFRTCVSMFRSWISIVMGALIDIQWKSGLFD 254
Cdd:cd18564 16 LLEPWPLKVVIDDVLGDKPLPGLLGLAPLLGPDPLALLLLAAAALVGIALLRGLASYAGTYLTALVGQRVVLDLRRDLFA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 255 HLMKLPLAYFEKRKLGDIQSRF-GSLDAIRTTFTTSIVSSIIDGIMSVGVFIMMFmyggWLVW----VAsgFTVLYVLLr 329
Cdd:cd18564 96 HLQRLSLSFHDRRRTGDLLSRLtGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMF----WLDWqlalIA--LAVAPLLL- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 330 LSTYRYY---RQASEEQLVKSAKASSHFMETLYSIATLKSLGLAGTRSQFWLNLNIDTANANIRVTKLDMFFGGVNAFLA 406
Cdd:cd18564 169 LAARRFSrriKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFARENRKSLRAGLRAARLQALLSPVVDVLV 248
|
250 260 270
....*....|....*....|....*....|....*
gi 727181609 407 ACDQIVILWLGASLVIDSQMTLGMFVAFNAYRGQF 441
Cdd:cd18564 249 AVGTALVLWFGAWLVLAGRLTPGDLLVFLAYLKNL 283
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
481-697 |
1.63e-21 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 100.49 E-value: 1.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 481 KICNPNEAV-TFEVRDLLYQYdsLSRPVIP---GLSLQIAAGESVAIVGPSGVGKTTLMKLM------------------ 538
Cdd:PTZ00265 1155 RIKNKNDIKgKIEIMDVNFRY--ISRPNVPiykDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfkneh 1232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 539 -----------------CGLLEPTE-------------------GRLFINGINIHDIGINNYRECIACVLQEDKLLAGSI 582
Cdd:PTZ00265 1233 tndmtneqdyqgdeeqnVGMKNVNEfsltkeggsgedstvfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSI 1312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 583 AENICSFDAHPDTEFIVECAKHCNIHDDIMKMPMGYETLVGELGGSLSGGQKQRVLIARALYRRPSILFMDEATSHLDLD 662
Cdd:PTZ00265 1313 YENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSN 1392
|
250 260 270
....*....|....*....|....*....|....*....
gi 727181609 663 NEKRVNEAISSLK----MTRVIIAHRPSTIASADRVITL 697
Cdd:PTZ00265 1393 SEKLIEKTIVDIKdkadKTIITIAHRIASIKRSDKIVVF 1431
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
492-660 |
6.01e-21 |
|
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: 91.76 E-value: 6.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDLLYQYDSLSRP--VIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINI----HDIGInnyr 565
Cdd:cd03293 2 EVRNVSKTYGGGGGAvtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVtgpgPDRGY---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 566 eciacVLQEDKLLA-GSIAENIcsfdahpdtEFIVECAKHcnIHDDIMKMPMGYETLVGELGGSLSGG------QKQRVL 638
Cdd:cd03293 78 -----VFQQDALLPwLTVLDNV---------ALGLELQGV--PKAEARERAEELLELVGLSGFENAYPhqlsggMRQRVA 141
|
170 180
....*....|....*....|..
gi 727181609 639 IARALYRRPSILFMDEATSHLD 660
Cdd:cd03293 142 LARALAVDPDVLLLDEPFSALD 163
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
179-441 |
9.68e-21 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 93.22 E-value: 9.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 179 FALSLVIEAVNLLMPVGTQLVMDHVI--QAGDHNLLVIICVGLLFFILFRTCVSMFRSWISIVMGALI--DIqwKSGLFD 254
Cdd:cd18544 5 LLLLLLATALELLGPLLIKRAIDDYIvpGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIiyDL--RRDLFS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 255 HLMKLPLAYFEKRKLGDIQSRFGS-LDAIRTTFTTSIVSSIIDGIMSVGVFIMMFMYGGWLVWVAsgFTVLYVLLrLSTY 333
Cdd:cd18544 83 HIQRLPLSFFDRTPVGRLVTRVTNdTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALIS--LLVLPLLL-LATY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 334 ---RYYRQASEEQLVKSAKASSHFMETLYSIATLKSLGL-AGTRSQFwLNLNIDTANANIRVTKLDMFFGGVNAFLAACD 409
Cdd:cd18544 160 lfrKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNReKREFEEF-DEINQEYRKANLKSIKLFALFRPLVELLSSLA 238
|
250 260 270
....*....|....*....|....*....|..
gi 727181609 410 QIVILWLGASLVIDSQMTLGMFVAFNAYRGQF 441
Cdd:cd18544 239 LALVLWYGGGQVLSGAVTLGVLYAFIQYIQRF 270
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
175-440 |
1.03e-20 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 92.93 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 175 LVKIFALSLVIEAVNLLMPVGTQLVMDHVIQAGDHNLLVIICVGLLFFILFRTCVSMFRSWISIVMGALIDIQWKSGLFD 254
Cdd:cd18550 1 LALVLLLILLSALLGLLPPLLLREIIDDALPQGDLGLLVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 255 HLMKLPLAYFEKRKLGDIQSRFGS-LDAIRTTFTTSIVSSIIDGIMSVGVFIMMFMYgGWLVWVASgFTVLYVLLRLSTY 333
Cdd:cd18550 81 HLQRMSLAFFTRTRTGEIQSRLNNdVGGAQSVVTGTLTSVVSNVVTLVATLVAMLAL-DWRLALLS-LVLLPLFVLPTRR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 334 --RYYRQASEEQLVKSAKASSHFMETLySI--ATL-KSLGLAGTRSQFWLNLNIDTANANIRVTKLDMFFGGVNAFLAAC 408
Cdd:cd18550 159 vgRRRRKLTREQQEKLAELNSIMQETL-SVsgALLvKLFGREDDEAARFARRSRELRDLGVRQALAGRWFFAALGLFTAI 237
|
250 260 270
....*....|....*....|....*....|..
gi 727181609 409 DQIVILWLGASLVIDSQMTLGMFVAFNAYRGQ 440
Cdd:cd18550 238 GPALVYWVGGLLVIGGGLTIGTLVAFTALLGR 269
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
492-695 |
1.35e-20 |
|
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: 95.74 E-value: 1.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDLLYQYDSLSRPVIP---GLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIG---INNYR 565
Cdd:COG1123 262 EVRNLSKRYPVRGKGGVRavdDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLRELR 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 566 ECIACVLQ------------EDkllagSIAENICSFDAHPDTE---FIVECAKHCNIHDDIM-KMP----MGyetlvgel 625
Cdd:COG1123 342 RRVQMVFQdpysslnprmtvGD-----IIAEPLRLHGLLSRAErreRVAELLERVGLPPDLAdRYPhelsGG-------- 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 727181609 626 ggslsggQKQRVLIARALYRRPSILFMDEATSHLDLDNEKRVNEAISSLK----MTRVIIAHRPSTIAS-ADRVI 695
Cdd:COG1123 409 -------QRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQrelgLTYLFISHDLAVVRYiADRVA 476
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
492-697 |
2.00e-20 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 95.56 E-value: 2.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDLLYQYDSlSRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINNYRECIACV 571
Cdd:PRK10790 342 DIDNVSFAYRD-DNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 572 LQEDKLLAGSIAENIcSFDAHPDTEFIVECAKHCNIHDDIMKMPMGYETLVGELGGSLSGGQKQRVLIARALYRRPSILF 651
Cdd:PRK10790 421 QQDPVVLADTFLANV-TLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILI 499
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 727181609 652 MDEATSHLDLDNEKRVNEAISSL--KMTRVIIAHRPSTIASADRVITL 697
Cdd:PRK10790 500 LDEATANIDSGTEQAIQQALAAVreHTTLVVIAHRLSTIVEADTILVL 547
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
504-697 |
3.27e-20 |
|
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: 90.32 E-value: 3.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 504 SRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIG---INNYRECIACVLQEDKLLAG 580
Cdd:cd03256 13 GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkaLRQLRRQIGMIFQQFNLIER 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 581 -SIAENICS--FDAHP------------DTEFIVECAKHCNIHDDIMKMpmgyetlvgelGGSLSGGQKQRVLIARALYR 645
Cdd:cd03256 93 lSVLENVLSgrLGRRStwrslfglfpkeEKQRALAALERVGLLDKAYQR-----------ADQLSGGQQQRVAIARALMQ 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 727181609 646 RPSILFMDEATSHLDLDNEKRVNEAISSLKMTR---VIIA-HRPSTIAS-ADRVITL 697
Cdd:cd03256 162 QPKLILADEPVASLDPASSRQVMDLLKRINREEgitVIVSlHQVDLAREyADRIVGL 218
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
492-698 |
3.53e-20 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 90.19 E-value: 3.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDLLYQYDSLSRPV--IPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHD----------- 558
Cdd:COG4181 10 ELRGLTKTVGTGAGELtiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAldedararlra 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 559 --IGInnyreciacVLQEDKLLAGSIA-ENI---CSFDAHPD-----TEFIV-----ECAKHcnihddimkMPM---GYE 619
Cdd:COG4181 90 rhVGF---------VFQSFQLLPTLTAlENVmlpLELAGRRDararaRALLErvglgHRLDH---------YPAqlsGGE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 620 tlvgelggslsggqKQRVLIARALYRRPSILFMDEATSHLDLDNEKRVNEAISSLK----MTRVIIAHRPSTIASADRVI 695
Cdd:COG4181 152 --------------QQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNrergTTLVLVTHDPALAARCDRVL 217
|
...
gi 727181609 696 TLQ 698
Cdd:COG4181 218 RLR 220
|
|
| ABC_6TM_LapB_like |
cd18587 |
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ... |
171-433 |
3.56e-20 |
|
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), such as LapB. LapB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion, LapA is a RTX (repeats in toxin) protein found in Pseudomonas fluorescens and is required for biofilm formation in this organism. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. In this T1SS system, LapB is a cytoplasmic membrane-localized ATPase, LapC is a membrane fusion protein, and LapE is an outer membrane protein.
Pssm-ID: 350031 Cd Length: 293 Bit Score: 91.34 E-value: 3.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 171 LKSALVKIFALSlvieavnllMPVGTQLVMDHVIQAGDHNLLVIICVGLLFFILFRTCVSMFRSWISIVMGALIDIQWKS 250
Cdd:cd18587 9 LAALLINLFALA---------SPLFVMNVYDRVVPNNAIETLWVLAIGVLIALLFDFILKLLRAYFIDVAGKRADVILSS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 251 GLFDHLMKLPLAYfEKRKLGDIQSRFGSLDAIRTTFTTSIVSSIIDgIMSVGVFI-MMFMYGGWLVWVASGFTVLYVLLR 329
Cdd:cd18587 80 RLFERVLGLRLEA-RPASVGSFANNLREFESVRDFFTSATLTALID-LPFVLLFLaVIALIGGPLALVPLVAIPLVLLYG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 330 LSTYRYYRQASEEQLVKSAKASSHFMETLYSIATLKSLGLAGTRSQFWLNLNIDTANANIRVTKLDMFFGGVNAFLAACD 409
Cdd:cd18587 158 LLLQKPLRRLVEESMRESAQKNALLVESLSGLETIKALGAEGRMQRRWEEAVAALARSSLKSRLLSSSATNFAQFVQQLV 237
|
250 260
....*....|....*....|....
gi 727181609 410 QIVILWLGASLVIDSQMTLGMFVA 433
Cdd:cd18587 238 TVAIVIVGVYLISDGELTMGGLIA 261
|
|
| C39G |
COG3271 |
Predicted double-glycine leader peptidase, C39-like (CLD) domain [Intracellular trafficking, ... |
17-142 |
3.93e-20 |
|
Predicted double-glycine leader peptidase, C39-like (CLD) domain [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442502 [Multi-domain] Cd Length: 179 Bit Score: 88.51 E-value: 3.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 17 RRKVPQVLQTEAAECGLASLAMVCGY-YGMHIDMLS----MRQKFDISARGATLSSLIAIAENLNLKTRALSLSLDEIHQ 91
Cdd:COG3271 40 LRFRNVVRQQYDYSCGAAALATLLNYhYGRPVSEAEvlegMLTHGDQRRRGFSLLDMKRYLEALGLRADGYRLTLDDLAQ 119
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 727181609 92 VKRPCILHWDM---NHFVVLVNIRGGRITLHDPAFGRRVIGLQEFSLHFTGIAL 142
Cdd:COG3271 120 LGIPAIVLINLggyKHFVVVKGVDDGRVLLADPALGNRSLSREEFEKMWDGNVL 173
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
488-697 |
7.66e-20 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 87.99 E-value: 7.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 488 AVTFEVRDLLYQYDS----LSRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEP--TEGRLFINGINIHDigi 561
Cdd:cd03213 1 GVTLSFRNLTVTVKSspskSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLDK--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 562 NNYRECIACVLQEDKLLAG-SIAENIcSFDAHpdtefivecakhcnihddIMKMPMGyetlvgelggslsggQKQRVLIA 640
Cdd:cd03213 78 RSFRKIIGYVPQDDILHPTlTVRETL-MFAAK------------------LRGLSGG---------------ERKRVSIA 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 727181609 641 RALYRRPSILFMDEATSHLDLDNEKRVNEAISSL-KMTRVIIA--HRPST--IASADRVITL 697
Cdd:cd03213 124 LELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLaDTGRTIICsiHQPSSeiFELFDKLLLL 185
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
504-660 |
1.10e-19 |
|
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: 88.90 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 504 SRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINNYRECIACVLQEDKLLAG-SI 582
Cdd:cd03295 13 GKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYVIQQIGLFPHmTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 583 AENICSFDA--HPDTEFIVECAkhcnihDDIMKM-PMGYETLVGELGGSLSGGQKQRVLIARALYRRPSILFMDEATSHL 659
Cdd:cd03295 93 EENIALVPKllKWPKEKIRERA------DELLALvGLDPAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGAL 166
|
.
gi 727181609 660 D 660
Cdd:cd03295 167 D 167
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
175-442 |
1.95e-19 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 89.38 E-value: 1.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 175 LVKIFALSLVIEAVNLLMPVGTQLVMDHVIQAG------DHNLLVIICVGLLFFILFRTCVSMFRSWI--SIVMGALIDI 246
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEGLgggggvDFSGLLRILLLLLGLYLLSALFSYLQNRLmaRVSQRTVYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 247 QWKsgLFDHLMKLPLAYFEKRKLGDIQSRFGS-LDAIRTTFTTSIVSSIIDGIMSVGVFIMMFMYGGWLVWVASGFTVLY 325
Cdd:cd18547 81 RKD--LFEKLQRLPLSYFDTHSHGDIMSRVTNdVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 326 VLL--RLS--TYRYYRQaseeQLVKSAKASSHFMETLYSIATLKSLGL-AGTRSQFwLNLNIDTANANIRVTKLDMFFGG 400
Cdd:cd18547 159 LLVtkFIAkrSQKYFRK----QQKALGELNGYIEEMISGQKVVKAFNReEEAIEEF-DEINEELYKASFKAQFYSGLLMP 233
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 727181609 401 VNAFLAACDQIVILWLGASLVIDSQMTLGMFVAFNAYRGQFS 442
Cdd:cd18547 234 IMNFINNLGYVLVAVVGGLLVINGALTVGVIQAFLQYSRQFS 275
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
177-441 |
3.10e-19 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349993 [Multi-domain] Cd Length: 295 Bit Score: 88.66 E-value: 3.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 177 KIFAL----SLVIEAVNLLMPVGTQLVMDHVIQAGDHNLLVIICVGLLFFILFRTCVSMFRSWISIVMGALIDIQWKSGL 252
Cdd:cd18549 2 KLFFLdlfcAVLIAALDLVFPLIVRYIIDDLLPSKNLRLILIIGAILLALYILRTLLNYFVTYWGHVMGARIETDMRRDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 253 FDHLMKLPLAYFEKRKLGDIQSRFgsldairttftTSIVSSI------------IDGIMSVGVFIMMFMYGGWLVWVASG 320
Cdd:cd18549 82 FEHLQKLSFSFFDNNKTGQLMSRI-----------TNDLFDIselahhgpedlfISIITIIGSFIILLTINVPLTLIVFA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 321 FTVLYVLLRLSTYRYYRQASEEQLVKSAKASSHFMETLYSIATLKSLGLAGT-RSQFwlnlniDTANANIRVTKLDMF-- 397
Cdd:cd18549 151 LLPLMIIFTIYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYeIEKF------DEGNDRFLESKKKAYka 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 727181609 398 ---FGGVNAFLAACDQIVILWLGASLVIDSQMTLGMFVAFNAYRGQF 441
Cdd:cd18549 225 mayFFSGMNFFTNLLNLVVLVAGGYFIIKGEITLGDLVAFLLYVNVF 271
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
506-697 |
5.14e-19 |
|
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: 86.48 E-value: 5.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 506 PVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDI---GINNYRECIACVLQEDKLLAG-S 581
Cdd:cd03258 19 TALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLsgkELRKARRRIGMIFQHFNLLSSrT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 582 IAENIcsfdAHP------DTEFIVECAkhcnihDDIMKMpMGYETLVGELGGSLSGGQKQRVLIARALYRRPSILFMDEA 655
Cdd:cd03258 99 VFENV----ALPleiagvPKAEIEERV------LELLEL-VGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 727181609 656 TSHLD-------LDNEKRVNEaisSLKMTRVIIAHRPSTIAS-ADRVITL 697
Cdd:cd03258 168 TSALDpettqsiLALLRDINR---ELGLTIVLITHEMEVVKRiCDRVAVM 214
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
504-660 |
9.40e-19 |
|
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: 85.38 E-value: 9.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 504 SRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINNyREcIACVLQEDKLLAG-SI 582
Cdd:cd03301 12 NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD-RD-IAMVFQNYALYPHmTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 583 AENIcsfdAHP------DTEFIVECAKhcnihdDIMKMpMGYETLVGELGGSLSGGQKQRVLIARALYRRPSILFMDEAT 656
Cdd:cd03301 90 YDNI----AFGlklrkvPKDEIDERVR------EVAEL-LQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPL 158
|
....
gi 727181609 657 SHLD 660
Cdd:cd03301 159 SNLD 162
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
491-695 |
1.03e-18 |
|
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: 85.27 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 491 FEVRDLLYQYDSLsrPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINI--HDIGINNYRECI 568
Cdd:cd03262 1 IEIKNLHKSFGDF--HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 569 ACVLQedkllagsiaenicSFDAHPdtefivecakHCNIHDDIMKMPM-------------GYETLVGELGGSLSGG--- 632
Cdd:cd03262 79 GMVFQ--------------QFNLFP----------HLTVLENITLAPIkvkgmskaeaeerALELLEKVGLADKADAypa 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 727181609 633 -----QKQRVLIARALYRRPSILFMDEATSHLDLDNEKRVNEAISSL---KMTRVIIAHRPSTI-ASADRVI 695
Cdd:cd03262 135 qlsggQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLaeeGMTMVVVTHEMGFArEVADRVI 206
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
492-660 |
1.69e-18 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 87.44 E-value: 1.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDLLYQYDSlsRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINNyREcIACV 571
Cdd:COG3839 5 ELENVSKSYGG--VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD-RN-IAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 572 LQEDKL---LagSIAENIcsfdahpdtEF---------------IVECAKHCNIHDDIMKMPM----Gyetlvgelggsl 629
Cdd:COG3839 81 FQSYALyphM--TVYENI---------AFplklrkvpkaeidrrVREAAELLGLEDLLDRKPKqlsgG------------ 137
|
170 180 190
....*....|....*....|....*....|.
gi 727181609 630 sggQKQRVLIARALYRRPSILFMDEATSHLD 660
Cdd:COG3839 138 ---QRQRVALGRALVREPKVFLLDEPLSNLD 165
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
491-698 |
1.84e-18 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 85.49 E-value: 1.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 491 FEVRDLLYQYDSlSRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIG---INNYREC 567
Cdd:COG3638 3 LELRNLSKRYPG-GTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRgraLRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 568 IACVLQEDKL----------LAGSIAEN------ICSFDAHpDTEFIVECAKHCNIHDDIMKMPmgyETLvgelggslSG 631
Cdd:COG3638 82 IGMIFQQFNLvprlsvltnvLAGRLGRTstwrslLGLFPPE-DRERALEALERVGLADKAYQRA---DQL--------SG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 727181609 632 GQKQRVLIARALYRRPSILFMDEATSHLDLDNEKRVNEAISSL----KMTRVIIAHRPSTIAS-ADRVITLQ 698
Cdd:COG3638 150 GQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIaredGITVVVNLHQVDLARRyADRIIGLR 221
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
179-455 |
1.98e-18 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 86.06 E-value: 1.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 179 FALSLVIEAVNLLMPVGTQLVMDHVIQAGD-----HNLLVIICVGLLFFILfrtcvSMFRSWISIVMGALIDIQWKSGLF 253
Cdd:cd18572 2 FVFLVVAALSELAIPHYTGAVIDAVVADGSreafyRAVLLLLLLSVLSGLF-----SGLRGGCFSYAGTRLVRRLRRDLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 254 DHLMKLPLAYFEKRKLGDIQSRFGS-LDAIRTTFTTSIVSSIIDGIMSVGVFIMMFMYGGWLVWVAsgFTVLYVLLRLST 332
Cdd:cd18572 77 RSLLRQDIAFFDATKTGELTSRLTSdCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLA--FITVPVIALITK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 333 Y--RYYRQASEEQLVKSAKASSHFMETLYSIATLKSLGLAGT---RSQFWLNlniDTANANIRVTKLDMFFGGVNAFLAA 407
Cdd:cd18572 155 VygRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEERearRYERALD---KALKLSVRQALAYAGYVAVNTLLQN 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 727181609 408 CDQIVILWLGASLVIDSQMTLGMFVAFNAYRGQFSDRASNLIDMVIRL 455
Cdd:cd18572 232 GTQVLVLFYGGHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSL 279
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
512-695 |
1.98e-18 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 84.81 E-value: 1.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 512 SLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGInnYRECIACVLQEDKLLAG-SIAENICsFD 590
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP--AERPVSMLFQENNLFPHlTVAQNIG-LG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 591 AHPD---TEF----IVECAKHCNIHDDIMKMPmgyETLvgelggslSGGQKQRVLIARALYRRPSILFMDEATSHLD--L 661
Cdd:COG3840 96 LRPGlklTAEqraqVEQALERVGLAGLLDRLP---GQL--------SGGQRQRVALARCLVRKRPILLLDEPFSALDpaL 164
|
170 180 190
....*....|....*....|....*....|....*..
gi 727181609 662 DNE--KRVNEAISSLKMTRVIIAHRPSTIAS-ADRVI 695
Cdd:COG3840 165 RQEmlDLVDELCRERGLTVLMVTHDPEDAARiADRVL 201
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
511-697 |
1.98e-18 |
|
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: 84.47 E-value: 1.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 511 LSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINnyRECIACVLQEDKLLAgsiaenicsfd 590
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFA----------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 591 aHPDTEFIVECAKHCNIH---DDIMKMP-----MGYETLVGELGGSLSGGQKQRVLIARALYRRPSILFMDEATSHLD-- 660
Cdd:cd03298 84 -HLTVEQNVGLGLSPGLKltaEDRQAIEvalarVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDpa 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 727181609 661 LDNE--KRVNEAISSLKMTRVIIAHRPSTIAS-ADRVITL 697
Cdd:cd03298 163 LRAEmlDLVLDLHAETKMTVLMVTHQPEDAKRlAQRVVFL 202
|
|
| Peptidase_C39_like |
cd02259 |
Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The ... |
25-142 |
2.13e-18 |
|
Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is not conserved in all sub-families.
Pssm-ID: 239073 [Multi-domain] Cd Length: 122 Bit Score: 81.66 E-value: 2.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 25 QTEAAECGLASLAMVCGYYGMHIDMLSMRQKFDISARGATLSSLIAIAENLNLKTRALSLSLDEIHQVKRPCILHWDMNH 104
Cdd:cd02259 1 GGGPLDCGLACLQMLLRYFGIPVRRDVLLNAQQRRQQGLSLADLVSLANKLGLTAQGVKLPLAALSRLQLPALLLWKQGH 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 727181609 105 FVVLVNIRGGRITLHDPAF-GRRVIGLQEFSLHFTGIAL 142
Cdd:cd02259 81 FVILYGADKGQVLIADPLEeGPVTLSESELEERWTGHWV 119
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
495-664 |
2.50e-18 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 84.63 E-value: 2.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 495 DLLYQYDSLsrPVipGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINnyRECIACVLQE 574
Cdd:PRK10771 6 DITWLYHHL--PM--RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 575 DKLLAG-SIAENIcSFDAHPDTEfiVECAKHCNIHDdiMKMPMGYETLVGELGGSLSGGQKQRVLIARALYRRPSILFMD 653
Cdd:PRK10771 80 NNLFSHlTVAQNI-GLGLNPGLK--LNAAQREKLHA--IARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLD 154
|
170
....*....|...
gi 727181609 654 EATSHLD--LDNE 664
Cdd:PRK10771 155 EPFSALDpaLRQE 167
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
179-437 |
4.46e-18 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 85.23 E-value: 4.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 179 FALSLVIEAVNLLMPVGTQLVMDHVIQAGDHNLLVIICVGLLFFILFRTCVSMFRSWISIVMGALIDIQWKSGLFDHLMK 258
Cdd:cd18543 5 LLAALLATLAGLAIPLLTRRAIDGPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFAHLQR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 259 LPLAYFEKRKLGDIQSRFGS-LDAIRTtFTTSIVSSIIDGIMSVGVFIMMFMYGGWL-VWVASGFTVLYVLLRLSTYRYY 336
Cdd:cd18543 85 LDGAFHDRWQSGQLLSRATSdLSLVQR-FLAFGPFLLGNLLTLVVGLVVMLVLSPPLaLVALASLPPLVLVARRFRRRYF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 337 RQASEEQlVKSAKASSHFMETLYSIATLKSLGlagtRSQFWLNLNIDTAN----ANIRVTKLDMFFGGVNAFLAACDQIV 412
Cdd:cd18543 164 PASRRAQ-DQAGDLATVVEESVTGIRVVKAFG----RERRELDRFEAAARrlraTRLRAARLRARFWPLLEALPELGLAA 238
|
250 260
....*....|....*....|....*
gi 727181609 413 ILWLGASLVIDSQMTLGMFVAFNAY 437
Cdd:cd18543 239 VLALGGWLVANGSLTLGTLVAFSAY 263
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
492-697 |
6.15e-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: 83.44 E-value: 6.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDLLYQYDSlsRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGInnYRECIACV 571
Cdd:cd03300 2 ELENVSKFYGG--FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPP--HKRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 572 LQEDKLLAG-SIAENICsFD---AHPDTEFIVECAKhcnihdDIMKMpMGYETLVGELGGSLSGGQKQRVLIARALYRRP 647
Cdd:cd03300 78 FQNYALFPHlTVFENIA-FGlrlKKLPKAEIKERVA------EALDL-VQLEGYANRKPSQLSGGQQQRVAIARALVNEP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 727181609 648 SILFMDEATSHLDLDNEKRVNEAISSLK----MTRVIIAHRPS-TIASADRVITL 697
Cdd:cd03300 150 KVLLLDEPLGALDLKLRKDMQLELKRLQkelgITFVFVTHDQEeALTMSDRIAVM 204
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
492-661 |
1.11e-17 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 85.15 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDLLYQYDSlsRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINNyREcIACV 571
Cdd:COG3842 7 ELENVSKRYGD--VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEK-RN-VGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 572 LQEDKL---LagSIAENIC---SFDAHPDTEfivecakhcnIHDDIMKM-------------PM----Gyetlvgelggs 628
Cdd:COG3842 83 FQDYALfphL--TVAENVAfglRMRGVPKAE----------IRARVAELlelvglegladryPHqlsgG----------- 139
|
170 180 190
....*....|....*....|....*....|...
gi 727181609 629 lsggQKQRVLIARALYRRPSILFMDEATSHLDL 661
Cdd:COG3842 140 ----QQQRVALARALAPEPRVLLLDEPLSALDA 168
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
252-572 |
2.06e-17 |
|
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: 86.01 E-value: 2.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 252 LFDHLMKLPLAYFEKRKLGDIQSRFGS-LDAIrTTFTTSIVSSIIDGIMSVGVFImmfmYGGWLVWVASGFTVLYVLLRL 330
Cdd:COG4615 87 LSRRILAAPLERLERIGAARLLAALTEdVRTI-SQAFVRLPELLQSVALVLGCLA----YLAWLSPPLFLLTLVLLGLGV 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 331 STYRYYRQASEEQLVKSAKASSHFMETLYSI-ATLKSLGLAGTRSQFWLNLNIDTANANIR--VTKLDMFFGGVNA---- 403
Cdd:COG4615 162 AGYRLLVRRARRHLRRAREAEDRLFKHFRALlEGFKELKLNRRRRRAFFDEDLQPTAERYRdlRIRADTIFALANNwgnl 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 404 -FLAAcdqI-VILWLGASLVIDSQMTLGMFVAFNAY-RGQFSdrasNLIDMVIRLRMLNLHNERLADIVLSTTEEEKPYR 480
Cdd:COG4615 242 lFFAL---IgLILFLLPALGWADPAVLSGFVLVLLFlRGPLS----QLVGALPTLSRANVALRKIEELELALAAAEPAAA 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 481 KICNPNEAVTF---EVRDLLYQYDSL--SRPVIPG-LSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGI 554
Cdd:COG4615 315 DAAAPPAPADFqtlELRGVTYRYPGEdgDEGFTLGpIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQ 394
|
330
....*....|....*...
gi 727181609 555 NIHDIGINNYRECIACVL 572
Cdd:COG4615 395 PVTADNREAYRQLFSAVF 412
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
179-452 |
3.43e-17 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 82.58 E-value: 3.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 179 FALSLVIEAVNLLMPVGTQLVMDHV-IQAGDHNLLVIICVGLLFFILFRTCVSMFRSWISIVMG--ALIDIQWKsgLFDH 255
Cdd:cd18778 5 LLCALLSTLLGLVPPWLIRELVDLVtIGSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEqkVVADLRSD--LYDK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 256 LMKLPLAYFEKRKLGDIQSRFGSlDAirTTFTTSIVSSIIDGIMS----VGVFIMMFmyggWLVWVASGFT------VLY 325
Cdd:cd18778 83 LQRLSLRYFDDRQTGDLMSRVIN-DV--ANVERLIADGIPQGITNvltlVGVAIILF----SINPKLALLTlipipfLAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 326 VLLRLSTY--RYYRQASEEqlvkSAKASSHFMETLYSIATLKSLGLAGTRSQFWLNLNIDTANANIRVTKLDMFFGGVNA 403
Cdd:cd18778 156 GAWLYSKKvrPRYRKVREA----LGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPLME 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 727181609 404 FLAACDQIVILWLGASLVIDSQMTLGMFVAFNAYRGQFSD---RASNLIDMV 452
Cdd:cd18778 232 FLTSLGTVLVLGFGGRLVLAGELTIGDLVAFLLYLGLFYEpitSLHGLNEML 283
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
511-698 |
4.86e-17 |
|
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: 83.24 E-value: 4.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 511 LSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHD----IGINNYRECIACVLQEDKLLAG-SIAEN 585
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgIFLPPEKRRIGYVFQEARLFPHlSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 586 IC--SFDAHPDTEFIVEcakhcnihDDIMKMpMGYETLVGELGGSLSGGQKQRVLIARALYRRPSILFMDEATSHLDldn 663
Cdd:TIGR02142 96 LRygMKRARPSERRISF--------ERVIEL-LGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD--- 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 727181609 664 EKRVNEAI-------SSLKMTRVIIAHRPSTIAS-ADRVITLQ 698
Cdd:TIGR02142 164 DPRKYEILpylerlhAEFGIPILYVSHSLQEVLRlADRVVVLE 206
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
492-698 |
5.21e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 81.70 E-value: 5.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDLLYQYDS-LSRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINNYRECIAC 570
Cdd:PRK13650 6 EVKNLTFKYKEdQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 571 VLQE-DKLLAGSIAENICSFD------AHPD-TEFIVECAKHCNIHDDIMKMPmgyetlvgelgGSLSGGQKQRVLIARA 642
Cdd:PRK13650 86 VFQNpDNQFVGATVEDDVAFGlenkgiPHEEmKERVNEALELVGMQDFKEREP-----------ARLSGGQKQRVAIAGA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 643 LYRRPSILFMDEATSHLDLDNEKRVNEAISSLK----MTRVIIAHRPSTIASADRVITLQ 698
Cdd:PRK13650 155 VAMRPKIIILDEATSMLDPEGRLELIKTIKGIRddyqMTVISITHDLDEVALSDRVLVMK 214
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
492-695 |
6.10e-17 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 80.81 E-value: 6.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDLLYQYDSLsrPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIG--INNYRECIA 569
Cdd:COG1126 3 EIENLHKSFGDL--EVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKkdINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 570 CVLQEDKL---LagSIAENIC---------SFDAhpdtefIVECAKHC----NIHDDIMKMPM----Gyetlvgelggsl 629
Cdd:COG1126 81 MVFQQFNLfphL--TVLENVTlapikvkkmSKAE------AEERAMELlervGLADKADAYPAqlsgG------------ 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 727181609 630 sggQKQRVLIARALYRRPSILFMDEATSHLDLDNEKRVNEAISSL---KMTRVIIAH-----RpstiASADRVI 695
Cdd:COG1126 141 ---QQQRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLakeGMTMVVVTHemgfaR----EVADRVV 207
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
510-694 |
6.90e-17 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 82.43 E-value: 6.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 510 GLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDI---GINNYRECIACVLQEDKLLAG-SIAEN 585
Cdd:COG1135 23 DVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALserELRAARRKIGMIFQHFNLLSSrTVAEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 586 IcsfdAHPdtefiVECAKhcnihddimkMPM-----------------------------GyetlvgelggslsggQKQR 636
Cdd:COG1135 103 V----ALP-----LEIAG----------VPKaeirkrvaellelvglsdkadaypsqlsgG---------------QKQR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 727181609 637 VLIARALYRRPSILFMDEATSHLD-------LDNEKRVNEaisSLKMTRVIIAHRPSTIAS-ADRV 694
Cdd:COG1135 149 VGIARALANNPKVLLCDEATSALDpettrsiLDLLKDINR---ELGLTIVLITHEMDVVRRiCDRV 211
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
511-695 |
1.53e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 80.48 E-value: 1.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 511 LSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGIN--NYRECIACVLQ--EDKLLAGSIAENI 586
Cdd:PRK13637 26 VNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKlsDIRKKVGLVFQypEYQLFEETIEKDI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 587 cSFDahpdtefivecAKHCNIHDD--------IMKM-PMGYETLVGELGGSLSGGQKQRVLIARALYRRPSILFMDEATS 657
Cdd:PRK13637 106 -AFG-----------PINLGLSEEeienrvkrAMNIvGLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTA 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 727181609 658 HLDLDNEKRVNEAISSL----KMTRVIIAHRPSTIAS-ADRVI 695
Cdd:PRK13637 174 GLDPKGRDEILNKIKELhkeyNMTIILVSHSMEDVAKlADRII 216
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
506-698 |
1.58e-16 |
|
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: 80.67 E-value: 1.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 506 PVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGInihdiginnyrecIACVLQEDKLLAGSIAEN 585
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSWIMPGTIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 586 I---CSFDAHPDTEFIvecaKHCNIHDDIMKMPMGYETLVGELGGSLSGGQKQRVLIARALYRRPSILFMDEATSHLDLD 662
Cdd:cd03291 118 IifgVSYDEYRYKSVV----KACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVF 193
|
170 180 190
....*....|....*....|....*....|....*....
gi 727181609 663 NEKRVNEAISSLKM---TRVIIAHRPSTIASADRVITLQ 698
Cdd:cd03291 194 TEKEIFESCVCKLMankTRILVTSKMEHLKKADKILILH 232
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
492-697 |
1.80e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 80.18 E-value: 1.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDLLYQYDSLSRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINNYRECIACV 571
Cdd:PRK13648 9 VFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 572 LQE-DKLLAGSIAENICSFD------AHPDTEFIVECAkhcnIHDDIMKMPMGYETlvgelgGSLSGGQKQRVLIARALY 644
Cdd:PRK13648 89 FQNpDNQFVGSIVKYDVAFGlenhavPYDEMHRRVSEA----LKQVDMLERADYEP------NALSGGQKQRVAIAGVLA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 727181609 645 RRPSILFMDEATSHLDLDNEKRVNEAISSLK----MTRVIIAHRPSTIASADRVITL 697
Cdd:PRK13648 159 LNPSVIILDEATSMLDPDARQNLLDLVRKVKsehnITIISITHDLSEAMEADHVIVM 215
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
506-698 |
2.07e-16 |
|
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: 78.91 E-value: 2.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 506 PVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINNY----RECIACVLQEDKLLAGS 581
Cdd:cd03290 15 ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATrsrnRYSVAYAAQKPWLLNAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 582 IAENIcSFDAHPDTEFIVECAKHCNIHDDIMKMPMGYETLVGELGGSLSGGQKQRVLIARALYRRPSILFMDEATSHLDL 661
Cdd:cd03290 95 VEENI-TFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDI 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 727181609 662 D-NEKRVNEAISSL----KMTRVIIAHRPSTIASADRVITLQ 698
Cdd:cd03290 174 HlSDHLMQEGILKFlqddKRTLVLVTHKLQYLPHADWIIAMK 215
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
492-683 |
2.17e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 79.70 E-value: 2.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDLLYQYDSlsRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLE-----PTEGRLFINGINIHD--IGINNY 564
Cdd:PRK14258 9 KVNNLSFYYDT--QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNIYErrVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 565 RECIACVLQEDKLLAGSIAENICS----FDAHPDTEF--IVECA-KHCNIHDDImkmpmgyETLVGELGGSLSGGQKQRV 637
Cdd:PRK14258 87 RRQVSMVHPKPNLFPMSVYDNVAYgvkiVGWRPKLEIddIVESAlKDADLWDEI-------KHKIHKSALDLSGGQQQRL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 727181609 638 LIARALYRRPSILFMDEATSHLDLDNEKRVNEAISSLK----MTRVIIAH 683
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrseLTMVIVSH 209
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
411-695 |
2.90e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 82.57 E-value: 2.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 411 IVILWLGASLVIDSQ-----------MTLGMF-------VAFNaYRGQF---SDRASNLIdmvirlrmlnlhnERLADIV 469
Cdd:PRK11160 260 VLMLWLAAGGVGGNAqpgalialfvfAALAAFealmpvaGAFQ-HLGQViasARRINEIT-------------EQKPEVT 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 470 LSTTEEEKPyrkicnpnEAVTFEVRDLLYQYDSLSRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRL 549
Cdd:PRK11160 326 FPTTSTAAA--------DQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEI 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 550 FINGINIHDIGINNYRECIACVLQEDKLLAGSIAENIcsfdahpdtefivECAKHcNIHDDIMK---MPMGYETLVGELG 626
Cdd:PRK11160 398 LLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNL-------------LLAAP-NASDEALIevlQQVGLEKLLEDDK 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 627 GSLSGG----------QKQRVLIARALYRRPSILFMDEATSHLDLDNEKRVNEAISSL---KmTRVIIAHRPSTIASADR 693
Cdd:PRK11160 464 GLNAWLgeggrqlsggEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHaqnK-TVLMITHRLTGLEQFDR 542
|
..
gi 727181609 694 VI 695
Cdd:PRK11160 543 IC 544
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
485-683 |
4.26e-16 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 78.54 E-value: 4.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 485 PNEAVTFEVRDL-LYqYDSlsRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGL--LEP---TEGRLFINGINIHD 558
Cdd:COG1117 6 STLEPKIEVRNLnVY-YGD--KQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPgarVEGEILLDGEDIYD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 559 IGINNY--RECIACVLQEDKLLAGSIAENIcsfdAHP----------DTEFIVE-CAKHCNIHDDI--------MKMPMG 617
Cdd:COG1117 83 PDVDVVelRRRVGMVFQKPNPFPKSIYDNV----AYGlrlhgiksksELDEIVEeSLRKAALWDEVkdrlkksaLGLSGG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 727181609 618 yetlvgelggslsggQKQRVLIARALYRRPSILFMDEATSHLDLDNEKRVNEAISSLK--MTRVIIAH 683
Cdd:COG1117 159 ---------------QQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKkdYTIVIVTH 211
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
256-660 |
5.51e-16 |
|
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: 82.65 E-value: 5.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 256 LMKLPLAYFEKRKLGDIQSRFGSLDAIRTTFTTSIVSSIIDGIMSV-GVFIMMFMYGGWLVWVASGFTVLYVLLRLstyr 334
Cdd:TIGR01271 968 VLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVlGAIFVVSVLQPYIFIAAIPVAVIFIMLRA---- 1043
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 335 YYRQASEE--QLVKSAKAS--SHFMETLYSIATLKSLGLAGT-RSQFWLNLNIDTANANIRVTKLdmffggvNAFLAACD 409
Cdd:TIGR01271 1044 YFLRTSQQlkQLESEARSPifSHLITSLKGLWTIRAFGRQSYfETLFHKALNLHTANWFLYLSTL-------RWFQMRID 1116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 410 QIVILWLGASLVI------DSQMTLGMFVAFNA-YRGQFS----------------DRASNLIDMVIRL-RMLNLHNERL 465
Cdd:TIGR01271 1117 IIFVFFFIAVTFIaigtnqDGEGEVGIILTLAMnILSTLQwavnssidvdglmrsvSRVFKFIDLPQEEpRPSGGGGKYQ 1196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 466 ADIVLSTteeEKPYRKICNPNEAvTFEVRDLLYQYDSLSRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEpT 545
Cdd:TIGR01271 1197 LSTVLVI---ENPHAQKCWPSGG-QMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-T 1271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 546 EGRLFINGINIHDIGINNYRECIACVLQEDKLLAGSIAENICSFDAHPDTEfIVECAKHCNIHDDIMKMPMGYETLVGEL 625
Cdd:TIGR01271 1272 EGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEE-IWKVAEEVGLKSVIEQFPDKLDFVLVDG 1350
|
410 420 430
....*....|....*....|....*....|....*
gi 727181609 626 GGSLSGGQKQRVLIARALYRRPSILFMDEATSHLD 660
Cdd:TIGR01271 1351 GYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLD 1385
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
175-434 |
6.44e-16 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 78.63 E-value: 6.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 175 LVKIFALSLVIEAVNLLMPVGTQLVMDHVIQAGDHNLLVIICVGLLFFILFRTCVSMF---RSWISIVMGAlidiqwKSG 251
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLIDALSAGGSSGGLLALLVALFLLQAVLSALSSYllgRTGERVVLDL------RRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 252 LFDHLMKLPLAYFEKRKLGDIQSRFGSlDA--IRTTFTTSIVSSIIDGIMSVGVFIMMFmyggWLVW---------VASG 320
Cdd:cd18551 75 LWRRLLRLPVSFFDRRRSGDLVSRVTN-DTtlLRELITSGLPQLVTGVLTVVGAVVLMF----LLDWvltlvtlavVPLA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 321 FTVLYVLLRLsTYRYYRQASEEQlvksAKASSHFMETLYSIATLKSLGlAGTRSQFWLNLNIDTA-NANIRVTKLDMFFG 399
Cdd:cd18551 150 FLIILPLGRR-IRKASKRAQDAL----GELSAALERALSAIRTVKASN-AEERETKRGGEAAERLyRAGLKAAKIEALIG 223
|
250 260 270
....*....|....*....|....*....|....*
gi 727181609 400 GVNAFLAACDQIVILWLGASLVIDSQMTLGMFVAF 434
Cdd:cd18551 224 PLMGLAVQLALLVVLGVGGARVASGALTVGTLVAF 258
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
491-698 |
7.85e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 78.21 E-value: 7.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 491 FEVRDLLYQYDSLSR-PVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINNYRECIA 569
Cdd:PRK13642 5 LEVENLVFKYEKESDvNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 570 CVLQE-DKLLAGSIAENICSFDAH----PDTEFIV---ECAKHCNIHDDIMKMPmgyetlvgelgGSLSGGQKQRVLIAR 641
Cdd:PRK13642 85 MVFQNpDNQFVGATVEDDVAFGMEnqgiPREEMIKrvdEALLAVNMLDFKTREP-----------ARLSGGQKQRVAVAG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 727181609 642 ALYRRPSILFMDEATSHLDLDNEKRVNEAISSLK----MTRVIIAHRPSTIASADRVITLQ 698
Cdd:PRK13642 154 IIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKekyqLTVLSITHDLDEAASSDRILVMK 214
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
509-697 |
9.77e-16 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 76.56 E-value: 9.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 509 PGLSLQIA---AGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHD----IGINNYRECIACVLQEDKLLAG- 580
Cdd:cd03297 11 PDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrkkINLPPQQRKIGLVFQQYALFPHl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 581 SIAENIC----SFDAHPDTEFIVEcakhcnihddiMKMPMGYETLVGELGGSLSGGQKQRVLIARALYRRPSILFMDEAT 656
Cdd:cd03297 91 NVRENLAfglkRKRNREDRISVDE-----------LLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPF 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 727181609 657 SHLD----LDNEKRVNEAISSLKMTRVIIAHRPSTIAS-ADRVITL 697
Cdd:cd03297 160 SALDralrLQLLPELKQIKKNLNIPVIFVTHDLSEAEYlADRIVVM 205
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
505-702 |
1.01e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 76.45 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 505 RPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGiniHDIGINNYRECIACVLQEDKL-LAGSIA 583
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG---GDIDDPDVAEACHYLGHRNAMkPALTVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 584 ENIcSFDAH---PDTEFIVECAKHCNIHdDIMKMPMGYetlvgelggsLSGGQKQRVLIARAL-YRRPsILFMDEATSHL 659
Cdd:PRK13539 92 ENL-EFWAAflgGEELDIAAALEAVGLA-PLAHLPFGY----------LSAGQKRRVALARLLvSNRP-IWILDEPTAAL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 727181609 660 DLDNEKRVNEAISS-LKMTRVIIA--HRPSTIASAdRVITLQPVNA 702
Cdd:PRK13539 159 DAAAVALFAELIRAhLAQGGIVIAatHIPLGLPGA-RELDLGPFAA 203
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
507-703 |
1.27e-15 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 78.99 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 507 VIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINNYRECIacVLQEDKLLAG-SIAEN 585
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICM--VFQSYALFPHmSLGEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 586 I---CSFDAHPDTEfIVECAKHCNIHDDIMKMPMGYETLVgelggslSGGQKQRVLIARALYRRPSILFMDEATSHLDLD 662
Cdd:PRK11432 99 VgygLKMLGVPKEE-RKQRVKEALELVDLAGFEDRYVDQI-------SGGQQQRVALARALILKPKVLLFDEPLSNLDAN 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 727181609 663 NEKRVNEAISSLK----MTRVIIAHRPS-TIASADRVITLQPVNAM 703
Cdd:PRK11432 171 LRRSMREKIRELQqqfnITSLYVTHDQSeAFAVSDTVIVMNKGKIM 216
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
492-661 |
1.75e-15 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 76.69 E-value: 1.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDLLYQYDSlsRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINNYRECIAcV 571
Cdd:COG4559 3 EAENLSVRLGG--RTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRA-V 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 572 LQEDKLLA-----------GSIAeniCSFDAHPDTEFIVECAKHCNIHDdimkmpMG---YETLvgelggslSGGQKQRV 637
Cdd:COG4559 80 LPQHSSLAfpftveevvalGRAP---HGSSAAQDRQIVREALALVGLAH------LAgrsYQTL--------SGGEQQRV 142
|
170 180 190
....*....|....*....|....*....|.
gi 727181609 638 LIARAL-------YRRPSILFMDEATSHLDL 661
Cdd:COG4559 143 QLARVLaqlwepvDGGPRWLFLDEPTSALDL 173
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
181-434 |
1.99e-15 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 77.14 E-value: 1.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 181 LSLVIEAV-NLLMPVGTQLVMDHVIQAGDHNLLVIICVGLLFFILFRTCVSMFRSWISIVMGALI--DIqwKSGLFDHLM 257
Cdd:cd18575 3 IALLIAAAaTLALGQGLRLLIDQGFAAGNTALLNRAFLLLLAVALVLALASALRFYLVSWLGERVvaDL--RKAVFAHLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 258 KLPLAYFEKRKLGDIQSRFGSlDA--IRTTFTTSIVSSIIDGIMSVGVFIMMFmyggWLVWVASGFTVL---YVLLRLST 332
Cdd:cd18575 81 RLSPSFFETTRTGEVLSRLTT-DTtlIQTVVGSSLSIALRNLLLLIGGLVMLF----ITSPKLTLLVLLvipLVVLPIIL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 333 Y-RYYRQASEEQLVKSAKASSHFMETLYSIATLKSLGLAGTRSQFWLNLNIDTANANIRVTKLDMFFGGVNAFLAACDQI 411
Cdd:cd18575 156 FgRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIV 235
|
250 260
....*....|....*....|...
gi 727181609 412 VILWLGASLVIDSQMTLGMFVAF 434
Cdd:cd18575 236 FVLWLGAHDVLAGRMSAGELSQF 258
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
492-683 |
2.15e-15 |
|
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: 75.87 E-value: 2.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDLLYQYDSLSrpVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGiniHDI--GINNYRECIA 569
Cdd:cd03265 2 EVENLVKKYGDFE--AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAG---HDVvrEPREVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 570 CVLQE---DKLLAGSiaENICSFDA------HPDTEFIVECAKHCNIHDDIMKMPMGYETlvgelggslsgGQKQRVLIA 640
Cdd:cd03265 77 IVFQDlsvDDELTGW--ENLYIHARlygvpgAERRERIDELLDFVGLLEAADRLVKTYSG-----------GMRRRLEIA 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 727181609 641 RALYRRPSILFMDEATSHLDLDNEKRVNEAISSLK----MTRVIIAH 683
Cdd:cd03265 144 RSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKeefgMTILLTTH 190
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
490-695 |
3.10e-15 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 75.94 E-value: 3.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 490 TFEVRDLLYQYDSlsRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIH-DIGINNYRECI 568
Cdd:PRK11264 3 AIEVKNLVKKFHG--QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDtARSLSQQKGLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 569 ACVLQEdkllAGSIAENICSFDAHPDTEFIVECAKHCNIHDDIMKMPMGYETLVGELGGSLSGG--------QKQRVLIA 640
Cdd:PRK11264 81 RQLRQH----VGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSyprrlsggQQQRVAIA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 727181609 641 RALYRRPSILFMDEATSHLDLDNEKRVNEAISSL---KMTRVIIAHRPSTIAS-ADRVI 695
Cdd:PRK11264 157 RALAMRPEVILFDEPTSALDPELVGEVLNTIRQLaqeKRTMVIVTHEMSFARDvADRAI 215
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
507-667 |
3.51e-15 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 75.80 E-value: 3.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 507 VIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIG---INNYRECIACVLQEDKLLAG-SI 582
Cdd:TIGR02315 17 ALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRgkkLRKLRRRIGMIFQHYNLIERlTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 583 AENICS--FDAHP------------DTEFIVECAKHCNIHDdimkmpmgyetLVGELGGSLSGGQKQRVLIARALYRRPS 648
Cdd:TIGR02315 97 LENVLHgrLGYKPtwrsllgrfseeDKERALSALERVGLAD-----------KAYQRADQLSGGQQQRVAIARALAQQPD 165
|
170
....*....|....*....
gi 727181609 649 ILFMDEATSHLDLDNEKRV 667
Cdd:TIGR02315 166 LILADEPIASLDPKTSKQV 184
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
512-694 |
4.45e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 78.52 E-value: 4.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 512 SLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGiniHDIGINNYREC----IACVLQEDKLLAG-SIAENI 586
Cdd:COG1129 24 SLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDG---EPVRFRSPRDAqaagIAIIHQELNLVPNlSVAENI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 587 CsFDAHPDTEFIV----------ECAKHCNIHDD----IMKMPMGyetlvgelggslsggQKQRVLIARALYRRPSILFM 652
Cdd:COG1129 101 F-LGREPRRGGLIdwramrrrarELLARLGLDIDpdtpVGDLSVA---------------QQQLVEIARALSRDARVLIL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 727181609 653 DEATSHLDLDNEKRVNEAISSLK---MTRVIIAHRPSTIAS-ADRV 694
Cdd:COG1129 165 DEPTASLTEREVERLFRIIRRLKaqgVAIIYISHRLDEVFEiADRV 210
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
489-558 |
4.55e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 75.58 E-value: 4.55e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 489 VTFEVRDLLYQYDSlsRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHD 558
Cdd:PRK13548 1 AMLEARNLSVRLGG--RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLAD 68
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
492-673 |
4.57e-15 |
|
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: 74.45 E-value: 4.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDLLYQYDSlsRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINNYRECIACV 571
Cdd:cd03231 2 EADELTCERDG--RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 572 LQEDKLLAGSIAENICSFDAHPDTEFIVECAKHCNIHddimkmpmGYETLVgelGGSLSGGQKQRVLIARALYRRPSILF 651
Cdd:cd03231 80 HAPGIKTTLSVLENLRFWHADHSDEQVEEALARVGLN--------GFEDRP---VAQLSAGQQRRVALARLLLSGRPLWI 148
|
170 180
....*....|....*....|..
gi 727181609 652 MDEATSHLDLDNEKRVNEAISS 673
Cdd:cd03231 149 LDEPTTALDKAGVARFAEAMAG 170
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
506-698 |
5.55e-15 |
|
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: 79.18 E-value: 5.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 506 PVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGInihdiginnyrecIACVLQEDKLLAGSIAEN 585
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPGTIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 586 I---CSFDAHPDTEFIvecaKHCNIHDDIMKMPMGYETLVGELGGSLSGGQKQRVLIARALYRRPSILFMDEATSHLDLD 662
Cdd:TIGR01271 507 IifgLSYDEYRYTSVI----KACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVV 582
|
170 180 190
....*....|....*....|....*....|....*....
gi 727181609 663 NEKRVNEAISSLKM---TRVIIAHRPSTIASADRVITLQ 698
Cdd:TIGR01271 583 TEKEIFESCLCKLMsnkTRILVTSKLEHLKKADKILLLH 621
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
510-694 |
7.56e-15 |
|
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: 74.68 E-value: 7.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 510 GLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIgiNNYRECIACVLQEDKLLAG-SIAENIcs 588
Cdd:cd03299 17 NVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNL--PPEKRDISYVPQNYALFPHmTVYKNI-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 589 fdahpdtEF--IVECAKHCNIHDDIMKMP--MGYETLVGELGGSLSGGQKQRVLIARALYRRPSILFMDEATSHLDLDNE 664
Cdd:cd03299 93 -------AYglKKRKVDKKEIERKVLEIAemLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTK 165
|
170 180 190
....*....|....*....|....*....|....*
gi 727181609 665 KRVNE----AISSLKMTRVIIAHRPSTIAS-ADRV 694
Cdd:cd03299 166 EKLREelkkIRKEFGVTVLHVTHDFEEAWAlADKV 200
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
492-697 |
9.54e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 75.12 E-value: 9.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDLLYQY----DSLSRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIG-INNYRE 566
Cdd:PRK13633 6 KCKNVSYKYesneESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDIRN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 567 CIACVLQE-DKLLAGSIAENICSFDAH-----PDT--EFIVECAKHCNIHDDIMKMPmgyetlvgelgGSLSGGQKQRVL 638
Cdd:PRK13633 86 KAGMVFQNpDNQIVATIVEEDVAFGPEnlgipPEEirERVDESLKKVGMYEYRRHAP-----------HLLSGGQKQRVA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 727181609 639 IARALYRRPSILFMDEATSHLDLDNEKRVNEAISSLK----MTRVIIAHRPSTIASADRVITL 697
Cdd:PRK13633 155 IAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNkkygITIILITHYMEEAVEADRIIVM 217
|
|
| Peptidase_C39G |
cd02423 |
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
23-144 |
1.30e-14 |
|
A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family of proteins with a single peptidase domain, which are lacking the nucleotide-binding transporter signature.
Pssm-ID: 239103 [Multi-domain] Cd Length: 129 Bit Score: 70.76 E-value: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 23 VLQTEAAECGLASLA-MVCGYYGMHIDMLSMRQKFDISARGATLSSLIAIAENLNLKTRALSLSLDEIHQVKRPCI---L 98
Cdd:cd02423 4 VRQSYDFSCGPAALAtLLRYYGGINITEQEVLKLMLIRSEGFSMLDLKRYAEALGLKANGYRLNLDKLNALQIPVIvlvN 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 727181609 99 HWDMNHFVVLVNIRGGRITLHDPAFGRRVIGLQEFSLHFTGIALEV 144
Cdd:cd02423 84 NGGYGHFVVIKGIDGDRVLVGDPALGNISMSREEFERIWTGNALFV 129
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
504-695 |
1.61e-14 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 73.94 E-value: 1.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 504 SRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIginnyRECIACVLQEDKLLA-GSI 582
Cdd:PRK11247 24 ERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA-----REDTRLMFQDARLLPwKKV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 583 AENI---CSFDAHPDTEFIVECakhcnihddimkmpMGYETLVGELGGSLSGGQKQRVLIARALYRRPSILFMDEATSHL 659
Cdd:PRK11247 99 IDNVglgLKGQWRDAALQALAA--------------VGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGAL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 727181609 660 DLDNEKRVNEAISSL----KMTRVIIAHRPS-TIASADRVI 695
Cdd:PRK11247 165 DALTRIEMQDLIESLwqqhGFTVLLVTHDVSeAVAMADRVL 205
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
493-662 |
1.73e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 76.64 E-value: 1.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 493 VRDLLYQYDSlsRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINginihdigiNNYRecIACVL 572
Cdd:COG0488 1 LENLSKSFGG--RPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP---------KGLR--IGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 573 QEDKLLAG-SIAENIcsFDAHPDTEFIVEcakhcNIHDDIMKMPMGYETLVGELGGSLSGG------------------- 632
Cdd:COG0488 68 QEPPLDDDlTVLDTV--LDGDAELRALEA-----ELEELEAKLAEPDEDLERLAELQEEFEalggweaearaeeilsglg 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 727181609 633 ----------------QKQRVLIARALYRRPSILFMDEATSHLDLD 662
Cdd:COG0488 141 fpeedldrpvselsggWRRRVALARALLSEPDLLLLDEPTNHLDLE 186
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
487-697 |
2.19e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 74.11 E-value: 2.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 487 EAVTFEVRDLLYQYDSLSRpVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFING--INIHDIGINNY 564
Cdd:PRK13636 2 EDYILKVEELNYNYSDGTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 565 RECIACVLQ--EDKLLAGSIAENIcSFDAH----PDTEfivecakhcnIH---DDIMKMpMGYETLVGELGGSLSGGQKQ 635
Cdd:PRK13636 81 RESVGMVFQdpDNQLFSASVYQDV-SFGAVnlklPEDE----------VRkrvDNALKR-TGIEHLKDKPTHCLSFGQKK 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 727181609 636 RVLIARALYRRPSILFMDEATSHLD----LDNEKRVNEAISSLKMTRVIIAHRPSTIA-SADRVITL 697
Cdd:PRK13636 149 RVAIAGVLVMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKELGLTIIIATHDIDIVPlYCDNVFVM 215
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
488-678 |
2.82e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 75.26 E-value: 2.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 488 AVTFEVRDLLYQYDSLsrPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINNYREC 567
Cdd:PRK09536 1 MPMIDVSDLSVEFGDT--TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 568 IACVLQEDKLlagsiaenicSFDAhpDTEFIVECAKHCNI-----HDD----IMKMPM---GYETLVGELGGSLSGGQKQ 635
Cdd:PRK09536 79 VASVPQDTSL----------SFEF--DVRQVVEMGRTPHRsrfdtWTEtdraAVERAMertGVAQFADRPVTSLSGGERQ 146
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 727181609 636 RVLIARALYRRPSILFMDEATSHLDldnekrVNEAISSLKMTR 678
Cdd:PRK09536 147 RVLLARALAQATPVLLLDEPTASLD------INHQVRTLELVR 183
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
492-694 |
3.00e-14 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 74.45 E-value: 3.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDLLYQYDSLSRPVIP--GLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINI---HDIGINNYRE 566
Cdd:PRK11153 3 ELKNISKVFPQGGRTIHAlnNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtalSEKELRKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 567 CIACVLQEDKLLAG-SIAENIcsfdAHP------DTEFI----------VECAKHcniHDdimKMPM----Gyetlvgel 625
Cdd:PRK11153 83 QIGMIFQHFNLLSSrTVFDNV----ALPlelagtPKAEIkarvtellelVGLSDK---AD---RYPAqlsgG-------- 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 727181609 626 ggslsggQKQRVLIARALYRRPSILFMDEATSHLD-------LDNEKRVNEaisSLKMTRVIIAHRPSTIAS-ADRV 694
Cdd:PRK11153 145 -------QKQRVAIARALASNPKVLLCDEATSALDpattrsiLELLKDINR---ELGLTIVLITHEMDVVKRiCDRV 211
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
490-660 |
3.03e-14 |
|
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: 72.76 E-value: 3.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 490 TFEVRDLLYQYDSLsrPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINNyREcIA 569
Cdd:cd03296 2 SIEVRNVSKRFGDF--VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE-RN-VG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 570 CVLQEDKLLAG-SIAENIcSF--DAHPDTEFIVECAKHCNIHdDIMKMpMGYETLVGELGGSLSGGQKQRVLIARALYRR 646
Cdd:cd03296 78 FVFQHYALFRHmTVFDNV-AFglRVKPRSERPPEAEIRAKVH-ELLKL-VQLDWLADRYPAQLSGGQRQRVALARALAVE 154
|
170
....*....|....
gi 727181609 647 PSILFMDEATSHLD 660
Cdd:cd03296 155 PKVLLLDEPFGALD 168
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
504-695 |
3.27e-14 |
|
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: 72.75 E-value: 3.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 504 SRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGInNYRECIACVLQEDKLLAGSI- 582
Cdd:cd03267 33 EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRK-KFLRRIGVVFGQKTQLWWDLp 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 583 -AENIcSFDAH----PDTEFIVECAKHCNIHD--DIMKMPMGYETLvgelggslsgGQKQRVLIARALYRRPSILFMDEA 655
Cdd:cd03267 112 vIDSF-YLLAAiydlPPARFKKRLDELSELLDleELLDTPVRQLSL----------GQRMRAEIAAALLHEPEILFLDEP 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 727181609 656 TSHLDLDNEKRVNEAISSL----KMTRVIIAHRPSTIAS-ADRVI 695
Cdd:cd03267 181 TIGLDVVAQENIRNFLKEYnrerGTTVLLTSHYMKDIEAlARRVL 225
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
492-697 |
3.45e-14 |
|
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: 72.47 E-value: 3.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDLLYQYDSLSrpVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINI-----HDI---GI-- 561
Cdd:cd03219 2 EVRGLTKRFGGLV--ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDItglppHEIarlGIgr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 562 -----NNY-----RECIACVLQEDKLLAGSIAENICSFDAHPDTefIVECAKHCNIhDDIMKMPMGyeTLvgelggslSG 631
Cdd:cd03219 80 tfqipRLFpeltvLENVMVAAQARTGSGLLLARARREEREARER--AEELLERVGL-ADLADRPAG--EL--------SY 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 632 GQKQRVLIARALYRRPSILFMDEATSHLDLDNEKRVNEAISSLK---MTRVIIAHRPSTIAS-ADRVITL 697
Cdd:cd03219 147 GQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRergITVLLVEHDMDVVMSlADRVTVL 216
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
492-683 |
3.95e-14 |
|
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: 70.17 E-value: 3.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDLLYQYDSlsRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLfinginIHDIGINnyrecIACV 571
Cdd:cd03221 2 ELENLSKTYGG--KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV------TWGSTVK-----IGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 572 LQedklLAGsiaenicsfdahpdtefivecakhcnihddimkmpmGyetlvgelggslsggQKQRVLIARALYRRPSILF 651
Cdd:cd03221 69 EQ----LSG------------------------------------G---------------EKMRLALAKLLLENPNLLL 93
|
170 180 190
....*....|....*....|....*....|..
gi 727181609 652 MDEATSHLDLDNEKRVNEAISSLKMTRVIIAH 683
Cdd:cd03221 94 LDEPTNHLDLESIEALEEALKEYPGTVILVSH 125
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
512-659 |
4.85e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 75.06 E-value: 4.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 512 SLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHdigINNYRECIAC----VLQEDKLLAG-SIAENI 586
Cdd:COG3845 25 SLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVR---IRSPRDAIALgigmVHQHFMLVPNlTVAENI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 587 C-----SFDAHPDT----EFIVECAKHCNIHDD----IMKMPMGyetlvgelggslsggQKQRVLIARALYRRPSILFMD 653
Cdd:COG3845 102 VlglepTKGGRLDRkaarARIRELSERYGLDVDpdakVEDLSVG---------------EQQRVEILKALYRGARILILD 166
|
....*.
gi 727181609 654 EATSHL 659
Cdd:COG3845 167 EPTAVL 172
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
491-662 |
4.95e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 75.10 E-value: 4.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 491 FEVRDLLYQYDSlsRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFInGINIHdIGinnY----RE 566
Cdd:COG0488 316 LELEGLSKSYGD--KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK-IG---YfdqhQE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 567 ciacVLQEDKllagSIAENICsfDAHPDTEfivecakhcNIH------------DDIMK----MPMGyetlvgelggsls 630
Cdd:COG0488 389 ----ELDPDK----TVLDELR--DGAPGGT---------EQEvrgylgrflfsgDDAFKpvgvLSGG------------- 436
|
170 180 190
....*....|....*....|....*....|..
gi 727181609 631 ggQKQRVLIARALYRRPSILFMDEATSHLDLD 662
Cdd:COG0488 437 --EKARLALAKLLLSPPNVLLLDEPTNHLDIE 466
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
504-660 |
6.21e-14 |
|
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: 71.53 E-value: 6.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 504 SRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEP---TEGRLFINGINIHdigINNYRECIACVLQEDKLLAG 580
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRK---PDQFQKCVAYVRQDDILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 581 -SIAENI----------CSFDAHPDTEFIVECAKHCN---IHDDIMKMPMGYEtlvgelggslsggqKQRVLIARALYRR 646
Cdd:cd03234 96 lTVRETLtytailrlprKSSDAIRKKRVEDVLLRDLAltrIGGNLVKGISGGE--------------RRRVSIAVQLLWD 161
|
170
....*....|....
gi 727181609 647 PSILFMDEATSHLD 660
Cdd:cd03234 162 PKVLILDEPTSGLD 175
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
506-696 |
7.78e-14 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 71.66 E-value: 7.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 506 PVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHD--IGINNYRECIACVLQEDKLLAGSIA 583
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkVDERLIRQEAGMVFQQFYLFPHLTA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 584 -ENICSFDAHpdtefiVECAKHCNIHDDIMKM--PMGYETLVGELGGSLSGGQKQRVLIARALYRRPSILFMDEATSHLD 660
Cdd:PRK09493 95 lENVMFGPLR------VRGASKEEAEKQARELlaKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALD 168
|
170 180 190
....*....|....*....|....*....|....*....
gi 727181609 661 --LDNEK-RVNEAISSLKMTRVIIAHRpstIASADRVIT 696
Cdd:PRK09493 169 peLRHEVlKVMQDLAEEGMTMVIVTHE---IGFAEKVAS 204
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
492-660 |
1.25e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 71.65 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDLLYQYDSLSRpVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFING--INIHDIGINNYRECIA 569
Cdd:PRK13639 3 ETRDLKYSYPDGTE-ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepIKYDKKSLLEVRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 570 CVLQ--EDKLLAGSIAENIcSFD------AHPDTEFIVEcakhcnihDDIMKMPM-GYETlvgELGGSLSGGQKQRVLIA 640
Cdd:PRK13639 82 IVFQnpDDQLFAPTVEEDV-AFGplnlglSKEEVEKRVK--------EALKAVGMeGFEN---KPPHHLSGGQKKRVAIA 149
|
170 180
....*....|....*....|
gi 727181609 641 RALYRRPSILFMDEATSHLD 660
Cdd:PRK13639 150 GILAMKPEIIVLDEPTSGLD 169
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
486-697 |
1.28e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 71.75 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 486 NEAVTFevRDLLYQYDSLSRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEP---TEGRLFINGINIHDIGIN 562
Cdd:PRK13640 3 DNIVEF--KHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 563 NYRECIACVLQE-DKLLAGSIAENICSFD----AHPDTEFIvecakhcNIHDDIMKmPMGYETLVGELGGSLSGGQKQRV 637
Cdd:PRK13640 81 DIREKVGIVFQNpDNQFVGATVGDDVAFGlenrAVPRPEMI-------KIVRDVLA-DVGMLDYIDSEPANLSGGQKQRV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 727181609 638 LIARALYRRPSILFMDEATSHLDLDNEKRVNEAISSLK----MTRVIIAHRPSTIASADRVITL 697
Cdd:PRK13640 153 AIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKkknnLTVISITHDIDEANMADQVLVL 216
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
491-697 |
1.31e-13 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 73.06 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 491 FEVRDLLYQYDSlsRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDI-----GIN--- 562
Cdd:PRK09452 15 VELRGISKSFDG--KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVpaenrHVNtvf 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 563 -NY--------RECIACVLQEDKLLAGSIAENIcsFDAhpdtefivecakhcnihddiMKMpMGYETLVGELGGSLSGGQ 633
Cdd:PRK09452 93 qSYalfphmtvFENVAFGLRMQKTPAAEITPRV--MEA--------------------LRM-VQLEEFAQRKPHQLSGGQ 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 727181609 634 KQRVLIARALYRRPSILFMDEATSHLDLDNEKRVNEAISSLK----MTRVIIAH-RPSTIASADRVITL 697
Cdd:PRK09452 150 QQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQrklgITFVFVTHdQEEALTMSDRIVVM 218
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
491-699 |
1.34e-13 |
|
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: 71.27 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 491 FEVRDLLYQYDSlsRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEG---RLF---INGINIHDIginny 564
Cdd:COG1119 4 LELRNVTVRRGG--KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvRLFgerRGGEDVWEL----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 565 RECIACV---LQEDKLLAGSIAENICS--FDA-----HPDTEfIVECAkhcnihDDIMKMpMGYETLVGELGGSLSGGQK 634
Cdd:COG1119 77 RKRIGLVspaLQLRFPRDETVLDVVLSgfFDSiglyrEPTDE-QRERA------RELLEL-LGLAHLADRPFGTLSQGEQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 635 QRVLIARALYRRPSILFMDEATSHLDLDNEKRVNEAISSL----KMTRVIIAHRPSTIASA-DRVITLQP 699
Cdd:COG1119 149 RRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLaaegAPTLVLVTHHVEEIPPGiTHVLLLKD 218
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
498-661 |
1.39e-13 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 71.64 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 498 YQYDSLSRP-----VIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDI---GINNYRECIA 569
Cdd:PRK10419 13 YAHGGLSGKhqhqtVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraQRKAFRRDIQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 570 CVLQED-------KLLAGSIAE---NICSFDAHPDTEFIVECAKHCNIHDDIM-KMPmgyetlvgelgGSLSGGQKQRVL 638
Cdd:PRK10419 93 MVFQDSisavnprKTVREIIREplrHLLSLDKAERLARASEMLRAVDLDDSVLdKRP-----------PQLSGGQLQRVC 161
|
170 180
....*....|....*....|...
gi 727181609 639 IARALYRRPSILFMDEATSHLDL 661
Cdd:PRK10419 162 LARALAVEPKLLILDEAVSNLDL 184
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
490-660 |
1.41e-13 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 71.43 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 490 TFEVRDLLYQYDSL--SRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINNyrec 567
Cdd:COG4525 3 MLTVRHVSVRYPGGgqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 568 iACVLQEDKLLAG-SIAENIcsfdahpdtEFI-----VECAKHCNIHDDIMKMpMGYETLVGELGGSLSGGQKQRVLIAR 641
Cdd:COG4525 79 -GVVFQKDALLPWlNVLDNV---------AFGlrlrgVPKAERRARAEELLAL-VGLADFARRRIWQLSGGMRQRVGIAR 147
|
170
....*....|....*....
gi 727181609 642 ALYRRPSILFMDEATSHLD 660
Cdd:COG4525 148 ALAADPRFLLMDEPFGALD 166
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
505-697 |
1.60e-13 |
|
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: 69.94 E-value: 1.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 505 RPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINNYRecIACVLQE----DKLLAG 580
Cdd:cd03268 13 KRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRR--IGALIEApgfyPNLTAR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 581 SIAENICSFDAHPDTEfIVECAKHCNIHDDIMKMPMGYETlvgelggslsgGQKQRVLIARALYRRPSILFMDEATSHLD 660
Cdd:cd03268 91 ENLRLLARLLGIRKKR-IDEVLDVVGLKDSAKKKVKGFSL-----------GMKQRLGIALALLGNPDLLILDEPTNGLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 727181609 661 LDNEKRVNEAISSLK---MTRVIIAHRPSTIAS-ADRVITL 697
Cdd:cd03268 159 PDGIKELRELILSLRdqgITVLISSHLLSEIQKvADRIGII 199
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
492-660 |
2.04e-13 |
|
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: 69.84 E-value: 2.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDLLYQYDSLSRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDiGINNYRECIACV 571
Cdd:cd03263 2 QIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 572 LQEDKLLAG-SIAENI---CSFDAHPDTEFIVECAKH---CNIHDDIMKMPMGYETlvgelggslsgGQKQRVLIARALY 644
Cdd:cd03263 81 PQFDALFDElTVREHLrfyARLKGLPKSEIKEEVELLlrvLGLTDKANKRARTLSG-----------GMKRKLSLAIALI 149
|
170
....*....|....*.
gi 727181609 645 RRPSILFMDEATSHLD 660
Cdd:cd03263 150 GGPSVLLLDEPTSGLD 165
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
404-697 |
3.32e-13 |
|
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: 73.44 E-value: 3.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 404 FLAA-CDQIVILWLGASLVIDSQMTLGMFVAFNAYRGQFsdrasNLIDMVI-RLRMLNLHNERLaDIVLSTtEEEKP--- 478
Cdd:TIGR00957 552 FLVAlITFAVYVTVDENNILDAEKAFVSLALFNILRFPL-----NILPMVIsSIVQASVSLKRL-RIFLSH-EELEPdsi 624
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 479 YRKICNPNEAVTFEVRDLLYQYDSLSRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGinihd 558
Cdd:TIGR00957 625 ERRTIKPGEGNSITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG----- 699
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 559 iginnyreCIACVLQEDKLLAGSIAENICsFDAHPDTEFIVECAKHCNIHDDIMKMPMGYETLVGELGGSLSGGQKQRVL 638
Cdd:TIGR00957 700 --------SVAYVPQQAWIQNDSLRENIL-FGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVS 770
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 727181609 639 IARALYRRPSILFMDEATSHLDLDNEKRVNEAISSLK-----MTRVIIAHRPSTIASADRVITL 697
Cdd:TIGR00957 771 LARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGPEgvlknKTRILVTHGISYLPQVDVIIVM 834
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
492-673 |
3.82e-13 |
|
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: 68.54 E-value: 3.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDLLYQYDSlsRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDiGINNYRECIACV 571
Cdd:TIGR01189 2 AARNLACSRGE--RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAE-QRDEPHENILYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 572 LQEDKLLAG-SIAENICSFDAHPDTEfivecakHCNIHDDIMKMPM-GYETLvgeLGGSLSGGQKQRVLIARALYRRPSI 649
Cdd:TIGR01189 79 GHLPGLKPElSALENLHFWAAIHGGA-------QRTIEDALAAVGLtGFEDL---PAAQLSAGQQRRLALARLWLSRRPL 148
|
170 180
....*....|....*....|....
gi 727181609 650 LFMDEATSHLDLDNEKRVNEAISS 673
Cdd:TIGR01189 149 WILDEPTTALDKAGVALLAGLLRA 172
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
492-699 |
4.34e-13 |
|
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: 69.39 E-value: 4.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDL-----LYQYDSLSRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFIN----GINI-----H 557
Cdd:COG4778 6 EVENLsktftLHLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLaqaspR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 558 DIgINNYRECIACVLQ--------------EDKLLAGSIAENICSFDAHpdtefivECAKHCNIHDDIMKMP----MGYE 619
Cdd:COG4778 86 EI-LALRRRTIGYVSQflrviprvsaldvvAEPLLERGVDREEARARAR-------ELLARLNLPERLWDLPpatfSGGE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 620 tlvgelggslsggqKQRVLIARALYRRPSILFMDEATSHLDLDNEKRVNEAISSLKM--TRVI-IAHRPSTIAS-ADRVI 695
Cdd:COG4778 158 --------------QQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKArgTAIIgIFHDEEVREAvADRVV 223
|
....
gi 727181609 696 TLQP 699
Cdd:COG4778 224 DVTP 227
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
492-697 |
6.79e-13 |
|
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: 68.55 E-value: 6.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDLLYQYDSLSRPV--IPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHdigiNNYREcia 569
Cdd:cd03266 3 TADALTKRFRDVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVV----KEPAE--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 570 cVLQEDKLLAGSIA--------ENICSFDAhpdtefiVECAKHCNIHDDIMKMP--MGYETLVGELGGSLSGGQKQRVLI 639
Cdd:cd03266 76 -ARRRLGFVSDSTGlydrltarENLEYFAG-------LYGLKGDELTARLEELAdrLGMEELLDRRVGGFSTGMRQKVAI 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 727181609 640 ARALYRRPSILFMDEATSHLDLDNEKRVNEAISSLK---MTRVIIAHRPSTIAS-ADRVITL 697
Cdd:cd03266 148 ARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRalgKCILFSTHIMQEVERlCDRVVVL 209
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
492-695 |
8.53e-13 |
|
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: 69.70 E-value: 8.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDLLYQYDSLSRPV--IPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEP---TEGRLFINGINIHDIG---INN 563
Cdd:COG0444 3 EVRNLKVYFPTRRGVVkaVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSekeLRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 564 YR-ECIACVLQEdkllAGS-----------IAENICSFDAHPDTEF---IVECAKHCNIHD--DIMKM-PM----Gyetl 621
Cdd:COG0444 83 IRgREIQMIFQD----PMTslnpvmtvgdqIAEPLRIHGGLSKAEArerAIELLERVGLPDpeRRLDRyPHelsgG---- 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 727181609 622 vgelggslsggQKQRVLIARALYRRPSILFMDEATSHLDLDNEKRVNEAISSLK----MTRVIIAHRPSTIAS-ADRVI 695
Cdd:COG0444 155 -----------MRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQrelgLAILFITHDLGVVAEiADRVA 222
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
504-702 |
8.65e-13 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 67.89 E-value: 8.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 504 SRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEP---TEGRLFINGINIHD-------IGInnyreciacvLQ 573
Cdd:COG4136 13 GRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTAlpaeqrrIGI----------LF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 574 EDKLLAG--SIAENICsFdAHPDTefIVECAKHCNIHDDIMKMPMGY------ETLvgelggslSGGQKQRVLIARALYR 645
Cdd:COG4136 83 QDDLLFPhlSVGENLA-F-ALPPT--IGRAQRRARVEQALEEAGLAGfadrdpATL--------SGGQRARVALLRALLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 727181609 646 RPSILFMDEATSHLD--LDNEKR--VNEAISSLKMTRVIIAHRPSTIASADRVITLQPVNA 702
Cdd:COG4136 151 EPRALLLDEPFSKLDaaLRAQFRefVFEQIRQRGIPALLVTHDEEDAPAAGRVLDLGNWQH 211
|
|
| Peptidase_C39E |
cd02424 |
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
23-144 |
1.17e-12 |
|
A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family, which contains Colicin V perocessing peptidase.
Pssm-ID: 239104 [Multi-domain] Cd Length: 129 Bit Score: 65.44 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 23 VLQTEAAECGLASLAMVCG-YYGMHIDMLSMRQKFDISARGATLSSLIAIAENLNLKTRALSLSLDEIHQVKRP---CIL 98
Cdd:cd02424 4 IKQTDLNDCGIAVIQMLYNhYYKKKYDLNELKIKANLKKNGLSIYDLENLAKKFGLETESYQGSFLEFLELKNKfiiLLK 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 727181609 99 HWDMNHFVVLVNIRGGRITLHDPAFGRRVIGLQEFSLHFTGIALEV 144
Cdd:cd02424 84 SNGLNHFVIVKKIKKNKFIVLDPKKGKYKITYKEFEKIFNNIIITV 129
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
497-697 |
1.30e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 68.54 E-value: 1.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 497 LYQYDSlSRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLE------PTEGRLFINGINIHDIGINNYRECIAC 570
Cdd:PRK14246 16 LYLYIN-DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLRKEVGM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 571 VLQEDKLLAG-SIAENIC-SFDAHPDTE------FIVECAKHCNIHDDImkmpmgYETLvGELGGSLSGGQKQRVLIARA 642
Cdd:PRK14246 95 VFQQPNPFPHlSIYDNIAyPLKSHGIKEkreikkIVEECLRKVGLWKEV------YDRL-NSPASQLSGGQQQRLTIARA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 727181609 643 LYRRPSILFMDEATSHLDLDNEKRVNEAISSLK--MTRVIIAHRPSTIAS-ADRVITL 697
Cdd:PRK14246 168 LALKPKVLLMDEPTSMIDIVNSQAIEKLITELKneIAIVIVSHNPQQVARvADYVAFL 225
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
498-676 |
1.55e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 67.53 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 498 YQYDSLSRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINNYREC----IACVLQ 573
Cdd:PRK11629 15 YQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELrnqkLGFIYQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 574 EDKLLAGSIA-ENIcsfdAHPdteFIVECAKHCNIHDDIMKM--PMGYETLVGELGGSLSGGQKQRVLIARALYRRPSIL 650
Cdd:PRK11629 95 FHHLLPDFTAlENV----AMP---LLIGKKKPAEINSRALEMlaAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLV 167
|
170 180
....*....|....*....|....*.
gi 727181609 651 FMDEATSHLDLDNEKRVNEAISSLKM 676
Cdd:PRK11629 168 LADEPTGNLDARNADSIFQLLGELNR 193
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
506-698 |
1.62e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 68.48 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 506 PVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGinnyreciacVLQEDKLLAGSIAEN 585
Cdd:PRK13644 16 PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFS----------KLQGIRKLVGIVFQN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 586 icsfdahPDTEFI---VE----------CAKHCNIHD--DIMKMPMGYETLVGELGGSLSGGQKQRVLIARALYRRPSIL 650
Cdd:PRK13644 86 -------PETQFVgrtVEedlafgpenlCLPPIEIRKrvDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 727181609 651 FMDEATSHLDLDNEKRVNEAISSLK---MTRVIIAHRPSTIASADRVITLQ 698
Cdd:PRK13644 159 IFDEVTSMLDPDSGIAVLERIKKLHekgKTIVYITHNLEELHDADRIIVMD 209
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
492-690 |
1.67e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 68.29 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDLLYQYDSlSRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINNYRECIACV 571
Cdd:PRK13652 5 ETRDLCYSYSG-SKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 572 LQ--EDKLLAGSIAENIC--SFDAHPDTEFIVECAkhcnihDDIMKMpMGYETLVGELGGSLSGGQKQRVLIARALYRRP 647
Cdd:PRK13652 84 FQnpDDQIFSPTVEQDIAfgPINLGLDEETVAHRV------SSALHM-LGLEELRDRVPHHLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 727181609 648 SILFMDEATSHLDLDNEKR----VNEAISSLKMTRVIIAHRPSTIAS 690
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKElidfLNDLPETYGMTVIFSTHQLDLVPE 203
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
510-697 |
1.81e-12 |
|
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: 66.83 E-value: 1.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 510 GLSLQIAAGESvAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGiNNYRECIACVLQE----DKLLAGSIAEN 585
Cdd:cd03264 18 GVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQP-QKLRRRIGYLPQEfgvyPNFTVREFLDY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 586 ICSFDAHPDTEF---IVECAKHCNIHDDIMKMPMGYEtlvgelggslsGGQKQRVLIARALYRRPSILFMDEATSHLDLD 662
Cdd:cd03264 96 IAWLKGIPSKEVkarVDEVLELVNLGDRAKKKIGSLS-----------GGMRRRVGIAQALVGDPSILIVDEPTAGLDPE 164
|
170 180 190
....*....|....*....|....*....|....*...
gi 727181609 663 NEKRVNEAISSLKMTRVII--AHRPSTIAS-ADRVITL 697
Cdd:cd03264 165 ERIRFRNLLSELGEDRIVIlsTHIVEDVESlCNQVAVL 202
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
492-694 |
1.82e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 67.94 E-value: 1.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDLLYQYDSlsRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLE-----PTEGRLFINGINIHDIGIN--NY 564
Cdd:PRK14267 6 ETVNLRVYYGS--NHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDpiEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 565 RECIACVLQ-EDKLLAGSIAENICS-------FDAHPDTEFIVECA-KHCNIHDDIMKMPMGYETlvgelggSLSGGQKQ 635
Cdd:PRK14267 84 RREVGMVFQyPNPFPHLTIYDNVAIgvklnglVKSKKELDERVEWAlKKAALWDEVKDRLNDYPS-------NLSGGQRQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 727181609 636 RVLIARALYRRPSILFMDEATSHLDLDNEKRVNEAISSLK--MTRVIIAHRPstiASADRV 694
Cdd:PRK14267 157 RLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKkeYTIVLVTHSP---AQAARV 214
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
492-689 |
2.10e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 67.63 E-value: 2.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDLLYQYDSLSrpVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLE-----PTEGRLFINGINIHDIGINNYRE 566
Cdd:PRK14247 5 EIRDLKVSFGQVE--VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 567 CIACVLQ-EDKLLAGSIAENIC-----------SFDAHPDTEFIVECAKHCNIHDDIMKMPMGyetlvgelggSLSGGQK 634
Cdd:PRK14247 83 RVQMVFQiPNPIPNLSIFENVAlglklnrlvksKKELQERVRWALEKAQLWDEVKDRLDAPAG----------KLSGGQQ 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 727181609 635 QRVLIARALYRRPSILFMDEATSHLDLDNEKRVNEAISSLK--MTRVIIAHRPSTIA 689
Cdd:PRK14247 153 QRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKkdMTIVLVTHFPQQAA 209
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
486-683 |
2.25e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 67.88 E-value: 2.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 486 NEAVTFEVRDL-LYQYDSLSrpvIPGLSLQIAAGESVAIVGPSGVGKTTLMKL---MCGLLEP--TEGRLFINGINIHDI 559
Cdd:PRK14243 6 GTETVLRTENLnVYYGSFLA---VKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIPGfrVEGKVTFHGKNLYAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 560 GIN--NYRECIACVLQEDKLLAGSIAENIcSFDA-----HPDTEFIVECA-KHCNIHDDIM-KMPMGYETLvgelggslS 630
Cdd:PRK14243 83 DVDpvEVRRRIGMVFQKPNPFPKSIYDNI-AYGAringyKGDMDELVERSlRQAALWDEVKdKLKQSGLSL--------S 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 727181609 631 GGQKQRVLIARALYRRPSILFMDEATSHLDLDNEKRVNEAISSLK--MTRVIIAH 683
Cdd:PRK14243 154 GGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKeqYTIIIVTH 208
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
492-660 |
2.66e-12 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 67.96 E-value: 2.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDLLYQYDSLSRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEpTEGRLFINGINIHDIGINNYRECIACV 571
Cdd:cd03289 4 TVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 572 LQEDKLLAGSIAENICSFDAHPDTEfIVECAKHCNIHDDIMKMPMGYETLVGELGGSLSGGQKQRVLIARALYRRPSILF 651
Cdd:cd03289 83 PQKVFIFSGTFRKNLDPYGKWSDEE-IWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILL 161
|
....*....
gi 727181609 652 MDEATSHLD 660
Cdd:cd03289 162 LDEPSAHLD 170
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
510-553 |
2.67e-12 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 67.03 E-value: 2.67e-12
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 727181609 510 GLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFING 553
Cdd:COG1134 44 DVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG 87
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
492-656 |
2.96e-12 |
|
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: 66.69 E-value: 2.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDLLYQYDSLsrPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINI-----HDIGinnyRE 566
Cdd:cd03224 2 EVENLNAGYGKS--QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDItglppHERA----RA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 567 CIACVLQEDKLLAG-SIAENI---CSFDAHPDTEFIVEcakhcnihdDIMKM-PMGYE-------TLvgelggslSGGQK 634
Cdd:cd03224 76 GIGYVPEGRRIFPElTVEENLllgAYARRRAKRKARLE---------RVYELfPRLKErrkqlagTL--------SGGEQ 138
|
170 180
....*....|....*....|..
gi 727181609 635 QRVLIARALYRRPSILFMDEAT 656
Cdd:cd03224 139 QMLAIARALMSRPKLLLLDEPS 160
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
492-697 |
3.60e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 67.45 E-value: 3.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDLLYQYDSLSRpVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINNYRECIACV 571
Cdd:PRK13647 6 EVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 572 LQ--EDKLLAGSIAENIC------SFDAHPDTEFIVECAKHCNIHDDIMKMP--MGYetlvgelggslsgGQKQRVLIAR 641
Cdd:PRK13647 85 FQdpDDQVFSSTVWDDVAfgpvnmGLDKDEVERRVEEALKAVRMWDFRDKPPyhLSY-------------GQKKRVAIAG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 642 ALYRRPSILFMDEATSHLDLDNEKRVNEAISSL--KMTRVIIAHRPSTIAS--ADRVITL 697
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLhnQGKTVIVATHDVDLAAewADQVIVL 211
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
505-557 |
5.17e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 65.60 E-value: 5.17e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 727181609 505 RPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIH 557
Cdd:PRK13538 14 RILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR 66
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
507-697 |
5.71e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 69.42 E-value: 5.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 507 VIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINNYRECIACVLQEDKLLAGSIAENI 586
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNV 1404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 587 CSF-DAHPdtEFIVECAKHCNIHDDIMKMPMGYETLVGELGGSLSGGQKQRVLIARALYRRPS-ILFMDEATSHLD--LD 662
Cdd:PTZ00243 1405 DPFlEASS--AEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSgFILMDEATANIDpaLD 1482
|
170 180 190
....*....|....*....|....*....|....*..
gi 727181609 663 NEKR--VNEAISSlkMTRVIIAHRPSTIASADRVITL 697
Cdd:PTZ00243 1483 RQIQatVMSAFSA--YTVITIAHRLHTVAQYDKIIVM 1517
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
507-695 |
6.82e-12 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 68.60 E-value: 6.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 507 VIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINNY----RECIACVLQEDKLLAG-S 581
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREHFGFIFQRYHLLSHlT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 582 IAENIcsfdAHPDTEFIVECAKHCNIHDDIMKMpMGYETLVGELGGSLSGGQKQRVLIARALYRRPSILFMDEATSHLDL 661
Cdd:PRK10535 103 AAQNV----EVPAVYAGLERKQRLLRAQELLQR-LGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDS 177
|
170 180 190
....*....|....*....|....*....|....*..
gi 727181609 662 DNEKRVNEAISSLK---MTRVIIAHRPSTIASADRVI 695
Cdd:PRK10535 178 HSGEEVMAILHQLRdrgHTVIIVTHDPQVAAQAERVI 214
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
492-660 |
6.87e-12 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 67.55 E-value: 6.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDLLYQYDSlsRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGinNYRECIACV 571
Cdd:PRK11607 21 EIRNLTKSFDG--QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP--PYQRPINMM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 572 LQEDKLLAGSIAENICSFDAHPDTEFIVECAKHCNIHDDIMKMpmgyETLVGELGGSLSGGQKQRVLIARALYRRPSILF 651
Cdd:PRK11607 97 FQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHM----QEFAKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
|
....*....
gi 727181609 652 MDEATSHLD 660
Cdd:PRK11607 173 LDEPMGALD 181
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
512-660 |
1.10e-11 |
|
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: 65.74 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 512 SLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINNYREC----IACVLQEDKLLAG-SIAENI 586
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrrkkISMVFQSFALLPHrTVLENV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 587 cSF-------DAHPDTEFIVECAKHCNIHDDIMKMPmgyetlvgelgGSLSGGQKQRVLIARALYRRPSILFMDEATSHL 659
Cdd:cd03294 124 -AFglevqgvPRAEREERAAEALELVGLEGWEHKYP-----------DELSGGMQQRVGLARALAVDPDILLMDEAFSAL 191
|
.
gi 727181609 660 D 660
Cdd:cd03294 192 D 192
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
492-660 |
1.12e-11 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 66.71 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDLLYQYDSlsRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFING----INIH----DIGInn 563
Cdd:COG1118 4 EVRNISKRFGS--FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGrdlfTNLPprerRVGF-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 564 yreciacVLQEDKL---LagSIAENICsF---DAHPDTEFIVECAkhcnihDDIMKM----------PM----Gyetlvg 623
Cdd:COG1118 80 -------VFQHYALfphM--TVAENIA-FglrVRPPSKAEIRARV------EELLELvqlegladryPSqlsgG------ 137
|
170 180 190
....*....|....*....|....*....|....*..
gi 727181609 624 elggslsggQKQRVLIARALYRRPSILFMDEATSHLD 660
Cdd:COG1118 138 ---------QRQRVALARALAVEPEVLLLDEPFGALD 165
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
500-696 |
1.37e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 64.59 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 500 YDSLSRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLE--PTEGRlfingINIHDIGINNYRECIACVLQEDKL 577
Cdd:COG2401 38 LRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGC-----VDVPDNQFGREASLIDAIGRKGDF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 578 LAGSIAENICSFDahpDTEFIVECAKHcnihddimkMPMGyetlvgelggslsggQKQRVLIARALYRRPSILFMDEATS 657
Cdd:COG2401 113 KDAVELLNAVGLS---DAVLWLRRFKE---------LSTG---------------QKFRFRLALLLAERPKLLVIDEFCS 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 727181609 658 HLDLDNEKRVNEAISSL----KMTRVIIAHRPSTIA--SADRVIT 696
Cdd:COG2401 166 HLDRQTAKRVARNLQKLarraGITLVVATHHYDVIDdlQPDLLIF 210
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
523-697 |
1.59e-11 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, 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 transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 65.98 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 523 IVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIhdIGINNYRECIACVLQEDKLLAG-SIAENIcSFDAHPDTEFIVEC 601
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDV--TNVPPHLRHINMVFQSYALFPHmTVEENV-AFGLKMRKVPRAEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 602 AKHCNihdDIMKMpMGYETLVGELGGSLSGGQKQRVLIARALYRRPSILFMDEATSHLDLDNEKRVNEAISSLK----MT 677
Cdd:TIGR01187 78 KPRVL---EALRL-VQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQeqlgIT 153
|
170 180
....*....|....*....|.
gi 727181609 678 RVIIAHRPS-TIASADRVITL 697
Cdd:TIGR01187 154 FVFVTHDQEeAMTMSDRIAIM 174
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
172-443 |
1.65e-11 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 65.58 E-value: 1.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 172 KSALVKIFALSLVIEAVNLLMPVGTQLVMDHVIQAGDHNLLVIICVGLLFFILFRTCVSmfrsWISIVMGALI------D 245
Cdd:cd18540 1 KKLLILLIILMLLVALLDAVFPLLTKYAIDHFITPGTLDGLTGFILLYLGLILIQALSV----FLFIRLAGKIemgvsyD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 246 IqwKSGLFDHLMKLPLAYFEKRKLGDIQSRFGSlDAIRTTfttSIVS-SIID----GIMSVGVFIMMFMYGgWL--VWVa 318
Cdd:cd18540 77 L--RKKAFEHLQTLSFSYFDKTPVGWIMARVTS-DTQRLG---EIISwGLVDlvwgITYMIGILIVMLILN-WKlaLIV- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 319 sgFTVLYVLLRLSTY------RYYRQASEEqlvkSAKASSHFMETLYSIATLKSLGLAGTRSQFWLNLNIDTANANIRVT 392
Cdd:cd18540 149 --LAVVPVLAVVSIYfqkkilKAYRKVRKI----NSRITGAFNEGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAA 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 727181609 393 KLDMFFGGVNAFLAACDQIVILWLGASLVIDSQMTLGMFVAFNAYRGQFSD 443
Cdd:cd18540 223 RLSALFLPIVLFLGSIATALVLWYGGILVLAGAITIGTLVAFISYATQFFE 273
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
518-699 |
1.66e-11 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 62.78 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 518 GESVAIVGPSGVGKTTLMKLMCGLLEPTEGR-LFINGINIHDIGINNYREciacvlqedkllagsiaenicsfdahpdte 596
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLLL------------------------------ 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 597 fivecakhcnihddimkmpmgyeTLVGELGGSLSGGQKQRVLIARALYRRPSILFMDEATSHLDLDNEKRVNEAISSLKM 676
Cdd:smart00382 52 -----------------------IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLL 108
|
170 180
....*....|....*....|...
gi 727181609 677 TRVIIAHRPSTIASADRVITLQP 699
Cdd:smart00382 109 LLLKSEKNLTVILTTNDEKDLGP 131
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
492-698 |
2.44e-11 |
|
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: 66.75 E-value: 2.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDLLYQYDSLSrpVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGL--LEPTEGRLF------------------- 550
Cdd:TIGR03269 2 EVKNLTKKFDGKE--VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpskvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 551 --------------INGINIHDIGINNYRECIACVLQEDKLLAG--SIAENIcsFDAHPDTEFIVECAKHCNIhdDIMKM 614
Cdd:TIGR03269 80 epcpvcggtlepeeVDFWNLSDKLRRRIRKRIAIMLQRTFALYGddTVLDNV--LEALEEIGYEGKEAVGRAV--DLIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 615 pMGYETLVGELGGSLSGGQKQRVLIARALYRRPSILFMDEATSHLDLDNEKRVNEAISSL----KMTRVIIAHRPSTIAS 690
Cdd:TIGR03269 156 -VQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvkasGISMVLTSHWPEVIED 234
|
....*....
gi 727181609 691 -ADRVITLQ 698
Cdd:TIGR03269 235 lSDKAIWLE 243
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
505-660 |
4.55e-11 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 63.95 E-value: 4.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 505 RPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINNyreciACVLQEDKLLA-GSIA 583
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----GVVFQNEGLLPwRNVQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 584 ENIcSFD---AHPDTEFIVECAKHcnihddiMKMPMGYETLVGELGGSLSGGQKQRVLIARALYRRPSILFMDEATSHLD 660
Cdd:PRK11248 89 DNV-AFGlqlAGVEKMQRLEIAHQ-------MLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
510-557 |
4.56e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 64.72 E-value: 4.56e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 727181609 510 GLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIH 557
Cdd:COG4586 40 DISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPF 87
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
510-660 |
5.93e-11 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 64.37 E-value: 5.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 510 GLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIG---INNYRECIACVLQeD--------KLL 578
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQ-DpyaslnprMTV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 579 AGSIAEnicSFDAHPDT------EFIVEcakhcnihddIMKM-----------PM----GyetlvgelggslsggQKQRV 637
Cdd:COG4608 115 GDIIAE---PLRIHGLAskaerrERVAE----------LLELvglrpehadryPHefsgG---------------QRQRI 166
|
170 180
....*....|....*....|...
gi 727181609 638 LIARALYRRPSILFMDEATSHLD 660
Cdd:COG4608 167 GIARALALNPKLIVCDEPVSALD 189
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
493-683 |
8.38e-11 |
|
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: 64.82 E-value: 8.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 493 VRDLLYQYDSLSRPVIP---GLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFI----NGINIHDIGINN-- 563
Cdd:TIGR03269 282 VRNVSKRYISVDRGVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPDGrg 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 564 -YRECIACVLQEDKLLA-GSIAENICsfDAhPDTEFIVECAKHCNIHddIMKMpMGY-----ETLVGELGGSLSGGQKQR 636
Cdd:TIGR03269 362 rAKRYIGILHQEYDLYPhRTVLDNLT--EA-IGLELPDELARMKAVI--TLKM-VGFdeekaEEILDKYPDELSEGERHR 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 727181609 637 VLIARALYRRPSILFMDEATSHLDLDNEKRVNEAI----SSLKMTRVIIAH 683
Cdd:TIGR03269 436 VALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkarEEMEQTFIIVSH 486
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
507-695 |
8.91e-11 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 63.95 E-value: 8.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 507 VIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGiniHDIGINNYRE-CIACVLQEDKLLAG-SIAE 584
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHG---TDVSRLHARDrKVGFVFQHYALFRHmTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 585 NIcSFD-------AHPDTEFI---VECakhcnihddIMKMpMGYETLVGELGGSLSGGQKQRVLIARALYRRPSILFMDE 654
Cdd:PRK10851 94 NI-AFGltvlprrERPNAAAIkakVTQ---------LLEM-VQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDE 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 727181609 655 ATSHLDLDNEKRVNEAI----SSLKMTRVIIAH-RPSTIASADRVI 695
Cdd:PRK10851 163 PFGALDAQVRKELRRWLrqlhEELKFTSVFVTHdQEEAMEVADRVV 208
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
491-556 |
1.28e-10 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 62.18 E-value: 1.28e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 727181609 491 FEVRDLLYQYDSlsRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINI 556
Cdd:cd03218 1 LRAENLSKRYGK--RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDI 64
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
505-661 |
1.85e-10 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 61.95 E-value: 1.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 505 RPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINNYRECIACVLQEDKLLAGSIAE 584
Cdd:PRK11231 15 KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGITVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 585 NICSFDAHP----------DTEFIVECAKHcnihddimkmPMGYETLVGELGGSLSGGQKQRVLIARALYRRPSILFMDE 654
Cdd:PRK11231 95 ELVAYGRSPwlslwgrlsaEDNARVNQAME----------QTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDE 164
|
....*..
gi 727181609 655 ATSHLDL 661
Cdd:PRK11231 165 PTTYLDI 171
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
505-553 |
2.12e-10 |
|
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: 61.01 E-value: 2.12e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 727181609 505 RPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFING 553
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG 83
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
512-698 |
2.65e-10 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 63.13 E-value: 2.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 512 SLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINNYREC----IACVLQEDKLLAGSIAENIC 587
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVrrkkIAMVFQSFALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 588 SFDAHPDTefiVECAKHCNIHDDIMKMpMGYETLVGELGGSLSGGQKQRVLIARALYRRPSILFMDEATSHLDLDNEKRV 667
Cdd:PRK10070 128 AFGMELAG---INAEERREKALDALRQ-VGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
|
170 180 190
....*....|....*....|....*....|....*.
gi 727181609 668 NEAISSLKM----TRVIIAHR-PSTIASADRVITLQ 698
Cdd:PRK10070 204 QDELVKLQAkhqrTIVFISHDlDEAMRIGDRIAIMQ 239
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
211-437 |
3.17e-10 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 61.56 E-value: 3.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 211 LLVIICVGLLFFILFRTCVsmfrswISIVMgALIDIQWKSGLFDHLMKLPLAYFEKRKLGDIQSRFGSldaiRTTFTTSI 290
Cdd:cd18784 41 IMGLLAIASSVAAGIRGGL------FTLAM-ARLNIRIRNLLFRSIVSQEIGFFDTVKTGDITSRLTS----DTTTMSDT 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 291 VSSIIDG-----IMSVGVFIMMFMyggwLVWVASGFT--VLYVLLRLSTY--RYYRQASEEQLVKSAKASSHFMETLYSI 361
Cdd:cd18784 110 VSLNLNIflrslVKAIGVIVFMFK----LSWQLSLVTliGLPLIAIVSKVygDYYKKLSKAVQDSLAKANEVAEETISSI 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 727181609 362 ATLKSL-GLAGTRSQFWLNLNiDTANANIRVTKLDMFFGGVNAFLAACDQIVILWLGASLVIDSQMTLGMFVAFNAY 437
Cdd:cd18784 186 RTVRSFaNEDGEANRYSEKLK-DTYKLKIKEALAYGGYVWSNELTELALTVSTLYYGGHLVITGQISGGNLISFILY 261
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
512-661 |
3.23e-10 |
|
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: 62.43 E-value: 3.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 512 SLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHD--IGIN--NYRECIACVLQEDKLLAG-SIAENI 586
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDsaRGIFlpPHRRRIGYVFQEARLFPHlSVRGNL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 587 C-----SFDAHPDTEFivecakhcnihDDIMKMpMGYETLVGELGGSLSGGQKQRVLIARALYRRPSILFMDEATSHLDL 661
Cdd:COG4148 99 LygrkrAPRAERRISF-----------DEVVEL-LGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDL 166
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
505-697 |
3.32e-10 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 60.66 E-value: 3.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 505 RPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGiniHDIGINNYREC------IACVLQEDKLL 578
Cdd:PRK10908 15 RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSG---HDITRLKNREVpflrrqIGMIFQDHHLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 579 AG-SIAENIcsfdAHPdteFIVECAKHCNIHDDIMKM--PMGYETLVGELGGSLSGGQKQRVLIARALYRRPSILFMDEA 655
Cdd:PRK10908 92 MDrTVYDNV----AIP---LIIAGASGDDIRRRVSAAldKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEP 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 727181609 656 TSHLD---LDNEKRVNEAISSLKMTRVIIAHRPSTIASAD-RVITL 697
Cdd:PRK10908 165 TGNLDdalSEGILRLFEEFNRVGVTVLMATHDIGLISRRSyRMLTL 210
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
179-437 |
3.40e-10 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 349998 [Multi-domain] Cd Length: 299 Bit Score: 61.67 E-value: 3.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 179 FALSLVIEAVNLLMPVGTQLVMDHVIQAGD-------HNLLVIICVGLLFFILFRTCVSMFRSWIS--IVMGALIDIQWK 249
Cdd:cd18554 5 IVIGLVRFGIPLLLPLILKYIVDDVIQGSSltldekvYKLFTIIGIMFFIFLILRPPVEYYRQYFAqwIANKILYDIRKD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 250 sgLFDHLMKLPLAYFEKRKLGDIQSR-FGSLDAIRTTFTTSIVSSIIDGIMSVGVFIMMFMYGGWLVWVASGFTVLYVLL 328
Cdd:cd18554 85 --LFDHLQKLSLRYYANNRSGEIISRvINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYILA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 329 RLSTYRYYRQASEEQLVKSAKASSHFMETLYSIATLKSLGLA-------GTRSQFWLNLNIDTANANIRVtkldmfFGGV 401
Cdd:cd18554 163 VKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEkheqkqfDKRNGHFLTRALKHTRWNAKT------FSAV 236
|
250 260 270
....*....|....*....|....*....|....*.
gi 727181609 402 NAFLAACDQIVIlWLGASLVIDSQMTLGMFVAFNAY 437
Cdd:cd18554 237 NTITDLAPLLVI-GFAAYLVIEGNLTVGTLVAFVGY 271
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
492-699 |
4.31e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 62.60 E-value: 4.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDLLYQYDSlsRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRL------------------FING 553
Cdd:PRK15064 321 EVENLTKGFDN--GPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkwsenanigyyaqdhaydFEND 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 554 INIHDiGINNYR------ECIACVLqeDKLLAGSiaenicsfdahpdtefivecakhcnihDDIMKMPM---GYEtlvge 624
Cdd:PRK15064 399 LTLFD-WMSQWRqegddeQAVRGTL--GRLLFSQ---------------------------DDIKKSVKvlsGGE----- 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 625 lggslsggqKQRVLIARALYRRPSILFMDEATSHLDLdnekrvnEAISSLKM-------TRVIIAHRPSTIAS-ADRVIT 696
Cdd:PRK15064 444 ---------KGRMLFGKLMMQKPNVLVMDEPTNHMDM-------ESIESLNMalekyegTLIFVSHDREFVSSlATRIIE 507
|
...
gi 727181609 697 LQP 699
Cdd:PRK15064 508 ITP 510
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
513-660 |
5.37e-10 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 61.58 E-value: 5.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 513 LQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINNyREcIACVLQEDKLLAG-SIAENIcSFD- 590
Cdd:PRK11000 24 LDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE-RG-VGMVFQSYALYPHlSVAENM-SFGl 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 727181609 591 --AHPDTEfivECAKHCNIHDDIMKMpmgyETLVGELGGSLSGGQKQRVLIARALYRRPSILFMDEATSHLD 660
Cdd:PRK11000 101 klAGAKKE---EINQRVNQVAEVLQL----AHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
510-697 |
6.27e-10 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 60.44 E-value: 6.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 510 GLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINI-----HDI---GI----------NNY--RECIA 569
Cdd:COG0411 22 DVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDItglppHRIarlGIartfqnprlfPELtvLENVL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 570 CVLQEdkLLAGSIAENICSFDAHPDTE-----FIVECAKHCNIHDDIMK----MPMGyetlvgelggslsggQKQRVLIA 640
Cdd:COG0411 102 VAAHA--RLGRGLLAALLRLPRARREEreareRAEELLERVGLADRADEpagnLSYG---------------QQRRLEIA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 727181609 641 RALYRRPSILFMDEATSHLDLDNEKRVNEAISSLK----MTRVIIAHRPSTIAS-ADRVITL 697
Cdd:COG0411 165 RALATEPKLLLLDEPAAGLNPEETEELAELIRRLRdergITILLIEHDMDLVMGlADRIVVL 226
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
486-703 |
8.45e-10 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 60.88 E-value: 8.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 486 NEAVTFEVRDLLYQYDSLSRPVIP-----------GLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGI 554
Cdd:PRK15079 4 GKKVLLEVADLKVHFDIKDGKQWFwqppktlkavdGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 555 NIHDIGINNYREC---IACVLQeDKL--------LAGSIAENICSFDAHPDTEFIVECAKHcnihddiMKMPMGY-ETLV 622
Cdd:PRK15079 84 DLLGMKDDEWRAVrsdIQMIFQ-DPLaslnprmtIGEIIAEPLRTYHPKLSRQEVKDRVKA-------MMLKVGLlPNLI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 623 GELGGSLSGGQKQRVLIARALYRRPSILFMDEATSHLDLDNEKRVNEAISSLK----MTRVIIAHRPSTIAS-ADRVITL 697
Cdd:PRK15079 156 NRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQremgLSLIFIAHDLAVVKHiSDRVLVM 235
|
....*.
gi 727181609 698 QPVNAM 703
Cdd:PRK15079 236 YLGHAV 241
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
505-697 |
9.54e-10 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 58.81 E-value: 9.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 505 RPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPT---EGRLFINGINIHDIGiNNYRECIACVLQEDkllags 581
Cdd:cd03233 20 IPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFA-EKYPGEIIYVSEED------ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 582 iaenicSFDAHPDTEFIVECAKHCNIHDDIMKMPMGyetlvgelggslsggQKQRVLIARALYRRPSILFMDEATSHLD- 660
Cdd:cd03233 93 ------VHFPTLTVRETLDFALRCKGNEFVRGISGG---------------ERKRVSIAEALVSRASVLCWDNSTRGLDs 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 727181609 661 ---LDNEKRVNEAISSLKMTRVIIAHRPSTIASA--DRVITL 697
Cdd:cd03233 152 staLEILKCIRTMADVLKTTTFVSLYQASDEIYDlfDKVLVL 193
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
498-695 |
9.79e-10 |
|
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: 59.73 E-value: 9.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 498 YQYDSLSRpVIPGLSLQIAAG-----ESVAIVGPSGVGKTTLMKLMCGLLEPTEGrlfinginihDIGINNyrECIACVL 572
Cdd:cd03237 1 YTYPTMKK-TLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEG----------DIEIEL--DTVSYKP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 573 QE---------DKLLAgSIAENICSfdahpDTEFIVECAKhcnihddimkmPMGYETLVGELGGSLSGGQKQRVLIARAL 643
Cdd:cd03237 68 QYikadyegtvRDLLS-SITKDFYT-----HPYFKTEIAK-----------PLQIEQILDREVPELSGGELQRVAIAACL 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 727181609 644 YRRPSILFMDEATSHLDLDNEKRVNEAISSL----KMTRVIIAHRPSTIAS-ADRVI 695
Cdd:cd03237 131 SKDADIYLLDEPSAYLDVEQRLMASKVIRRFaennEKTAFVVEHDIIMIDYlADRLI 187
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
492-694 |
1.12e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 61.22 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDLLYQYDSLsrPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINI--------HDIGInn 563
Cdd:PRK15439 13 CARSISKQYSGV--EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCarltpakaHQLGI-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 564 YreciaCVLQEDKLLAG-SIAENIC-SFDAHPD-----TEFIVECAKHCNIHddimkMPMGyeTLvgelggslSGGQKQR 636
Cdd:PRK15439 89 Y-----LVPQEPLLFPNlSVKENILfGLPKRQAsmqkmKQLLAALGCQLDLD-----SSAG--SL--------EVADRQI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 727181609 637 VLIARALYRRPSILFMDEATSHLDLDNEKRVNEAISSLKMTRV---IIAHR-PSTIASADRV 694
Cdd:PRK15439 149 VEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQGVgivFISHKlPEIRQLADRI 210
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
487-680 |
1.64e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.98 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 487 EAVTFEVR---------------DLLYQYDSLSRPVIPGlslQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFI 551
Cdd:PRK13409 322 EPIEFEERpprdeseretlveypDLTKKLGDFSLEVEGG---EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 552 nginihDIGIN---NYRECIACVLQEDKLlaGSIAENIcsfdahpDTEFI-VECAKHCNIHdDIMKMPM----GYETlvg 623
Cdd:PRK13409 399 ------ELKISykpQYIKPDYDGTVEDLL--RSITDDL-------GSSYYkSEIIKPLQLE-RLLDKNVkdlsGGEL--- 459
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 727181609 624 elggslsggqkQRVLIARALYRRPSILFMDEATSHLDLdnEKRvneaissLKMTRVI 680
Cdd:PRK13409 460 -----------QRVAIAACLSRDADLYLLDEPSAHLDV--EQR-------LAVAKAI 496
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
507-678 |
1.65e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 59.23 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 507 VIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINNYRECIAcVLQEDKLLAGSIA-EN 585
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIG-LLAQNATTPGDITvQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 586 ICSFDAHPDTEFIVECAKHcniHDDIMKMPM---GYETLVGELGGSLSGGQKQRVLIARALYRRPSILFMDEATSHLDLD 662
Cdd:PRK10253 101 LVARGRYPHQPLFTRWRKE---DEEAVTKAMqatGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIS 177
|
170
....*....|....*.
gi 727181609 663 NEKRVNEAISSLKMTR 678
Cdd:PRK10253 178 HQIDLLELLSELNREK 193
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
513-661 |
2.63e-09 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 59.50 E-value: 2.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 513 LQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDI--GIN---NYREcIACVLQEDKLLAG-SIAENI 586
Cdd:PRK11144 19 LTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAekGIClppEKRR-IGYVFQDARLFPHyKVRGNL 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 727181609 587 CSFDAHPDTE-FivecakhcnihDDIMKMpMGYETLVGELGGSLSGGQKQRVLIARALYRRPSILFMDEATSHLDL 661
Cdd:PRK11144 98 RYGMAKSMVAqF-----------DKIVAL-LGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDL 161
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
492-683 |
2.64e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 58.63 E-value: 2.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDLLYQYDSlsRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLM--CGLLEP---TEGRLFINGINIHDIGIN--NY 564
Cdd:PRK14239 7 QVSDLSVYYNK--KKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPevtITGSIVYNGHNIYSPRTDtvDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 565 RECIACVLQEDKLLAGSIAENIC-------SFDAHPDTEFIVECAKHCNI--------HDDIMKMPMGyetlvgelggsl 629
Cdd:PRK14239 85 RKEIGMVFQQPNPFPMSIYENVVyglrlkgIKDKQVLDEAVEKSLKGASIwdevkdrlHDSALGLSGG------------ 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 727181609 630 sggQKQRVLIARALYRRPSILFMDEATSHLDLDNEKRVNEAISSLK--MTRVIIAH 683
Cdd:PRK14239 153 ---QQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKddYTMLLVTR 205
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
507-656 |
2.64e-09 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 57.92 E-value: 2.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 507 VIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINI-----HDiginNYRECIACVLQEDKLLAG- 580
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDItklppHE----RARAGIAYVPQGREIFPRl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 581 SIAENICS-FDAHPDtefivecaKHCNIHDDI---------MKMPMGyetlvgelgGSLSGGQKQRVLIARALYRRPSIL 650
Cdd:TIGR03410 91 TVEENLLTgLAALPR--------RSRKIPDEIyelfpvlkeMLGRRG---------GDLSGGQQQQLAIARALVTRPKLL 153
|
....*.
gi 727181609 651 FMDEAT 656
Cdd:TIGR03410 154 LLDEPT 159
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
506-656 |
2.93e-09 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 58.07 E-value: 2.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 506 PVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINI-----HDIGinnyRECIACVLQEDKLLAG 580
Cdd:COG0410 17 HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDItglppHRIA----RLGIGYVPEGRRIFPS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 581 -SIAENI-CSFDAHPDTEfivecakhcNIHDDIMKMpmgYE--------------TLvgelggslSGGQKQRVLIARALY 644
Cdd:COG0410 93 lTVEENLlLGAYARRDRA---------EVRADLERV---YElfprlkerrrqragTL--------SGGEQQMLAIGRALM 152
|
170
....*....|..
gi 727181609 645 RRPSILFMDEAT 656
Cdd:COG0410 153 SRPKLLLLDEPS 164
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
491-549 |
3.37e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.96 E-value: 3.37e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 727181609 491 FEVRDLLYQYDSlsRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRL 549
Cdd:PRK11147 320 FEMENVNYQIDG--KQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI 376
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
491-660 |
4.12e-09 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II 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. In members of 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: 213182 [Multi-domain] Cd Length: 182 Bit Score: 56.67 E-value: 4.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 491 FEVRDLlyqydSLSRPViPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGiniHDIGINNYRECIA- 569
Cdd:cd03215 5 LEVRGL-----SVKGAV-RDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDG---KPVTRRSPRDAIRa 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 570 --CVLQEDKLLAG-----SIAENIcsfdahpdtefivecakhcnihddimkmpmgyetlvgelggsLSGGQ-----KQRV 637
Cdd:cd03215 76 giAYVPEDRKREGlvldlSVAENI------------------------------------------ALSSLlsggnQQKV 113
|
170 180
....*....|....*....|...
gi 727181609 638 LIARALYRRPSILFMDEATSHLD 660
Cdd:cd03215 114 VLARWLARDPRVLILDEPTRGVD 136
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
484-556 |
5.24e-09 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 57.85 E-value: 5.24e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 727181609 484 NPNEAVTFEVRDLLYQYDSlsRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINI 556
Cdd:PRK11831 1 EQSVANLVDMRGVSFTRGN--RCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENI 71
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
487-680 |
6.55e-09 |
|
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: 59.03 E-value: 6.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 487 EAVTFEVR---------------DLLYQYDSLSRPVIPGlslQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFI 551
Cdd:COG1245 323 EPIEFEVHaprrekeeetlveypDLTKSYGGFSLEVEGG---EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDE 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 552 nginihDIGIN---NYRECIACVLQEDkLLAGSIAENIcsfdahPDTEFIVECAKHCNIHdDIMKMPM----GYETlvge 624
Cdd:COG1245 400 ------DLKISykpQYISPDYDGTVEE-FLRSANTDDF------GSSYYKTEIIKPLGLE-KLLDKNVkdlsGGEL---- 461
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 727181609 625 lggslsggqkQRVLIARALYRRPSILFMDEATSHLDLdnEKRVNeaisslkMTRVI 680
Cdd:COG1245 462 ----------QRVAIAACLSRDADLYLLDEPSAHLDV--EQRLA-------VAKAI 498
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
507-683 |
7.31e-09 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 57.29 E-value: 7.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 507 VIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINNYRECIAcvlqeDKLLAGSIAENI 586
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLKVA-----DKNQLRLLRTRL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 587 CSFDAHpdtefiVECAKHCNIHDDIMKMPMGYETLVGELGGSLSGG----------------------QKQRVLIARALY 644
Cdd:PRK10619 95 TMVFQH------FNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKylakvgideraqgkypvhlsggQQQRVSIARALA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 727181609 645 RRPSILFMDEATSHLD--LDNEK-RVNEAISSLKMTRVIIAH 683
Cdd:PRK10619 169 MEPEVLLFDEPTSALDpeLVGEVlRIMQQLAEEGKTMVVVTH 210
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
508-697 |
7.55e-09 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 56.71 E-value: 7.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 508 IPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINNyreciACVLQEDKLLAG-SIAENI 586
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDR-----MVVFQNYSLLPWlTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 587 CsfdahpdteFIVECAKHC-------NIHDDIMKMpMGYETLVGELGGSLSGGQKQRVLIARALYRRPSILFMDEATSHL 659
Cdd:TIGR01184 76 A---------LAVDRVLPDlskserrAIVEEHIAL-VGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGAL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 727181609 660 DLDNEKRVNEAISSL----KMTRVIIAHR-PSTIASADRVITL 697
Cdd:TIGR01184 146 DALTRGNLQEELMQIweehRVTVLMVTHDvDEALLLSDRVVML 188
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
505-660 |
7.60e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 57.92 E-value: 7.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 505 RPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDiGINNYRECIACVLQEDKL-LAGSIA 583
Cdd:PRK13536 54 KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIGVVPQFDNLdLEFTVR 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 584 ENICSFDAHpdtefiveCAKHCNIHDDIMKMPMGY---ETLVGELGGSLSGGQKQRVLIARALYRRPSILFMDEATSHLD 660
Cdd:PRK13536 133 ENLLVFGRY--------FGMSTREIEAVIPSLLEFarlESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLD 204
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
504-683 |
8.12e-09 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 56.95 E-value: 8.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 504 SRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMcGLLE-PTEGRLfinginihdiginnyreciacvlqedkllagSI 582
Cdd:COG4161 14 SHQALFDINLECPSGETLVLLGPSGAGKSSLLRVL-NLLEtPDSGQL-------------------------------NI 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 583 AENICSFDAHPDTEFIVECAK-------------HCNIHDDIMKMPMGYETLVGELGGSLSGG----------------- 632
Cdd:COG4161 62 AGHQFDFSQKPSEKAIRLLRQkvgmvfqqynlwpHLTVMENLIEAPCKVLGLSKEQAREKAMKllarlrltdkadrfplh 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 727181609 633 ----QKQRVLIARALYRRPSILFMDEATSHLDLDNEKRVNEAISSLK---MTRVIIAH 683
Cdd:COG4161 142 lsggQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSqtgITQVIVTH 199
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
507-698 |
8.23e-09 |
|
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: 56.13 E-value: 8.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 507 VIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFING-----INIHDIGinnYreciacvLQEDKLL--A 579
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGkpldiAARNRIG---Y-------LPEERGLypK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 580 GSIAENICSF---------DAHPDTEFI---VECAKHCNIHddIMKMPMGyetlvgelggslsggQKQRVLIARALYRRP 647
Cdd:cd03269 85 MKVIDQLVYLaqlkglkkeEARRRIDEWlerLELSEYANKR--VEELSKG---------------NQQKVQFIAAVIHDP 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 727181609 648 SILFMDEATSHLDLDNEKRVNEAISSLK---MTRVIIAHRPSTI-ASADRVITLQ 698
Cdd:cd03269 148 ELLILDEPFSGLDPVNVELLKDVIRELAragKTVILSTHQMELVeELCDRVLLLN 202
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
488-698 |
9.13e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 57.06 E-value: 9.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 488 AVTFEVRDLLYQYDS-LSRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGIN---- 562
Cdd:PRK13649 2 GINLQNVSYTYQAGTpFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNkdik 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 563 NYRECIACVLQ--EDKLLAGSIAENIcsfdAHPDTEFIVECAKHCNIHDDIMKMPMGYETLVGELGGSLSGGQKQRVLIA 640
Cdd:PRK13649 82 QIRKKVGLVFQfpESQLFEETVLKDV----AFGPQNFGVSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 727181609 641 RALYRRPSILFMDEATSHLDLDNEKRVNEAISSLK---MTRVIIAHRPSTIAS-ADRVITLQ 698
Cdd:PRK13649 158 GILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHqsgMTIVLVTHLMDDVANyADFVYVLE 219
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
447-697 |
9.40e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 58.83 E-value: 9.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 447 NLIDMVIRLrmlNLHNERLADIVLStteEEKpyrkICNPNEAV-----TFEVRDLLYQYDS-LSRPVIPGLSLQIAAGES 520
Cdd:PLN03232 576 NLLSQVVNA---NVSLQRIEELLLS---EER----ILAQNPPLqpgapAISIKNGYFSWDSkTSKPTLSDINLEIPVGSL 645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 521 VAIVGPSGVGKTTLMKLMCGLLEPTEGRLFInginihdiginnYRECIACVLQEDKLLAGSIAENICsFDAHPDTEFIVE 600
Cdd:PLN03232 646 VAIVGGTGEGKTSLISAMLGELSHAETSSVV------------IRGSVAYVPQVSWIFNATVRENIL-FGSDFESERYWR 712
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 601 CAKHCNIHDDIMKMPMGYETLVGELGGSLSGGQKQRVLIARALYRRPSILFMDEATSHLDLDNEKRVNEAISSLKM---T 677
Cdd:PLN03232 713 AIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELkgkT 792
|
250 260
....*....|....*....|
gi 727181609 678 RVIIAHRPSTIASADRVITL 697
Cdd:PLN03232 793 RVLVTNQLHFLPLMDRIILV 812
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
252-434 |
1.19e-08 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 57.14 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 252 LFDHLMKLPLAYFEKRKLGDIQSRFGSlDAirTTFTTSIVSSIIDG----IMSVGVFIMMF-------MYGGWLVWVASG 320
Cdd:cd18573 80 LFKSILRQDAAFFDKNKTGELVSRLSS-DT--SVVGKSLTQNLSDGlrslVSGVGGIGMMLyispkltLVMLLVVPPIAV 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 321 FTVLYvllrlstYRYYRQASEEQLVKSAKASSHFMETLYSIATLKSLGlAGTRSQFWLNLNIDTA-NANIRVTKLDMFFG 399
Cdd:cd18573 157 GAVFY-------GRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFA-AERKEVERYAKKVDEVfDLAKKEALASGLFF 228
|
170 180 190
....*....|....*....|....*....|....*
gi 727181609 400 GVNAFLAACDQIVILWLGASLVIDSQMTLGMFVAF 434
Cdd:cd18573 229 GSTGFSGNLSLLSVLYYGGSLVASGELTVGDLTSF 263
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
179-390 |
1.33e-08 |
|
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350024 [Multi-domain] Cd Length: 294 Bit Score: 56.74 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 179 FALSLVIEAVNLLMPVGTQLVMDHVIQA--------GDHNLLVIICVGLLFFILFRTCVSMFrsWISIVMGALIDIQWKs 250
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDwssspnssSGYYLGVYAALLVLASVLLVLLRWLL--FVLAGLRASRRLHDK- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 251 gLFDHLMKLPLAYFEKRKLGDIQSRFGS-LDAIRTTFTTSIVSSIIDGIMSVGVFIMMFMYGGWLVWVASGFTVLYVLLR 329
Cdd:cd18580 78 -LLRSVLRAPMSFFDTTPSGRILNRFSKdIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLLQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 727181609 330 lstyRYYRQASEE--QLVKSAKAS--SHFMETLYSIATLKSLGlagtRSQFWLNLNIDTANANIR 390
Cdd:cd18580 157 ----RYYLRTSRQlrRLESESRSPlySHFSETLSGLSTIRAFG----WQERFIEENLRLLDASQR 213
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
510-659 |
2.20e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 57.25 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 510 GLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLePT---EGRLFINGINIHDIGI-NNYRECIACVLQEDKLLAG-SIAE 584
Cdd:PRK13549 23 NVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNIrDTERAGIAIIHQELALVKElSVLE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 585 NIcsFDAHPDTEF--------IVECAK-------HCNIHDDIMKMPMGyetlvgelggslsggQKQRVLIARALYRRPSI 649
Cdd:PRK13549 102 NI--FLGNEITPGgimdydamYLRAQKllaqlklDINPATPVGNLGLG---------------QQQLVEIAKALNKQARL 164
|
170
....*....|
gi 727181609 650 LFMDEATSHL 659
Cdd:PRK13549 165 LILDEPTASL 174
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
504-654 |
2.66e-08 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 55.04 E-value: 2.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 504 SRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDI--------GINnY----------- 564
Cdd:COG1137 15 KRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLpmhkrarlGIG-Ylpqeasifrkl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 565 --RECIACVLQEDKLLAGSIAENIcsfDAHPDtEF-IVECAKHcnihddimkmpMGYeTLvgelggslSGGQKQRVLIAR 641
Cdd:COG1137 94 tvEDNILAVLELRKLSKKEREERL---EELLE-EFgITHLRKS-----------KAY-SL--------SGGERRRVEIAR 149
|
170
....*....|...
gi 727181609 642 ALYRRPSILFMDE 654
Cdd:COG1137 150 ALATNPKFILLDE 162
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
479-656 |
2.73e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 56.95 E-value: 2.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 479 YRKICNPNEAVTFEVRDLLyqydslSRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGiniHD 558
Cdd:COG1129 245 FPKRAAAPGEVVLEVEGLS------VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDG---KP 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 559 IGINNYRECIA---CVLQEDK-----LLAGSIAENIC--SFDAHPDTEFI-----VECAKHcNIHD-DImKMPmGYETLV 622
Cdd:COG1129 316 VRIRSPRDAIRagiAYVPEDRkgeglVLDLSIRENITlaSLDRLSRGGLLdrrreRALAEE-YIKRlRI-KTP-SPEQPV 392
|
170 180 190
....*....|....*....|....*....|....*....
gi 727181609 623 gelggslsgGQ-----KQRVLIARALYRRPSILFMDEAT 656
Cdd:COG1129 393 ---------GNlsggnQQKVVLAKWLATDPKVLILDEPT 422
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
511-660 |
3.16e-08 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 55.23 E-value: 3.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 511 LSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGiniHDIGINNYR---ECIACVLQED------KLLAGS 581
Cdd:COG4167 32 VSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILING---HKLEYGDYKyrcKHIRMIFQDPntslnpRLNIGQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 582 IAE-----NICsFDAHPDTEFIVECAK-------HCNIHDDIMkmpmgyetlvgelggslSGGQKQRVLIARALYRRPSI 649
Cdd:COG4167 109 ILEeplrlNTD-LTAEEREERIFATLRlvgllpeHANFYPHML-----------------SSGQKQRVALARALILQPKI 170
|
170
....*....|.
gi 727181609 650 LFMDEATSHLD 660
Cdd:COG4167 171 IIADEALAALD 181
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
506-553 |
3.44e-08 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 56.01 E-value: 3.44e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 727181609 506 PVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFING 553
Cdd:PRK11650 18 QVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGG 65
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
498-698 |
3.56e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 55.56 E-value: 3.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 498 YQYDSLSRpvipgLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIH----DIGINNYRECIACVLQ 573
Cdd:PRK13646 18 YEHQAIHD-----VNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIThktkDKYIRPVRKRIGMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 574 --EDKLLAGSIAENIcsfdahpdtEFiveCAKHCNIHDDIMK-------MPMGYETLVGELG-GSLSGGQKQRVLIARAL 643
Cdd:PRK13646 93 fpESQLFEDTVEREI---------IF---GPKNFKMNLDEVKnyahrllMDLGFSRDVMSQSpFQMSGGQMRKIAIVSIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 644 YRRPSILFMDEATSHLDLDNEKRVNEAISSLKM----TRVIIAHRPSTIAS-ADRVITLQ 698
Cdd:PRK13646 161 AMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTdenkTIILVSHDMNEVARyADEVIVMK 220
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
511-698 |
3.64e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 57.10 E-value: 3.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 511 LSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFInginihdiginnyRECIACVLQEDKLLAGSIAENICSFD 590
Cdd:PTZ00243 679 VSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWA-------------ERSIAYVPQQAWIMNATVRGNILFFD 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 591 AHpDTEFIVECAKHCNIHDDIMKMPMGYETLVGELGGSLSGGQKQRVLIARALYRRPSILFMDEATSHLDLDNEKRVNEA 670
Cdd:PTZ00243 746 EE-DAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEE 824
|
170 180 190
....*....|....*....|....*....|.
gi 727181609 671 --ISSLK-MTRVIIAHRPSTIASADRVITLQ 698
Cdd:PTZ00243 825 cfLGALAgKTRVLATHQVHVVPRADYVVALG 855
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
492-560 |
4.00e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 55.50 E-value: 4.00e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 727181609 492 EVRDLLYQYDSlsRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFING-----INIHDIG 560
Cdd:COG4152 3 ELKGLTKRFGD--KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGepldpEDRRRIG 74
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
510-661 |
4.09e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 55.74 E-value: 4.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 510 GLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINI------------HDIGI---NNY-----RECIA 569
Cdd:PRK11308 33 GVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlkadpeaqkllrQKIQIvfqNPYgslnpRKKVG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 570 CVLQE-----DKLLAGSIAENICSFDAHP--DTEFivecakhcniHDDIMKMPMGyetlvgelggslsgGQKQRVLIARA 642
Cdd:PRK11308 113 QILEEpllinTSLSAAERREKALAMMAKVglRPEH----------YDRYPHMFSG--------------GQRQRIAIARA 168
|
170
....*....|....*....
gi 727181609 643 LYRRPSILFMDEATSHLDL 661
Cdd:PRK11308 169 LMLDPDVVVADEPVSALDV 187
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
489-698 |
4.45e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 55.12 E-value: 4.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 489 VTFEVRDLLYQYDS-LSRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIG----INN 563
Cdd:PRK13643 2 IKFEKVNYTYQPNSpFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 564 YRECIACVLQ--EDKLLAGSIAENIcsfdAHPDTEFIVECAKHCNIHDDIMKMPMGYETLVGELGGSLSGGQKQRVLIAR 641
Cdd:PRK13643 82 VRKKVGVVFQfpESQLFEETVLKDV----AFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAG 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 727181609 642 ALYRRPSILFMDEATSHLDLDNE---KRVNEAISSLKMTRVIIAHRPSTIAS-ADRVITLQ 698
Cdd:PRK13643 158 ILAMEPEVLVLDEPTAGLDPKARiemMQLFESIHQSGQTVVLVTHLMDDVADyADYVYLLE 218
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
510-558 |
5.56e-08 |
|
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: 55.85 E-value: 5.56e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 727181609 510 GLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLePTEGRLFINGINIHD 558
Cdd:COG4172 304 GVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDG 351
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
181-437 |
5.88e-08 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 54.95 E-value: 5.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 181 LSLVIEAV-NLLMPVGTQLVMDHVIQAGDH---------NLLVIICVGLLFFILFRTcvsMFRSWISIVMGALIDIQWKS 250
Cdd:cd18780 3 IALLVSSGtNLALPYFFGQVIDAVTNHSGSggeealralNQAVLILLGVVLIGSIAT---FLRSWLFTLAGERVVARLRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 251 GLFDHLMKLPLAYFEKRKLGDIQSRFGSLDAIRTTFTTSIVSSIIDGIMSV-GVFIMMFMyggwLVWVASGFTVLYV-LL 328
Cdd:cd18780 80 RLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIiGGLVFMFT----TSWKLTLVMLSVVpPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 329 RLSTY---RYYRQASEEQLVKSAKASSHFMETLYSIATLKSL-GLAGTRSQFWLNLNiDTANANIRVTKLDMFFGGVNAF 404
Cdd:cd18780 156 SIGAViygKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFaKETKEVSRYSEKIN-ESYLLGKKLARASGGFNGFMGA 234
|
250 260 270
....*....|....*....|....*....|...
gi 727181609 405 LAACDQIVILWLGASLVIDSQMTLGMFVAFNAY 437
Cdd:cd18780 235 AAQLAIVLVLWYGGRLVIDGELTTGLLTSFLLY 267
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
493-695 |
7.07e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 56.28 E-value: 7.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 493 VRDLLYQYDS-LSRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFInginihdiginnYRECIACV 571
Cdd:PLN03130 617 IKNGYFSWDSkAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV------------IRGTVAYV 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 572 LQEDKLLAGSIAENICsFDAHPDTEFIVECAKHCNIHDDIMKMPMGYETLVGELGGSLSGGQKQRVLIARALYRRPSILF 651
Cdd:PLN03130 685 PQVSWIFNATVRDNIL-FGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYI 763
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 727181609 652 MDEATSHLDLDNEKRVNEaiSSLK-----MTRVIIAHRPSTIASADRVI 695
Cdd:PLN03130 764 FDDPLSALDAHVGRQVFD--KCIKdelrgKTRVLVTNQLHFLSQVDRII 810
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
485-660 |
8.43e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 54.43 E-value: 8.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 485 PNEAVTFEVRDLLYQYDSlsRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGiNNY 564
Cdd:PRK13537 2 PMSVAPIDFRNVEKRYGD--KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRA-RHA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 565 RECIACVLQEDKLLAG-SIAENICSF------DAHPDTEFI---VECAKHCNIHDDIMKMPMGyetlvgelggslsgGQK 634
Cdd:PRK13537 79 RQRVGVVPQFDNLDPDfTVRENLLVFgryfglSAAAARALVpplLEFAKLENKADAKVGELSG--------------GMK 144
|
170 180
....*....|....*....|....*.
gi 727181609 635 QRVLIARALYRRPSILFMDEATSHLD 660
Cdd:PRK13537 145 RRLTLARALVNDPDVLVLDEPTTGLD 170
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
486-661 |
8.59e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 54.03 E-value: 8.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 486 NEAVTFEVRDLLYQYDSLSrpVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHdIGINNYR 565
Cdd:PRK15112 9 NLSKTFRYRTGWFRRQTVE--AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLH-FGDYSYR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 566 -ECIACVLQEDkllagSIAEN-------ICSFDAHPDTEFIVEcAKHCNIHDDIMKMPMGYETlVGELGGSLSGGQKQRV 637
Cdd:PRK15112 86 sQRIRMIFQDP-----STSLNprqrisqILDFPLRLNTDLEPE-QREKQIIETLRQVGLLPDH-ASYYPHMLAPGQKQRL 158
|
170 180
....*....|....*....|....
gi 727181609 638 LIARALYRRPSILFMDEATSHLDL 661
Cdd:PRK15112 159 GLARALILRPKVIIADEALASLDM 182
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
461-540 |
9.29e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.02 E-value: 9.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 461 HNERLADIVLSTTEEekPYRKICNPNEAVTFEVRDLLYQYDSlsRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCG 540
Cdd:PRK10938 233 HSEQLEGVQLPEPDE--PSARHALPANEPRIVLNNGVVSYND--RPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG 308
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
480-586 |
9.99e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 55.03 E-value: 9.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 480 RKICNPNEAVtFEVRDLLYQyDSLSRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDI 559
Cdd:COG3845 248 KAPAEPGEVV-LEVENLSVR-DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGL 325
|
90 100 110
....*....|....*....|....*....|...
gi 727181609 560 GINNYREC-IACVlQEDKLLAG-----SIAENI 586
Cdd:COG3845 326 SPRERRRLgVAYI-PEDRLGRGlvpdmSVAENL 357
|
|
| Peptidase_C39_likeA |
cd02417 |
A sub-family of peptidase C39 which contains Cyclolysin and Hemolysin processing peptidases. ... |
27-139 |
1.04e-07 |
|
A sub-family of peptidase C39 which contains Cyclolysin and Hemolysin processing peptidases. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is not conserved in this sub-family.
Pssm-ID: 239098 [Multi-domain] Cd Length: 121 Bit Score: 51.09 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 27 EAAECGLASLAMVCGYYGMHIDMLSMRQKFDISARGATLSSLIAIAENLNLKTRALSLSLDEIHQVKRPCILHWDMNHFV 106
Cdd:cd02417 3 TKPDSGLLALVLLARYHGIAADPEQLRHEFGLAGEPFNSTELLLAAKSLGLKAKAVRQPVERLARLPLPALAWDDDGGHF 82
|
90 100 110
....*....|....*....|....*....|....
gi 727181609 107 VLVNIRGGRITLHDPAFGR-RVIGLQEFSLHFTG 139
Cdd:cd02417 83 ILAKLDGQKYLIQDPISQRpEVLSREEFEARWSG 116
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
507-698 |
1.16e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 53.24 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 507 VIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINnyreciacvlQEDKLLAGSIAENI 586
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEE----------ARAKLRAKHVGFVF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 587 CSF------DAHPDTEFIV----ECAKHCNIHDDIMKMPMGYETLVGELGGSLSGGQKQRVLIARALYRRPSILFMDEAT 656
Cdd:PRK10584 95 QSFmliptlNALENVELPAllrgESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPT 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 727181609 657 SHLDLDNEKRVNEAISSLK----MTRVIIAHRPSTIASADRVITLQ 698
Cdd:PRK10584 175 GNLDRQTGDKIADLLFSLNrehgTTLILVTHDLQLAARCDRRLRLV 220
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
511-684 |
1.16e-07 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 53.48 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 511 LSLQIAAGESVAIVGPSGVGKTTLMKLMCGLL---EPTEGRLFINGINIHDIG-----INNYRECIACVLQEDKLLAG-S 581
Cdd:PRK09984 23 VDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQREGrlardIRKSRANTGYIFQQFNLVNRlS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 582 IAENICsFDAHPDTEFIVEC------AKHCNIHDDIMKMPMGYetLVGELGGSLSGGQKQRVLIARALYRRPSILFMDEA 655
Cdd:PRK09984 103 VLENVL-IGALGSTPFWRTCfswftrEQKQRALQALTRVGMVH--FAHQRVSTLSGGQQQRVAIARALMQQAKVILADEP 179
|
170 180 190
....*....|....*....|....*....|...
gi 727181609 656 TSHLDLDNEKRVNEAISSLK----MTRVIIAHR 684
Cdd:PRK09984 180 IASLDPESARIVMDTLRDINqndgITVVVTLHQ 212
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
521-662 |
1.51e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 54.87 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 521 VAIVGPSGVGKTTLMKLMCGLLEPTEGRLF--------------INGINIHDIGINNYRECIACVLqEDKLLAgsiaeNI 586
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGTVFrsakvrmavfsqhhVDGLDLSSNPLLYMMRCFPGVP-EQKLRA-----HL 611
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 727181609 587 CSFdahpdtefivecakhcNIHDDIMKMPMgyETLvgelggslSGGQKQRVLIARALYRRPSILFMDEATSHLDLD 662
Cdd:PLN03073 612 GSF----------------GVTGNLALQPM--YTL--------SGGQKSRVAFAKITFKKPHILLLDEPSNHLDLD 661
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
507-686 |
1.55e-07 |
|
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: 54.75 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 507 VIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINginihdiginnyREC-IACVLQEDKLLAGSIAEN 585
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKP------------AKGkLFYVPQRPYMTLGTLRDQ 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 586 IC----SFD------AHPDTEFIVEcakhcNIH-DDIMKMPMGYETlVGELGGSLSGGQKQRVLIARALYRRPSILFMDE 654
Cdd:TIGR00954 535 IIypdsSEDmkrrglSDKDLEQILD-----NVQlTHILEREGGWSA-VQDWMDVLSGGEKQRIAMARLFYHKPQFAILDE 608
|
170 180 190
....*....|....*....|....*....|..
gi 727181609 655 ATSHLDLDNEKRVNEAISSLKMTRVIIAHRPS 686
Cdd:TIGR00954 609 CTSAVSVDVEGYMYRLCREFGITLFSVSHRKS 640
|
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
178-451 |
1.92e-07 |
|
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents the HMT1 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster. HMT1 is closely related to Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria.
Pssm-ID: 350027 [Multi-domain] Cd Length: 290 Bit Score: 53.30 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 178 IFALSLVIEAVNLLMPVGTQLVMDHVIQAGDHnllvIICVGLLFFILFR-----TCVSMFRSWISIVMGALIDIQWKSGL 252
Cdd:cd18583 1 CFLCLLAERVLNVLVPRQLGIIVDSLSGGSGK----SPWKEIGLYVLLRflqsgGGLGLLRSWLWIPVEQYSYRALSTAA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 253 FDHLMKLPLAYFEKRKLGDIQSRFGSLDAIRTTFTT---SIVSSIIDGIMSVGVFIMMF-MYGGWLVwVASGFTVLYVLL 328
Cdd:cd18583 77 FNHVMNLSMDFHDSKKSGEVLKAIEQGSSINDLLEQilfQIVPMIIDLVIAIVYLYYLFdPYMGLIV-AVVMVLYVWSTI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 329 RLSTYR--YYRQASEeqlvKSAKASSHFMETL------------------YSIATLKSLGlAGTRSQFWLNLnidtANAn 388
Cdd:cd18583 156 KLTSWRtkLRRDMID----ADREERSILTESLlnwetvkyfnrepyekerYREAVKNYQK-AERKYLFSLNL----LNA- 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 727181609 389 irVTKLDMFFGgvnaFLAACdqivilWLGASLVIDSQMTLGMFVAFNAYRGQ-----------FSDRASNLIDM 451
Cdd:cd18583 226 --VQSLILTLG----LLAGC------FLAAYQVSQGQATVGDFVTLLTYWAQlsgplnffatlYRSIQSDLIDA 287
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
489-697 |
3.30e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 52.33 E-value: 3.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 489 VTFEVRDLLYQYDS-LSRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFInGINIHDIGINN---- 563
Cdd:PRK13634 3 ITFQKVEHRYQYKTpFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGKKNkklk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 564 -YRECIACVLQ--EDKLLAGSIAENICsFDAhpdTEFIVECAKHCNIHDDIMKMPMGYETLVGELGGSLSGGQKQRVLIA 640
Cdd:PRK13634 82 pLRKKVGIVFQfpEHQLFEETVEKDIC-FGP---MNFGVSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 727181609 641 RALYRRPSILFMDEATSHLDLDNEKRVNEAISSLK----MTRVIIAHRPSTIAS-ADRVITL 697
Cdd:PRK13634 158 GVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHkekgLTTVLVTHSMEDAARyADQIVVM 219
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
495-660 |
3.49e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 52.32 E-value: 3.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 495 DLLYQYDSlsRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFING--INIHDIGINNYRECIACVL 572
Cdd:PRK13638 6 DLWFRYQD--EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 573 QEDKllagsiaENICSFDAHPDTEFIVEcakhcNI---HDDIMKMPMGYETLVGEL------GGSLSGGQKQRVLIARAL 643
Cdd:PRK13638 84 QDPE-------QQIFYTDIDSDIAFSLR-----NLgvpEAEITRRVDEALTLVDAQhfrhqpIQCLSHGQKKRVAIAGAL 151
|
170
....*....|....*..
gi 727181609 644 YRRPSILFMDEATSHLD 660
Cdd:PRK13638 152 VLQARYLLLDEPTAGLD 168
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
511-698 |
3.84e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 52.14 E-value: 3.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 511 LSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIH----DIGINNYRECIACVLQ--EDKLLAGSIAE 584
Cdd:PRK13641 26 ISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKKLRKKVSLVFQfpEAQLFENTVLK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 585 NI----CSFDAHPD--TEFIVECAKHCNIHDDIM-KMPMgyetlvgelggSLSGGQKQRVLIARALYRRPSILFMDEATS 657
Cdd:PRK13641 106 DVefgpKNFGFSEDeaKEKALKWLKKVGLSEDLIsKSPF-----------ELSGGQMRRVAIAGVMAYEPEILCLDEPAA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 727181609 658 HLDLDNEKRVNEAISSLKM---TRVIIAHRPSTIAS-ADRVITLQ 698
Cdd:PRK13641 175 GLDPEGRKEMMQLFKDYQKaghTVILVTHNMDDVAEyADDVLVLE 219
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
505-694 |
3.90e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 52.02 E-value: 3.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 505 RPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINNYREC------IACVLQEDKLL 578
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNYRDVlefrrrVGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 579 AGSIAENICS-FDAH---PDTEF-------IVECAKHCNIHDDIMKMPMgyetlvgelggSLSGGQKQRVLIARALYRRP 647
Cdd:PRK14271 114 PMSIMDNVLAgVRAHklvPRKEFrgvaqarLTEVGLWDAVKDRLSDSPF-----------RLSGGQQQLLCLARTLAVNP 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 727181609 648 SILFMDEATSHLDLDNEKRVNEAISSL--KMTRVIIAHrpsTIASADRV 694
Cdd:PRK14271 183 EVLLLDEPTSALDPTTTEKIEEFIRSLadRLTVIIVTH---NLAQAARI 228
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
507-697 |
4.97e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 52.16 E-value: 4.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 507 VIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINI-HDIG------------INNY---RECIAC 570
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIgDKKNnhelitnpyskkIKNFkelRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 571 VLQ-----------EDKLLAGSIAENICSFDAHPDTEFIVEcakhcnihddimKMPMGYETLvGELGGSLSGGQKQRVLI 639
Cdd:PRK13631 121 VFQfpeyqlfkdtiEKDIMFGPVALGVKKSEAKKLAKFYLN------------KMGLDDSYL-ERSPFGLSGGQKRRVAI 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 727181609 640 ARALYRRPSILFMDEATSHLDLDNEKRVNEAISSLKM---TRVIIAHRPSTIAS-ADRVITL 697
Cdd:PRK13631 188 AGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAnnkTVFVITHTMEHVLEvADEVIVM 249
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
478-697 |
5.01e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 52.94 E-value: 5.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 478 PYRKICNPNEAVTFEVRDLLYQYDSLSRPVIPGLSLQIAAGESVAIVGPSGVGKT-TLMKLMcGLLEPTEG-----RLFI 551
Cdd:PRK10261 2 PHSDELDARDVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALM-RLLEQAGGlvqcdKMLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 552 NGINIHDIGINNYREC---------IACVLQEDKL-------LAGSIAENICSFDAHPDTEFIVECAKHCnihdDIMKMP 615
Cdd:PRK10261 81 RRRSRQVIELSEQSAAqmrhvrgadMAMIFQEPMTslnpvftVGEQIAESIRLHQGASREEAMVEAKRML----DQVRIP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 616 MGyETLVGELGGSLSGGQKQRVLIARALYRRPSILFMDEATSHLDLDNEKRVNEAISSLK----MTRVIIAHRPSTIAS- 690
Cdd:PRK10261 157 EA-QTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQkemsMGVIFITHDMGVVAEi 235
|
....*..
gi 727181609 691 ADRVITL 697
Cdd:PRK10261 236 ADRVLVM 242
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
490-571 |
5.48e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 52.67 E-value: 5.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 490 TFEVRDLLYQYDSLSRPVIPgLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINNYRECIA 569
Cdd:PRK10522 322 TLELRNVTFAYQDNGFSVGP-INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFS 400
|
..
gi 727181609 570 CV 571
Cdd:PRK10522 401 AV 402
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
511-683 |
5.54e-07 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 51.17 E-value: 5.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 511 LSLQIAAGESVAIVGPSGVGKTTLMKLMcGLLE-PTEGRLfinginihdiginnyreciacvlqedkllagSIAENICSF 589
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKSSLLRVL-NLLEmPRSGTL-------------------------------NIAGNHFDF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 590 DAHPDTEFIVECAK-------------HCNIHDDIMKMPMGYETLVGELGGSLSGG---------------------QKQ 635
Cdd:PRK11124 69 SKTPSDKAIRELRRnvgmvfqqynlwpHLTVQQNLIEAPCRVLGLSKDQALARAEKllerlrlkpyadrfplhlsggQQQ 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 727181609 636 RVLIARALYRRPSILFMDEATSHLDLDNEKRVNEAISSLK---MTRVIIAH 683
Cdd:PRK11124 149 RVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAetgITQVIVTH 199
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
476-695 |
6.40e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 52.70 E-value: 6.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 476 EKPYRKICNPNEAVTFEVRDLlyqydslSRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGin 555
Cdd:PRK10762 243 EDQYPRLDKAPGEVRLKVDNL-------SGPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDG-- 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 556 iHDIGINNYRECIAC---VLQEDK-----LLAGSIAEN--ICSFDA---------HPD-----TEFIvecaKHCNIHDDI 611
Cdd:PRK10762 314 -HEVVTRSPQDGLANgivYISEDRkrdglVLGMSVKENmsLTALRYfsraggslkHADeqqavSDFI----RLFNIKTPS 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 612 MKMPMGyetlvgelggSLSGGQKQRVLIARALYRRPSILFMDEATSHLDLDNEKRVNEAISSLK---MTRVIIAHR-PST 687
Cdd:PRK10762 389 MEQAIG----------LLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKaegLSIILVSSEmPEV 458
|
....*...
gi 727181609 688 IASADRVI 695
Cdd:PRK10762 459 LGMSDRIL 466
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
492-562 |
6.88e-07 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 50.22 E-value: 6.88e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 727181609 492 EVRDLLYQYDSlsRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGL--LEPTEGRLFINGINIHDIGIN 562
Cdd:cd03217 2 EIKDLHVSVGG--KEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPE 72
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
512-660 |
7.39e-07 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 52.03 E-value: 7.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 512 SLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIG----INNYRECIACVLQEDKLLAG-SIAENi 586
Cdd:COG4175 47 SFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSkkelRELRRKKMSMVFQHFALLPHrTVLEN- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 587 csfdahpdTEF---------------------IVECAKHCNihddimKMP------MgyetlvgelggslsggqKQRVLI 639
Cdd:COG4175 126 --------VAFgleiqgvpkaerrerarealeLVGLAGWED------SYPdelsggM-----------------QQRVGL 174
|
170 180
....*....|....*....|.
gi 727181609 640 ARALYRRPSILFMDEATSHLD 660
Cdd:COG4175 175 ARALATDPDILLMDEAFSALD 195
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
492-660 |
7.54e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 51.63 E-value: 7.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDLLYQYD---SLSRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHD---------- 558
Cdd:PRK13651 4 KVKNIVKIFNkklPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNkkktkekekv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 559 -----IG---------INNYRECIACVLQ--EDKLLAGSIAENICsFDAhpdTEFIVECAKHCNIHDDIMKMPMGYETLV 622
Cdd:PRK13651 84 leklvIQktrfkkikkIKEIRRRVGVVFQfaEYQLFEQTIEKDII-FGP---VSMGVSKEEAKKRAAKYIELVGLDESYL 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 727181609 623 GELGGSLSGGQKQRVLIARALYRRPSILFMDEATSHLD 660
Cdd:PRK13651 160 QRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLD 197
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
506-553 |
9.16e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 50.23 E-value: 9.16e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 727181609 506 PVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFING 553
Cdd:PRK13543 25 PVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDG 72
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
511-659 |
9.21e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 52.09 E-value: 9.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 511 LSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINI----HDIGinnYRECIACVLQE----DKLlagSI 582
Cdd:PRK09700 24 VNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYnkldHKLA---AQLGIGIIYQElsviDEL---TV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 583 AENIcSFDAHPDTEF----IVECAKhCNIHDDIMKMPMGYETLVGELGGSLSGGQKQRVLIARALYRRPSILFMDEATSH 658
Cdd:PRK09700 98 LENL-YIGRHLTKKVcgvnIIDWRE-MRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSS 175
|
.
gi 727181609 659 L 659
Cdd:PRK09700 176 L 176
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
491-559 |
1.59e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 50.03 E-value: 1.59e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 727181609 491 FEVRDLLYQYDSlsRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGllEP----TEGRLFINGINIHDI 559
Cdd:CHL00131 8 LEIKNLHASVNE--NEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPaykiLEGDILFKGESILDL 76
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
180-442 |
1.65e-06 |
|
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1/ABCB7 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.
Pssm-ID: 350026 [Multi-domain] Cd Length: 292 Bit Score: 50.19 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 180 ALSLVI--EAVNLLMPVGTQLVMDHvIQAGDHNLLVIICVGLLFFILFRTCVSMFRSWISIVMG-ALIDIQWKSGL--FD 254
Cdd:cd18582 1 ALLLLVlaKLLNVAVPFLLKYAVDA-LSAPASALLAVPLLLLLAYGLARILSSLFNELRDALFArVSQRAVRRLALrvFR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 255 HLMKLPLAYFEKRKLGDIQSrfgSLD----AIRTTFTT---SIVSSIIDGIMSVGvfIMMFMYGGWLVWVASGFTVLYVL 327
Cdd:cd18582 80 HLHSLSLRFHLSRKTGALSR---AIErgtrGIEFLLRFllfNILPTILELLLVCG--ILWYLYGWSYALITLVTVALYVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 328 --LRLSTYR--YYRQASEeqlvKSAKASSHFMETLYSIATLKSLGLAGTRSQFWLNLNIDTANANIRVTKLDMFFGGVNA 403
Cdd:cd18582 155 ftIKVTEWRtkFRREMNE----ADNEANAKAVDSLLNYETVKYFNNEEYEAERYDKALAKYEKAAVKSQTSLALLNIGQA 230
|
250 260 270
....*....|....*....|....*....|....*....
gi 727181609 404 FLAACDQIVILWLGASLVIDSQMTLGMFVAFNAYRGQFS 442
Cdd:cd18582 231 LIISLGLTAIMLLAAQGVVAGTLTVGDFVLVNTYLLQLY 269
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
508-659 |
2.12e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 50.98 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 508 IPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLE--PTEGRLFINGINIHDIGINNY-RECIACVLQEDKLLAG-SIA 583
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVPElSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 584 ENICSFD--AHP-----DTEFIVECAK---HCNIHDDIMKMPMGYETLvgelggslsgGQKQRVLIARALYRRPSILFMD 653
Cdd:TIGR02633 97 ENIFLGNeiTLPggrmaYNAMYLRAKNllrELQLDADNVTRPVGDYGG----------GQQQLVEIAKALNKQARLLILD 166
|
....*.
gi 727181609 654 EATSHL 659
Cdd:TIGR02633 167 EPSSSL 172
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
181-429 |
2.83e-06 |
|
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350005 [Multi-domain] Cd Length: 289 Bit Score: 49.59 E-value: 2.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 181 LSLVIEAVNLLMPVGTQLVMDHVIQAGDHNLLVIICVGLLFFILFRTCVSMFRSWISIVMGALIDIQWKSGLFDHLMKLP 260
Cdd:cd18561 4 LGLLITALYIAQAWLLARALARIFAGGPWEDIMPPLAGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRLFAKLLKLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 261 LAYFEKRKLGDIQSRF-GSLDAIRTTFTTSIVSSIIDGIMSVGVFIMMFmyggWLVWVASG-----FTVLYVLLRLStYR 334
Cdd:cd18561 84 PGYLEGERTGELQTTVvDGVEALEAYYGRYLPQLLVALLGPLLILIYLF----FLDPLVALillvfALLIPLSPALW-DR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 335 YYRQASEEQLVKSAKASSHFMETLYSIATLKSLGLAGTRSQFWLNLNIDTANANIRVTKLDMFFGGVNAFLAACDQIVIL 414
Cdd:cd18561 159 LAKDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSLLSSGIMGLATALGTALAL 238
|
250
....*....|....*
gi 727181609 415 WLGASLVIDSQMTLG 429
Cdd:cd18561 239 GVGALRVLGGQLTLS 253
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
173-451 |
3.09e-06 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 49.49 E-value: 3.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 173 SALVKIFAL------SLVIEAVNLLMPVGTQLVMDHVIQAGDHNLLVIicVGLLFFILFrtCVSMFRSWISivmgaliDI 246
Cdd:cd18565 8 SILNRLFDLapplliGVAIDAVFNGEASFLPLVPASLGPADPRGQLWL--LGGLTVAAF--LLESLFQYLS-------GV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 247 QWKS-----------GLFDHLMKLPLAYFEKRKLGDIQS----------RFgsldairttFTTSIVSSIIDGIMSVGVFI 305
Cdd:cd18565 77 LWRRfaqrvqhdlrtDTYDHVQRLDMAFFEDRQTGDLMSvlnndvnqleRF---------LDDGANSIIRVVVTVLGIGA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 306 MMFMYGGWLVWVAsgFTVLYVLLrLSTYRYYRQASEEQL-VKSA--KASSHFMETLYSIATLKSLglagTRSQFwLNLNI 382
Cdd:cd18565 148 ILFYLNWQLALVA--LLPVPLII-AGTYWFQRRIEPRYRaVREAvgDLNARLENNLSGIAVIKAF----TAEDF-ERERV 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 383 DTA-----NANIRVTKLDMFFGGVNAFLAACDQIVILWLGASLVID------SQMTLGMFVAFNAYRGQF---SDRASNL 448
Cdd:cd18565 220 ADAseeyrDANWRAIRLRAAFFPVIRLVAGAGFVATFVVGGYWVLDgpplftGTLTVGTLVTFLFYTQRLlwpLTRLGDL 299
|
...
gi 727181609 449 IDM 451
Cdd:cd18565 300 IDQ 302
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
492-551 |
3.46e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 50.32 E-value: 3.46e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 492 EVRDLLYQYDSlsRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFI 551
Cdd:TIGR03719 324 EAENLTKAFGD--KLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI 381
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
494-699 |
4.04e-06 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 48.01 E-value: 4.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 494 RDLLYQYD--SLSRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEP--TEGRLFINGINIHDiginNYRECIA 569
Cdd:cd03232 7 KNLNYTVPvkGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgvITGEILINGRPLDK----NFQRSTG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 570 CVLQEDkllagsiaenicsfdAHPDTEFIVECAK-HCNIHDdimkmpmgyetlvgelggsLSGGQKQRVLIARALYRRPS 648
Cdd:cd03232 83 YVEQQD---------------VHSPNLTVREALRfSALLRG-------------------LSVEQRKRLTIGVELAAKPS 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 727181609 649 ILFMDEATSHLDLDNEKRVNEAISSLKMT-RVIIA--HRPS--TIASADRVITLQP 699
Cdd:cd03232 129 ILFLDEPTSGLDSQAAYNIVRFLKKLADSgQAILCtiHQPSasIFEKFDRLLLLKR 184
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
500-564 |
4.80e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 48.02 E-value: 4.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 500 YDSLSRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINI---------------HDIGINNY 564
Cdd:PRK13540 9 FDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIkkdlctyqkqlcfvgHRSGINPY 88
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
504-675 |
5.88e-06 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 48.19 E-value: 5.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 504 SRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRlfinginihdiginnyreciacVLQEDKLLAGSIA 583
Cdd:PRK09544 16 QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGV----------------------IKRNGKLRIGYVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 584 ENIcsfdaHPDTEFIVECAKHCNIHDDIMK---MP----MGYETLVGELGGSLSGGQKQRVLIARALYRRPSILFMDEAT 656
Cdd:PRK09544 74 QKL-----YLDTTLPLTVNRFLRLRPGTKKediLPalkrVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPT 148
|
170
....*....|....*....
gi 727181609 657 SHLDLDNEKRVNEAISSLK 675
Cdd:PRK09544 149 QGVDVNGQVALYDLIDQLR 167
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
253-432 |
7.92e-06 |
|
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH transporter; The CydC protein, together with the CydD protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350029 [Multi-domain] Cd Length: 290 Bit Score: 48.25 E-value: 7.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 253 FDHLMKLPLAYFEKRKLGDIQSRF-GSLDAIRTTFTTSIVSSIIDGIMSVGVFIMMFMYGGWL-VWVASGFTVLYVLLRL 330
Cdd:cd18585 75 YRKLEPLAPARLQKYRSGDLLNRIvADIDTLDNLYLRVLSPPVVALLVILATILFLAFFSPALaLILLAGLLLAGVVIPL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 331 STYRYYRQASEEQLVKSAKASSHFMETLYSIATLKSLGLAGTRSQFWLNLNIDTANANIRVTKLDMFFGGVNAFLAACDQ 410
Cdd:cd18585 155 LFYRLGKKIGQQLVQLRAELRTELVDGLQGMAELLIFGALERQRQQLEQLSDALIKEQRRLARLSGLSQALMILLSGLTV 234
|
170 180
....*....|....*....|....*
gi 727181609 411 IVILWLGASLVIDSQMT---LGMFV 432
Cdd:cd18585 235 WLVLWLGAPLVQNGALDgalLAMLV 259
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
495-698 |
9.08e-06 |
|
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: 46.80 E-value: 9.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 495 DLLYQYDSLSRPVIPGlslQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIhdiginNYREciacvlQE 574
Cdd:cd03222 5 DCVKRYGVFFLLVELG---VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITP------VYKP------QY 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 575 DKLLAGSIaenicsfdahpdtefivecakhcnihddimkmpmgyetlvgelggslsggqkQRVLIARALYRRPSILFMDE 654
Cdd:cd03222 70 IDLSGGEL----------------------------------------------------QRVAIAAALLRNATFYLFDE 97
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 727181609 655 ATSHLDLDNEKRVNEAISSLKM----TRVIIAHRPSTIAS-ADRVITLQ 698
Cdd:cd03222 98 PSAYLDIEQRLNAARAIRRLSEegkkTALVVEHDLAVLDYlSDRIHVFE 146
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
181-437 |
1.02e-05 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 47.78 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 181 LSLVIEAV-NLLMPVGTQLVMDHVIQAGDHNLLVIICVGLLFFILFRTCVSMFRSWISIVMGALIDIQWKSGLFDHLMKL 259
Cdd:cd18548 6 LFKLLEVLlELLLPTLMADIIDEGIANGDLSYILRTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 260 PLAYFEK--------RKLGDIQsrfgsldAIRTTFTTSIVSSIIDGIMSVGVFIMMFMYGGWLVWVASG-----FTVLYV 326
Cdd:cd18548 86 SFAEIDKfgtsslitRLTNDVT-------QVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVaipilALVVFL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 327 LLRLSTYRYYR-QASEEQLVKSAKasshfmETLYSIATLKSLGLAGTRSQFWLNLNIDTANANIRVTKLDMFFGGVNAFL 405
Cdd:cd18548 159 IMKKAIPLFKKvQKKLDRLNRVVR------ENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLI 232
|
250 260 270
....*....|....*....|....*....|..
gi 727181609 406 AACDQIVILWLGASLVIDSQMTLGMFVAFNAY 437
Cdd:cd18548 233 MNLAIVAILWFGGHLINAGSLQVGDLVAFINY 264
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
252-456 |
2.22e-05 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 46.70 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 252 LFDHLMKLPLAYFEKRKLGDIQSrfgsldaiRTTFTTSIVSSIIDGIMSV-------GVFIMMFMYggWLVWVASGFT-- 322
Cdd:cd18589 75 VFAAVLRQEIAFFDSNQTGDIVS--------RVTTDTEDMSESLSENLSLlmwylarGLFLFIFML--WLSPKLALLTal 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 323 ---VLYVLLRLSTyrYYRQASEEQLVKS-AKASSHFMETLYSIATLKSLGlagtrsqfwlnlNIDTANANIR-------- 390
Cdd:cd18589 145 glpLLLLVPKFVG--KFQQSLAVQVQKSlARANQVAVETFSAMKTVRSFA------------NEEGEAQRYRqrlqktyr 210
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 391 VTKLDMFFGGVN----AFLAACDQIVILWLGASLVIDSQMTLGMFVAFNAYRGQFSDRASNLIDMVIRLR 456
Cdd:cd18589 211 LNKKEAAAYAVSmwtsSFSGLALKVGILYYGGQLVTAGTVSSGDLVTFVLYELQFTSAVEVLLSYYPSVM 280
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
511-553 |
2.76e-05 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 46.08 E-value: 2.76e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 727181609 511 LSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLePTEGRLFING 553
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAG 56
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
493-586 |
3.03e-05 |
|
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: 47.70 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 493 VRDLLYQYDSLSRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIhDIGINNYRECIACVL 572
Cdd:TIGR01257 931 VKNLVKIFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCP 1009
|
90
....*....|....*
gi 727181609 573 QEDKLLAG-SIAENI 586
Cdd:TIGR01257 1010 QHNILFHHlTVAEHI 1024
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
507-654 |
3.26e-05 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 46.03 E-value: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 507 VIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINN-YRECIACVLQEDKLLAG-SIAE 584
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMREAVAIVPEGRRVFSRmTVEE 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 585 NICSFDAHPDTEFIVEcakhcNIHDDIMKMPMGYETLVGELGGSLSGGQkQRVLIARALYRRPSILFMDE 654
Cdd:PRK11614 100 NLAMGGFFAERDQFQE-----RIKWVYELFPRLHERRIQRAGTMSGGEQ-QMLAIGRALMSQPRLLLLDE 163
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
510-684 |
3.30e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 46.83 E-value: 3.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 510 GLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHdigINNYREC----IACVLQEDKLLAG-SIAE 584
Cdd:PRK11288 22 DISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMR---FASTTAAlaagVAIIYQELHLVPEmTVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 585 NIC---------SFDAHPDTEFIVECAKHCNIHDDiMKMPMGYETLvgelggslsgGQKQRVLIARALYRRPSILFMDEA 655
Cdd:PRK11288 99 NLYlgqlphkggIVNRRLLNYEAREQLEHLGVDID-PDTPLKYLSI----------GQRQMVEIAKALARNARVIAFDEP 167
|
170 180 190
....*....|....*....|....*....|....*
gi 727181609 656 TSHL---DLDNEKRVneaISSLKMT-RVII--AHR 684
Cdd:PRK11288 168 TSSLsarEIEQLFRV---IRELRAEgRVILyvSHR 199
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
505-660 |
3.42e-05 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 46.04 E-value: 3.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 505 RPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGIN-NYRECIACVLQE--------- 574
Cdd:PRK10895 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHaRARRGIGYLPQEasifrrlsv 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 575 -DKLLAG-SIAENICSFDAHPDTEFIVECAKHCNIHDDIMKMPMGYEtlvgelggslsggqKQRVLIARALYRRPSILFM 652
Cdd:PRK10895 96 yDNLMAVlQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGE--------------RRRVEIARALAANPKFILL 161
|
....*...
gi 727181609 653 DEATSHLD 660
Cdd:PRK10895 162 DEPFAGVD 169
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
504-697 |
3.50e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 45.97 E-value: 3.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 504 SRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCG-LLEPTE-------GRLFINGINIHDIGINNYrECIACVL--Q 573
Cdd:PRK13547 13 HRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGGAprgarvtGDVTLNGEPLAAIDAPRL-ARLRAVLpqA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 574 EDKLLAGSIAEnICSFDAHPDtefiVECAKHCNIHD-DIMKMPM---GYETLVGELGGSLSGGQKQRVLIARAL------ 643
Cdd:PRK13547 92 AQPAFAFSARE-IVLLGRYPH----ARRAGALTHRDgEIAWQALalaGATALVGRDVTTLSGGELARVQFARVLaqlwpp 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 727181609 644 ---YRRPSILFMDEATSHLDLDNEKRVNEAISSL----KMTRVIIAHRPSTIAS-ADRVITL 697
Cdd:PRK13547 167 hdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLardwNLGVLAIVHDPNLAARhADRIAML 228
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
505-683 |
3.67e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.09 E-value: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 505 RPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRL-FINGINI-----HDIginNYRECIACVLQEDKLL 578
Cdd:PRK10636 325 RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLgyfaqHQL---EFLRADESPLQHLARL 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 579 AGSIAEN-----ICSFDAHPDtefivecakhcNIHDDIMKMPMGyetlvgelggslsggQKQRVLIARALYRRPSILFMD 653
Cdd:PRK10636 402 APQELEQklrdyLGGFGFQGD-----------KVTEETRRFSGG---------------EKARLVLALIVWQRPNLLLLD 455
|
170 180 190
....*....|....*....|....*....|
gi 727181609 654 EATSHLDLDNEKRVNEAISSLKMTRVIIAH 683
Cdd:PRK10636 456 EPTNHLDLDMRQALTEALIDFEGALVVVSH 485
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
492-556 |
4.03e-05 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 46.60 E-value: 4.03e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 727181609 492 EVRDL--LYQYDSLSRPVIPGLSLQIAAGESVAIVGPSGVGKT-TLMKLMcGLLEP----TEGRLFINGINI 556
Cdd:COG4172 8 SVEDLsvAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSIL-RLLPDpaahPSGSILFDGQDL 78
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
518-671 |
4.58e-05 |
|
The ATP-binding cassette domain 1 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, RLIs 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: 213203 [Multi-domain] Cd Length: 255 Bit Score: 45.44 E-value: 4.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 518 GESVAIVGPSGVGKTTLMKLMCGLLEPTEGRlFINGINIHDIgINNYReciACVLQE--DKLLAGSI--AENICSFDAHP 593
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGK-FDDPPDWDEI-LDEFR---GSELQNyfTKLLEGDVkvIVKPQYVDLIP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 594 -----DTEFIVECAKHCNIHDDIMKMpMGYETLVGELGGSLSGGQKQRVLIARALYRRPSILFMDEATSHLDLdnEKRVN 668
Cdd:cd03236 101 kavkgKVGELLKKKDERGKLDELVDQ-LELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI--KQRLN 177
|
...
gi 727181609 669 EAI 671
Cdd:cd03236 178 AAR 180
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
505-660 |
5.12e-05 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 46.47 E-value: 5.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 505 RPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFIN-GINIhdiginNYREciacvlQEDKL------ 577
Cdd:TIGR03719 18 KEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQpGIKV------GYLP------QEPQLdptktv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 578 ------LAGSIAENICSFD------AHPDTEF---IVECAK------HCNIHD---------DIMKMPMGyETLVGELGG 627
Cdd:TIGR03719 86 renveeGVAEIKDALDRFNeisakyAEPDADFdklAAEQAElqeiidAADAWDldsqleiamDALRCPPW-DADVTKLSG 164
|
170 180 190
....*....|....*....|....*....|...
gi 727181609 628 SlsggQKQRVLIARALYRRPSILFMDEATSHLD 660
Cdd:TIGR03719 165 G----ERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
512-559 |
6.11e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 46.27 E-value: 6.11e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 727181609 512 SLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEG--RLFINGINIHDI 559
Cdd:NF033858 286 SFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGeaWLFGQPVDAGDI 335
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
199-370 |
7.83e-05 |
|
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH transporter, and a homolog AarD; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350028 [Multi-domain] Cd Length: 290 Bit Score: 45.09 E-value: 7.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 199 VMDHVIQAGDH-NLLVIICVGLLFFILFRTCVSMFRSWISIVMGALIDIQWKSGLFDHLMKLPLAYFEKRKLGDIQSRFG 277
Cdd:cd18584 22 IIAGVFLEGAGlAALLPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLLARLLALGPALLRRQSSGELATLLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 278 S-LDAIRTTFTTSIVSSIIDGIMSVGVFIMMFmyggWLVWVaSGFTVL---------YVLLRLSTyryyRQASEEQLVKS 347
Cdd:cd18584 102 EgVDALDGYFARYLPQLVLAAIVPLLILVAVF----PLDWV-SALILLvtapliplfMILIGKAA----QAASRRQWAAL 172
|
170 180
....*....|....*....|...
gi 727181609 348 AKASSHFMETLYSIATLKSLGLA 370
Cdd:cd18584 173 SRLSGHFLDRLRGLPTLKLFGRA 195
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
634-683 |
8.53e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 45.65 E-value: 8.53e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 727181609 634 KQRVLIARALYRRPSILFMDEATSHLDLDNEKRVNEAISSLKMTRVIIAH 683
Cdd:PRK15064 161 KLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISH 210
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
512-549 |
1.02e-04 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 44.53 E-value: 1.02e-04
10 20 30
....*....|....*....|....*....|....*...
gi 727181609 512 SLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRL 549
Cdd:PRK11701 26 SFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEV 63
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
219-440 |
1.29e-04 |
|
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group represents the Atm1/ABCB7/HMT1/ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster.
Pssm-ID: 350004 [Multi-domain] Cd Length: 292 Bit Score: 44.52 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 219 LLFFILFRTCVSMFRS-----WISIVMGALIDIQWKsgLFDHLMKLPLAYFEKRKLGDIQSRF----GSLDAIRTTFTTS 289
Cdd:cd18560 41 ILLYALLRFSSKLLKElrsllYRRVQQNAYRELSLK--TFAHLHSLSLDWHLSKKTGEVVRIMdrgtESANTLLSYLVFY 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 290 IVSSIIDGIMSVGVFimMFMYGGWLVWVASGFTVLY----VLLRLSTYRYYRQASEEQLVKSAKASSHFM--ETL----- 358
Cdd:cd18560 119 LVPTLLELIVVSVVF--AFHFGAWLALIVFLSVLLYgvftIKVTEWRTKFRRAANKKDNEAHDIAVDSLLnfETVkyftn 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 359 -----------------YSIATLKSLGLAGTRSQFWLNLNidtananirvtkldmffggvnafLAACdqiviLWLGASLV 421
Cdd:cd18560 197 ekyevdrygeavkeyqkSSVKVQASLSLLNVGQQLIIQLG-----------------------LTLG-----LLLAGYRV 248
|
250
....*....|....*....
gi 727181609 422 IDSQMTLGMFVAFNAYRGQ 440
Cdd:cd18560 249 VDGGLSVGDFVAVNTYIFQ 267
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
505-551 |
1.47e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 45.11 E-value: 1.47e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 727181609 505 RPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFI 551
Cdd:PRK11819 337 RLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI 383
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
505-698 |
2.00e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 44.70 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 505 RPVIPGLSLQIAAGESVAIVGPSGVGKT-TLMKLMCGLLEP----TEGRLFINGINIHDIGINNYREC----IACVLQE- 574
Cdd:PRK15134 22 RTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRGVrgnkIAMIFQEp 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 575 ----------DKLLAGSIAENICSFDAHPDTEfIVECAKHCNIHD------DIMKMPMGYEtlvgelggslsggqKQRVL 638
Cdd:PRK15134 102 mvslnplhtlEKQLYEVLSLHRGMRREAARGE-ILNCLDRVGIRQaakrltDYPHQLSGGE--------------RQRVM 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 727181609 639 IARALYRRPSILFMDEATSHLDLDNEKRV----NEAISSLKMTRVIIAHRPSTIAS-ADRVITLQ 698
Cdd:PRK15134 167 IAMALLTRPELLIADEPTTALDVSVQAQIlqllRELQQELNMGLLFITHNLSIVRKlADRVAVMQ 231
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
511-697 |
2.57e-04 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 43.94 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 511 LSLQIAAGESVAIVGPSGVGKT-TLMKLMcGLLEP---TEGRLFING---INIHDIGINNYR-ECIACVLQE-------- 574
Cdd:PRK09473 35 LNFSLRAGETLGIVGESGSGKSqTAFALM-GLLAAngrIGGSATFNGreiLNLPEKELNKLRaEQISMIFQDpmtslnpy 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 575 ----DKLL-----------AGSIAENICSFDAHPdtefIVECAKHcnihddiMKM-PMGYETlvgelggslsgGQKQRVL 638
Cdd:PRK09473 114 mrvgEQLMevlmlhkgmskAEAFEESVRMLDAVK----MPEARKR-------MKMyPHEFSG-----------GMRQRVM 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 727181609 639 IARALYRRPSILFMDEATSHLDLDNEKRVNEAISSLKM---TRVI-IAHRPSTIA-SADRVITL 697
Cdd:PRK09473 172 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefnTAIImITHDLGVVAgICDKVLVM 235
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
490-698 |
2.89e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 44.33 E-value: 2.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 490 TFEVRDLLYQ--YDSLSRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEP---TEGRLFINGINIHdigiNNY 564
Cdd:TIGR00956 759 IFHWRNLTYEvkIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPLD----SSF 834
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 565 RECIACVLQEDKLLAGSIAENICSFDAH---PDTEFIVECAKHCNIHDDIMKMPMGYETLVGELGGSLSGGQKQRVLIAR 641
Cdd:TIGR00956 835 QRSIGYVQQQDLHLPTSTVRESLRFSAYlrqPKSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGEGLNVEQRKRLTIGV 914
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 727181609 642 ALYRRP-SILFMDEATSHLDLDNEKRVNEAISSLKMT-RVIIA--HRPSTI--ASADRVITLQ 698
Cdd:TIGR00956 915 ELVAKPkLLLFLDEPTSGLDSQTAWSICKLMRKLADHgQAILCtiHQPSAIlfEEFDRLLLLQ 977
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
489-683 |
2.92e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 43.93 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 489 VTFEVRDLLYQYDSLSRPVIPGLSLQIAAGESVAIVGPSGVGKTT----LMKLMcgllePTEGRLFINGINIHDIGINN- 563
Cdd:PRK15134 283 VAFPIRKGILKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRRQl 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 564 --YRECIACVLQE-----------DKLLAGSIAENICSFDAHPDTEFIVECAKHCNIHDDI-MKMPMGYETlvgelggsl 629
Cdd:PRK15134 358 lpVRHRIQVVFQDpnsslnprlnvLQIIEEGLRVHQPTLSAAQREQQVIAVMEEVGLDPETrHRYPAEFSG--------- 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 727181609 630 sgGQKQRVLIARALYRRPSILFMDEATSHLDLDNEKRVNEAISSLKMTR----VIIAH 683
Cdd:PRK15134 429 --GQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHqlayLFISH 484
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
518-686 |
4.04e-04 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 43.50 E-value: 4.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 518 GESVAIVGPSGVGKTTLMKLMCGLLEP---TEGRLFINGiniHDIGINNYREcIACVLQEDKLLAGSI-AENICSFDAHP 593
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNG---MPIDAKEMRA-ISAYVQQDDLFIPTLtVREHLMFQAHL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 594 DTEFIVECAKHCNIHDDIMKMpMGY----ETLVGELGGSLSGG--QKQRVLIARALYRRPSILFMDEATSHLDLDNEKRV 667
Cdd:TIGR00955 127 RMPRRVTKKEKRERVDEVLQA-LGLrkcaNTRIGVPGRVKGLSggERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSV 205
|
170 180
....*....|....*....|..
gi 727181609 668 NEAISSLKMTRVIIA---HRPS 686
Cdd:TIGR00955 206 VQVLKGLAQKGKTIIctiHQPS 227
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
505-694 |
4.07e-04 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 42.76 E-value: 4.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 505 RPVIPGLSLQIAAGESVAIVGPSGVGKTtlmkLMC----GLLEP----TEGRLFINGINIHDIGINNYRecIACVLQEDK 576
Cdd:PRK10418 16 QPLVHGVSLTLQRGRVLALVGGSGSGKS----LTCaaalGILPAgvrqTAGRVLLDGKPVAPCALRGRK--IATIMQNPR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 577 -------LLAGSIAENICSFDAHPDTEFIVECAKHCNIHDD--IMKM---PMGYETLvgelggslsggqkQRVLIARALY 644
Cdd:PRK10418 90 safnplhTMHTHARETCLALGKPADDATLTAALEAVGLENAarVLKLypfEMSGGML-------------QRMMIALALL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 727181609 645 RRPSILFMDEATSHLDLDNEKRVNEAISSLKMTR----VIIAHRPSTIAS-ADRV 694
Cdd:PRK10418 157 CEAPFIIADEPTTDLDVVAQARILDLLESIVQKRalgmLLVTHDMGVVARlADDV 211
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
201-436 |
5.08e-04 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 42.85 E-value: 5.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 201 DHVIQAGDHNLLVIICVGLLFFILfrTCVSMFrSWIsiVMGALIDIQWKSGLFDHLMKLPLAYFEKRKLGDIQSRFGS-L 279
Cdd:cd18577 40 DEFLDDVNKYALYFVYLGIGSFVL--SYIQTA-CWT--ITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSdT 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 280 DAIRTTFTTSIVSSIIDGIMSVGVFIMMFMYGgW-LVWVASGFTVLYVLLRLSTYRYYRQASEEQLVKSAKASSHFMETL 358
Cdd:cd18577 115 NLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYS-WkLTLVLLATLPLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEAL 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 727181609 359 YSIATLKSLGLAGTRSQFWLNLNIDTANANIRVTKLDMFFGGVNAFLAACDQIVILWLGASLVIDSQMTLG-MFVAFNA 436
Cdd:cd18577 194 SSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLFFIIFAMYALAFWYGSRLVRDGEISPGdVLTVFFA 272
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
510-586 |
6.35e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 43.07 E-value: 6.35e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 727181609 510 GLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINNYREC-IACVLQEDKLLAG-SIAENI 586
Cdd:PRK10762 22 GAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAgIGIIHQELNLIPQlTIAENI 100
|
|
| Peptidase_C39_likeD |
cd02421 |
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
33-142 |
6.41e-04 |
|
A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is not conserved in this sub-family.
Pssm-ID: 239102 [Multi-domain] Cd Length: 124 Bit Score: 40.30 E-value: 6.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 33 LASLAMVCGYYG--MHIDMLSMRQKFDiSARgATLSSLIAIAENLNLKTRALSLSLDEIHQVKRPCILHWDMNHFVVLVN 110
Cdd:cd02421 9 LDCLVLLARQFGkpASRDSLVAGLPLD-DGR-LSPALFPRAAARAGLSARVVRRPLDAIPTLLLPAILLLKNGRACVLLG 86
|
90 100 110
....*....|....*....|....*....|....
gi 727181609 111 IRGGRITLHDPAFGRRV--IGLQEFSLHFTGIAL 142
Cdd:cd02421 87 VDDGHARILDPESGGGEveISLEELEEEYSGYAI 120
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
492-557 |
6.67e-04 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 41.90 E-value: 6.67e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 727181609 492 EVRDLLYQYDSLSrpVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIH 557
Cdd:PRK11300 7 SVSGLMMRFGGLL--AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIE 70
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
253-368 |
9.17e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350050 [Multi-domain] Cd Length: 290 Bit Score: 41.69 E-value: 9.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 253 FDHLMKLPLAYFEKRKLGDIQSRFG----SLD-----AIRTTFTTsiVSSIIdgimsvGVFIMMFMYGGWLVWVASGFTV 323
Cdd:cd18606 75 LKRVLRAPMSFFDTTPLGRILNRFSkdtdVLDnelpdSLRMFLYT--LSSII------GTFILIIIYLPWFAIALPPLLV 146
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 727181609 324 LYVLLrlstYRYYRQASEEqlVK---SAKAS---SHFMETLYSIATLKSLG 368
Cdd:cd18606 147 LYYFI----ANYYRASSRE--LKrleSILRSfvyANFSESLSGLSTIRAYG 191
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
505-660 |
1.05e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.41 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 505 RPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFI-NGINIhdiGI----------NNYRECIACVLQ 573
Cdd:PRK11819 20 KQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPaPGIKV---GYlpqepqldpeKTVRENVEEGVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 574 EDK-LLA--GSIAENIcsfdAHPDTEF---IVECAK------HCNIHD---------DIMKMPMGyETLVGELGGSlsgg 632
Cdd:PRK11819 97 EVKaALDrfNEIYAAY----AEPDADFdalAAEQGElqeiidAADAWDldsqleiamDALRCPPW-DAKVTKLSGG---- 167
|
170 180
....*....|....*....|....*...
gi 727181609 633 QKQRVLIARALYRRPSILFMDEATSHLD 660
Cdd:PRK11819 168 ERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
513-697 |
1.22e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 42.24 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 513 LQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINginihdiginnyRECIACVLQED--KLLAGS----IAENI 586
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE------------QDLIVARLQQDppRNVEGTvydfVAEGI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 587 CSFDAH--------------PDTEFIVECAK------HCN-------IHDDIMKMPMGYETLVGELGGSLSggqkQRVLI 639
Cdd:PRK11147 92 EEQAEYlkryhdishlvetdPSEKNLNELAKlqeqldHHNlwqlenrINEVLAQLGLDPDAALSSLSGGWL----RKAAL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 727181609 640 ARALYRRPSILFMDEATSHLDLDNEKRVNEAISSLKMTRVIIAHRPSTIAS-ADRVITL 697
Cdd:PRK11147 168 GRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNmATRIVDL 226
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
509-586 |
1.47e-03 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 41.82 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 509 PGL----SLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGiniHDIGINNYRECIAC--VL-QEDKLLAG- 580
Cdd:PRK11288 266 PGLrepiSFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDG---KPIDIRSPRDAIRAgiMLcPEDRKAEGi 342
|
90
....*....|
gi 727181609 581 ----SIAENI 586
Cdd:PRK11288 343 ipvhSVADNI 352
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
512-694 |
1.52e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 41.70 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 512 SLQIAAGESVAIVGPSGVGKTTLMKLMCGLLePT---EGRLFINGINIHDIGINNYREC-IACVLQEDKLLAG-SIAENI 586
Cdd:NF040905 21 NLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGEVCRFKDIRDSEALgIVIIHQELALIPYlSIAENI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 587 csFDAHPDTEFIV-----------ECAKHCNIHDD----IMKMPMGyetlvgelggslsggQKQRVLIARALYRRPSILF 651
Cdd:NF040905 100 --FLGNERAKRGVidwnetnrrarELLAKVGLDESpdtlVTDIGVG---------------KQQLVEIAKALSKDVKLLI 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 727181609 652 MDEATSHLDLDNEKRVNEAISSLK---MTRVIIAHRPSTIAS-ADRV 694
Cdd:NF040905 163 LDEPTAALNEEDSAALLDLLLELKaqgITSIIISHKLNEIRRvADSI 209
|
|
| ABC_6TM_ABCB6 |
cd18581 |
Six-transmembrane helical domain of the ATP-binding cassette subfamily B member 6, ... |
179-440 |
1.54e-03 |
|
Six-transmembrane helical domain of the ATP-binding cassette subfamily B member 6, mitochondrial; This group represents the ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, ABCB6 (ABC transporter subfamily B, member 6) is closely related to yeast ATM1 and human ABCB7, which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.
Pssm-ID: 350025 [Multi-domain] Cd Length: 300 Bit Score: 41.08 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 179 FALSLVIEAVNLLMPVGTQLVMDHVIQAGDHNL------LVIICVGLLFFILFRTC----VSMFRSWISIVMGALIDIQW 248
Cdd:cd18581 2 LLLLAAGRVVNVLVPILYKKIVDSLTPDSADSPlafpwaLILLYVFLKFLQGGGSGsvglLSNLRSFLWIPVQQFTTREI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 249 KSGLFDHLMKLPLAYFEKRKLGD---IQSR-FGSLDAIRTTFTTSIVSSIIDGIMSVGVFIMMF-MYGGWLVWVA-SGFT 322
Cdd:cd18581 82 SVKLFAHLHSLSLRWHLSRKTGEvlrVMDRgTSSINSLLSYVLFNIGPTIADIIIAIIYFAIAFnPWFGLIVFVTmALYL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 323 VLYVLLRLSTYRYYRQASEEQLVKSAKASSHFM--ETL-------YSIATLKSLGLAGTRSQFWLNLNIDTANANIRVTk 393
Cdd:cd18581 162 ILTIIITEWRTKFRREMNKLDNEKRAKAVDSLLnfETVkyynaerFEVERYRRAIDDYQVAEWKSNASLNLLNTAQNLI- 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 727181609 394 ldmffggVNAFLAAcdqivILWLGASLVIDSQMTLGMFVAFNAYRGQ 440
Cdd:cd18581 241 -------ITIGLLA-----GSLLCAYFVVEGKLTVGDFVLFLTYIIQ 275
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
510-540 |
1.59e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 42.03 E-value: 1.59e-03
10 20 30
....*....|....*....|....*....|.
gi 727181609 510 GLSLQIAAGESVAIVGPSGVGKTTLMKLMCG 540
Cdd:NF033858 19 DVSLDIPAGCMVGLIGPDGVGKSSLLSLIAG 49
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
511-660 |
3.18e-03 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 40.80 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 511 LSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFINGINIHDIGINNYRECIACVLQEDKLLAG-----SIAEN 585
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVYLPEDRQSSGlyldaPLAWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 586 ICSFdAHPDTEFIVECAKH--------------CNIHDDIMKMPMGyetlvgelggslsgGQKQRVLIARALYRRPSILF 651
Cdd:PRK15439 362 VCAL-THNRRGFWIKPAREnavleryrralnikFNHAEQAARTLSG--------------GNQQKVLIAKCLEASPQLLI 426
|
....*....
gi 727181609 652 MDEATSHLD 660
Cdd:PRK15439 427 VDEPTRGVD 435
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
505-556 |
4.41e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 39.39 E-value: 4.41e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 727181609 505 RPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGL--LEPTEGRLFINGINI 556
Cdd:PRK09580 14 KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDL 67
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
485-697 |
5.77e-03 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 39.81 E-value: 5.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 485 PNEA-----VTFEVRDL-LYQYDSLSRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPT-EGRLFINGiniH 557
Cdd:TIGR02633 247 PHEPheigdVILEARNLtCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFING---K 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 558 DIGINNYRECIA---CVLQEDKLLAG-----SIAENIC-----SF------DAHPDTEFIVECAKHCNIHDDIMKMPMGy 618
Cdd:TIGR02633 324 PVDIRNPAQAIRagiAMVPEDRKRHGivpilGVGKNITlsvlkSFcfkmriDAAAELQIIGSAIQRLKVKTASPFLPIG- 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 619 etlvgelggSLSGGQKQRVLIARALYRRPSILFMDEATSHLDLDNEKRVNEAISSLKMTRVII----AHRPSTIASADRV 694
Cdd:TIGR02633 403 ---------RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIivvsSELAEVLGLSDRV 473
|
...
gi 727181609 695 ITL 697
Cdd:TIGR02633 474 LVI 476
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
518-674 |
6.59e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 39.79 E-value: 6.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 518 GESVAIVGPSGVGKTTLMKLMCGLLEPTEGRlFINGINIHDIgINNYReciACVLQE--DKLLAGSI--AENICSFDAHP 593
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILSGELIPNLGD-YEEEPSWDEV-LKRFR---GTELQNyfKKLYNGEIkvVHKPQYVDLIP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 594 D-----TEFIVECAKHCNIHDDIMKMpMGYETLVGELGGSLSGGQKQRVLIARALYRRPSILFMDEATSHLDLDNEKRVN 668
Cdd:PRK13409 174 KvfkgkVRELLKKVDERGKLDEVVER-LGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVA 252
|
....*.
gi 727181609 669 EAISSL 674
Cdd:PRK13409 253 RLIREL 258
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
484-553 |
7.67e-03 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 39.00 E-value: 7.67e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 484 NPNEAVTFEVRDLLYQYDSlsRPVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFING 553
Cdd:PRK10575 5 TNHSDTTFALRNVSFRVPG--RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDA 72
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
522-660 |
8.62e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 39.44 E-value: 8.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 522 AIVGPSGVGKTTLMKLMCGllEPTEGrlFINGinihDIGINNY---RECIA-----C---------VLQEDKLLAGS--- 581
Cdd:PLN03140 910 ALMGVSGAGKTTLMDVLAG--RKTGG--YIEG----DIRISGFpkkQETFArisgyCeqndihspqVTVRESLIYSAflr 981
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 582 IAENICSFDAHPDTEFIVECAKHCNIHDDIMKMP--MGYETlvgelggslsgGQKQRVLIARALYRRPSILFMDEATSHL 659
Cdd:PLN03140 982 LPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPgvTGLST-----------EQRKRLTIAVELVANPSIIFMDEPTSGL 1050
|
.
gi 727181609 660 D 660
Cdd:PLN03140 1051 D 1051
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
473-553 |
9.09e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 39.10 E-value: 9.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727181609 473 TEEEKPYRKICNPNEAVTFEVRDLLYQYdslsrpVIPGLSLQIAAGESVAIVGPSGVGKTTLMKLMCGLLEPTEGRLFIN 552
Cdd:PRK13545 11 TKKYKMYNKPFDKLKDLFFRSKDGEYHY------ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIK 84
|
.
gi 727181609 553 G 553
Cdd:PRK13545 85 G 85
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
635-697 |
9.99e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 38.57 E-value: 9.99e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 727181609 635 QRVLIARALYRRPSILFMDEATSHLDLDNEKRVNEAISSLK----MTRVIIAHRPSTIA-SADRVITL 697
Cdd:PRK11022 160 QRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQqkenMALVLITHDLALVAeAAHKIIVM 227
|
|
| |
