|
Name |
Accession |
Description |
Interval |
E-value |
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
18-700 |
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: 686.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 18 KSRFPMIHQTESSECGLACLAMICGYYGKNIDIFTLRQKFKLSSRGTDLASLNDIAVKMHMSTRAVSVELDELHSVKLPC 97
Cdd:COG2274 1 RRKVPFVLQMEAADCGLACLAMIARYYGRPVSLEELREALGVSRDGLSLLGLLRAARRLGLRARGVRLDLEELAELPLPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 98 ILHWDFNHFVVLTKIKNGKFTVHDPSVGIVKVAKSELSKKFTGIVLEIWPGNSFLKENVKnKISLRAMLENTHGLYSALT 177
Cdd:COG2274 81 ILHWDGNHFVVLEGVDGDKVTIADPATGRRKLSLEEFAESWTGVALLLEPTPEFDKRGEK-PFGLRWFLRLLRRYRRLLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 178 KIFFLSIIIESINLVMPVATQLVMDHAIPANDSGLLTLICFGLVFFVALRTITGLIRSWTVLIMSSFINAQWQKGLLQHL 257
Cdd:COG2274 160 QVLLASLLINLLALATPLFTQVVIDRVLPNQDLSTLWVLAIGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 258 LKLPLEYFERRKIGDIQSRFGSLNTLQETFTTSVVGAIIDSIMIIGLLIMLVLYGGWLTWFVILFTCLYVFIRVLTYNRY 337
Cdd:COG2274 240 LRLPLSFFESRSVGDLASRFRDVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 338 RQLSEESLIKDARANSFFMETLYGIATVKVQGLNKRREENWFNLEVDSINTGIKVSRLNLFFGGINTLIATMEQILILWL 417
Cdd:COG2274 320 RRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 418 GASLVISGNMTIGMFVAFSSYRGQFSDRIASFIDFLLRLQIMSLHNERVSDIALTEVTPFKDDIPVKNDMCPVSLSAKNI 497
Cdd:COG2274 400 GAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPPEREEGRSKLSLPRLKGDIELENV 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 498 SYKYDSYASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKLIACVLQDDR 577
Cdd:COG2274 480 SFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVF 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 578 LFSGTLRDNICSFSTQIDDNWLIECARFAQIHDDIERMPMGYDTLIGELGEGLSGGQKQRIFIARAIYKKPSILFMDEAT 657
Cdd:COG2274 560 LFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEAT 639
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1533513286 658 SSLDHTNEQYINDAIKSL--NITRIVIAHRKSTINSADRIIALQE 700
Cdd:COG2274 640 SALDAETEAIILENLRRLlkGRTVIIIAHRLSTIRLADRIIVLDK 684
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
20-700 |
1.70e-122 |
|
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: 381.21 E-value: 1.70e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 20 RFPMIHQTESSECGLACLAMICGYYGKNIDIFTLRQKFKLSSRGTDLASLNDIAVKMHMSTRAVSVELDELHSVKLPCIL 99
Cdd:TIGR03796 1 RTPTVLQMEAVECGAASLAMILAYYGRYVPLEELREECGVSRDGSKASNLLKAARSYGLEAKGFRKELDALAELPLPYIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 100 HWDFNHFVVLTKIKNGKFTVHDPSVGIVKVAKSELSKKFTGIVLEIWPGNSFLKENVKNKIsLRAMLENTHGLYSALTKI 179
Cdd:TIGR03796 81 FWNFNHFVVVEGFRGGRVYLNDPALGPRTVSLEEFDESFTGVVLTFEPGPEFQKGGRKPSL-LRALWRRLRGSRGALLYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 180 FFLSIIIESINLVMPVATQLVMDHAIPANDSGLLTLICFGLVFFVALRTI------TGLIRSWTVLIMSSFINAQWQkgl 253
Cdd:TIGR03796 160 LLAGLLLVLPGLVIPAFSQIFVDEILVQGRQDWLRPLLLGMGLTALLQGVltwlqlYYLRRLEIKLAVGMSARFLWH--- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 254 lqhLLKLPLEYFERRKIGDIQSRFGSLNTLQETFTTSVVGAIIDSIMIIGLLIMLVLYGGWLTWFVILFTCLYVFirVLT 333
Cdd:TIGR03796 237 ---ILRLPVRFFAQRHAGDIASRVQLNDQVAEFLSGQLATTALDAVMLVFYALLMLLYDPVLTLIGIAFAAINVL--ALQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 334 YN-RYRQLSEESLIKD-ARANSFFMETLYGIATVKVQGLNKRREENWFNLEVDSINTGIKVSRLNLFFGGINTLIATMEQ 411
Cdd:TIGR03796 312 LVsRRRVDANRRLQQDaGKLTGVAISGLQSIETLKASGLESDFFSRWAGYQAKLLNAQQELGVLTQILGVLPTLLTSLNS 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 412 ILILWLGASLVISGNMTIGMFVAFSSYRGQFSDRIASFIDFLLRLQIMSLHNERVSDIALTEVTP-FKDDIPVKNDMCPV 490
Cdd:TIGR03796 392 ALILVVGGLRVMEGQLTIGMLVAFQSLMSSFLEPVNNLVGFGGTLQELEGDLNRLDDVLRNPVDPlLEEPEGSAATSEPP 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 491 S-LSA----KNISYKYDSYASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNY 565
Cdd:TIGR03796 472 RrLSGyvelRNITFGYSPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVL 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 566 QKLIACVLQDDRLFSGTLRDNICSFSTQIDDNWLIECARFAQIHDDIERMPMGYDTLIGELGEGLSGGQKQRIFIARAIY 645
Cdd:TIGR03796 552 ANSVAMVDQDIFLFEGTVRDNLTLWDPTIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALV 631
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 1533513286 646 KKPSILFMDEATSSLDHTNEQYINDAIKSLNITRIVIAHRKSTINSADRIIALQE 700
Cdd:TIGR03796 632 RNPSILILDEATSALDPETEKIIDDNLRRRGCTCIIVAHRLSTIRDCDEIIVLER 686
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
174-466 |
1.97e-116 |
|
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: 351.38 E-value: 1.97e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 174 SALTKIFFLSIIIESINLVMPVATQLVMDHAIPANDSGLLTLICFGLVFFVALRTITGLIRSWTVLIMSSFINAQWQKGL 253
Cdd:cd18567 2 RALLQILLLSLALELFALASPLYLQLVIDEVIVSGDRDLLTVLAIGFGLLLLLQALLSALRSWLVLYLSTSLNLQWTSNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 254 LQHLLKLPLEYFERRKIGDIQSRFGSLNTLQETFTTSVVGAIIDSIMIIGLLIMLVLYGGWLTWFVILFTCLYVFIRVLT 333
Cdd:cd18567 82 FRHLLRLPLSYFEKRHLGDIVSRFGSLDEIQQTLTTGFVEALLDGLMAILTLVMMFLYSPKLALIVLAAVALYALLRLAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 334 YNRYRQLSEESLIKDARANSFFMETLYGIATVKVQGLNKRREENWFNLEVDSINTGIKVSRLNLFFGGINTLIATMEQIL 413
Cdd:cd18567 162 YPPLRRATEEQIVASAKEQSHFLETIRGIQTIKLFGREAEREARWLNLLVDAINADIRLQRLQILFSAANGLLFGLENIL 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1533513286 414 ILWLGASLVISGNMTIGMFVAFSSYRGQFSDRIASFIDFLLRLQIMSLHNERV 466
Cdd:cd18567 242 VIYLGALLVLDGEFTVGMLFAFLAYKDQFSSRASSLIDKLFELRMLRLHLERL 294
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
176-700 |
5.78e-113 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 352.54 E-value: 5.78e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 176 LTKIFFLSIIIESINLVMPVATQLVMDHAIPANDSGLLTLICFGLVFFVALRTITGLIRSWTVLIMSSFINAQWQKGLLQ 255
Cdd:COG1132 23 LILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLFE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 256 HLLKLPLEYFERRKIGDIQSRFGS-LNTLQETFTTSVVGAIIDSIMIIGLLIMLVLYGGWLTWFVILFTCLYVFIRVLTY 334
Cdd:COG1132 103 HLLRLPLSFFDRRRTGDLLSRLTNdVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 335 NRYRQLSEESLIKDARANSFFMETLYGIATVKVQGLnKRREENWFNLEVDSI-NTGIKVSRLNLFFGGINTLIATMEQIL 413
Cdd:COG1132 183 RRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGR-EERELERFREANEELrRANLRAARLSALFFPLMELLGNLGLAL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 414 ILWLGASLVISGNMTIGMFVAFSSYRGQFSDRIASFIDFLLRLQIMSLHNERVSDI--ALTEVTPFKDDIPVKNDmcPVS 491
Cdd:COG1132 262 VLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELldEPPEIPDPPGAVPLPPV--RGE 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISYKYDSyASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKLIAC 571
Cdd:COG1132 340 IEFENVSFSYPG-DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGV 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 572 VLQDDRLFSGTLRDNICSFSTQIDDNWLIECARFAQIHDDIERMPMGYDTLIgelgeglsggQKQRIFIARAIYKKPSIL 651
Cdd:COG1132 419 VPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVgergvnlsggQRQRIAIARALLKDPPIL 498
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1533513286 652 FMDEATSSLDHTNEQYINDAIKSL--NITRIVIAHRKSTINSADRIIALQE 700
Cdd:COG1132 499 ILDEATSALDTETEALIQEALERLmkGRTTIVIAHRLSTIRNADRILVLDD 549
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
33-700 |
2.42e-85 |
|
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: 283.17 E-value: 2.42e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 33 GLACLAMICGYYGKNIDIFTLRQKFKLSSRGTDLASLNDIAVKMHMSTRAVSVELDELHSVKLPCILhWDFNHFVVLTKI 112
Cdd:TIGR01846 1 GLEALSLLAQVHNIAVTPSQLRHMLGHAGASLDDLEILLAAKQLGLKAKAVKVSIGRLNKLPLPALI-DGEGGWFVLGKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 113 KNGKFTVHDP-SVGIVKVAKSELSKKFTGIVLEIWPGNSFLKEnVKNKIS--LRAMLENTHglysALTKIFFLSIIIESI 189
Cdd:TIGR01846 80 TANGVTIYDPpGDAPEVLSREVLEALWSGTVILLATRSVAGKA-LKFGFSwfIPAIIRYRK----QFREVLLISLALQLF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 190 NLVMPVATQLVMDHAIPANDSGLLTLICFGLVFFVALRTITGLIRSWTVLIMSSFINAQWQKGLLQHLLKLPLEYFERRK 269
Cdd:TIGR01846 155 ALVTPLLFQVVIDKVLVHRGLSTLSVLALAMLAVAIFEPALGGLRTYLFAHLTSRIDVELGARLYRHLLGLPLGYFESRR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 270 IGDIQSRFGSLNTLQETFTTSVVGAIIDSIMIIGLLIMLVLYGGWLTWFVILFTCLYVFIRVLTYNRYRQLSEESLIKDA 349
Cdd:TIGR01846 235 VGDTVARVRELEQIRNFLTGSALTVVLDLLFVVVFLAVMFFYSPTLTGVVIGSLVCYALLSVFVGPILRKRVEDKFERSA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 350 RANSFFMETLYGIATVKVQGLNKRREENWFNLEVDSINTGIKVSRLNLFFGGINTLIATMEQILILWLGASLVISGNMTI 429
Cdd:TIGR01846 315 AATSFLVESVTGIETIKATATEPQFQNRWDRQLAAYVAASFRVTNLGNIAGQAIELIQKLTFAILLWFGAHLVIGGALSP 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 430 GMFVAFSSYRGQFSDRIASFIDFLLRLQIMSLHNERVSDIALTEVTPFKDD---IPVKNDmcpvSLSAKNISYKYDSYAS 506
Cdd:TIGR01846 395 GQLVAFNMLAGRVTQPVLRLAQLWQDFQQTGIALERLGDILNSPTEPRSAGlaaLPELRG----AITFENIRFRYAPDSP 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 507 YTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKLIACVLQDDRLFSGTLRDN 586
Cdd:TIGR01846 471 EVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDN 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 587 ICSFSTQIDDNWLIECARFAQIHDDIERMPMGYDTLIGELGEGLSGGQKQRIFIARAIYKKPSILFMDEATSSLDHTNEQ 666
Cdd:TIGR01846 551 IALCNPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEA 630
|
650 660 670
....*....|....*....|....*....|....*.
gi 1533513286 667 YINDAIKSL--NITRIVIAHRKSTINSADRIIALQE 700
Cdd:TIGR01846 631 LIMRNMREIcrGRTVIIIAHRLSTVRACDRIIVLEK 666
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
107-700 |
1.01e-82 |
|
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: 276.07 E-value: 1.01e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 107 VVLTKIKNGKFTVHDPSVGIVKVAKSELSKKFTGIVLEIWPGnsfLKENvknKISLRAMLENT-HGLYSALTKIFFLSII 185
Cdd:TIGR03797 74 VALLPVSRGGYEIFDPATGTRRRVDAAMAATLAPEAYMFYRP---LPDK---ALGLRDLLRFAlRGARRDLLAILAMGLL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 186 IESINLVMPVATQLVMDHAIPANDSGLLTLICFGLVFFVALRTITGLIRSWTVLIMSSFINAQWQKGLLQHLLKLPLEYF 265
Cdd:TIGR03797 148 GTLLGMLVPIATGILIGTAIPDADRSLLVQIALALLAAAVGAAAFQLAQSLAVLRLETRMDASLQAAVWDRLLRLPVSFF 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 266 ERRKIGDIQSRFGSLNTLQETFTTSVVGAIIDSIMIIGLLIMLVLYGGWLTWFVILFTclYVFIRVLTYNRYRQLSEESL 345
Cdd:TIGR03797 228 RQYSTGDLASRAMGISQIRRILSGSTLTTLLSGIFALLNLGLMFYYSWKLALVAVALA--LVAIAVTLVLGLLQVRKERR 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 346 IK--DARANSFFMETLYGIATVKVQGLNKRREENWFNLEVDSINTGIKVSRLNLFFGGINTLIATMEQILILWLGASLVI 423
Cdd:TIGR03797 306 LLelSGKISGLTVQLINGISKLRVAGAENRAFARWAKLFSRQRKLELSAQRIENLLTVFNAVLPVLTSAALFAAAISLLG 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 424 SGNMTIGMFVAFSSYRGQFSDRIASFIDFLLrlQIMSL--HNERVSDI--ALTEVTPFKDDipvkndmcPVSLSAK---- 495
Cdd:TIGR03797 386 GAGLSLGSFLAFNTAFGSFSGAVTQLSNTLI--SILAVipLWERAKPIleALPEVDEAKTD--------PGKLSGAievd 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 496 NISYKYDSYASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGlF--PASeGNIFVDGIDIKELGVNNYQKLIACVL 573
Cdd:TIGR03797 456 RVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLG-FetPES-GSVFYDGQDLAGLDVQAVRRQLGVVL 533
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 574 QDDRLFSGTLRDNIC-SFSTQIDDNWliECARFAQIHDDIERMPMGYDTLIGELGEGLSGGQKQRIFIARAIYKKPSILF 652
Cdd:TIGR03797 534 QNGRLMSGSIFENIAgGAPLTLDEAW--EAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILL 611
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 1533513286 653 MDEATSSLDHTNEQYINDAIKSLNITRIVIAHRKSTINSADRIIALQE 700
Cdd:TIGR03797 612 FDEATSALDNRTQAIVSESLERLKVTRIVIAHRLSTIRNADRIYVLDA 659
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
26-700 |
6.69e-76 |
|
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: 258.13 E-value: 6.69e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 26 QTESSECGLACLAMICGYYGKNIDIFTLRQKFKLSSRGTDLASLNDIAVKMHMSTRAVSVELD--ELHSVKLPCILH--- 100
Cdd:TIGR01193 1 QVDEKDCGIAALSMILKKYGTEYSLAKLRQLAKTDLEGTTVLGLVKAAEYLNFEAKAIQADMSlfEDKNLPLPFIAHvik 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 101 -WDFNHFVVLTKIKNGKFTVHDP--SVGIVKVAKSELSKKFTGIVLEIWPGNSFLKENVKNKiSLRAMLENTHGLYSALT 177
Cdd:TIGR01193 81 nGKLPHYYVVYGVTKNHLIIADPdpTVGITKISKEDFYEEWTGIAIFISPTPEYKPIKEKEN-SLLKFIPLITRQKKLIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 178 KIFFLSIIIESINLVMPVATQLVMDHAIPANDSGLLTLICFGLVFFVALRTITGLIRSWTVLIMSSFINAQWQKGLLQHL 257
Cdd:TIGR01193 160 NIVIAAIIVTLISIAGSYYLQKIIDTYIPHKMMGTLGIISIGLIIAYIIQQILSYIQIFLLNVLGQRLSIDIILSYIKHL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 258 LKLPLEYFERRKIGDIQSRFGSLNTLQETFTTSVVGAIIDSIMIIGLLIMLVLYGGWLTWFVILFTCLYVFIRVLTYNRY 337
Cdd:TIGR01193 240 FELPMSFFSTRRTGEIVSRFTDASSIIDALASTILSLFLDMWILVIVGLFLVRQNMLLFLLSLLSIPVYAVIIILFKRTF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 338 RQLSEESLIKDARANSFFMETLYGIATVKVQGLNKRREENWFNLEVDSINTGIKVSRLNLFFGGINTLIATMEQILILWL 417
Cdd:TIGR01193 320 NKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAERYSKIDSEFGDYLNKSFKYQKADQGQQAIKAVTKLILNVVILWT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 418 GASLVISGNMTIGMFVAFSSYRGQFSDRIASFIDFLLRLQIMSLHNERVSDIALTEVTPFKDDIPVKNDMCPVSLSAKNI 497
Cdd:TIGR01193 400 GAYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEVYLVDSEFINKKKRTELNNLNGDIVINDV 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 498 SYKYdSYASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKLIACVLQDDR 577
Cdd:TIGR01193 480 SYSY-GYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPY 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 578 LFSGTLRDNICSFS---TQIDDnwLIECARFAQIHDDIERMPMGYDTLIGELGEGLSGGQKQRIFIARAIYKKPSILFMD 654
Cdd:TIGR01193 559 IFSGSILENLLLGAkenVSQDE--IWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILD 636
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1533513286 655 EATSSLDHTNEQYINDAIKSLN-ITRIVIAHRKSTINSADRIIALQE 700
Cdd:TIGR01193 637 ESTSNLDTITEKKIVNNLLNLQdKTIIFVAHRLSVAKQSDKIIVLDH 683
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
176-466 |
1.07e-67 |
|
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: 224.31 E-value: 1.07e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 176 LTKIFFLSIIIESINLVMPVATQLVMDHAIPANDSGLLTLICFGLVFFVALRTITGLIRSWTVLIMSSFINAQWQKGLLQ 255
Cdd:cd18555 4 LISILLLSLLLQLLTLLIPILTQYVIDNVIVPGNLNLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSDFFE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 256 HLLKLPLEYFERRKIGDIQSRFGSLNTLQETFTTSVVGAIIDSIMIIGLLIMLVLYGGWLTWFVILFTCLYVFIRVLTYN 335
Cdd:cd18555 84 HLLKLPYSFFENRSSGDLLFRANSNVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLLTRK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 336 RYRQLSEESLIKDARANSFFMETLYGIATVKVQGLNKRREENWFNLEVDSINTGIKVSRLNLFFGGINTLIATMEQILIL 415
Cdd:cd18555 164 KIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNILNSISSSIQFIAPLLIL 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1533513286 416 WLGASLVISGNMTIGMFVAFSSYRGQFSDRIASFIDFLLRLQIMSLHNERV 466
Cdd:cd18555 244 WIGAYLVINGELTLGELIAFSSLAGSFLTPIVSLINSYNQFILLKSYLERL 294
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
179-700 |
4.04e-65 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 225.73 E-value: 4.04e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 179 IFFLsIIIESINLVMPVATQLVMDHAIPANDSGLLTLICFGLVFFVALRTITGLIRSWTVLIMSSFINAQWQKGLLQHLL 258
Cdd:TIGR02204 24 LVAL-LITAAATLSLPYAVRLMIDHGFSKDSSGLLNRYFAFLLVVALVLALGTAARFYLVTWLGERVVADIRRAVFAHLI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 259 KLPLEYFERRKIGDIQSRFgslnTLQETFTTSVVGAII-----DSIMIIGLLIMLVLYGGWLTWFVILFTCLYVFIRVLT 333
Cdd:TIGR02204 103 SLSPSFFDKNRSGEVVSRL----TTDTTLLQSVIGSSLsmalrNALMCIGGLIMMFITSPKLTSLVLLAVPLVLLPILLF 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 334 YNRYRQLSEESLIKDARANSFFMETLYGIATVKV-------QGLNKRREENWFNLEVDSINTGIKVSRLNLF--FGGInt 404
Cdd:TIGR02204 179 GRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAfghedaeRSRFGGAVEKAYEAARQRIRTRALLTAIVIVlvFGAI-- 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 405 liatmeqILILWLGASLVISGNMTIGMFVAFSSYRGQFSDRIASFIDFLLRLQIMSLHNERVSDIALTEvtpfkDDIPVK 484
Cdd:TIGR02204 257 -------VGVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELLQAE-----PDIKAP 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 485 NDmcPVSLSAK--------NISYKYDSYASY-TLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGI 555
Cdd:TIGR02204 325 AH--PKTLPVPlrgeiefeQVNFAYPARPDQpALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGV 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 556 DIKELGVNNYQKLIACVLQDDRLFSGTLRDNICSFSTQIDDNWLIECARFAQIHDDIERMPMGYDTLIGELGEGLSGGQK 635
Cdd:TIGR02204 403 DLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQR 482
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1533513286 636 QRIFIARAIYKKPSILFMDEATSSLDHTNEQYINDAIKSL--NITRIVIAHRKSTINSADRIIALQE 700
Cdd:TIGR02204 483 QRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLmkGRTTLIIAHRLATVLKADRIVVMDQ 549
|
|
| Peptidase_C39C |
cd02419 |
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
22-147 |
7.53e-63 |
|
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: 205.18 E-value: 7.53e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 22 PMIHQTESSECGLACLAMICGYYGKNIDIFTLRQKFKLSSRGTDLASLNDIAVKMHMSTRAVSVELDELHSVKLPCILHW 101
Cdd:cd02419 2 PVILQTEAAECGLACLAMIASYHGHHVDLASLRQRFPVSLKGATLADLIDIAQQLGLSTRALRLDLEELGQLKLPCILHW 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1533513286 102 DFNHFVVLTKIKNGKFTVHDPSVGIVKVAKSELSKKFTGIVLEIWP 147
Cdd:cd02419 82 DMNHFVVLKKVSRRRIVIHDPALGKRKLSLEEASRHFTGVALELWP 127
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
492-700 |
4.67e-62 |
|
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: 204.76 E-value: 4.67e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISYKYDSYASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKLIAC 571
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 572 VLQDDRLFSGTLRDNICSfstqiddnwliecarfaqihddiermpmgydtligelgeglsGGQKQRIFIARAIYKKPSIL 651
Cdd:cd03246 81 LPQDDELFSGSIAENILS------------------------------------------GGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1533513286 652 FMDEATSSLDHTNEQYINDAIKSLNI---TRIVIAHRKSTINSADRIIALQE 700
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAALKAagaTRIVIAHRPETLASADRILVLED 170
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
174-700 |
5.33e-62 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 216.45 E-value: 5.33e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 174 SALTKIFFLSIIIESINLVMPVATQLVMDHAIP-ANDSGL--LTLICFGLVFFVALRTItglIRSWTVLIMSSFINAQWQ 250
Cdd:TIGR01842 6 RTFIIVGLFSFVINILMLAPPLYMLQVYDRVLTsGSVPTLlmLTVLALGLYLFLGLLDA---LRSFVLVRIGEKLDGALN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 251 KGLLQHLLKLPleyFERRKIGDIQSrFGSLNTLQETFTTSVVGAIID---SIMIIGLLIMLVLYGGWLTWF--VILFTcL 325
Cdd:TIGR01842 83 QPIFAASFSAT---LRRGSGDGLQA-LRDLDQLRQFLTGPGLFAFFDapwMPIYLLVCFLLHPWIGILALGgaVVLVG-L 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 326 YVFIRVLTYNRYRQLSEESLikdaRANSFFMETLYGIATVKVQGLNKRREENWFNLEVDSINTGIKVSRLNLFFGGINTL 405
Cdd:TIGR01842 158 ALLNNRATKKPLKEATEASI----RANNLADSALRNAEVIEAMGMMGNLTKRWGRFHSKYLSAQSAASDRAGMLSNLSKY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 406 IATMEQILILWLGASLVISGNMTIGMFVAFSSYRGqfsdRIASFIDFLLRL--QIMSlhnervSDIALTEVTPFKDDIPV 483
Cdd:TIGR01842 234 FRIVLQSLVLGLGAYLAIDGEITPGMMIAGSILVG----RALAPIDGAIGGwkQFSG------ARQAYKRLNELLANYPS 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 484 KNDMCPV-----SLSAKNISYKYDSYASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIK 558
Cdd:TIGR01842 304 RDPAMPLpepegHLSVENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLK 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 559 ELGVNNYQKLIACVLQDDRLFSGTLRDNICSFSTQIDDNWLIECARFAQIHDDIERMPMGYDTLIGELGEGLSGGQKQRI 638
Cdd:TIGR01842 384 QWDRETFGKHIGYLPQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRI 463
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1533513286 639 FIARAIYKKPSILFMDEATSSLDHTNEQYINDAIKSLN---ITRIVIAHRKSTINSADRIIALQE 700
Cdd:TIGR01842 464 ALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKargITVVVITHRPSLLGCVDKILVLQD 528
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
153-700 |
1.33e-61 |
|
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: 215.77 E-value: 1.33e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 153 KENVKNKISLRAMLentHGLYSALTKIFFLSIIIESINLVMPVATQLVMDHAIPandSG------LLTLICFGLVFFVAL 226
Cdd:COG4618 2 SRASAGRSELRAAL---RACRRAFLSVGLFSFFINLLMLTPPLYMLQVYDRVLT---SRsvdtllMLTLLALGLYAVMGL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 227 rtitgL--IRSWTVLIMSSFINAQWQKgllqHLLKLPLEYFERRKIGDIQSRFGSLNTLQETFTTSVVGAIIDSI-MIIG 303
Cdd:COG4618 76 -----LdaVRSRILVRVGARLDRRLGP----RVFDAAFRAALRGGGGAAAQALRDLDTLRQFLTGPGLFALFDLPwAPIF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 304 LLIMLVLYGgWLTWFVILFTCLYVFIRVLTYNRYRQLSEESLIKDARANSFFMETLYGIATVKVQGLNKRREENWFNLEV 383
Cdd:COG4618 147 LAVLFLFHP-LLGLLALVGALVLVALALLNERLTRKPLKEANEAAIRANAFAEAALRNAEVIEAMGMLPALRRRWQRANA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 384 DSINTGIKVSRLNLFFGGINTLIATMEQILILWLGASLVISGNMTIGMFVA---------------FSSYRGQFSDRIAs 448
Cdd:COG4618 226 RALALQARASDRAGGFSALSKFLRLLLQSAVLGLGAYLVIQGEITPGAMIAasilmgralapieqaIGGWKQFVSARQA- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 449 fidfLLRL-QIMSLHNERVSDIALTEVTPfkddipvkndmcpvSLSAKNISYKYDSYASYTLRHLNIEIQPGEHVAITGA 527
Cdd:COG4618 305 ----YRRLnELLAAVPAEPERMPLPRPKG--------------RLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGP 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 528 SGTGKTTLLKVLCGLFPASEGNIFVDGIDIK-----ELGvnnyqKLIACVLQDDRLFSGTLRDNICSFsTQIDDNWLIEC 602
Cdd:COG4618 367 SGSGKSTLARLLVGVWPPTAGSVRLDGADLSqwdreELG-----RHIGYLPQDVELFDGTIAENIARF-GDADPEKVVAA 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 603 ARFAQIHDDIERMPMGYDTLIGELGEGLSGGQKQRIFIARAIYKKPSILFMDEATSSLDHTNEQYINDAIKSL---NITR 679
Cdd:COG4618 441 AKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkarGATV 520
|
570 580
....*....|....*....|.
gi 1533513286 680 IVIAHRKSTINSADRIIALQE 700
Cdd:COG4618 521 VVITHRPSLLAAVDKLLVLRD 541
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
492-701 |
6.30e-58 |
|
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: 195.91 E-value: 6.30e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISYKYDSYASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKLIAC 571
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 572 VLQDDRLFSGTLRDNICSFSTQIDDNWLIECARFAQIHDDIERMPMGYDTLIGELGEGLSGGQKQRIFIARAIYKKPSIL 651
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1533513286 652 FMDEATSSLDHTNEQYINDAIKSL--NITRIVIAHRKSTINSADRIIALQEN 701
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLmkNRTTFVIAHRLSTIENADRIVVLEDG 212
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
492-700 |
3.43e-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: 191.44 E-value: 3.43e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISYKYDSYASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKLIAC 571
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 572 VLQDDRLFSGTLRDNICSfstqiddnwliecarfaqihddiermpmgydtligelgeglsGGQKQRIFIARAIYKKPSIL 651
Cdd:cd03228 81 VPQDPFLFSGTIRENILS------------------------------------------GGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1533513286 652 FMDEATSSLDHTNEQYINDAIKSL--NITRIVIAHRKSTINSADRIIALQE 700
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALakGKTVIVIAHRLSTIRDADRIIVLDD 169
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
193-698 |
7.76e-56 |
|
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: 200.33 E-value: 7.76e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 193 MPVATQLVMDHAIPANDSGLLTLICFGLVFFVALRTITGLIRSWTVLIMSSFINAQWQKGLLQHLLKLPLEYFERRKIGD 272
Cdd:TIGR02203 33 LAALLKPLLDDGFGGRDRSVLWWVPLVVIGLAVLRGICSFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGT 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 273 IQSRFGSLNtlqETFTTSVVGAII----DSIMIIGLLIMLvLYGGW-LTWFVILFTCLYVFIRVLTYNRYRQLSEESLIK 347
Cdd:TIGR02203 113 LLSRITFDS---EQVASAATDAFIvlvrETLTVIGLFIVL-LYYSWqLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNS 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 348 DARANSFFMETLYGIATVKVQGlNKRREENWFNlEVDSINTG--IKVSRLNLFFGGINTLIATMEQILILWLGASLVISG 425
Cdd:TIGR02203 189 MGQVTTVAEETLQGYRVVKLFG-GQAYETRRFD-AVSNRNRRlaMKMTSAGSISSPITQLIASLALAVVLFIALFQAQAG 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 426 NMTIGMFVAFSSYRGQFSDRIASFIDFLLRLQIMSLHNERVsdIALTEVTPFKDDIPVKNDMCPVSLSAKNISYKYDSYA 505
Cdd:TIGR02203 267 SLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESL--FTLLDSPPEKDTGTRAIERARGDVEFRNVTFRYPGRD 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 506 SYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKLIACVLQDDRLFSGTLRD 585
Cdd:TIGR02203 345 RPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIAN 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 586 NIC-SFSTQIDDNWLIECARFAQIHDDIERMPMGYDTLIGELGEGLSGGQKQRIFIARAIYKKPSILFMDEATSSLDHTN 664
Cdd:TIGR02203 425 NIAyGRTEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNES 504
|
490 500 510
....*....|....*....|....*....|....*.
gi 1533513286 665 EQYINDAIKSL--NITRIVIAHRKSTINSADRIIAL 698
Cdd:TIGR02203 505 ERLVQAALERLmqGRTTLVIAHRLSTIEKADRIVVM 540
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
495-698 |
1.79e-55 |
|
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: 188.97 E-value: 1.79e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 495 KNISYKYDSYASyTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKLIACVLQ 574
Cdd:cd03254 6 ENVNFSYDEKKP-VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 575 DDRLFSGTLRDNICSFSTQIDDNWLIECARFAQIHDDIERMPMGYDTLIGELGEGLSGGQKQRIFIARAIYKKPSILFMD 654
Cdd:cd03254 85 DTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILD 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1533513286 655 EATSSLDHTNEQYINDAIKSL--NITRIVIAHRKSTINSADRIIAL 698
Cdd:cd03254 165 EATSNIDTETEKLIQEALEKLmkGRTSIIIAHRLSTIKNADKILVL 210
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
495-700 |
6.71e-55 |
|
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: 187.82 E-value: 6.71e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 495 KNISYKYDSyASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKLIACVLQ 574
Cdd:cd03253 4 ENVTFAYDP-GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 575 DDRLFSGTLRDNICSFSTQIDDNWLIECARFAQIHDDIERMPMGYDTLIGELGEGLSGGQKQRIFIARAIYKKPSILFMD 654
Cdd:cd03253 83 DTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1533513286 655 EATSSLDHTNEQYINDAIKSL--NITRIVIAHRKSTINSADRIIALQE 700
Cdd:cd03253 163 EATSALDTHTEREIQAALRDVskGRTTIVIAHRLSTIVNADKIIVLKD 210
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
489-699 |
1.41e-54 |
|
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: 196.52 E-value: 1.41e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 489 PVSLSAKNISYKYDSyASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKL 568
Cdd:COG4988 334 PPSIELEDVSFSYPG-GRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQ 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 569 IACVLQDDRLFSGTLRDNICSFSTQIDDNWLIECARFAQIHDDIERMPMGYDTLIGELGEGLSGGQKQRIFIARAIYKKP 648
Cdd:COG4988 413 IAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDA 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1533513286 649 SILFMDEATSSLDHTNEQYINDAIKSLNITR--IVIAHRKSTINSADRIIALQ 699
Cdd:COG4988 493 PLLLLDEPTAHLDAETEAEILQALRRLAKGRtvILITHRLALLAQADRILVLD 545
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
495-699 |
2.32e-54 |
|
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: 185.87 E-value: 2.32e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 495 KNISYKYDSYASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKLIACVLQ 574
Cdd:cd03245 6 RNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYVPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 575 DDRLFSGTLRDNICSFSTQIDDNWLIECARFAQIHDDIERMPMGYDTLIGELGEGLSGGQKQRIFIARAIYKKPSILFMD 654
Cdd:cd03245 86 DVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1533513286 655 EATSSLDHTNEQYINDAIKSL--NITRIVIAHRKSTINSADRIIALQ 699
Cdd:cd03245 166 EPTSAMDMNSEERLKERLRQLlgDKTLIIITHRPSLLDLVDRIIVMD 212
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
495-700 |
6.04e-53 |
|
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: 182.69 E-value: 6.04e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 495 KNISYKYDSYASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKLIACVLQ 574
Cdd:cd03252 4 EHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 575 DDRLFSGTLRDNICSFSTQIDDNWLIECARFAQIHDDIERMPMGYDTLIGELGEGLSGGQKQRIFIARAIYKKPSILFMD 654
Cdd:cd03252 84 ENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1533513286 655 EATSSLDHTNEQYINDAIKSL--NITRIVIAHRKSTINSADRIIALQE 700
Cdd:cd03252 164 EATSALDYESEHAIMRNMHDIcaGRTVIIIAHRLSTVKNADRIIVMEK 211
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
265-700 |
8.86e-53 |
|
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: 191.52 E-value: 8.86e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 265 FERRKIGDIQSRFGS-LNTLQE----TFTTSVVGAIIDSIMIIGLLIMLVLYGGWLtwFVILFTCLyVFIRVLTYNRYRQ 339
Cdd:COG4987 106 LARLRSGDLLNRLVAdVDALDNlylrVLLPLLVALLVILAAVAFLAFFSPALALVL--ALGLLLAG-LLLPLLAARLGRR 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 340 LSEEslIKDARA--NSFFMETLYGIATVKVQGLNKRREENWFNLEVDSINTGIKVSRLNLFFGGINTLIATMEQILILWL 417
Cdd:COG4987 183 AGRR--LAAARAalRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWL 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 418 GASLVISGNMT---IGMFV--AFSSyrgqFsDRIASFIDFLLRLQIMSLHNERVSDIA-LTEVTPFKDDIPVKNDmcPVS 491
Cdd:COG4987 261 AAPLVAAGALSgplLALLVlaALAL----F-EALAPLPAAAQHLGRVRAAARRLNELLdAPPAVTEPAEPAPAPG--GPS 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISYKYDSYASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKLIAC 571
Cdd:COG4987 334 LELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAV 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 572 VLQDDRLFSGTLRDNICSFSTQIDDNWLIECARFAQIHDDIERMPMGYDTLIGELGEGLSGGQKQRIFIARAIYKKPSIL 651
Cdd:COG4987 414 VPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPIL 493
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1533513286 652 FMDEATSSLDHTNEQYINDAIKSL--NITRIVIAHRKSTINSADRIIALQE 700
Cdd:COG4987 494 LLDEPTEGLDAATEQALLADLLEAlaGRTVLLITHRLAGLERMDRILVLED 544
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
180-700 |
7.82e-52 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 191.47 E-value: 7.82e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 180 FFLSIIIESINLVMPVATQLVMDhaIPANDSGLLTLI--CFGLVFFVALRTITGLIRSWTVLIMSSFINAQWQKGLLQHL 257
Cdd:TIGR00958 167 FVFLTLSSLGEMFIPFYTGRVID--TLGGDKGPPALAsaIFFMCLLSIASSVSAGLRGGSFNYTMARINLRIREDLFRSL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 258 LKLPLEYFERRKIGDIQSRFGS-LNTLQETFTTSVVGAIIDSIMIIGLLIMLVlyggWLTW---FVILFTCLYVFIRVLT 333
Cdd:TIGR00958 245 LRQDLGFFDENKTGELTSRLSSdTQTMSRSLSLNVNVLLRNLVMLLGLLGFML----WLSPrltMVTLINLPLVFLAEKV 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 334 YN-RYRQLSEESLIKDARANSFFMETLYGIATVKVQGlNKRREENWFNLEVDSINT-GIKVSRLNLFFGGINTLIATMEQ 411
Cdd:TIGR00958 321 FGkRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFA-AEEGEASRFKEALEETLQlNKRKALAYAGYLWTTSVLGMLIQ 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 412 ILILWLGASLVISGNMTIGMFVAFSSYRGQFSDRIASFIDFLLRLQIMSLHNERVSDiaLTEVTPfkdDIPVKNDMCPVS 491
Cdd:TIGR00958 400 VLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFE--YLDRKP---NIPLTGTLAPLN 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAK----NISYKYDSYASY-TLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQ 566
Cdd:TIGR00958 475 LEGLiefqDVSFSYPNRPDVpVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLH 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 567 KLIACVLQDDRLFSGTLRDNICSFSTQIDDNWLIECARFAQIHDDIERMPMGYDTLIGELGEGLSGGQKQRIFIARAIYK 646
Cdd:TIGR00958 555 RQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVR 634
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1533513286 647 KPSILFMDEATSSLDHTNEQYINDAIKSLNITRIVIAHRKSTINSADRIIALQE 700
Cdd:TIGR00958 635 KPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAHRLSTVERADQILVLKK 688
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
495-699 |
1.52e-51 |
|
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: 178.89 E-value: 1.52e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 495 KNISYKYDSYASYT-LRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKLIACVL 573
Cdd:cd03249 4 KNVSFRYPSRPDVPiLKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 574 QDDRLFSGTLRDNICSFSTQIDDNWLIECARFAQIHDDIERMPMGYDTLIGELGEGLSGGQKQRIFIARAIYKKPSILFM 653
Cdd:cd03249 84 QEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1533513286 654 DEATSSLDHTNEQYINDAIK--SLNITRIVIAHRKSTINSADRIIALQ 699
Cdd:cd03249 164 DEATSALDAESEKLVQEALDraMKGRTTIVIAHRLSTIRNADLIAVLQ 211
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
290-700 |
2.75e-51 |
|
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: 188.11 E-value: 2.75e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 290 SVVGAIIDSIMIIGllIMLVLYGGWLTWFVILFTCLYV-FIRVLTYNR---YRQLSEEslikDARANSFFMETLYGIATV 365
Cdd:COG5265 158 NILPTLLEIALVAG--ILLVKYDWWFALITLVTVVLYIaFTVVVTEWRtkfRREMNEA----DSEANTRAVDSLLNYETV 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 366 KVQGlNKRRE-----ENWFNLEVDSINTGIKVSRLNLffgGINTLIATMeQILILWLGASLVISGNMTIGMFVAFSSYRG 440
Cdd:COG5265 232 KYFG-NEAREarrydEALARYERAAVKSQTSLALLNF---GQALIIALG-LTAMMLMAAQGVVAGTMTVGDFVLVNAYLI 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 441 QFSdRIASFIDFLLRlQI-MSLHN-ERVsdIALTEVTPfkdDIPVKNDMCPVSLSA-----KNISYKYDSyASYTLRHLN 513
Cdd:COG5265 307 QLY-IPLNFLGFVYR-EIrQALADmERM--FDLLDQPP---EVADAPDAPPLVVGGgevrfENVSFGYDP-ERPILKGVS 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 514 IEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKLIACVLQDDRLFSGTLRDNICSFSTQ 593
Cdd:COG5265 379 FEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPD 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 594 IDDNWLIECARFAQIHDDIERMPMGYDTLIGELGEGLSGGQKQRIFIARAIYKKPSILFMDEATSSLDHTNEQYINDAIK 673
Cdd:COG5265 459 ASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALR 538
|
410 420
....*....|....*....|....*....
gi 1533513286 674 SL--NITRIVIAHRKSTINSADRIIALQE 700
Cdd:COG5265 539 EVarGRTTLVIAHRLSTIVDADEILVLEA 567
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
174-466 |
1.58e-49 |
|
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: 175.04 E-value: 1.58e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 174 SALTKIFFLSIIIESINLVMPVATQLVMDHAIPANDSGLLTLICFGLVFFVALRTITGLIRSWTVLIMSSFINAQWQKGL 253
Cdd:cd18779 2 GLLGQILLASLLLQLLGLALPLLTGVLVDRVIPRGDRDLLGVLGLGLAALVLTQLLAGLLRSHLLLRLRTRLDTQLTLGF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 254 LQHLLKLPLEYFERRKIGDIQSRFGSLNTLQETFTTSVVGAIIDSIMIIGLLIMLVLYGGWLTWFVILFTCLYVFIRVLT 333
Cdd:cd18779 82 LEHLLRLPYRFFQQRSTGDLLMRLSSNATIRELLTSQTLSALLDGTLVLGYLALLFAQSPLLGLVVLGLAALQVALLLAT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 334 YNRYRQLSEESLIKDARANSFFMETLYGIATVKVQGLNKRREENWFNLEVDSINTGIKVSRLNLFFGGINTLIATMEQIL 413
Cdd:cd18779 162 RRRVRELMARELAAQAEAQSYLVEALSGIETLKASGAEDRALDRWSNLFVDQLNASLRRGRLDALVDALLATLRLAAPLV 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1533513286 414 ILWLGASLVISGNMTIGMFVAFSSYRGQFSDRIASFIDFLLRLQIMSLHNERV 466
Cdd:cd18779 242 LLWVGAWQVLDGQLSLGTMLALNALAGAFLAPLASLVGTAQQLQLLGSHLERL 294
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
174-457 |
5.05e-47 |
|
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: 168.51 E-value: 5.05e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 174 SALTKIFFLSIIIESINLVMPVATQLVMDHAIPANDSGLLTLICFGLVFFVALRTITGLIRSWTVL---------IMSSF 244
Cdd:cd18568 2 KLLAEILLASLLLQLLGLALPLFTQIILDRVLVHKNISLLNLILIGLLIVGIFQILLSAVRQYLLDyfanridlsLLSDF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 245 INaqwqkgllqHLLKLPLEYFERRKIGDIQSRFGSLNTLQETFTTSVVGAIIDSIMIIGLLIMLVLYGGWLTWFVILFTC 324
Cdd:cd18568 82 YK---------HLLSLPLSFFASRKVGDIITRFQENQKIRRFLTRSALTTILDLLMVFIYLGLMFYYNLQLTLIVLAFIP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 325 LYVFIRVLTYNRYRQLSEESLIKDARANSFFMETLYGIATVKVQGLNKRREENWFNLEVDSINTGIKVSRLNLFFGGINT 404
Cdd:cd18568 153 LYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERPIRWRWENKFAKALNTRFRGQKLSIVLQLISS 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1533513286 405 LIATMEQILILWLGASLVISGNMTIGMFVAFSSYRGQFSDRIASFIDFLLRLQ 457
Cdd:cd18568 233 LINHLGTIAVLWYGAYLVISGQLTIGQLVAFNMLFGSVINPLLALVGLWDELQ 285
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
495-698 |
1.20e-46 |
|
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: 164.97 E-value: 1.20e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 495 KNISYKYDSYASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKLIACVLQ 574
Cdd:cd03244 6 KNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 575 DDRLFSGTLRDNICSFStQIDDNWLIECARFAQIHDDIERMPMGYDTLIGELGEGLSGGQKQRIFIARAIYKKPSILFMD 654
Cdd:cd03244 86 DPVLFSGTIRSNLDPFG-EYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLD 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1533513286 655 EATSSLDHTNEQYINDAIKSL--NITRIVIAHRKSTINSADRIIAL 698
Cdd:cd03244 165 EATASVDPETDALIQKTIREAfkDCTVLTIAHRLDTIIDSDRILVL 210
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
401-698 |
1.38e-45 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 171.68 E-value: 1.38e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 401 GINTLIATMEQILILWLGASLVISGNMTIG---MFVAFSSYRGQFSDRIASFIDfllrlqimSLHNERVSdiaLTEVTPF 477
Cdd:PRK13657 244 VLNRAASTITMLAILVLGAALVQKGQLRVGevvAFVGFATLLIGRLDQVVAFIN--------QVFMAAPK---LEEFFEV 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 478 KDDIPVKND----MCPVSLSA----KNISYKYDSYASyTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGN 549
Cdd:PRK13657 313 EDAVPDVRDppgaIDLGRVKGavefDDVSFSYDNSRQ-GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGR 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 550 IFVDGIDIKELGVNNYQKLIACVLQDDRLFSGTLRDNICSFSTQIDDNWLIECARFAQIHDDIERMPMGYDTLIGELGEG 629
Cdd:PRK13657 392 ILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQ 471
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1533513286 630 LSGGQKQRIFIARAIYKKPSILFMDEATSSLDHTNEQYINDAIKSL--NITRIVIAHRKSTINSADRIIAL 698
Cdd:PRK13657 472 LSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELmkGRTTFIIAHRLSTVRNADRILVF 542
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
176-457 |
2.90e-45 |
|
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: 163.39 E-value: 2.90e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 176 LTKIFFLSIIIESINLVMPVATQLVMDHAIPANDSGLLTLICFGLVFFVALRTITGLIRSWTVLIMSSFINAQWQKGLLQ 255
Cdd:cd18570 4 LILILLLSLLITLLGIAGSFFFQILIDDIIPSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGYFK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 256 HLLKLPLEYFERRKIGDIQSRFGSLNTLQETFTTSVVGAIIDSIMIIGLLIMLVLYGGWLTWFVILFTCLYVFIRVLTYN 335
Cdd:cd18570 84 HLLKLPLSFFETRKTGEIISRFNDANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLYILIILLFNK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 336 RYRQLSEESLIKDARANSFFMETLYGIATVKVQGLNKRREENWFNLEVDSINTGIKVSRLNLFFGGINTLIATMEQILIL 415
Cdd:cd18570 164 PFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLIGSLLIL 243
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1533513286 416 WLGASLVISGNMTIGMFVAFSSYRGQFSDRIASFIDFLLRLQ 457
Cdd:cd18570 244 WIGSYLVIKGQLSLGQLIAFNALLGYFLGPIENLINLQPKIQ 285
|
|
| Peptidase_C39 |
pfam03412 |
Peptidase C39 family; Lantibiotic and non-lantibiotic bacteriocins are synthesized as ... |
20-150 |
3.52e-45 |
|
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: 157.39 E-value: 3.52e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 20 RFPMIHQTESSECGLACLAMICGYYGKNIDIFTLRQKFKLSSRGTDLASLNDIAVKMHMSTRAVSVELDELHSVKLPCIL 99
Cdd:pfam03412 1 KYKIVLQVDENDCGLACLAMILKYYGSNVSLEELRELAGTPAEGTSLLGLKKAAEKLGFKAKAIKADLSELKELPLPFIA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1533513286 100 HWDFN--HFVVLTKIKNGKFTVHDPSVGIVKVAKSELSKKFTGIVLEIWPGNS 150
Cdd:pfam03412 81 HWDGNggHFVVVYGIKKNKVLIADPAVGKIKLSREEFEKEWTGVALLVAPKPS 133
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
175-443 |
3.09e-40 |
|
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: 149.57 E-value: 3.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 175 ALTKIFFLSIIIESINLVMPVATQLVMDHAIPANDSGLLTLICFGLVFFVALRTITGLIRSWTVLIMSSFINAQWQKGLL 254
Cdd:cd18588 3 LLGEVLLASLFLQLFALVTPLFFQVIIDKVLVHRSLSTLDVLAIGLLVVALFEAVLSGLRTYLFSHTTNRIDAELGARLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 255 QHLLKLPLEYFERRKIGDIQSRFGSLNTLQETFTTSVVGAIIDSIMIIGLLIMLVLYGGWLTWFVILFTCLYVFIRVLTY 334
Cdd:cd18588 83 RHLLRLPLSYFESRQVGDTVARVRELESIRQFLTGSALTLVLDLVFSVVFLAVMFYYSPTLTLIVLASLPLYALLSLLVT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 335 NRYRQLSEESLIKDARANSFFMETLYGIATVKVQGLNKRREENWFNLEVDSINTGIKVSRLNLFFGGINTLIATMEQILI 414
Cdd:cd18588 163 PILRRRLEEKFQRGAENQSFLVETVTGIETVKSLAVEPQFQRRWEELLARYVKASFKTANLSNLASQIVQLIQKLTTLAI 242
|
250 260
....*....|....*....|....*....
gi 1533513286 415 LWLGASLVISGNMTIGMFVAFSSYRGQFS 443
Cdd:cd18588 243 LWFGAYLVMDGELTIGQLIAFNMLAGQVS 271
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
180-700 |
1.93e-38 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 150.94 E-value: 1.93e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 180 FFLSIIIESINLVMPVATQLVM--------DHAIPANDSGLLTLICFGLVFFVALRTITGLIRSWTVLIMSSFINAQWQK 251
Cdd:PRK11176 23 FKAGLIVAGVALILNAASDTFMlsllkpllDDGFGKADRSVLKWMPLVVIGLMILRGITSFISSYCISWVSGKVVMTMRR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 252 GLLQHLLKLPLEYFERRKIGDIQSR--FGSlntlqETFTTSVVGAII----DSIMIIGLLIMLVLYGGWLTWFVILFTCL 325
Cdd:PRK11176 103 RLFGHMMGMPVSFFDKQSTGTLLSRitYDS-----EQVASSSSGALItvvrEGASIIGLFIMMFYYSWQLSLILIVIAPI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 326 YVFIRVLTYNRYRQLSEEslikdaransffMETLYGIATVKVQGLNK-----------RREENWFNLEVDSI-NTGIKVS 393
Cdd:PRK11176 178 VSIAIRVVSKRFRNISKN------------MQNTMGQVTTSAEQMLKghkevlifggqEVETKRFDKVSNRMrQQGMKMV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 394 RLNLFFGGINTLIATMEQILILWLGASLVISGNMTIGMF-VAFSSYRG-------------QFSDRIAS----Fidfllr 455
Cdd:PRK11176 246 SASSISDPIIQLIASLALAFVLYAASFPSVMDTLTAGTItVVFSSMIAlmrplksltnvnaQFQRGMAAcqtlF------ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 456 lQIMSLHNERvsDIALTEVTPFKDDIPVKNdmcpvslsaknISYKYDSYASYTLRHLNIEIQPGEHVAITGASGTGKTTL 535
Cdd:PRK11176 320 -AILDLEQEK--DEGKRVIERAKGDIEFRN-----------VTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTI 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 536 LKVLCGLFPASEGNIFVDGIDIKELGVNNYQKLIACVLQDDRLFSGTLRDNICSFST-QIDDNWLIECARFAQIHDDIER 614
Cdd:PRK11176 386 ANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTeQYSREQIEEAARMAYAMDFINK 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 615 MPMGYDTLIGELGEGLSGGQKQRIFIARAIYKKPSILFMDEATSSLDHTNEQYINDAIKSL--NITRIVIAHRKSTINSA 692
Cdd:PRK11176 466 MDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELqkNRTSLVIAHRLSTIEKA 545
|
....*...
gi 1533513286 693 DRIIALQE 700
Cdd:PRK11176 546 DEILVVED 553
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
489-698 |
1.65e-37 |
|
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: 147.43 E-value: 1.65e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 489 PVSLSAKNISYKYDSyASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKL 568
Cdd:TIGR02857 319 ASSLEFSGVSVAYPG-RRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQ 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 569 IACVLQDDRLFSGTLRDNICSFSTQIDDNWLIECARFAQIHDDIERMPMGYDTLIGELGEGLSGGQKQRIFIARAIYKKP 648
Cdd:TIGR02857 398 IAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDA 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1533513286 649 SILFMDEATSSLDHTNEQYINDAIKSL--NITRIVIAHRKSTINSADRIIAL 698
Cdd:TIGR02857 478 PLLLLDEPTAHLDAETEAEVLEALRALaqGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
175-466 |
1.95e-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: 350055 [Multi-domain] Cd Length: 294 Bit Score: 141.58 E-value: 1.95e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 175 ALTKIFFLSIIIESINLVMPVATQLVMDHAIPANDSGLLTLICFGLVFFVALRTITGLIRSWTVLIMSSFINAQWQKGLL 254
Cdd:cd18782 3 ALIEVLALSFVVQLLGLANPLLFQVIIDKVLVQQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTII 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 255 QHLLKLPLEYFERRKIGDIQSRFGSLNTLQETFTTSVVGAIIDSIMIIGLLIMLVLYGGWLTwFVILFTC-----LYVFI 329
Cdd:cd18782 83 DHLLRLPLGFFDKRPVGELSTRISELDTIRGFLTGTALTTLLDVLFSVIYIAVLFSYSPLLT-LVVLATVplqllLTFLF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 330 RVLTYNRYRQLSEESlikdARANSFFMETLYGIATVKVQGLNKRREENWFNLEVDSINTGIKVSRLNLFFGGINTLIATM 409
Cdd:cd18782 162 GPILRRQIRRRAEAS----AKTQSYLVESLTGIQTVKAQNAELKARWRWQNRYARSLGEGFKLTVLGTTSGSLSQFLNKL 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1533513286 410 EQILILWLGASLVISGNMTIGMFVAFSSYRGQFSDRIASFIDFLLRLQIMSLHNERV 466
Cdd:cd18782 238 SSLLVLWVGAYLVLRGELTLGQLIAFRILSGYVTGPILRLSTLWQQFQELRVSLERL 294
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
179-457 |
2.51e-37 |
|
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: 141.15 E-value: 2.51e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 179 IFFLSIIIESINLVMPVATQLVMDHAIPANDSGLLTLICFGLVFFVALRTITGLIRSWTVLIMSSFINAQWQKGLLQHLL 258
Cdd:cd07346 4 ALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 259 KLPLEYFERRKIGDIQSRFGS-LNTLQETFTTSVVGAIIDSIMIIGLLIMLVLYGGWLTWFVILFTCLYVFIRVLTYNRY 337
Cdd:cd07346 84 RLSLSFFDRNRTGDLMSRLTSdVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 338 RQLSEESLIKDARANSFFMETLYGIATVKvqGLNK-RREENWFNLEVDSI-NTGIKVSRLNLFFGGINTLIATMEQILIL 415
Cdd:cd07346 164 RKASREVRESLAELSAFLQESLSGIRVVK--AFAAeEREIERFREANRDLrDANLRAARLSALFSPLIGLLTALGTALVL 241
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1533513286 416 WLGASLVISGNMTIGMFVAFSSYRGQFSDRIASFIDFLLRLQ 457
Cdd:cd07346 242 LYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQ 283
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
495-700 |
1.47e-36 |
|
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: 136.83 E-value: 1.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 495 KNISYKYDSY-ASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKLIACVL 573
Cdd:cd03248 15 QNVTFAYPTRpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 574 QDDRLFSGTLRDNICSFSTQIDDNWLIECARFAQIHDDIERMPMGYDTLIGELGEGLSGGQKQRIFIARAIYKKPSILFM 653
Cdd:cd03248 95 QEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLIL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1533513286 654 DEATSSLDHTNEQYINDAIKSLNITR--IVIAHRKSTINSADRIIALQE 700
Cdd:cd03248 175 DEATSALDAESEQQVQQALYDWPERRtvLVIAHRLSTVERADQILVLDG 223
|
|
| Peptidase_C39B |
cd02418 |
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
21-150 |
2.80e-36 |
|
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: 132.72 E-value: 2.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 21 FPMIHQTESSECGLACLAMICGYYGKNIDIFTLRQKFKLSSRGTDLASLNDIAVKMHMSTRAV--SVELDELHSVKLPCI 98
Cdd:cd02418 1 YPYVLQVDEMDCGAACLAMIAKYYGKNYSLAKLRELAGTDREGTSLLGLVKAAEKLGFETRAVkaDMDLFELKDIPLPFI 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1533513286 99 LH----WDFNHFVVLTKIKNGKFTVHDPSVGIVKVAKSELSKKFTGIVLEIWPGNS 150
Cdd:cd02418 81 AHvikeWKLNHYVVVYKIKKKKILIADPAVGITKISKEEFEKEWTGVALFLEPTPN 136
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
176-443 |
3.86e-35 |
|
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: 134.31 E-value: 3.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 176 LTKIFFLSIIIESINLVMPVATQLVMDHAIPANDSG--LLTLICFGLVFFVALRTITGLIRSWTVLIMSSFINAQWQKGL 253
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPEtqALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 254 LQHLLKLPLEYFERRKIGDIQSRFGS-LNTLQETFTTSVVGAIIDSIMIIGLLIMLVLYGGWLTWFVILFTCLYVFIRVL 332
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNdTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 333 TYNRYRQLSEESLIKDARANSFFMETLYGIATVKVQGLNKRREENWFNLEVDSINTGIKVSRLNLFFGGINTLIATMEQI 412
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
|
250 260 270
....*....|....*....|....*....|.
gi 1533513286 413 LILWLGASLVISGNMTIGMFVAFSSYRGQFS 443
Cdd:pfam00664 241 LALWFGAYLVISGELSVGDLVAFLSLFAQLF 271
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
492-700 |
1.24e-33 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 128.01 E-value: 1.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISYKYDSYasYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKLIAC 571
Cdd:COG4619 1 LELEGLSFRVGGK--PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 572 VLQDDRLFSGTLRDNI--------CSFSTQIDDNWLiecARF----AQIHDDIERMPMGydtligelgeglsggQKQRIF 639
Cdd:COG4619 79 VPQEPALWGGTVRDNLpfpfqlreRKFDRERALELL---ERLglppDILDKPVERLSGG---------------ERQRLA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1533513286 640 IARAIYKKPSILFMDEATSSLDHTN----EQYINDAIKSLNITRIVIAHRKSTINS-ADRIIALQE 700
Cdd:COG4619 141 LIRALLLQPDVLLLDEPTSALDPENtrrvEELLREYLAEEGRAVLWVSHDPEQIERvADRVLTLEA 206
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
491-698 |
5.80e-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: 125.99 E-value: 5.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 491 SLSAKNISYKYDSYASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKLIA 570
Cdd:cd03369 6 EIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 571 CVLQDDRLFSGTLRDNICSFSTQIDDnwliecarfaQIHDDIeRMPMGYDTLigelgeglSGGQKQRIFIARAIYKKPSI 650
Cdd:cd03369 86 IIPQDPTLFSGTIRSNLDPFDEYSDE----------EIYGAL-RVSEGGLNL--------SQGQRQLLCLARALLKRPRV 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1533513286 651 LFMDEATSSLDHTNEQYINDAIKSL--NITRIVIAHRKSTINSADRIIAL 698
Cdd:cd03369 147 LVLDEATASIDYATDALIQKTIREEftNSTILTIAHRLRTIIDYDKILVM 196
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
493-700 |
1.27e-32 |
|
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: 125.27 E-value: 1.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 493 SAKNISYKYDSYASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKLIACV 572
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 573 LQ--DDRLFSGTLRDNICsFS-----------TQIDDNWLIECARFAQIHDDIERMPMGydtligelgeglsggQKQRIF 639
Cdd:cd03225 81 FQnpDDQFFGPTVEEEVA-FGlenlglpeeeiEERVEEALELVGLEGLRDRSPFTLSGG---------------QKQRVA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1533513286 640 IARAIYKKPSILFMDEATSSLDHTNEQYINDAIKSLN---ITRIVIAHRKSTI-NSADRIIALQE 700
Cdd:cd03225 145 IAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKaegKTIIIVTHDLDLLlELADRVIVLED 209
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
512-699 |
5.83e-32 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 131.51 E-value: 5.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 512 LNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPaSEGNIFVDGIDIKELGVNNYQKLIACVLQDDRLFSGTLRDNICSFS 591
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP-YQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGN 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 592 TQIDDNWLIECARFAQIHDDIERMPMGYDTLIGELGEGLSGGQKQRIFIARAIYKKPSILFMDEATSSLDHTNEQYINDA 671
Cdd:PRK11174 448 PDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQA 527
|
170 180 190
....*....|....*....|....*....|
gi 1533513286 672 IK--SLNITRIVIAHRKSTINSADRIIALQ 699
Cdd:PRK11174 528 LNaaSRRQTTLMVTHQLEDLAQWDQIWVMQ 557
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
176-436 |
8.38e-32 |
|
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: 125.39 E-value: 8.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 176 LTKIFFLSIIIESINLVMPVATQLVMDHAIPANDSGLLTLICFGLVFFVALRTITGLIRSWTVLIMSSFINAQWQKGLLQ 255
Cdd:cd18566 4 LPQVLLASLFINILALATPLFILQVYDRVIPNESIPTLQVLVIGVVIAILLESLLRLLRSYILAWIGARFDHRLSNAAFE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 256 HLLKLPLEYFERRKIGDIQSRFGSLNTLQETFTTSVVGAIIDSIMIIGLLIMLVLYGGWLTWFVILFTCLYVFIRVLTYN 335
Cdd:cd18566 84 HLLSLPLSFFEREPSGAHLERLNSLEQIREFLTGQALLALLDLPFVLIFLGLIWYLGGKLVLVPLVLLGLFVLVAILLGP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 336 RYRQLSEESLIKDARANSFFMETLYGIATVKVQGLNKRREENWFNLEVDSINTGIKVSRLNLFFGGINTLIATMEQILIL 415
Cdd:cd18566 164 ILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEPQMLRRYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSMVAVV 243
|
250 260
....*....|....*....|.
gi 1533513286 416 WLGASLVISGNMTIGMFVAFS 436
Cdd:cd18566 244 AFGALLVINGDLTVGALIACT 264
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
174-435 |
2.68e-31 |
|
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: 124.17 E-value: 2.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 174 SALTKIFFLSIIIESINLVMPVATQLVMDHAIPANDSGLLTLICFGLVFFVALRTITGLIRSWTVLIMSSFINAQWQKGL 253
Cdd:cd18783 2 RLFRDVAIASLILHVLALAPPIFFQIVIDKVLVHQSYSTLYVLTIGVVIALLFEGILGYLRRYLLLVATTRIDARLALRT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 254 LQHLLKLPLEYFERRKIGDIQSRFGSLNTLQETFTTSVVGAIIDSIMIIGLLIMLVLYGGWLTWFVILFTCLYVFIRVLT 333
Cdd:cd18783 82 FDRLLSLPIDFFERTPAGVLTKHMQQIERIRQFLTGQLFGTLLDATSLLVFLPVLFFYSPTLALVVLAFSALIALIILAF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 334 YNRYRQLSEESLIKDARANSFFMETLYGIATVKVQGLNKRREENWFNLEVDSINTGIKVSRLNLFfggINTLIATMEQIL 413
Cdd:cd18783 162 LPPFRRRLQALYRAEGERQAFLVETVHGIRTVKSLALEPRQRREWDERVARAIRARFAVGRLSNW---PQTLTGPLEKLM 238
|
250 260
....*....|....*....|....*
gi 1533513286 414 ---ILWLGASLVISGNMTIGMFVAF 435
Cdd:cd18783 239 tvgVIWVGAYLVFAGSLTVGALIAF 263
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
292-700 |
2.75e-31 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 129.06 E-value: 2.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 292 VGAIIDSiMIIGLLIMLVLyGGWLTWFVILFTCLYVFIRVLTYNRY-RQLSEEslIKDARA-----NSFFMETLYGIATV 365
Cdd:PRK10789 114 VLTLVDS-LVMGCAVLIVM-STQISWQLTLLALLPMPVMAIMIKRYgDQLHER--FKLAQAafsslNDRTQESLTSIRMI 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 366 KVQGLNKRREENWFNLEVDSINTGIKVSRLNLFFGGINTLIATMEQILILWLGASLVISGNMTIGMFVAFSSYRGQFsdr 445
Cdd:PRK10789 190 KAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDPTIYIAIGMANLLAIGGGSWMVVNGSLTLGQLTSFVMYLGLM--- 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 446 iasfIDFLLRLQIMSLHNERVSdIALTEVTPFKDDIPVKND------MCPVSLSAKNISYKYDSYASYTLRHLNIEIQPG 519
Cdd:PRK10789 267 ----IWPMLALAWMFNIVERGS-AAYSRIRAMLAEAPVVKDgsepvpEGRGELDVNIRQFTYPQTDHPALENVNFTLKPG 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 520 EHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKLIACVLQDDRLFSGTLRDNI---CSFSTQIDd 596
Cdd:PRK10789 342 QMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIalgRPDATQQE- 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 597 nwLIECARFAQIHDDIERMPMGYDTLIGELGEGLSGGQKQRIFIARAIYKKPSILFMDEATSSLDHTNEQYINDAIKSLN 676
Cdd:PRK10789 421 --IEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWG 498
|
410 420
....*....|....*....|....*.
gi 1533513286 677 ITRIVI--AHRKSTINSADRIIALQE 700
Cdd:PRK10789 499 EGRTVIisAHRLSALTEASEILVMQH 524
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
264-698 |
6.18e-31 |
|
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: 130.45 E-value: 6.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 264 YFERRKIGDIQSRFGSLNTLQETFTTSVVGAIIDSIM-IIGLLIMLVLYGGWLTWFVILFTCLYVFIRVLTYNRYRQLSE 342
Cdd:TIGR00957 1055 FFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFnVIGALIVILLATPIAAVIIPPLGLLYFFVQRFYVASSRQLKR 1134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 343 ESLIKDARANSFFMETLYGIATVKVQGlNKRREENWFNLEVDSINTGIKVSrlnlffggintLIATMeqililWLGASLV 422
Cdd:TIGR00957 1135 LESVSRSPVYSHFNETLLGVSVIRAFE-EQERFIHQSDLKVDENQKAYYPS-----------IVANR------WLAVRLE 1196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 423 ISGNMTIgMFVAFSSYRGQ-------------FSDRIASFIDFLLRLQIMSLHN----ERVSDIALTEV-TPFKDDIPVK 484
Cdd:TIGR00957 1197 CVGNCIV-LFAALFAVISRhslsaglvglsvsYSLQVTFYLNWLVRMSSEMETNivavERLKEYSETEKeAPWQIQETAP 1275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 485 NDMCPVS--LSAKNISYKYDSYASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGV 562
Cdd:TIGR00957 1276 PSGWPPRgrVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGL 1355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 563 NNYQKLIACVLQDDRLFSGTLRDNICSFSTQIDDN--WLIEcarFAQIHDDIERMPMGYDTLIGELGEGLSGGQKQRIFI 640
Cdd:TIGR00957 1356 HDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEvwWALE---LAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCL 1432
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 641 ARAIYKKPSILFMDEATSSLDHTNEQYINDAIKSL--NITRIVIAHRKSTINSADRIIAL 698
Cdd:TIGR00957 1433 ARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQfeDCTVLTIAHRLNTIMDYTRVIVL 1492
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
496-700 |
7.34e-31 |
|
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: 121.55 E-value: 7.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 496 NISYKYDSYASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKLIACVLQD 575
Cdd:cd03288 24 DLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 576 DRLFSGTLRDNICSFSTQIDDNwLIECARFAQIHDDIERMPMGYDTLIGELGEGLSGGQKQRIFIARAIYKKPSILFMDE 655
Cdd:cd03288 104 PILFSGSIRFNLDPECKCTDDR-LWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDE 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1533513286 656 ATSSLDHTNEQYINDAIKSLNITRIV--IAHRKSTINSADRIIALQE 700
Cdd:cd03288 183 ATASIDMATENILQKVVMTAFADRTVvtIAHRVSTILDADLVLVLSR 229
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
401-685 |
1.57e-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: 126.32 E-value: 1.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 401 GINTLIATMEQILILWLGASLVISGNM---TIGMFV-----AFSSYrGQFSDRIASfidfLLRLQImSLHneRVSDIALT 472
Cdd:TIGR02868 242 ALTLLAAGLAVLGALWAGGPAVADGRLapvTLAVLVllplaAFEAF-AALPAAAQQ----LTRVRA-AAE--RIVEVLDA 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 473 EVTPFKDDIPVKNDMCP--VSLSAKNISYKYDSyASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNI 550
Cdd:TIGR02868 314 AGPVAEGSAPAAGAVGLgkPTLELRDLSAGYPG-APPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEV 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 551 FVDGIDIKELGVNNYQKLIACVLQDDRLFSGTLRDNICSFSTQIDDNWLIECARFAQIHDDIERMPMGYDTLIGELGEGL 630
Cdd:TIGR02868 393 TLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARL 472
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1533513286 631 SGGQKQRIFIARAIYKKPSILFMDEATSSLD-HTNEQYINDAIKSLN-ITRIVIAHR 685
Cdd:TIGR02868 473 SGGERQRLALARALLADAPILLLDEPTEHLDaETADELLEDLLAALSgRTVVLITHH 529
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
492-700 |
1.77e-30 |
|
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: 118.73 E-value: 1.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISYKYDS---YASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGidikelgvnnyqkL 568
Cdd:cd03250 1 ISVEDASFTWDSgeqETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 569 IACVLQDDRLFSGTLRDNICsFSTQIDDNWLIECARFAQIHDDIERMPMGYDTLIGELGEGLSGGQKQRIFIARAIYKKP 648
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENIL-FGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1533513286 649 SILFMDEATSSLD-HTNEQYINDAIKSL---NITRIVIAHRKSTINSADRIIALQE 700
Cdd:cd03250 147 DIYLLDDPLSAVDaHVGRHIFENCILGLllnNKTRILVTHQLQLLPHADQIVVLDN 202
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
509-658 |
4.71e-30 |
|
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: 115.82 E-value: 4.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 509 LRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKLIACVLQDDRLFSG-TLRDNI 587
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1533513286 588 ------CSFSTQIDDnwliecarfAQIHDDIERMPMGY--DTLIGELGEGLSGGQKQRIFIARAIYKKPSILFMDEATS 658
Cdd:pfam00005 81 rlglllKGLSKREKD---------ARAEEALEKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
487-699 |
6.11e-30 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 118.22 E-value: 6.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 487 MCPVsLSAKNISYKYDSYASYT--LRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNN 564
Cdd:COG1136 1 MSPL-LELRNLTKSYGTGEGEVtaLRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 565 YQKL----IACVLQDDRLFSG-TLRDNIC------SFSTQIDDNWLIECARFAQIHDDIERMPM----Gydtligelgeg 629
Cdd:COG1136 80 LARLrrrhIGFVFQFFNLLPElTALENVAlplllaGVSRKERRERARELLERVGLGDRLDHRPSqlsgG----------- 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1533513286 630 lsggQKQRIFIARAIYKKPSILFMDEATSSLDHTNEQYINDAIKSLN----ITRIVIAHRKSTINSADRIIALQ 699
Cdd:COG1136 149 ----QQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNrelgTTIVMVTHDPELAARADRVIRLR 218
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
493-700 |
2.39e-29 |
|
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: 113.88 E-value: 2.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 493 SAKNISYKYDSyaSYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKLIACV 572
Cdd:cd00267 1 EIENLSFRYGG--RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 573 LQddrlFSGtlrdnicsfstqiddnwliecarfaqihddiermpmGydtligelgeglsggQKQRIFIARAIYKKPSILF 652
Cdd:cd00267 79 PQ----LSG------------------------------------G---------------QRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1533513286 653 MDEATSSLDHTNEQYINDAIKSL---NITRIVIAHRKSTI-NSADRIIALQE 700
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELaeeGRTVIIVTHDPELAeLAADRVIVLKD 155
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
492-700 |
2.73e-29 |
|
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: 116.05 E-value: 2.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISYKY--DSYASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKL- 568
Cdd:cd03255 1 IELKNLSKTYggGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 569 ---IACVLQDDRLFSG-TLRDNI---CSFSTQI---DDNWLIECARFAQIHDDIERMPM----GydtligelgeglsggQ 634
Cdd:cd03255 81 rrhIGFVFQSFNLLPDlTALENVelpLLLAGVPkkeRRERAEELLERVGLGDRLNHYPSelsgG---------------Q 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 635 KQRIFIARAIYKKPSILFMDEATSSLDHTNEQYINDAIKSLN----ITRIVIAHRKSTINSADRIIALQE 700
Cdd:cd03255 146 QQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNkeagTTIVVVTHDPELAEYADRIIELRD 215
|
|
| Peptidase_C39F |
cd02425 |
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
22-145 |
2.90e-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: 239105 [Multi-domain] Cd Length: 126 Bit Score: 112.74 E-value: 2.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 22 PMIHQTESSECGLACLAMICGYYGKNIDIFTLRQKFKLSSRGTDLASLNDIAVKMHMSTRAVSVELDE-LHSVKLPCILH 100
Cdd:cd02425 2 KPILQNNQTECGLACYAMILNYFGYKVSLNELREKYELGRDGLSLSYLKQLLEEYGFKCKVYKISFKKnLYPLKLPVIIF 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1533513286 101 WDFNHFVVLTKIKNGKFTVHDPSVGIVKVAKSELSKKFTGIVLEI 145
Cdd:cd02425 82 WNNNHFVVLEKIKKNKVTIVDPAIGRIKISIDEFLENFSGYILTF 126
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
268-699 |
3.40e-29 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 124.70 E-value: 3.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 268 RKIGDIQSRFGSL-----NTLQETFTTSVVGAIIDSIMIIGLLIMLvlyggwltwfvILFTCLYVFIRvltyNRYRQLSE 342
Cdd:PLN03232 1015 KDIGDIDRNVANLmnmfmNQLWQLLSTFALIGTVSTISLWAIMPLL-----------ILFYAAYLYYQ----STSREVRR 1079
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 343 ESLIKDARANSFFMETLYGIATVKVQGLNKRREEnwfnLEVDSINTGIKVSRLNLFFGGINTLIATMEQILILWLGASLV 422
Cdd:PLN03232 1080 LDSVTRSPIYAQFGEALNGLSSIRAYKAYDRMAK----INGKSMDNNIRFTLANTSSNRWLTIRLETLGGVMIWLTATFA 1155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 423 ISGNMTIGMFVAFSSYRG---QFSDRIASFIDFLLRlQIMSLHN-----ERVSD-IALTEVTP--FKDDIPVKNDMCPVS 491
Cdd:PLN03232 1156 VLRNGNAENQAGFASTMGlllSYTLNITTLLSGVLR-QASKAENslnsvERVGNyIDLPSEATaiIENNRPVSGWPSRGS 1234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISYKYDSYASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKLIAC 571
Cdd:PLN03232 1235 IKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSI 1314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 572 VLQDDRLFSGTLRDNICSFSTQiDDNWLIECARFAQIHDDIERMPMGYDTLIGELGEGLSGGQKQRIFIARAIYKKPSIL 651
Cdd:PLN03232 1315 IPQSPVLFSGTVRFNIDPFSEH-NDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKIL 1393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1533513286 652 FMDEATSSLDHTNEQYINDAIKS--LNITRIVIAHRKSTINSADRIIALQ 699
Cdd:PLN03232 1394 VLDEATASVDVRTDSLIQRTIREefKSCTMLVIAHRLNTIIDCDKILVLS 1443
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
492-700 |
8.53e-29 |
|
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: 114.74 E-value: 8.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISYKYDSyASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKLIAC 571
Cdd:COG1122 1 IELENLSFSYPG-GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 572 VLQ--DDRLFSGTLRDNIcSFS---TQIDDNWLIECARFA----QIHDDIERMP----MGydtligelgeglsggQKQRI 638
Cdd:COG1122 80 VFQnpDDQLFAPTVEEDV-AFGpenLGLPREEIRERVEEAlelvGLEHLADRPPhelsGG---------------QKQRV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1533513286 639 FIARAIYKKPSILFMDEATSSLDHTNEQYINDAIKSLN---ITRIVIAHRKSTI-NSADRIIALQE 700
Cdd:COG1122 144 AIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNkegKTVIIVTHDLDLVaELADRVIVLDD 209
|
|
| ABC_6TM_peptidase_like |
cd18571 |
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and ... |
176-457 |
1.26e-28 |
|
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: 116.39 E-value: 1.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 176 LTKIFFLSIIIESINLVMPVATQLVMDHAIPANDSGLLTLICFGLVFFVALRTITGLIRSWTVLIMSSFINAQWQKGLLQ 255
Cdd:cd18571 4 ILQLLLGLLLGSLLQLIFPFLTQSIVDKGINNKDLNFIYLILIAQLVLFLGSTSIEFIRSWILLHISSRINISIISDFLI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 256 HLLKLPLEYFERRKIGDIQSRFGSLNTLQETFTTSVVGAIIDSIMIIGLLIMLVLYGGWLTWFVILFTCLYVF------- 328
Cdd:cd18571 84 KLMRLPISFFDTKMTGDILQRINDHSRIESFLTSSSLSILFSLLNLIVFSIVLAYYNLTIFLIFLIGSVLYILwillflk 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 329 -IRVLTYNRYRQLSEEslikdaraNSFFMETLYGIATVKVQGLNKRREENWFNLEVDSINTGIKVSRLNLFFGGINTLIA 407
Cdd:cd18571 164 kRKKLDYKRFDLSSEN--------QSKLIELINGMQEIKLNNSERQKRWEWERIQAKLFKINIKSLKLDQYQQIGALFIN 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1533513286 408 TMEQILILWLGASLVISGNMTIGMFVAFSSYRGQFSDRIASFIDFLLRLQ 457
Cdd:cd18571 236 QLKNILITFLAAKLVIDGEITLGMMLAIQYIIGQLNSPIEQLIGFIQSLQ 285
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
495-698 |
1.94e-26 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 116.28 E-value: 1.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 495 KNISYKYDSYASYTL-RHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFV-DGIDIKELGVNNYQKLIACV 572
Cdd:PTZ00265 386 KNVRFHYDTRKDVEIyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVV 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 573 LQDDRLFSGTLRDNIC-------------------SFSTQ--------------------------------------ID 595
Cdd:PTZ00265 466 SQDPLLFSNSIKNNIKyslyslkdlealsnyynedGNDSQenknkrnscrakcagdlndmsnttdsneliemrknyqtIK 545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 596 DNWLIECARFAQIHDDIERMPMGYDTLIGELGEGLSGGQKQRIFIARAIYKKPSILFMDEATSSLDHTNEQYINDAIKSL 675
Cdd:PTZ00265 546 DSEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNL 625
|
250 260
....*....|....*....|....*..
gi 1533513286 676 ----NITRIVIAHRKSTINSADRIIAL 698
Cdd:PTZ00265 626 kgneNRITIIIAHRLSTIRYANTIFVL 652
|
|
| ABC_6TM_NHLM_bacteriocin |
cd18569 |
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ... |
174-466 |
1.94e-26 |
|
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: 109.87 E-value: 1.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 174 SALTKIFFLSIIIESINLVMPVATQLVMDHAIPANDSGLLTLICFGLVFFVALRTITGLIRSWTVLIM---------SSF 244
Cdd:cd18569 2 SALLFVVLAGLLLVIPGLVIPVFSRIFIDDILVGGLPDWLRPLLLGMALTALLQGLLTWLQQYYLLRLetklalsssSRF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 245 InaqWQkgllqhLLKLPLEYFERRKIGDIQSRFGSLNTLQETFTTSVVGAIIDSIMIIGLLIMLVLYGGWLTWFVILFTC 324
Cdd:cd18569 82 F---WH------VLRLPVEFFSQRYAGDIASRVQSNDRVANLLSGQLATTVLNLVMAVFYALLMLQYDVPLTLIGIAIAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 325 LYVFIRVLTYNRYRQLSEESLIKDARANSFFMETLYGIATVKVQGlnkrREENWFN----LEVDSINTGIKVSRLNLFFG 400
Cdd:cd18569 153 LNLLVLRLVSRKRVDLNRRLLQDSGKLTGTTMSGLQMIETLKASG----AESDFFSrwagYQAKVLNAQQELGRTNQLLG 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1533513286 401 GINTLIATMEQILILWLGASLVISGNMTIGMFVAFSSYRGQFSDRIASFIDFLLRLQIMSLHNERV 466
Cdd:cd18569 229 ALPTLLSALTNAAILGLGGLLVMDGALTIGMLVAFQSLMASFLAPVNSLVGLGGTLQEMRGDMERL 294
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
487-700 |
2.67e-26 |
|
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: 113.46 E-value: 2.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 487 MCPVsLSAKNISYKYDSYASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPAS---EGNIFVDGIDIKELGVN 563
Cdd:COG1123 1 MTPL-LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 564 NYQKLIACVLQD--DRLFSGTLRDnicsfstQIDDNWLIECARFAQIHDDIERM--PMGYDTLIGELGEGLSGGQKQRIF 639
Cdd:COG1123 80 LRGRRIGMVFQDpmTQLNPVTVGD-------QIAEALENLGLSRAEARARVLELleAVGLERRLDRYPHQLSGGQRQRVA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1533513286 640 IARAIYKKPSILFMDEATSSLDHTNEQYINDAIKSL----NITRIVIAHRKSTI-NSADRIIALQE 700
Cdd:COG1123 153 IAMALALDPDLLIADEPTTALDVTTQAEILDLLRELqrerGTTVLLITHDLGVVaEIADRVVVMDD 218
|
|
| Peptidase_C39D |
cd02420 |
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
22-144 |
5.59e-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: 239101 [Multi-domain] Cd Length: 125 Bit Score: 103.28 E-value: 5.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 22 PMIHQTESSECGLACLAMICGYYGKNIDIFTLRQKFKLSSRGTDLASLNDIAVKMHMSTRAVSVELDELHSVKLPCILHW 101
Cdd:cd02420 2 PTVLQMEATECGAASLAIILAYYGRYVPLSELRIACGVSRDGSNASNLLKAAREYGLTAKGYKKDLEALREVSLPAIVFW 81
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1533513286 102 DFNHFVVLTKIKNGKFTVHDPSVGIVKVAKSELSKKFTGIVLE 144
Cdd:cd02420 82 NFNHFLVVEGFDKRKVFLNDPATGRRTVSLEEFDQSFTGVVLT 124
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
394-701 |
9.49e-26 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 112.21 E-value: 9.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 394 RLNLFFGGINTLIatmeQILILWLGASLVISGNMTIGMFV----AFSSYRGQFS------DRIASFIDFLLRLQimSLHN 463
Cdd:COG4178 267 NLTFFTTGYGQLA----VIFPILVAAPRYFAGEITLGGLMqaasAFGQVQGALSwfvdnyQSLAEWRATVDRLA--GFEE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 464 ervsdiALTEVTPFKDDIPVKNDMCPVSLSAKNISYKYDSYASyTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLF 543
Cdd:COG4178 341 ------ALEAADALPEAASRIETSEDGALALEDLTLRTPDGRP-LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLW 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 544 PASEGNIFV-DGIDIkelgvnnyqkliaCVL-QDDRLFSGTLRDNIC--SFSTQIDDNWLIE----------CARFAQIH 609
Cdd:COG4178 414 PYGSGRIARpAGARV-------------LFLpQRPYLPLGTLREALLypATAEAFSDAELREaleavglghlAERLDEEA 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 610 DDIERMPMGydtligelgeglsggQKQRIFIARAIYKKPSILFMDEATSSLDHTNEQYINDAIKSL--NITRIVIAHRKS 687
Cdd:COG4178 481 DWDQVLSLG---------------EQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREElpGTTVISVGHRST 545
|
330
....*....|....
gi 1533513286 688 TINSADRIIALQEN 701
Cdd:COG4178 546 LAAFHDRVLELTGD 559
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
492-698 |
9.85e-26 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 107.41 E-value: 9.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISYKYDSYASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKLIAC 571
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 572 VLQD-DRLFSG-TLRDNIcSFS---TQIDDNWLIEcarfaQIHDDIERMPMgyDTLIGELGEGLSGGQKQRIFIARAIYK 646
Cdd:PRK13635 86 VFQNpDNQFVGaTVQDDV-AFGlenIGVPREEMVE-----RVDQALRQVGM--EDFLNREPHRLSGGQKQRVAIAGVLAL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1533513286 647 KPSILFMDEATSSLDHTNEQYINDAIKSL----NITRIVIAHRKSTINSADRIIAL 698
Cdd:PRK13635 158 QPDIIILDEATSMLDPRGRREVLETVRQLkeqkGITVLSITHDLDEAAQADRVIVM 213
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
509-698 |
1.28e-25 |
|
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: 106.05 E-value: 1.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 509 LRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKL---IACVLQDDRLFSG-TLR 584
Cdd:cd03261 16 LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLrrrMGMLFQSGALFDSlTVF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 585 DNICSF---STQIDDNWL----IECARFAQIHDDIERMP------MgydtligelgeglsggqKQRIFIARAIYKKPSIL 651
Cdd:cd03261 96 ENVAFPlreHTRLSEEEIreivLEKLEAVGLRGAEDLYPaelsggM-----------------KKRVALARALALDPELL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1533513286 652 FMDEATSSLDHTNEQYINDAIKSLN----ITRIVIAHRKSTINS-ADRIIAL 698
Cdd:cd03261 159 LYDEPTAGLDPIASGVIDDLIRSLKkelgLTSIMVTHDLDTAFAiADRIAVL 210
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
492-700 |
1.31e-25 |
|
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: 105.29 E-value: 1.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISYKYDSyaSYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVnnYQKLIAC 571
Cdd:cd03259 1 LELKGLSKTYGS--VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPP--ERRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 572 VLQDDRLFSG-TLRDNICsF--------STQIDDNWLiECARFAQIHDDIERMPmgyDTLigelgeglSGGQKQRIFIAR 642
Cdd:cd03259 77 VFQDYALFPHlTVAENIA-FglklrgvpKAEIRARVR-ELLELVGLEGLLNRYP---HEL--------SGGQQQRVALAR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1533513286 643 AIYKKPSILFMDEATSSLD-HTNEQ---YINDAIKSLNITRIVIAHRKSTINS-ADRIIALQE 700
Cdd:cd03259 144 ALAREPSLLLLDEPLSALDaKLREElreELKELQRELGITTIYVTHDQEEALAlADRIAVMNE 206
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
176-457 |
1.45e-25 |
|
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: 107.21 E-value: 1.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 176 LTKIFFLSIIIESINLVMPVATQLVMDHAI----PANDSGLLTLICFGLVFFVALRTITGLIRSWTVLIMSSFINAQWQK 251
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPYLTKILIDDVLiqlgPGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 252 GLLQHLLKLPLEYFERRKIGDIQSRFGS-LNTLQETFTTSVVGAIIDSIMIIGLLIMLVLYGGWLTWFVILFTCLYVFIR 330
Cdd:cd18563 81 DLYEHLQRLSLSFFDKRQTGSLMSRVTSdTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 331 VLTYNRYRQLSEESLIKDARANSFFMETLYGIATVKVQGLNKRREENWFNLEVDSINTGIKVSRLNLFFGGINTLIATME 410
Cdd:cd18563 161 YFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFLTSLG 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1533513286 411 QILILWLGASLVISGNMTIGMFVAFSSYRGQFSDRIASFIDFLLRLQ 457
Cdd:cd18563 241 TLIVWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWIT 287
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
413-698 |
1.88e-25 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 111.35 E-value: 1.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 413 LILWLGASLVisGNMTIGMFVAFSSYRGQFSDRIASFIDFLLRLQIMSLHNERVSDIALTEVTPF-KDDIPVKNDmcpvS 491
Cdd:PRK10790 267 LLMLFGFSAS--GTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERVFELMDGPRQQYgNDDRPLQSG----R 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISYKYDSyASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKLIAC 571
Cdd:PRK10790 341 IDIDNVSFAYRD-DNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAM 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 572 VLQDDRLFSGTLRDNIcSFSTQIDDNWLIECARFAQIHDDIERMPMGYDTLIGELGEGLSGGQKQRIFIARAIYKKPSIL 651
Cdd:PRK10790 420 VQQDPVVLADTFLANV-TLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQIL 498
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1533513286 652 FMDEATSSLDHTNEQYINDAIKSL--NITRIVIAHRKSTINSADRIIAL 698
Cdd:PRK10790 499 ILDEATANIDSGTEQAIQQALAAVreHTTLVVIAHRLSTIVEADTILVL 547
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
509-698 |
2.45e-25 |
|
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: 103.00 E-value: 2.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 509 LRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIfvdgiDIKElgvnnyqkliacvlQDDRLF--------S 580
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-----GMPE--------------GEDLLFlpqrpylpL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 581 GTLRDNICSfstqiddNWliecarfaqihddiermpmgYDTLigelgeglSGGQKQRIFIARAIYKKPSILFMDEATSSL 660
Cdd:cd03223 78 GTLREQLIY-------PW--------------------DDVL--------SGGEQQRLAFARLLLHKPKFVFLDEATSAL 122
|
170 180 190
....*....|....*....|....*....|....*...
gi 1533513286 661 DHTNEQYINDAIKSLNITRIVIAHRKSTINSADRIIAL 698
Cdd:cd03223 123 DEESEDRLYQLLKELGITVISVGHRPSLWKFHDRVLDL 160
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
492-700 |
2.57e-25 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 103.16 E-value: 2.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISYKYDSYASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGvNNYQKLIAC 571
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 572 VLQDDRLFSGTLRDNIcsfstqiddnwlieCARFAqihddiermpmgydtligelgeglsGGQKQRIFIARAIYKKPSIL 651
Cdd:cd03247 80 LNQRPYLFDTTLRNNL--------------GRRFS-------------------------GGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1533513286 652 FMDEATSSLDHTNEQYINDAIKSL--NITRIVIAHRKSTINSADRIIALQE 700
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVlkDKTLIWITHHLTGIEHMDKILFLEN 171
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
492-699 |
2.70e-25 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 104.80 E-value: 2.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISYKYDsyASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKLIAC 571
Cdd:PRK10247 8 LQLQNVGYLAG--DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 572 VLQDDRLFSGTLRDNICsFSTQIdDNWLIECARFAqihDDIERMPMGyDTLIGELGEGLSGGQKQRIFIARAIYKKPSIL 651
Cdd:PRK10247 86 CAQTPTLFGDTVYDNLI-FPWQI-RNQQPDPAIFL---DDLERFALP-DTILTKNIAELSGGEKQRISLIRNLQFMPKVL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1533513286 652 FMDEATSSLDHTNEQYINDAIKSL----NITRIVIAHRKSTINSADRIIALQ 699
Cdd:PRK10247 160 LLDEITSALDESNKHNVNEIIHRYvreqNIAVLWVTHDKDEINHADKVITLQ 211
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
493-698 |
4.01e-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: 103.77 E-value: 4.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 493 SAKNISYKYDSYAsyTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELgvnnyQKLIACV 572
Cdd:cd03235 1 EVEDLTVSYGGHP--VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 573 LQD---DRLFSGTLRDNICSfSTQIDDNWL--IECARFAQIHDDIERMPMG------YDTLigelgeglSGGQKQRIFIA 641
Cdd:cd03235 74 PQRrsiDRDFPISVRDVVLM-GLYGHKGLFrrLSKADKAKVDEALERVGLSeladrqIGEL--------SGGQQQRVLLA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1533513286 642 RAIYKKPSILFMDEATSSLDHTNEQYINDAIKSLN---ITRIVIAH-RKSTINSADRIIAL 698
Cdd:cd03235 145 RALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRregMTILVVTHdLGLVLEYFDRVLLL 205
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
413-698 |
4.41e-25 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 111.75 E-value: 4.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 413 LILWLGASLVISGNMTIGMFVAFSSYRG---QFSDRIASFIDFLLRLQIM---SLHN-ERVSD-IALTEVTPfkddiPVK 484
Cdd:PLN03130 1149 LMIWLTASFAVMQNGRAENQAAFASTMGlllSYALNITSLLTAVLRLASLaenSLNAvERVGTyIDLPSEAP-----LVI 1223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 485 NDMCPV-------SLSAKNISYKYDSYASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDI 557
Cdd:PLN03130 1224 ENNRPPpgwpssgSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDI 1303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 558 KELGVNNYQKLIACVLQDDRLFSGTLRDNICSFSTQID-DNWliECARFAQIHDDIERMPMGYDTLIGELGEGLSGGQKQ 636
Cdd:PLN03130 1304 SKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDaDLW--ESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQ 1381
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1533513286 637 RIFIARAIYKKPSILFMDEATSSLDHTNEQYINDAIKS--LNITRIVIAHRKSTINSADRIIAL 698
Cdd:PLN03130 1382 LLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREefKSCTMLIIAHRLNTIIDCDRILVL 1445
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
175-457 |
9.37e-25 |
|
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: 104.86 E-value: 9.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 175 ALTKIFFLSIIIESINLVMPVATQLVMDHAIPANDSGLLTLICFGLVFFVALRTITGLIRSWTVLIMSS----------F 244
Cdd:cd18545 1 KLLLALLLMLLSTAASLAGPYLIKIAIDEYIPNGDLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQrilydlrqdlF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 245 INAQWQKgllqhllklpLEYFERRKIGDIQSRF-GSLNTLQETFTTSVVGAIIDSIMIIGLLIMLVLYGGWLTwfVILFT 323
Cdd:cd18545 81 SHLQKLS----------FSFFDSRPVGKILSRViNDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLA--LVTLA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 324 CLYVFIRVLTY--NRYRQLSEESLIKDARANSFFMETLYGIATVKVQGLNKRREENWFNLEVDSINTGIKVSRLNLFFGG 401
Cdd:cd18545 149 VLPLLVLVVFLlrRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWP 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1533513286 402 INTLIATMEQILILWLGASLVISGNMTIGMFVAFSSYRGQFSDRIASFIDFLLRLQ 457
Cdd:cd18545 229 LVELISALGTALVYWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQ 284
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
493-700 |
1.01e-24 |
|
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: 101.74 E-value: 1.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 493 SAKNISYKYDSYASytLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKLIACV 572
Cdd:cd03214 1 EVENLSVGYGGRTV--LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 573 LQddrlfsgtlrdnicsfstqiddnwlieCARFAQIHDDIERmpmGYDTLigelgeglSGGQKQRIFIARAIYKKPSILF 652
Cdd:cd03214 79 PQ---------------------------ALELLGLAHLADR---PFNEL--------SGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1533513286 653 MDEATSSLDHTNE----QYINDAIKSLNITRIVIAHrksTINSA----DRIIALQE 700
Cdd:cd03214 121 LDEPTSHLDIAHQiellELLRRLARERGKTVVMVLH---DLNLAaryaDRVILLKD 173
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
181-457 |
1.28e-24 |
|
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: 104.49 E-value: 1.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 181 FLSIIIES-INLVMPVATQLVMDHAIPANDSGLLTLICFGLVFFVALRTITGLIRSWTVLIMSSFINAQWQKGLLQHLLK 259
Cdd:cd18576 2 LILLLLSSaIGLVFPLLAGQLIDAALGGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 260 LPLEYFERRKIGDIQSRFGS-LNTLQETFTTSVVGAIIDSIMIIGLLIMLVLYGGWLTWFVILFTCLYVFIRVLTYNRYR 338
Cdd:cd18576 82 LPLSFFHERRVGELTSRLSNdVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRIR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 339 QLSEESLIKDARANSFFMETLYGIATVKVQGlNKRREENWFNLEVDSI-NTGIKVSRLNLFFGGINTLIATMEQILILWL 417
Cdd:cd18576 162 KLSKKVQDELAEANTIVEETLQGIRVVKAFT-REDYEIERYRKALERVvKLALKRARIRALFSSFIIFLLFGAIVAVLWY 240
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1533513286 418 GASLVISGNMTIGMFVAFSSYRGQFSDRIASFIDFLLRLQ 457
Cdd:cd18576 241 GGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQ 280
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
300-700 |
1.70e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 108.37 E-value: 1.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 300 MIIGLLIMLVLYGG--WLTWFVILFTC-----LYVFIRVLTYNRYRQLSEESLIKDARANSFFMETLYGIATVKVQGLNK 372
Cdd:PRK11160 141 LVAALVVILVLTIGlsFFDLTLALTLGgilllLLLLLPLLFYRLGKKPGQDLTHLRAQYRVQLTEWLQGQAELTLFGAED 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 373 RREENWFNLEVDSINTGIKVSRLNLFFGGINTLIATMEQILILWLGASLVisGNMT-----IGMFVaFSSyrgqfsdrIA 447
Cdd:PRK11160 221 RYRQQLEQTEQQWLAAQRRQANLTGLSQALMILANGLTVVLMLWLAAGGV--GGNAqpgalIALFV-FAA--------LA 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 448 SFiDFLLRLQIMSLH-------NERVSDIalTEVTP---FKDDIPVKNDmcPVSLSAKNISYKYDSYASYTLRHLNIEIQ 517
Cdd:PRK11160 290 AF-EALMPVAGAFQHlgqviasARRINEI--TEQKPevtFPTTSTAAAD--QVSLTLNNVSFTYPDQPQPVLKGLSLQIK 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 518 PGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKLIACVLQDDRLFSGTLRDNICSFSTQIDDN 597
Cdd:PRK11160 365 AGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDE 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 598 WLIECARFAQIHDDIERmPMGYDTLIGELGEGLSGGQKQRIFIARAIYKKPSILFMDEATSSLDHTNEQYINDAIKSL-- 675
Cdd:PRK11160 445 ALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHaq 523
|
410 420
....*....|....*....|....*
gi 1533513286 676 NITRIVIAHRKSTINSADRIIALQE 700
Cdd:PRK11160 524 NKTVLMITHRLTGLEQFDRICVMDN 548
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
492-698 |
2.02e-24 |
|
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: 100.55 E-value: 2.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISYKYDSYASytLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVnNYQKLIAC 571
Cdd:cd03230 1 IEVRNLSKRYGKKTA--LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPE-EVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 572 VLQDDRLFSG-TLRDNIcsfstqiddnwliecarfaqihddieRMPMGydtligelgeglsggQKQRIFIARAIYKKPSI 650
Cdd:cd03230 78 LPEEPSLYENlTVRENL--------------------------KLSGG---------------MKQRLALAQALLHDPEL 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1533513286 651 LFMDEATSSLDHTNEQYINDAIKSLN---ITRIVIAHRKSTINS-ADRIIAL 698
Cdd:cd03230 117 LILDEPTSGLDPESRREFWELLRELKkegKTILLSSHILEEAERlCDRVAIL 168
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
180-466 |
2.08e-24 |
|
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: 103.79 E-value: 2.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 180 FFLSIIIESINLVMPVATQLVMDHAIPANDSGLLTLICFGLVFFVALRTITGLIRSWTVLIMSSFINAQWQKGLLQHLLK 259
Cdd:cd18557 2 LLFLLISSAAQLLLPYLIGRLIDTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 260 LPLEYFERRKIGDIQSRFGS-LNTLQETFTTSVVGAIIDSIMIIGLLIMLVLYGGWLTWFVILFTCLYVFIRVLTYNRYR 338
Cdd:cd18557 82 QEIAFFDKHKTGELTSRLSSdTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 339 QLSEESLIKDARANSFFMETLYGIATVKVQGlNKRREENWFNLEVDSI-NTGIKVSRLNLFFGGINTLIATMEQILILWL 417
Cdd:cd18557 162 KLSKEVQDALAKAGQVAEESLSNIRTVRSFS-AEEKEIRRYSEALDRSyRLARKKALANALFQGITSLLIYLSLLLVLWY 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1533513286 418 GASLVISGNMTIGMFVAFSSYRGQFSDRIASFIDFLLRLQIMSLHNERV 466
Cdd:cd18557 241 GGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
492-700 |
2.37e-24 |
|
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: 102.81 E-value: 2.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISYKYDSYAsyTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKLIAC 571
Cdd:COG1120 2 LEAENLSVGYGGRP--VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 572 VLQDDRL-FSGTLRDnicsfstqiddnwLIECARFAQI--------HDD------IERMPMG------YDTLigelgegl 630
Cdd:COG1120 80 VPQEPPApFGLTVRE-------------LVALGRYPHLglfgrpsaEDReaveeaLERTGLEhladrpVDELsg------ 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1533513286 631 sggQKQRIFIARAIYKKPSILFMDEATSSLDHTNEQYINDAIKSLNIT--RIVIA--HrksTINSA----DRIIALQE 700
Cdd:COG1120 141 --gERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErgRTVVMvlH---DLNLAaryaDRLVLLKD 213
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
492-684 |
1.51e-23 |
|
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: 99.56 E-value: 1.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISYKYDSyaSYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGL------FPaSEGNIFVDGIDIKELGVN-- 563
Cdd:cd03260 1 IELRDLNVYYGD--KHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipgAP-DEGEVLLDGKDIYDLDVDvl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 564 NYQKLIACVLQDDRLFSGTLRDNIcSFSTQIDDNWLI--------ECARFAQIHDDIERMPMGYDtligelgegLSGGQK 635
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNV-AYGLRLHGIKLKeelderveEALRKAALWDEVKDRLHALG---------LSGGQQ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1533513286 636 QRIFIARAIYKKPSILFMDEATSSLDHTNEQYINDAIKSLN--ITRIVIAH 684
Cdd:cd03260 148 QRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKkeYTIVIVTH 198
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
492-672 |
3.96e-23 |
|
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: 97.93 E-value: 3.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISYKYDsyasYT--LRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVnNYQKLI 569
Cdd:COG4133 3 LEAENLSCRRG----ERllFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARE-DYRRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 570 ACVLQDDRLFSG-TLRDNI---CSFSTQIDDNWLIE--CARF---AQIHDDIERMPMGydtligelgeglsggQKQRIFI 640
Cdd:COG4133 78 AYLGHADGLKPElTVRENLrfwAALYGLRADREAIDeaLEAVglaGLADLPVRQLSAG---------------QKRRVAL 142
|
170 180 190
....*....|....*....|....*....|..
gi 1533513286 641 ARAIYKKPSILFMDEATSSLDHTNEQYINDAI 672
Cdd:COG4133 143 ARLLLSPAPLWLLDEPFTALDAAGVALLAELI 174
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
492-696 |
4.81e-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: 98.35 E-value: 4.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISYKYDSYASYT--LRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELG---VNNYQ 566
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 567 KLIACVLQD-----DRLFsgTLRDNIC---SFSTQIDDNWLIECARFA---QIHDDIERMPM-------Gydtligelge 628
Cdd:cd03257 82 KEIQMVFQDpmsslNPRM--TIGEQIAeplRIHGKLSKKEARKEAVLLllvGVGLPEEVLNRyphelsgG---------- 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1533513286 629 glsggQKQRIFIARAIYKKPSILFMDEATSSLDHTNEQYINDAIKSL----NITRIVIAHRKSTINS-ADRII 696
Cdd:cd03257 150 -----QRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLqeelGLTLLFITHDLGVVAKiADRVA 217
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
487-684 |
1.95e-22 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 97.08 E-value: 1.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 487 MCPVSLSAKNISYKYDSYAsyTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGvnnyq 566
Cdd:COG1121 2 MMMPAIELENLTVSYGGRP--VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRAR----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 567 KLIACVLQD---DRLFSGTLRD----------NICSFSTQIDDnwliecarfAQIHDDIERMPM-------------Gyd 620
Cdd:COG1121 75 RRIGYVPQRaevDWDFPITVRDvvlmgrygrrGLFRRPSRADR---------EAVDEALERVGLedladrpigelsgG-- 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1533513286 621 tligelgeglsggQKQRIFIARAIYKKPSILFMDEATSSLDHTNEQYINDAIKSLN---ITRIVIAH 684
Cdd:COG1121 144 -------------QQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRregKTILVVTH 197
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
509-700 |
3.83e-22 |
|
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: 95.82 E-value: 3.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 509 LRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKL---IACVLQDDRLFSG-TLR 584
Cdd:COG1127 21 LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELrrrIGMLFQGGALFDSlTVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 585 DNICsFS----TQIDDNWLIECARFA----QIHDDIERMP------MgydtligelgeglsggQKqRIFIARAIYKKPSI 650
Cdd:COG1127 101 ENVA-FPlrehTDLSEAEIRELVLEKlelvGLPGAADKMPselsggM----------------RK-RVALARALALDPEI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1533513286 651 LFMDEATSSLDHTNEQYINDAI----KSLNITRIVIAHRKSTINS-ADRIIALQE 700
Cdd:COG1127 163 LLYDEPTAGLDPITSAVIDELIrelrDELGLTSVVVTHDLDSAFAiADRVAVLAD 217
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
492-700 |
3.88e-22 |
|
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: 96.08 E-value: 3.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISYKYDSyaSYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELgVNNYQKLIAC 571
Cdd:COG4555 2 IEVENLSKKYGK--VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKE-PREARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 572 VLQDDRLFSG-TLRDNICSFSTQIDDNWLIECARFAQIhddIERMPMG--YDTLIgelgEGLSGGQKQRIFIARAIYKKP 648
Cdd:COG4555 79 LPDERGLYDRlTVRENIRYFAELYGLFDEELKKRIEEL---IELLGLEefLDRRV----GELSTGMKKKVALARALVHDP 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1533513286 649 SILFMDEATSSLDHTNEQYINDAIKSL-NITRIVI--AHRKSTI-NSADRIIALQE 700
Cdd:COG4555 152 KVLLLDEPTNGLDVMARRLLREILRALkKEGKTVLfsSHIMQEVeALCDRVVILHK 207
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
495-700 |
5.89e-22 |
|
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: 93.41 E-value: 5.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 495 KNISYKYDSyaSYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNN--YQKLIACV 572
Cdd:cd03229 4 KNVSKRYGQ--KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRRIGMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 573 LQDDRLFSG-TLRDNIcsfstqiddnwliecarfaqihddieRMPM--GydtligelgeglsggQKQRIFIARAIYKKPS 649
Cdd:cd03229 82 FQDFALFPHlTVLENI--------------------------ALGLsgG---------------QQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1533513286 650 ILFMDEATSSLDHTNEQYINDAIKSLN----ITRIVIAHR-KSTINSADRIIALQE 700
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQaqlgITVVLVTHDlDEAARLADRVVVLRD 176
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
180-435 |
1.45e-21 |
|
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: 95.57 E-value: 1.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 180 FFLSIIIESINLVMPVATQLVMDHAIPANDSGLLTLICFGLVFFVALRTITGLIRSWTVLIMSSFINAQWQKGLLQHLLK 259
Cdd:cd18552 5 ILGMILVAATTAALAWLLKPLLDDIFVEKDLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFDKLLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 260 LPLEYFERRKIGDIQSRFGS-LNTLQETFTTSVVGAIIDSIMIIGLLIMLVLYGGWLTWFVILFTCLYVF-IRVLTyNRY 337
Cdd:cd18552 85 LPLSFFDRNSSGDLISRITNdVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALpIRRIG-KRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 338 RQLSEESLIKDARANSFFMETLYGIATVKVQGLnKRREENWFNLEVDSI-NTGIKVSRLNLFFGGINTLIATMEQILILW 416
Cdd:cd18552 164 RKISRRSQESMGDLTSVLQETLSGIRVVKAFGA-EDYEIKRFRKANERLrRLSMKIARARALSSPLMELLGAIAIALVLW 242
|
250
....*....|....*....
gi 1533513286 417 LGASLVISGNMTIGMFVAF 435
Cdd:cd18552 243 YGGYQVISGELTPGEFISF 261
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
492-700 |
1.85e-21 |
|
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: 94.80 E-value: 1.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISYKYDSYASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIK-ELGVNNYQKLIA 570
Cdd:TIGR04520 1 IEVENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLdEENLWEIRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 571 CVLQ--DDRLFSGTLRDNIcSFS------------TQIDdnwliECARFAQIHDDIERMPM----Gydtligelgeglsg 632
Cdd:TIGR04520 81 MVFQnpDNQFVGATVEDDV-AFGlenlgvpreemrKRVD-----EALKLVGMEDFRDREPHllsgG-------------- 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1533513286 633 gQKQRIFIARAIYKKPSILFMDEATSSLDHTNEQYINDAIKSLN----ITRIVIAHRKSTINSADRIIALQE 700
Cdd:TIGR04520 141 -QKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNkeegITVISITHDMEEAVLADRVIVMNK 211
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
492-661 |
2.10e-21 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 93.59 E-value: 2.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISYKYDSYASytLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNnYQKLIAC 571
Cdd:COG1131 1 IEVRGLTKRYGDKTA--LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAE-VRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 572 VLQDDRLFSG-TLRDN------ICSFSTQIDDNWLIECARFAQIHDDIERMPMGYDTligelgeglsgGQKQRIFIARAI 644
Cdd:COG1131 78 VPQEPALYPDlTVRENlrffarLYGLPRKEARERIDELLELFGLTDAADRKVGTLSG-----------GMKQRLGLALAL 146
|
170
....*....|....*..
gi 1533513286 645 YKKPSILFMDEATSSLD 661
Cdd:COG1131 147 LHDPELLILDEPTSGLD 163
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
489-661 |
2.26e-21 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 94.39 E-value: 2.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 489 PVSLSAKNISYKYDSYASYT--LRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNnyq 566
Cdd:COG1116 5 APALELRGVSKRFPTGGGGVtaLDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 567 klIACVLQDDRLFs-gTLRDNICsFSTQIddNWLIECARFAQIHDDIERM---------P----MGydtligelgeglsg 632
Cdd:COG1116 82 --RGVVFQEPALLpwlTVLDNVA-LGLEL--RGVPKAERRERARELLELVglagfedayPhqlsGG-------------- 142
|
170 180
....*....|....*....|....*....
gi 1533513286 633 gQKQRIFIARAIYKKPSILFMDEATSSLD 661
Cdd:COG1116 143 -MRQRVAIARALANDPEVLLMDEPFGALD 170
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
481-700 |
2.55e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 94.29 E-value: 2.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 481 IPVKNDMCPVslsaKNISYKYDSYASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKEL 560
Cdd:PRK13632 1 IKNKSVMIKV----ENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 561 GVNNYQKLIACVLQD-DRLFSG-TLRDNIcSFSTQiddNWLIECARFAQIHDDIERMpMGYDTLIGELGEGLSGGQKQRI 638
Cdd:PRK13632 77 NLKEIRKKIGIIFQNpDNQFIGaTVEDDI-AFGLE---NKKVPPKKMKDIIDDLAKK-VGMEDYLDKEPQNLSGGQKQRV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1533513286 639 FIARAIYKKPSILFMDEATSSLD----HTNEQYINDAIKSLNITRIVIAHRKSTINSADRIIALQE 700
Cdd:PRK13632 152 AIASVLALNPEIIIFDESTSMLDpkgkREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSE 217
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
495-700 |
8.78e-21 |
|
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: 91.87 E-value: 8.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 495 KNISYKYDSYASYT--LRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKEL---GVNNYQKLI 569
Cdd:cd03258 5 KNVSKVFGDTGGKVtaLKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLsgkELRKARRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 570 ACVLQDDRLFSG-TLRDNIcSFSTQIDD----------NWLIEcarFAQIHDDIERMPM----GydtligelgeglsggQ 634
Cdd:cd03258 85 GMIFQHFNLLSSrTVFENV-ALPLEIAGvpkaeieervLELLE---LVGLEDKADAYPAqlsgG---------------Q 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1533513286 635 KQRIFIARAIYKKPSILFMDEATSSLDHTNEQYINDAIKSLN----ITRIVIAHRKSTINS-ADRIIALQE 700
Cdd:cd03258 146 KQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINrelgLTIVLITHEMEVVKRiCDRVAVMEK 216
|
|
| Peptidase_C39_like |
cd02259 |
Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The ... |
31-145 |
9.02e-21 |
|
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: 88.21 E-value: 9.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 31 ECGLACLAMICGYYGKNIDIFTLRQKFKLSSRGTDLASLNDIAVKMHMSTRAVSVELDELHSVKLPCILHWDFNHFVVLT 110
Cdd:cd02259 6 DCGLACLQMLLRYFGIPVRRDVLLNAQQRRQQGLSLADLVSLANKLGLTAQGVKLPLAALSRLQLPALLLWKQGHFVILY 85
|
90 100 110
....*....|....*....|....*....|....*..
gi 1533513286 111 KIKNGKFTVHDP-SVGIVKVAKSELSKKFTG-IVLEI 145
Cdd:cd02259 86 GADKGQVLIADPlEEGPVTLSESELEERWTGhWVLLL 122
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
492-698 |
1.54e-20 |
|
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: 90.61 E-value: 1.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISYKYDSYASYT--LRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNnyqklI 569
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVtaLEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 570 ACVLQDDRLFS-GTLRDNIcSFSTQIddNWLIECARFAQIHDDIERMPM-------------GydtligelgeglsggQK 635
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNV-ALGLEL--QGVPKAEARERAEELLELVGLsgfenayphqlsgG---------------MR 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1533513286 636 QRIFIARAIYKKPSILFMDEATSSLD-HTNEQYINDaikslnITRIVIAHRKSTI---NS-------ADRIIAL 698
Cdd:cd03293 138 QRVALARALAVDPDVLLLDEPFSALDaLTREQLQEE------LLDIWRETGKTVLlvtHDideavflADRVVVL 205
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
495-700 |
1.65e-20 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 90.88 E-value: 1.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 495 KNISYKYDSyASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKL---IAC 571
Cdd:COG2884 5 ENVSKRYPG-GREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLrrrIGV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 572 VLQDDRLFSG-TLRDNIcSFSTQIddnwlIECARfAQIHDDIE-------------RMPM----Gydtligelgeglsgg 633
Cdd:COG2884 84 VFQDFRLLPDrTVYENV-ALPLRV-----TGKSR-KEIRRRVRevldlvglsdkakALPHelsgG--------------- 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1533513286 634 QKQRIFIARAIYKKPSILFMDEATSSLDHTNEQYINDAIKSLN---ITrIVIA-HRKSTINSAD-RIIALQE 700
Cdd:COG2884 142 EQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINrrgTT-VLIAtHDLELVDRMPkRVLELED 212
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
493-701 |
2.45e-20 |
|
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: 89.62 E-value: 2.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 493 SAKNISYKYdSYASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKElgvNNYQKLIACV 572
Cdd:cd03226 1 RIENISFSY-KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA---KERRKSIGYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 573 LQD--DRLFSGTLRDNICSFSTQIDD-NWLIECA-RFAQIHDDIERMP----MGydtligelgeglsggQKQRIFIARAI 644
Cdd:cd03226 77 MQDvdYQLFTDSVREELLLGLKELDAgNEQAETVlKDLDLYALKERHPlslsGG---------------QKQRLAIAAAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1533513286 645 YKKPSILFMDEATSSLDHTNEQYINDAIKSLN---ITRIVIAHRKSTI-NSADRIIALQEN 701
Cdd:cd03226 142 LSGKDLLIFDEPTSGLDYKNMERVGELIRELAaqgKAVIVITHDYEFLaKVCDRVLLLANG 202
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
495-699 |
4.88e-20 |
|
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: 89.24 E-value: 4.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 495 KNISYKYDSYasYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNnyQKLIACVLQ 574
Cdd:cd03301 4 ENVTKRFGNV--TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK--DRDIAMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 575 DDRLFSG-TLRDNICS------FSTQIDDNWLIECARFAQIHDDIERMPmgydtligelgEGLSGGQKQRIFIARAIYKK 647
Cdd:cd03301 80 NYALYPHmTVYDNIAFglklrkVPKDEIDERVREVAELLQIEHLLDRKP-----------KQLSGGQRQRVALGRAIVRE 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1533513286 648 PSILFMDEATSSLD-HTNEQY---INDAIKSLNITRIVIAH-RKSTINSADRIIALQ 699
Cdd:cd03301 149 PKVFLMDEPLSNLDaKLRVQMraeLKRLQQRLGTTTIYVTHdQVEAMTMADRIAVMN 205
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
489-698 |
1.05e-19 |
|
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: 87.61 E-value: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 489 PVSLSAKNISYKYDSYASYT----LRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGL--FPASEGNIFVDGIDIKElgv 562
Cdd:cd03213 1 GVTLSFRNLTVTVKSSPSKSgkqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPLDK--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 563 NNYQKLIACVLQDDRLFSG-TLRDNIcSFSTQiddnwliecarfaqihddIERMPMGydtligelgeglsggQKQRIFIA 641
Cdd:cd03213 78 RSFRKIIGYVPQDDILHPTlTVRETL-MFAAK------------------LRGLSGG---------------ERKRVSIA 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1533513286 642 RAIYKKPSILFMDEATSSLDHTNEQYINDAIKSL---NITRIVIAHRKST--INSADRIIAL 698
Cdd:cd03213 124 LELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLadtGRTIICSIHQPSSeiFELFDKLLLL 185
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
487-696 |
1.28e-19 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 90.93 E-value: 1.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 487 MCPVSLSAKNISYKYDSYASytLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVnnYQ 566
Cdd:COG3842 1 MAMPALELENVSKRYGDVTA--LDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPP--EK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 567 KLIACVLQDDRLFSG-TLRDNICsF--------STQID---DNWL--IECARFAqihddiERMPM----Gydtligelge 628
Cdd:COG3842 77 RNVGMVFQDYALFPHlTVAENVA-FglrmrgvpKAEIRarvAELLelVGLEGLA------DRYPHqlsgG---------- 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1533513286 629 glsggQKQRIFIARAIYKKPSILFMDEATSSLD-HTNEQ---YINDAIKSLNITRIVIAHRKS---TInsADRII 696
Cdd:COG3842 140 -----QQQRVALARALAPEPRVLLLDEPLSALDaKLREEmreELRRLQRELGITFIYVTHDQEealAL--ADRIA 207
|
|
| Peptidase_C39E |
cd02424 |
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
23-145 |
1.42e-19 |
|
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: 85.08 E-value: 1.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 23 MIHQTESSECGLACLAMICG-YYGKNIDIFTLRQKFKLSSRGTDLASLNDIAVKMHMSTRAVSVELDELHSVKLP---CI 98
Cdd:cd02424 3 IIKQTDLNDCGIAVIQMLYNhYYKKKYDLNELKIKANLKKNGLSIYDLENLAKKFGLETESYQGSFLEFLELKNKfiiLL 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1533513286 99 LHWDFNHFVVLTKIKNGKFTVHDPSVGIVKVAKSELSKKFTGIVLEI 145
Cdd:cd02424 83 KSNGLNHFVIVKKIKKNKFIVLDPKKGKYKITYKEFEKIFNNIIITV 129
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
509-698 |
1.61e-19 |
|
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: 88.39 E-value: 1.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 509 LRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKL---IACVLQDDRL------- 578
Cdd:cd03256 17 LKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLrrqIGMIFQQFNLierlsvl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 579 ---------FSGTLRdNICSFSTQIDDNWLIECARFAQIHDDIERMPmgyDTLigelgeglSGGQKQRIFIARAIYKKPS 649
Cdd:cd03256 97 envlsgrlgRRSTWR-SLFGLFPKEEKQRALAALERVGLLDKAYQRA---DQL--------SGGQQQRVAIARALMQQPK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1533513286 650 ILFMDEATSSLDHTNEQYINDAIKSLN----ITRIVIAHRKSTINS-ADRIIAL 698
Cdd:cd03256 165 LILADEPVASLDPASSRQVMDLLKRINreegITVIVSLHQVDLAREyADRIVGL 218
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
487-661 |
1.71e-19 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 90.52 E-value: 1.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 487 MCPVSLsaKNISYKYDSYasYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGV---N 563
Cdd:COG3839 1 MASLEL--ENVSKSYGGV--EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPkdrN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 564 nyqklIACVLQDDRLF-SGTLRDNIcSFS--------TQIDDnWLIECARFAQIHDDIERMPM----Gydtligelgegl 630
Cdd:COG3839 77 -----IAMVFQSYALYpHMTVYENI-AFPlklrkvpkAEIDR-RVREAAELLGLEDLLDRKPKqlsgG------------ 137
|
170 180 190
....*....|....*....|....*....|.
gi 1533513286 631 sggQKQRIFIARAIYKKPSILFMDEATSSLD 661
Cdd:COG3839 138 ---QRQRVALGRALVREPKVFLLDEPLSNLD 165
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
492-684 |
2.12e-19 |
|
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: 88.32 E-value: 2.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNIS--YKYDSYASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKLI 569
Cdd:COG1124 2 LEVRNLSvsYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 570 ACVLQD-----------DRLFSGTLRdnicsfstqiddnwlieCARFAQIHDDIERM--------------PM----Gyd 620
Cdd:COG1124 82 QMVFQDpyaslhprhtvDRILAEPLR-----------------IHGLPDREERIAELleqvglppsfldryPHqlsgG-- 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1533513286 621 tligelgeglsggQKQRIFIARAIYKKPSILFMDEATSSLD-HTNEQ---YINDAIKSLNITRIVIAH 684
Cdd:COG1124 143 -------------QRQRVAIARALILEPELLLLDEPTSALDvSVQAEilnLLKDLREERGLTYLFVSH 197
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
546-696 |
2.39e-19 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 93.17 E-value: 2.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 546 SEGNIFVDGIDIKELGVNNYQKLIACVLQDDRLFSGTLRDNICSFSTQIDDNWLIECARFAQIHDDIERMPMGYDTLIGE 625
Cdd:PTZ00265 1275 NSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGP 1354
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1533513286 626 LGEGLSGGQKQRIFIARAIYKKPSILFMDEATSSLDHTNEQYINDAIKSL----NITRIVIAHRKSTINSADRII 696
Cdd:PTZ00265 1355 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdkaDKTIITIAHRIASIKRSDKIV 1429
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
509-700 |
2.68e-19 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 87.80 E-value: 2.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 509 LRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKL---IACVLQD----DRLfsg 581
Cdd:COG3638 19 LDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLrrrIGMIFQQfnlvPRL--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 582 TLRDNICsfstqiddnwlieCARFAQIH-----------DDI-------ERMPM-------------Gydtligelgegl 630
Cdd:COG3638 96 SVLTNVL-------------AGRLGRTStwrsllglfppEDReralealERVGLadkayqradqlsgG------------ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1533513286 631 sggQKQRIFIARAIYKKPSILFMDEATSSLDHTNEQYINDAIKSLN----ITRIVIAH-----RKstinSADRIIALQE 700
Cdd:COG3638 151 ---QQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAredgITVVVNLHqvdlaRR----YADRIIGLRD 222
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
491-696 |
7.49e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 87.41 E-value: 7.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 491 SLSAKNISYKYDS---YASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDI--KELGVNNY 565
Cdd:PRK13637 2 SIKIENLTHIYMEgtpFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 566 QKLIACVLQ--DDRLFSGTLRDNIcSFSTQ---IDDNwliecarfaQIHDDIER-MPM---GYDTLIGELGEGLSGGQKQ 636
Cdd:PRK13637 82 RKKVGLVFQypEYQLFEETIEKDI-AFGPInlgLSEE---------EIENRVKRaMNIvglDYEDYKDKSPFELSGGQKR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1533513286 637 RIFIARAIYKKPSILFMDEATSSLDHTNEQYINDAIKSL----NITRIVIAHRKSTINS-ADRII 696
Cdd:PRK13637 152 RVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELhkeyNMTIILVSHSMEDVAKlADRII 216
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
492-698 |
1.01e-18 |
|
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: 83.63 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISYKYDsyASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKL-IA 570
Cdd:cd03216 1 LELRGITKRFG--GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAgIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 571 CVLQddrlfsgtlrdnicsfstqiddnwliecarfaqihddierMPMGydtligelgeglsggQKQRIFIARAIYKKPSI 650
Cdd:cd03216 79 MVYQ----------------------------------------LSVG---------------ERQMVEIARALARNARL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1533513286 651 LFMDEATSSLDHTNEQYINDAIKSL---NITRIVIAHRKSTI-NSADRIIAL 698
Cdd:cd03216 104 LILDEPTAALTPAEVERLFKVIRRLraqGVAVIFISHRLDEVfEIADRVTVL 155
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
301-700 |
1.16e-18 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 91.34 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 301 IIGLLIMLVLYGGWLTWFVILFTCLYVFIRVLTYNRYRQLSEESLIKDARANSFFMETLYGIATVKVQGLnkrreENWFN 380
Cdd:PLN03130 428 IIIAMVLLYQQLGVASLIGSLMLVLMFPIQTFIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAW-----ENSFQ 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 381 LEVDSI-NTGIKVSRLNLFFGGINTLIATMEQIL--ILWLGASLVISGNMTIGMfvAFSSYrGQFSdrIASFIDFLLRLQ 457
Cdd:PLN03130 503 SKVQTVrDDELSWFRKAQLLSAFNSFILNSIPVLvtVVSFGVFTLLGGDLTPAR--AFTSL-SLFA--VLRFPLFMLPNL 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 458 IMSLHNERVS-----DIALTEVTPFKDDIPVKNDMCPVSLsaKNISYKYDSYASY-TLRHLNIEIQPGEHVAITGASGTG 531
Cdd:PLN03130 578 ITQAVNANVSlkrleELLLAEERVLLPNPPLEPGLPAISI--KNGYFSWDSKAERpTLSNINLDVPVGSLVAIVGSTGEG 655
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 532 KTTLLKVLCGLFPA-SEGNIFVDGIdikelgvnnyqklIACVLQDDRLFSGTLRDNICsFSTQIDDNWLIECARFAQIHD 610
Cdd:PLN03130 656 KTSLISAMLGELPPrSDASVVIRGT-------------VAYVPQVSWIFNATVRDNIL-FGSPFDPERYERAIDVTALQH 721
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 611 DIERMPMGYDTLIGELGEGLSGGQKQRIFIARAIYKKPSILFMDEATSSLD-HTNEQYINDAIKS--LNITRIVIAHRKS 687
Cdd:PLN03130 722 DLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDaHVGRQVFDKCIKDelRGKTRVLVTNQLH 801
|
410
....*....|...
gi 1533513286 688 TINSADRIIALQE 700
Cdd:PLN03130 802 FLSQVDRIILVHE 814
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
492-700 |
1.38e-18 |
|
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: 89.58 E-value: 1.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISYKYDSYASYT---LRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKL 568
Cdd:COG1123 261 LEVRNLSKRYPVRGKGGvraVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 569 ---IACVLQD-----DRLFsgTLRDNIC---SFSTQIDDNWLIECAR--FAQIH---DDIERMP----MGydtligelge 628
Cdd:COG1123 341 rrrVQMVFQDpysslNPRM--TVGDIIAeplRLHGLLSRAERRERVAelLERVGlppDLADRYPhelsGG---------- 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1533513286 629 glsggQKQRIFIARAIYKKPSILFMDEATSSLDHTNE----QYINDAIKSLNITRIVIAHRKSTINS-ADRIIALQE 700
Cdd:COG1123 409 -----QRQRVAIARALALEPKLLILDEPTSALDVSVQaqilNLLRDLQRELGLTYLFISHDLAVVRYiADRVAVMYD 480
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
180-438 |
1.59e-18 |
|
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: 86.72 E-value: 1.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 180 FFLSIIIESINLVMPVATQLVMDHAIPANDSGLLTLICFGLVFFVALRTITGLIRSWTVLIMS----------------- 242
Cdd:cd18542 5 ILALLLATALNLLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASqkvaydlrndlydhlqr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 243 -SFinaqwqkgllqhllklplEYFERRKIGDIQSRFGS-LNTLQETFTTSVVGAIIDSIMIIGLLIMLVLYGGWLTWFVI 320
Cdd:cd18542 85 lSF------------------SFHDKARTGDLMSRCTSdVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 321 LFTCLYVFIRVLTYNRYRQLSEESLIKDARANSFFMETLYGIATVKVQG-----LNKRREENWFNLEvdsinTGIKVSRL 395
Cdd:cd18542 147 AIIPFIALFSYVFFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAredyeIEKFDKENEEYRD-----LNIKLAKL 221
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1533513286 396 NLFFGGINTLIATMEQILILWLGASLVISGNMTIGMFVAFSSY 438
Cdd:cd18542 222 LAKYWPLMDFLSGLQIVLVLWVGGYLVINGEITLGELVAFISY 264
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
281-702 |
2.32e-18 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 90.04 E-value: 2.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 281 NTLQETFTTSVVGAIIDSIMIIGLLIMLVLYGGWLTWFVI---------------LFTCLYVFIRV----LTYNRYRQLS 341
Cdd:PLN03232 389 HEARKNFASGKVTNMITTDANALQQIAEQLHGLWSAPFRIivsmvllyqqlgvasLFGSLILFLLIplqtLIVRKMRKLT 468
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 342 EESLIKDARANSFFMETLYGIATVKVQGLNKRreenwFNLEVDSI-NTGIKVSRLNLFFGGINTLIATMEQILI--LWLG 418
Cdd:PLN03232 469 KEGLQWTDKRVGIINEILASMDTVKCYAWEKS-----FESRIQGIrNEELSWFRKAQLLSAFNSFILNSIPVVVtlVSFG 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 419 ASLVISGNMT-------IGMFVAFSSYRGQFSDRIASFIDF---LLRLQIMSLHNERVsdiaLTEVTPFKDDIPvkndmc 488
Cdd:PLN03232 544 VFVLLGGDLTparaftsLSLFAVLRSPLNMLPNLLSQVVNAnvsLQRIEELLLSEERI----LAQNPPLQPGAP------ 613
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 489 pvSLSAKNISYKYDSYASY-TLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCG-LFPASEGNIFVDGIdikelgvnnyq 566
Cdd:PLN03232 614 --AISIKNGYFSWDSKTSKpTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGeLSHAETSSVVIRGS----------- 680
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 567 klIACVLQDDRLFSGTLRDNICsFSTQIDDNWLIECARFAQIHDDIERMPmGYD-TLIGELGEGLSGGQKQRIFIARAIY 645
Cdd:PLN03232 681 --VAYVPQVSWIFNATVRENIL-FGSDFESERYWRAIDVTALQHDLDLLP-GRDlTEIGERGVNISGGQKQRVSMARAVY 756
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 646 KKPSILFMDEATSSLD-HTNEQYINDAIKS--LNITRIVIAHRKSTINSADRIIALQENL 702
Cdd:PLN03232 757 SNSDIYIFDDPLSALDaHVAHQVFDSCMKDelKGKTRVLVTNQLHFLPLMDRIILVSEGM 816
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
509-699 |
2.35e-18 |
|
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: 84.38 E-value: 2.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 509 LRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKL---IACVLQDDRLFSG-TLR 584
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLrrkIGVVFQDFRLLPDrNVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 585 DNIcSFSTQIDDnwliECARFAQihddiERMPMGYDTL-----IGELGEGLSGGQKQRIFIARAIYKKPSILFMDEATSS 659
Cdd:cd03292 97 ENV-AFALEVTG----VPPREIR-----KRVPAALELVglshkHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGN 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1533513286 660 LDHTNEQYINDAIKSLNI--TRIVIA-HRKSTINS-ADRIIALQ 699
Cdd:cd03292 167 LDPDTTWEIMNLLKKINKagTTVVVAtHAKELVDTtRHRVIALE 210
|
|
| ABC_6TM_PrtD_like |
cd18586 |
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ... |
181-436 |
2.37e-18 |
|
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: 86.12 E-value: 2.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 181 FLSIIIES--INLVM---PVATQLVMDHAIP-ANDSGL--LTLICFGLVFF-VALRTItgliRSWTVLIMSSFINAQWQK 251
Cdd:cd18586 4 FVEVGLFSffINLLAlapPIFMLQVYDRVLPsGSLSTLlgLTLGMVVLLAFdGLLRQV----RSRILQRVGLRLDVELGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 252 GLLQHLLKLPleyFERRKIGDIQSRFGSLNTLQETFTTSVVGAIIDSIMIIGLLIMLVLYGGWLTWFVILFTCLYVFIRV 331
Cdd:cd18586 80 RVFRAVLELP---LESRPSGYWQQLLRDLDTLRNFLTGPSLFAFFDLPWAPLFLAVIFLIHPPLGWVALVGAPVLVGLAW 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 332 LTYNRYRQLSEESLIKDARANSFFMETLYGIATVKVQGLNKRREENWFNLEVDSINTGIKVSRLNLFFGGINTLIATMEQ 411
Cdd:cd18586 157 LNHRATRKPLGEANEAQAARDALAAETLRNAETIKALGMLGNLRRRWEARHAETLELQIRASDLAGAISAIGKTLRMALQ 236
|
250 260
....*....|....*....|....*
gi 1533513286 412 ILILWLGASLVISGNMTIGMFVAFS 436
Cdd:cd18586 237 SLILGVGAYLVIDGELTIGALIAAS 261
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
503-684 |
4.15e-18 |
|
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: 83.92 E-value: 4.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 503 SYASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQklIACVLQDDRLFSG- 581
Cdd:cd03299 9 DWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRD--ISYVPQNYALFPHm 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 582 TLRDNIcSFSTQIDDNWLIECARfaQIHDdIERMpMGYDTLIGELGEGLSGGQKQRIFIARAIYKKPSILFMDEATSSLD 661
Cdd:cd03299 87 TVYKNI-AYGLKKRKVDKKEIER--KVLE-IAEM-LGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALD 161
|
170 180
....*....|....*....|....*..
gi 1533513286 662 -HTNEQYIND---AIKSLNITRIVIAH 684
Cdd:cd03299 162 vRTKEKLREElkkIRKEFGVTVLHVTH 188
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
180-442 |
5.88e-18 |
|
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: 84.75 E-value: 5.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 180 FFLSIIIESINLVMPVATQLVMDHAIPANDSGLLTLICFGLVFFVALrTITGLIRSWTVLIMSS-------------FIN 246
Cdd:cd18544 5 LLLLLLATALELLGPLLIKRAIDDYIVPGQGDLQGLLLLALLYLGLL-LLSFLLQYLQTYLLQKlgqriiydlrrdlFSH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 247 AQWQKgllqhllklpLEYFERRKIGDIQSRFGS-LNTLQETFTTSVVGAIIDSIMIIGLLIMLVLYGGWLTWFVILFTCL 325
Cdd:cd18544 84 IQRLP----------LSFFDRTPVGRLVTRVTNdTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 326 YVFIRVLTYNRYRQLSEESLIKDARANSFFMETLYGIATVKVQGLNKRREEnwfnlEVDSIN-----TGIKVSRLNLFFG 400
Cdd:cd18544 154 LLLATYLFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFE-----EFDEINqeyrkANLKSIKLFALFR 228
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1533513286 401 GINTLIATMEQILILWLGASLVISGNMTIGMFVAFSSYRGQF 442
Cdd:cd18544 229 PLVELLSSLALALVLWYGGGQVLSGAVTLGVLYAFIQYIQRF 270
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
287-579 |
6.09e-18 |
|
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: 87.55 E-value: 6.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 287 FTTSVVGAIIDSIMIIGLLImlvlYGGWLTWFVILFTCLYVFIRVLTYNRYRQLSEESLIK--DARANSF--FMETLYGI 362
Cdd:COG4615 121 AFVRLPELLQSVALVLGCLA----YLAWLSPPLFLLTLVLLGLGVAGYRLLVRRARRHLRRarEAEDRLFkhFRALLEGF 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 363 ATVKvqgLNKRREENWFNLEVDSinTGIKVSRLNLFFGGINTLIATMEQI-------LILWLGASLVISGNMTIGMFV-- 433
Cdd:COG4615 197 KELK---LNRRRRRAFFDEDLQP--TAERYRDLRIRADTIFALANNWGNLlffaligLILFLLPALGWADPAVLSGFVlv 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 434 -------------AFSSY-RGQFS-DRIASfidflLRLQIMSLHNERVSDIALTEVTPFKddipvkndmcpvSLSAKNIS 498
Cdd:COG4615 272 llflrgplsqlvgALPTLsRANVAlRKIEE-----LELALAAAEPAAADAAAPPAPADFQ------------TLELRGVT 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 499 YKYDSYA---SYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKLIACVLQD 575
Cdd:COG4615 335 YRYPGEDgdeGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSD 414
|
....
gi 1533513286 576 DRLF 579
Cdd:COG4615 415 FHLF 418
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
495-700 |
1.13e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 84.01 E-value: 1.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 495 KNISYKYDS-YASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKLIACVL 573
Cdd:PRK13650 8 KNLTFKYKEdQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 574 QD-DRLFSG-TLRDNIC------SFSTQIDDNWLIECARFAQIHDDIERMPmgydtligelgEGLSGGQKQRIFIARAIY 645
Cdd:PRK13650 88 QNpDNQFVGaTVEDDVAfglenkGIPHEEMKERVNEALELVGMQDFKEREP-----------ARLSGGQKQRVAIAGAVA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1533513286 646 KKPSILFMDEATSSLDHTNE----QYINDAIKSLNITRIVIAHRKSTINSADRIIALQE 700
Cdd:PRK13650 157 MRPKIIILDEATSMLDPEGRleliKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKN 215
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
492-700 |
4.90e-17 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 80.74 E-value: 4.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISYKYDSYASytLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIkeLGVNNYQKLIAC 571
Cdd:cd03300 1 IELENVSKFYGGFVA--LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 572 VLQDDRLFSG-TLRDNIC------SFSTQIDDNWLIECARFAQIHDDIERMPmgyDTLigelgeglSGGQKQRIFIARAI 644
Cdd:cd03300 77 VFQNYALFPHlTVFENIAfglrlkKLPKAEIKERVAEALDLVQLEGYANRKP---SQL--------SGGQQQRVAIARAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1533513286 645 YKKPSILFMDEATSSLD---HTNEQYINDAI-KSLNITRIVIAHRKS-TINSADRIIALQE 700
Cdd:cd03300 146 VNEPKVLLLDEPLGALDlklRKDMQLELKRLqKELGITFVFVTHDQEeALTMSDRIAVMNK 206
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
179-441 |
5.53e-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: 349994 [Multi-domain] Cd Length: 294 Bit Score: 82.15 E-value: 5.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 179 IFFLSIIIES-INLVMPVATQLVMDHAIPANDSGLLTLICFGLVFFVALRTITGLIRSW-TVLIMSSFI---------NA 247
Cdd:cd18550 3 LVLLLILLSAlLGLLPPLLLREIIDDALPQGDLGLLVLLALGMVAVAVASALLGVVQTYlSARIGQGVMydlrvqlyaHL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 248 QWQkgllqhllklPLEYFERRKIGDIQSRFGS-LNTLQETFTTSVVGAIIDSIMIIGLLI-MLVLygGW-LTWFVILFTC 324
Cdd:cd18550 83 QRM----------SLAFFTRTRTGEIQSRLNNdVGGAQSVVTGTLTSVVSNVVTLVATLVaMLAL--DWrLALLSLVLLP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 325 LYVFIRVLTYNRYRQLSEESLIKDARANSFFMETLY--GIATVKVQGlNKRREENWFNLEVDSI-NTGIKVSRLNLFFGG 401
Cdd:cd18550 151 LFVLPTRRVGRRRRKLTREQQEKLAELNSIMQETLSvsGALLVKLFG-REDDEAARFARRSRELrDLGVRQALAGRWFFA 229
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1533513286 402 INTLIATMEQILILWLGASLVISGNMTIGMFVAFSSYRGQ 441
Cdd:cd18550 230 ALGLFTAIGPALVYWVGGLLVIGGGLTIGTLVAFTALLGR 269
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
492-661 |
6.56e-17 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 80.57 E-value: 6.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISYKYDSYAsytlRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIkeLGVNNYQKLIAC 571
Cdd:COG3840 2 LRLDDLTYRYGDFP----LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDL--TALPPAERPVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 572 VLQDDRLFSG-TLRDNI-------CSFSTQiDDNWLIECARFAQIHDDIERMPmgyDTLigelgeglSGGQKQRIFIARA 643
Cdd:COG3840 76 LFQENNLFPHlTVAQNIglglrpgLKLTAE-QRAQVEQALERVGLAGLLDRLP---GQL--------SGGQRQRVALARC 143
|
170
....*....|....*....
gi 1533513286 644 -IYKKPsILFMDEATSSLD 661
Cdd:COG3840 144 lVRKRP-ILLLDEPFSALD 161
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
492-698 |
1.19e-16 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 82.30 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISYKYDSYAsyTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKelGVNNYQKLIAC 571
Cdd:PRK09452 15 VELRGISKSFDGKE--VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT--HVPAENRHVNT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 572 VLQDDRLFSG-TLRDNIcSF--------STQIDDNwLIECARFAQIHDDIERMPmgydtligelgEGLSGGQKQRIFIAR 642
Cdd:PRK09452 91 VFQSYALFPHmTVFENV-AFglrmqktpAAEITPR-VMEALRMVQLEEFAQRKP-----------HQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1533513286 643 AIYKKPSILFMDEATSSLDHTNEQYINDAIKSL----NITRIVIAH-RKSTINSADRIIAL 698
Cdd:PRK09452 158 AVVNKPKVLLLDESLSALDYKLRKQMQNELKALqrklGITFVFVTHdQEEALTMSDRIVVM 218
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
509-698 |
1.93e-16 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 84.06 E-value: 1.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 509 LRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKLIACVLQDDRLFSGTLRDNIC 588
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVD 1405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 589 SFSTqiddnwliecARFAQIHDDIERMPM---------GYDTLIGELGEGLSGGQKQRIFIARAIYKKPS-ILFMDEATS 658
Cdd:PTZ00243 1406 PFLE----------ASSAEVWAALELVGLrervaseseGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSgFILMDEATA 1475
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1533513286 659 SLDHTNEQYINDAIKSL--NITRIVIAHRKSTINSADRIIAL 698
Cdd:PTZ00243 1476 NIDPALDRQIQATVMSAfsAYTVITIAHRLHTVAQYDKIIVM 1517
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
181-438 |
2.10e-16 |
|
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: 80.22 E-value: 2.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 181 FLSIIIES-INLVMPVATQLVMDHAIPANDSGLLTLICFGLVFFVALRTITGLIRSWTVLIMSSFINAQWQKGLLQHLLK 259
Cdd:cd18575 2 LIALLIAAaATLALGQGLRLLIDQGFAAGNTALLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 260 LPLEYFERRKIGDIQSRfgsLNT----LQETFTTSVVGAIIDSIMIIGLLIMLVLYGGWLTWFVILFTCLYVFIRVLTYN 335
Cdd:cd18575 82 LSPSFFETTRTGEVLSR---LTTdttlIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 336 RYRQLSEESLIKDARANSFFMETLYGIATVKVQGLNKRREENWFNLEVDSINTGIKVSRLN---------LFFGGIntli 406
Cdd:cd18575 159 RVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARalltalvifLVFGAI---- 234
|
250 260 270
....*....|....*....|....*....|..
gi 1533513286 407 atmeqILILWLGASLVISGNMTIGMFVAFSSY 438
Cdd:cd18575 235 -----VFVLWLGAHDVLAGRMSAGELSQFVFY 261
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
180-457 |
3.60e-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: 79.40 E-value: 3.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 180 FFLSIIIESINLVMPVATQLVMDHAipaNDSGLLTLICFGLVFFVALRTITGLIRSWTVLIMSSFINAQWQKGLLQHLLK 259
Cdd:cd18551 5 LLLSLLGTAASLAQPLLVKNLIDAL---SAGGSSGGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRRLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 260 LPLEYFERRKIGDIQSRFGS-LNTLQETFTTSVVGAIIDSIMIIGLLIMLVLYGGWLTWFVILFTCLYVFIRVLTYNRYR 338
Cdd:cd18551 82 LPVSFFDRRRSGDLVSRVTNdTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLGRRIR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 339 QLSEESLIKDARANSFFMETLYGIATVKVQGLNKRREENwFNLEVDSI-NTGIKVSRLNLFFGGINTLIATMEQILILWL 417
Cdd:cd18551 162 KASKRAQDALGELSAALERALSAIRTVKASNAEERETKR-GGEAAERLyRAGLKAAKIEALIGPLMGLAVQLALLVVLGV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1533513286 418 GASLVISGNMTIGMFVAFSSYRGQFSDRIASFIDFLLRLQ 457
Cdd:cd18551 241 GGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQ 280
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
494-700 |
3.84e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 79.36 E-value: 3.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 494 AKNISYKY----DSYASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELG-------- 561
Cdd:PRK13633 7 CKNVSYKYesneESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnlwdirnk 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 562 -----VNNYQKLIACVLQDDRLFS----GTLRDNIcsfSTQIDDNW----LIECARFAqihddiERMPMGydtligelge 628
Cdd:PRK13633 87 agmvfQNPDNQIVATIVEEDVAFGpenlGIPPEEI---RERVDESLkkvgMYEYRRHA------PHLLSG---------- 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1533513286 629 glsgGQKQRIFIARAIYKKPSILFMDEATSSLDHTNEQYINDAIKSLN----ITRIVIAHRKSTINSADRIIALQE 700
Cdd:PRK13633 148 ----GQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNkkygITIILITHYMEEAVEADRIIVMDS 219
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
492-675 |
4.47e-16 |
|
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: 77.93 E-value: 4.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISYKYDSYASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKLIAC 571
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 572 VlQDDRLFSG-TLRDNI-------CSFSTQID---DNWLIECARFAQIHDDIERMPMGydtligelgeglsggQKQRIFI 640
Cdd:cd03263 81 P-QFDALFDElTVREHLrfyarlkGLPKSEIKeevELLLRVLGLTDKANKRARTLSGG---------------MKRKLSL 144
|
170 180 190
....*....|....*....|....*....|....*
gi 1533513286 641 ARAIYKKPSILFMDEATSSLDHTNEQYINDAIKSL 675
Cdd:cd03263 145 AIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEV 179
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
181-442 |
5.65e-16 |
|
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: 79.07 E-value: 5.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 181 FLSIIIESI-NLVMPVATQLVMDHAIPANDSGLLTLICFGLVFFVALRTITGLIRSWTV----------LIMSSFINAQw 249
Cdd:cd18546 5 LLLVVVDTAaSLAGPLLVRYGIDSGVRAGDLGVLLLAAAAYLAVVLAGWVAQRAQTRLTgrtgerllydLRLRVFAHLQ- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 250 qkgllqhllKLPLEYFERRKIGDIQSRFGS-LNTLQETFTTSVVGAIIDSIMIIGLLIMLVlyggWLTW---------FV 319
Cdd:cd18546 84 ---------RLSLDFHERETSGRIMTRMTSdIDALSELLQTGLVQLVVSLLTLVGIAVVLL----VLDPrlalvalaaLP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 320 ILFTCLYVFIRVLTyNRYRQLSEESlikdARANSFFMETLYGIATVKVQGLNKRREENWFNLEVDSINTGIKVSRLN-LF 398
Cdd:cd18546 151 PLALATRWFRRRSS-RAYRRARERI----AAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVaIY 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1533513286 399 FGGINtLIATMEQILILWLGASLVISGNMTIGMFVAFSSYRGQF 442
Cdd:cd18546 226 FPGVE-LLGNLATAAVLLVGAWRVAAGTLTVGVLVAFLLYLRRF 268
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
492-701 |
7.26e-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: 82.27 E-value: 7.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISYKYDSYASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFpASEGNIFVDGIDIKELGVNNYQKLIAC 571
Cdd:TIGR01271 1218 MDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLL-STEGEIQIDGVSWNSVTLQTWRKAFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 572 VLQDDRLFSGTLRDNICSFStQIDDNWLIECARFAQIHDDIERMPMGYDTLIGELGEGLSGGQKQRIFIARAIYKKPSIL 651
Cdd:TIGR01271 1297 IPQKVFIFSGTFRKNLDPYE-QWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKIL 1375
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1533513286 652 FMDEATSSLDHTNEQYINDAIKSL--NITRIVIAHRKSTINSADRIIALQEN 701
Cdd:TIGR01271 1376 LLDEPSAHLDPVTLQIIRKTLKQSfsNCTVILSEHRVEALLECQQFLVIEGS 1427
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
497-701 |
8.28e-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: 76.95 E-value: 8.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 497 ISYKYDSYasytlrHLNIEIQ-PGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDG--IDIKELGVN--NYQKLIAC 571
Cdd:cd03297 6 IEKRLPDF------TLKIDFDlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvLFDSRKKINlpPQQRKIGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 572 VLQDDRLFSG-TLRDNICsFSTQIDDNwliecarfAQIHDDIERM--PMGYDTLIGELGEGLSGGQKQRIFIARAIYKKP 648
Cdd:cd03297 80 VFQQYALFPHlNVRENLA-FGLKRKRN--------REDRISVDELldLLGLDHLLNRYPAQLSGGEKQRVALARALAAQP 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1533513286 649 SILFMDEATSSLD-HTNEQ---YINDAIKSLNITRIVIAHRKSTINS-ADRIIALQEN 701
Cdd:cd03297 151 ELLLLDEPFSALDrALRLQllpELKQIKKNLNIPVIFVTHDLSEAEYlADRIVVMEDG 208
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
179-438 |
8.53e-16 |
|
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: 78.61 E-value: 8.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 179 IFFLsIIIESINLVMPVATQLVMDH-AIPANDSGLLTLICFGLVFFVALRTITGLIRSWTVLIMSSFIN--------AQW 249
Cdd:cd18541 5 ILFL-ILVDLLQLLIPRIIGRAIDAlTAGTLTASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEydlrndlfAHL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 250 QKgllqhllkLPLEYFERRKIGDIQSRFGS-LNTLQETFTTSVVgAIIDSIMIIGL-LIMLVLYGGWLTWFV-----ILF 322
Cdd:cd18541 84 LT--------LSPSFYQKNRTGDLMARATNdLNAVRMALGPGIL-YLVDALFLGVLvLVMMFTISPKLTLIAllplpLLA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 323 TCLYVFIRVLtYNRYRQlSEESLikdARANSFFMETLYGIATVKVQGLNKRREENWFNLEVDSINTGIKVSRLNLFFGGI 402
Cdd:cd18541 155 LLVYRLGKKI-HKRFRK-VQEAF---SDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPL 229
|
250 260 270
....*....|....*....|....*....|....*.
gi 1533513286 403 NTLIATMEQILILWLGASLVISGNMTIGMFVAFSSY 438
Cdd:cd18541 230 IGLLIGLSFLIVLWYGGRLVIRGTITLGDLVAFNSY 265
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
492-701 |
1.00e-15 |
|
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: 77.97 E-value: 1.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISYKYDSYASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFpASEGNIFVDGIDIKELGVNNYQKLIAC 571
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL-NTEGDIQIDGVSWNSVPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 572 VLQDDRLFSGTLRDNICSFStQIDDNWLIECARFAQIHDDIERMPMGYDTLIGELGEGLSGGQKQRIFIARAIYKKPSIL 651
Cdd:cd03289 82 IPQKVFIFSGTFRKNLDPYG-KWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKIL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1533513286 652 FMDEATSSLDHTNEQYINDAIKS--LNITRIVIAHRKSTINSADRIIALQEN 701
Cdd:cd03289 161 LLDEPSAHLDPITYQVIRKTLKQafADCTVILSEHRIEAMLECQRFLVIEEN 212
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
492-696 |
1.10e-15 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 76.96 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISYKYDSYasYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDI--KELGVNNYQKLI 569
Cdd:COG1126 2 IEIENLHKSFGDL--EVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 570 ACVLQDDRLFSG-TLRDNICsfstqiddnwliecarFAQIH-----------------------DDIERMPM----Gydt 621
Cdd:COG1126 80 GMVFQQFNLFPHlTVLENVT----------------LAPIKvkkmskaeaeeramellervglaDKADAYPAqlsgG--- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 622 ligelgeglsggQKQRIFIARAIYKKPSILFMDEATSSLD--HTNEqyINDAIKSL---NITRIVIAH-----RKstinS 691
Cdd:COG1126 141 ------------QQQRVAIARALAMEPKVMLFDEPTSALDpeLVGE--VLDVMRDLakeGMTMVVVTHemgfaRE----V 202
|
....*
gi 1533513286 692 ADRII 696
Cdd:COG1126 203 ADRVV 207
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
491-661 |
1.83e-15 |
|
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: 76.61 E-value: 1.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 491 SLSAKNISYKYDSYASytLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQklIA 570
Cdd:cd03296 2 SIEVRNVSKRFGDFVA--LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERN--VG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 571 CVLQDDRLFSG-TLRDNIcSFSTQIDDNwlIECARFAQIHDDIERM--PMGYDTLIGELGEGLSGGQKQRIFIARAIYKK 647
Cdd:cd03296 78 FVFQHYALFRHmTVFDNV-AFGLRVKPR--SERPPEAEIRAKVHELlkLVQLDWLADRYPAQLSGGQRQRVALARALAVE 154
|
170
....*....|....
gi 1533513286 648 PSILFMDEATSSLD 661
Cdd:cd03296 155 PKVLLLDEPFGALD 168
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
509-698 |
1.96e-15 |
|
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: 76.32 E-value: 1.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 509 LRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKL-IACVLQDDRLFSG-TLRDN 586
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLgIGRTFQIPRLFPElTVLEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 587 I---CSFSTQIDDNWLIECARFAQIHDDIERM--PMGYDTLIGELGEGLSGGQKQRIFIARAIYKKPSILFMDEATSSLD 661
Cdd:cd03219 96 VmvaAQARTGSGLLLARARREEREARERAEELleRVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLN 175
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1533513286 662 HTNEQYINDAIKSLN---ITRIVIAHRKSTINS-ADRIIAL 698
Cdd:cd03219 176 PEETEELAELIRELRergITVLLVEHDMDVVMSlADRVTVL 216
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
504-700 |
2.13e-15 |
|
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: 77.20 E-value: 2.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 504 YASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIfvdgidiKELGVNNYQKLIACVLqddrlfSGTL 583
Cdd:cd03291 48 VGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI-------KHSGRISFSSQFSWIM------PGTI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 584 RDNICsFSTQIDDNWLIECARFAQIHDDIERMPMGYDTLIGELGEGLSGGQKQRIFIARAIYKKPSILFMDEATSSLDHT 663
Cdd:cd03291 115 KENII-FGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVF 193
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1533513286 664 NEQYINDAIKS---LNITRIVIAHRKSTINSADRIIALQE 700
Cdd:cd03291 194 TEKEIFESCVCklmANKTRILVTSKMEHLKKADKILILHE 233
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
492-689 |
2.35e-15 |
|
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: 76.28 E-value: 2.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISYKYDSyaSYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCG-LFPASEGNIFV-----DGIDIKELgvnny 565
Cdd:COG1119 4 LELRNVTVRRGG--KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdLPPTYGNDVRLfgerrGGEDVWEL----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 566 QKLIACV---LQDDRLFSGTLRDNICS--FST-----QIDDN-------WL--IECARFAQIHddIERMPMGydtligel 626
Cdd:COG1119 77 RKRIGLVspaLQLRFPRDETVLDVVLSgfFDSiglyrEPTDEqrerareLLelLGLAHLADRP--FGTLSQG-------- 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1533513286 627 geglsggQKQRIFIARAIYKKPSILFMDEATSSLDHTNEQYINDAIKSL----NITRIVIAHRKSTI 689
Cdd:COG1119 147 -------EQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLaaegAPTLVLVTHHVEEI 206
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
182-442 |
2.74e-15 |
|
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: 77.17 E-value: 2.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 182 LSIIIESINLVMPVATQLVMDHAIPANDSGLLTLICFGLVFFVALRTI--------TGLIRSWTVLIMSSFINAQWQKgl 253
Cdd:cd18564 22 LKVVIDDVLGDKPLPGLLGLAPLLGPDPLALLLLAAAALVGIALLRGLasyagtylTALVGQRVVLDLRRDLFAHLQR-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 254 lqhllkLPLEYFERRKIGDIQSRF-GSLNTLQETFTTSVVGAIIDSIMIIGLLIMLVlyggWLTW---FVILFTC--LYV 327
Cdd:cd18564 100 ------LSLSFHDRRRTGDLLSRLtGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMF----WLDWqlaLIALAVAplLLL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 328 FIRVLTyNRYRQLSEESLIKDARANSFFMETLYGIATVKVQGLnKRREENWFNLEVD-SINTGIKVSRLNLFFGGINTLI 406
Cdd:cd18564 170 AARRFS-RRIKEASREQRRREGALASVAQESLSAIRVVQAFGR-EEHEERRFARENRkSLRAGLRAARLQALLSPVVDVL 247
|
250 260 270
....*....|....*....|....*....|....*.
gi 1533513286 407 ATMEQILILWLGASLVISGNMTIGMFVAFSSYRGQF 442
Cdd:cd18564 248 VAVGTALVLWFGAWLVLAGRLTPGDLLVFLAYLKNL 283
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
179-443 |
3.10e-15 |
|
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: 77.06 E-value: 3.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 179 IFFLSIIIESINLVMPVATQLVMDHAIPAN------DSGLLTLICFGLVFFVALRTITGLIRSWTVLIMSSFINAQWQKG 252
Cdd:cd18547 4 VIILAIISTLLSVLGPYLLGKAIDLIIEGLgggggvDFSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDLRKD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 253 LLQHLLKLPLEYFERRKIGDIQSRFGS-LNTLQETFTTSVVGAIIDSIMIIGLLIMLVLYGGWLTWFVILFTCL-YVFIR 330
Cdd:cd18547 84 LFEKLQRLPLSYFDTHSHGDIMSRVTNdVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLsLLVTK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 331 VL---TYNRYRQLSEESlikdARANSFFMETLYGIATVKVQGLNKRREEnwfnlEVDSIN-----TGIKVSRLNLFFGGI 402
Cdd:cd18547 164 FIakrSQKYFRKQQKAL----GELNGYIEEMISGQKVVKAFNREEEAIE-----EFDEINeelykASFKAQFYSGLLMPI 234
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1533513286 403 NTLIATMEQILILWLGASLVISGNMTIGMFVAFSSYRGQFS 443
Cdd:cd18547 235 MNFINNLGYVLVAVVGGLLVINGALTVGVIQAFLQYSRQFS 275
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
495-661 |
4.10e-15 |
|
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: 75.41 E-value: 4.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 495 KNISYKYDSyASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKLIACVLQ 574
Cdd:cd03295 4 ENVTKRYGG-GKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYVIQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 575 DDRLFSG-TLRDNICSFSTQIddNWLIECARfAQIHDDIERMPMGYDTLIGELGEGLSGGQKQRIFIARAIYKKPSILFM 653
Cdd:cd03295 83 QIGLFPHmTVEENIALVPKLL--KWPKEKIR-ERADELLALVGLDPAEFADRYPHELSGGQQQRVGVARALAADPPLLLM 159
|
....*...
gi 1533513286 654 DEATSSLD 661
Cdd:cd03295 160 DEPFGALD 167
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
509-699 |
5.03e-15 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 79.44 E-value: 5.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 509 LRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVdgidikelgvnnyQKLIACVLQDDRLFSGTLRDNIC 588
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWA-------------ERSIAYVPQQAWIMNATVRGNIL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 589 SFSTQiDDNWLIECARFAQIHDDIERMPMGYDTLIGELGEGLSGGQKQRIFIARAIYKKPSILFMDEATSSLD-HTNEQY 667
Cdd:PTZ00243 743 FFDEE-DAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDaHVGERV 821
|
170 180 190
....*....|....*....|....*....|....
gi 1533513286 668 INDAIKS--LNITRIVIAHRKSTINSADRIIALQ 699
Cdd:PTZ00243 822 VEECFLGalAGKTRVLATHQVHVVPRADYVVALG 855
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
508-700 |
5.07e-15 |
|
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: 74.67 E-value: 5.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 508 TLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKL----IACVLQDDRLFSGTL 583
Cdd:cd03290 16 TLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLLNATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 584 RDNIcSFSTQIDDNWLIECARFAQIHDDIERMPMGYDTLIGELGEGLSGGQKQRIFIARAIYKKPSILFMDEATSSLD-H 662
Cdd:cd03290 96 EENI-TFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDiH 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1533513286 663 TNEQYINDAIKSL----NITRIVIAHRKSTINSADRIIALQE 700
Cdd:cd03290 175 LSDHLMQEGILKFlqddKRTLVLVTHKLQYLPHADWIIAMKD 216
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
524-698 |
1.24e-14 |
|
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: 75.61 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 524 ITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKElgVNNYQKLIACVLQDDRLFSG-TLRDNIcSFSTQID------- 595
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTN--VPPHLRHINMVFQSYALFPHmTVEENV-AFGLKMRkvpraei 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 596 DNWLIECARFAQIHDDIERMPmgydtligelgEGLSGGQKQRIFIARAIYKKPSILFMDEATSSLDHT----NEQYINDA 671
Cdd:TIGR01187 78 KPRVLEALRLVQLEEFADRKP-----------HQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKlrdqMQLELKTI 146
|
170 180
....*....|....*....|....*...
gi 1533513286 672 IKSLNITRIVIAHRKS-TINSADRIIAL 698
Cdd:TIGR01187 147 QEQLGITFVFVTHDQEeAMTMSDRIAIM 174
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
492-696 |
1.33e-14 |
|
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: 73.33 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISYKYDSYasYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDI--KELGVNNYQKLI 569
Cdd:cd03262 1 IEIKNLHKSFGDF--HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 570 ACVLQDDRLFSG-TLRDNICSFSTQI---DDNWLIECAR--------FAQIHDDIERMPMGydtligelgeglsggQKQR 637
Cdd:cd03262 79 GMVFQQFNLFPHlTVLENITLAPIKVkgmSKAEAEERALellekvglADKADAYPAQLSGG---------------QQQR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1533513286 638 IFIARAIYKKPSILFMDEATSSLDHTNEQYINDAIKSL---NITRIVIAH-----RKstinSADRII 696
Cdd:cd03262 144 VAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLaeeGMTMVVVTHemgfaRE----VADRVI 206
|
|
| Peptidase_C39G |
cd02423 |
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
26-143 |
1.44e-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: 1.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 26 QTESSECGLACLA-MICGYYGKNIDIFTLRQKFKLSSRGTDLASLNDIAVKMHMSTRAVSVELDELHSVKLPCI---LHW 101
Cdd:cd02423 6 QSYDFSCGPAALAtLLRYYGGINITEQEVLKLMLIRSEGFSMLDLKRYAEALGLKANGYRLNLDKLNALQIPVIvlvNNG 85
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1533513286 102 DFNHFVVLTKIKNGKFTVHDPSVGIVKVAKSELSKKFTGIVL 143
Cdd:cd02423 86 GYGHFVVIKGIDGDRVLVGDPALGNISMSREEFERIWTGNAL 127
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
492-666 |
2.13e-14 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 73.74 E-value: 2.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISYKYDSYASYT--LRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNyqkli 569
Cdd:COG4525 4 LTVRHVSVRYPGGGQPQpaLQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 570 ACVLQDDRLFSG-TLRDNIcSFSTQIddNWLIECARFAQIHDDIERMpmGYDTLIGELGEGLSGGQKQRIFIARAIYKKP 648
Cdd:COG4525 79 GVVFQKDALLPWlNVLDNV-AFGLRL--RGVPKAERRARAEELLALV--GLADFARRRIWQLSGGMRQRVGIARALAADP 153
|
170
....*....|....*....
gi 1533513286 649 SILFMDEATSSLDH-TNEQ 666
Cdd:COG4525 154 RFLLMDEPFGALDAlTREQ 172
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
507-696 |
2.42e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 72.68 E-value: 2.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 507 YTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVdgiDIKELGVNNYQKLIACVLQDDRLFSGTLRDN 586
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCV---DVPDNQFGREASLIDAIGRKGDFKDAVELLN 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 587 ICSFStqidDNWLIEcARFAQIHDDiermpmgydtligelgeglsggQKQRIFIARAIYKKPSILFMDEATSSLDHTNEQ 666
Cdd:COG2401 121 AVGLS----DAVLWL-RRFKELSTG----------------------QKFRFRLALLLAERPKLLVIDEFCSHLDRQTAK 173
|
170 180 190
....*....|....*....|....*....|....*.
gi 1533513286 667 Y----INDAIKSLNITRIVIAHRKSTIN--SADRII 696
Cdd:COG2401 174 RvarnLQKLARRAGITLVVATHHYDVIDdlQPDLLI 209
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
509-698 |
3.09e-14 |
|
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: 72.40 E-value: 3.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 509 LRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKLiaCVLQD-----DRLfsgTL 583
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRL--GFVSDstglyDRL---TA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 584 RDNICSFS-------TQIDD--NWLIECARFAQIhddIERMPMGYDTligelgeglsgGQKQRIFIARAIYKKPSILFMD 654
Cdd:cd03266 96 RENLEYFAglyglkgDELTArlEELADRLGMEEL---LDRRVGGFST-----------GMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1533513286 655 EATSSLDHTNEQYINDAI---KSLNITRIVIAHRKSTINS-ADRIIAL 698
Cdd:cd03266 162 EPTTGLDVMATRALREFIrqlRALGKCILFSTHIMQEVERlCDRVVVL 209
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
492-682 |
4.42e-14 |
|
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: 71.84 E-value: 4.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISYKYDSYASytLRHLNIEIQPGEHvAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKElGVNNYQKLIAC 571
Cdd:cd03264 1 LQLENLTKRYGKKRA--LDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 572 VLQDDRLFSG-TLR---DNICsfstqiddnWLIECARfAQIHDDIERM------------PMGydtligelgeGLSGGQK 635
Cdd:cd03264 77 LPQEFGVYPNfTVReflDYIA---------WLKGIPS-KEVKARVDEVlelvnlgdrakkKIG----------SLSGGMR 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1533513286 636 QRIFIARAIYKKPSILFMDEATSSLDhtNEQYI--NDAIKSLNITRIVI 682
Cdd:cd03264 137 RRVGIAQALVGDPSILIVDEPTAGLD--PEERIrfRNLLSELGEDRIVI 183
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
494-684 |
6.27e-14 |
|
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: 71.63 E-value: 6.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 494 AKNISYKYDSYASytLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDI-KELGvnNYQKLIACV 572
Cdd:cd03265 3 VENLVKKYGDFEA--VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVvREPR--EVRRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 573 LQD---DRLFSGtlRDN------ICSFSTQIDDNWLIECARFAQIHDDIERMPMGYDTligelgeglsgGQKQRIFIARA 643
Cdd:cd03265 79 FQDlsvDDELTG--WENlyiharLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSG-----------GMRRRLEIARS 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1533513286 644 IYKKPSILFMDEATSSLD-HTNEQ---YINDAIKSLNITRIVIAH 684
Cdd:cd03265 146 LVHRPEVLFLDEPTIGLDpQTRAHvweYIEKLKEEFGMTILLTTH 190
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
495-698 |
6.89e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 72.48 E-value: 6.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 495 KNISYKYDSYASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKLIACVLQ 574
Cdd:PRK13648 11 KNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIVFQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 575 D-DRLFSGTLrdnicsfsTQIDDNWLIEcaRFAQIHDDIERM------PMGYDTLIGELGEGLSGGQKQRIFIARAIYKK 647
Cdd:PRK13648 91 NpDNQFVGSI--------VKYDVAFGLE--NHAVPYDEMHRRvsealkQVDMLERADYEPNALSGGQKQRVAIAGVLALN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1533513286 648 PSILFMDEATSSLDHTNEQYINDAIKSL----NITRIVIAHRKSTINSADRIIAL 698
Cdd:PRK13648 161 PSVIILDEATSMLDPDARQNLLDLVRKVksehNITIISITHDLSEAMEADHVIVM 215
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
509-684 |
7.58e-14 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 73.19 E-value: 7.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 509 LRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKEL---GVNNYQKLIACVLQDDRLFSG-TLR 584
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALserELRAARRKIGMIFQHFNLLSSrTVA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 585 DNICsFStqiddnwlIECARF--AQIHDDIERM-------------PM----GydtligelgeglsggQKQRIFIARAIY 645
Cdd:COG1135 101 ENVA-LP--------LEIAGVpkAEIRKRVAELlelvglsdkadayPSqlsgG---------------QKQRVGIARALA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1533513286 646 KKPSILFMDEATSSLDHTNEQYINDAIKSLN----ITRIVIAH 684
Cdd:COG1135 157 NNPKVLLCDEATSALDPETTRSILDLLKDINrelgLTIVLITH 199
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
492-685 |
8.19e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 74.28 E-value: 8.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISyKydSYASYT-LRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDG--------IDIKELGv 562
Cdd:COG1129 5 LEMRGIS-K--SFGGVKaLDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepvrfrspRDAQAAG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 563 nnyqklIACVLQDDRLFSG-TLRDNIC------SFSTqIDDNWLIECAR--FAQIHDDI------ERMPMGydtligelg 627
Cdd:COG1129 81 ------IAIIHQELNLVPNlSVAENIFlgreprRGGL-IDWRAMRRRARelLARLGLDIdpdtpvGDLSVA--------- 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1533513286 628 eglsggQKQRIFIARAIYKKPSILFMDEATSSLDHTNEQYINDAIKSL---NITRIVIAHR 685
Cdd:COG1129 145 ------QQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLkaqGVAIIYISHR 199
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
504-700 |
8.89e-14 |
|
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: 75.33 E-value: 8.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 504 YASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGidikelgvnnyqkLIACVLQDDRLFSGTL 583
Cdd:TIGR01271 437 YVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTI 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 584 RDNICsFSTQIDDNWLIECARFAQIHDDIERMPMGYDTLIGELGEGLSGGQKQRIFIARAIYKKPSILFMDEATSSLDHT 663
Cdd:TIGR01271 504 KDNII-FGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVV 582
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1533513286 664 NEQYINDA--IKSL-NITRIVIAHRKSTINSADRIIALQE 700
Cdd:TIGR01271 583 TEKEIFESclCKLMsNKTRILVTSKLEHLKKADKILLLHE 622
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
492-700 |
1.56e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 71.42 E-value: 1.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISYKYdSYASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDG--IDIKELGVNNYQKLI 569
Cdd:PRK13636 6 LKVEELNYNY-SDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 570 ACVLQ--DDRLFSGTLRDNIcSF---STQIDDNwliecarfaQIHDDIERM--PMGYDTLIGELGEGLSGGQKQRIFIAR 642
Cdd:PRK13636 85 GMVFQdpDNQLFSASVYQDV-SFgavNLKLPED---------EVRKRVDNAlkRTGIEHLKDKPTHCLSFGQKKRVAIAG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1533513286 643 AIYKKPSILFMDEATSSLD--HTNE--QYINDAIKSLNITRIVIAHRKSTIN-SADRIIALQE 700
Cdd:PRK13636 155 VLVMEPKVLVLDEPTAGLDpmGVSEimKLLVEMQKELGLTIIIATHDIDIVPlYCDNVFVMKE 217
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
495-684 |
2.23e-13 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 71.76 E-value: 2.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 495 KNIS--YKYDSYASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKL---I 569
Cdd:PRK11153 5 KNISkvFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKArrqI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 570 ACVLQDDRLFSG-TLRDNIcSFSTQIDdNW-----------LIECARFAQIHDdieRMPM----Gydtligelgeglsgg 633
Cdd:PRK11153 85 GMIFQHFNLLSSrTVFDNV-ALPLELA-GTpkaeikarvteLLELVGLSDKAD---RYPAqlsgG--------------- 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1533513286 634 QKQRIFIARAIYKKPSILFMDEATSSLDHTNEQYINDAIKSLN----ITRIVIAH 684
Cdd:PRK11153 145 QKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINrelgLTIVLITH 199
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
492-701 |
2.24e-13 |
|
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: 67.86 E-value: 2.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISYKYDSyaSYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVdGIDIKelgvnnyqklIAC 571
Cdd:cd03221 1 IELENLSKTYGG--KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW-GSTVK----------IGY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 572 VLQddrlFSGtlrdnicsfstqiddnwliecarfaqihddiermpmGydtligelgeglsggQKQRIFIARAIYKKPSIL 651
Cdd:cd03221 68 FEQ----LSG------------------------------------G---------------EKMRLALAKLLLENPNLL 92
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1533513286 652 FMDEATSSLDHTNEQYINDAIKSLNITRIVIAHRKSTINS-ADRIIALQEN 701
Cdd:cd03221 93 LLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQvATKIIELEDG 143
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
492-700 |
3.39e-13 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 70.22 E-value: 3.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISYKYDSYASY-------TLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKEL---G 561
Cdd:TIGR02769 3 LEVRDVTHTYRTGGLFgakqrapVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLdrkQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 562 VNNYQKLIACVLQDdrlfsgtlrdNICSFSTQIDDNWLI-----------ECARFAQIHDDIERMPMGYDTLiGELGEGL 630
Cdd:TIGR02769 83 RRAFRRDVQLVFQD----------SPSAVNPRMTVRQIIgeplrhltsldESEQKARIAELLDMVGLRSEDA-DKLPRQL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1533513286 631 SGGQKQRIFIARAIYKKPSILFMDEATSSLDHTNEQYINDAIKSLN----ITRIVIAHRKSTINS-ADRIIALQE 700
Cdd:TIGR02769 152 SGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQqafgTAYLFITHDLRLVQSfCQRVAVMDK 226
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
180-451 |
3.46e-13 |
|
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: 70.65 E-value: 3.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 180 FFLSIIIESINLVMPVATQLVMDHAIPANDSGLLTLICFGLVFFVALRTITGLIRSWTVLIMSSFINAQWQKGLLQHLLK 259
Cdd:cd18572 2 FVFLVVAALSELAIPHYTGAVIDAVVADGSREAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 260 LPLEYFERRKIGDIQSRFGS-LNTLQETFTTSVVGAIIDSIMIIGLLIMLVlyggWLTWF---VILFTCLYVFIRVLTYN 335
Cdd:cd18572 82 QDIAFFDATKTGELTSRLTSdCQKVSDPLSTNLNVFLRNLVQLVGGLAFMF----SLSWRltlLAFITVPVIALITKVYG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 336 RY-RQLSEESLIKDARANSFFMETLYGIATVKVQGlNKRREENWFNlevDSINTGIKVSRLNLFFGGINTLIATM----E 410
Cdd:cd18572 158 RYyRKLSKEIQDALAEANQVAEEALSNIRTVRSFA-TEEREARRYE---RALDKALKLSVRQALAYAGYVAVNTLlqngT 233
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1533513286 411 QILILWLGASLVISGNMTIGMFVAFSSYRGQFSDRIASFID 451
Cdd:cd18572 234 QVLVLFYGGHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGD 274
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
495-687 |
3.58e-13 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 71.29 E-value: 3.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 495 KNISYKYDSyaSYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNnyQKLIACVLQ 574
Cdd:PRK11432 10 KNITKRFGS--NTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRDICMVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 575 DDRLFSG-TLRDNI-----------CSFSTQIDDNW-LIECARFAQIHDDieRMPMGydtligelgeglsggQKQRIFIA 641
Cdd:PRK11432 86 SYALFPHmSLGENVgyglkmlgvpkEERKQRVKEALeLVDLAGFEDRYVD--QISGG---------------QQQRVALA 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1533513286 642 RAIYKKPSILFMDEATSSLDHTNEQYINDAI----KSLNITRIVIAHRKS 687
Cdd:PRK11432 149 RALILKPKVLLFDEPLSNLDANLRRSMREKIrelqQQFNITSLYVTHDQS 198
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
507-700 |
4.02e-13 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 69.87 E-value: 4.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 507 YTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGidiKELGVNNYQ---KLIACVLQDD------R 577
Cdd:COG4167 27 EAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILING---HKLEYGDYKyrcKHIRMIFQDPntslnpR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 578 LFSGTLRDNICSFSTQIDDNwliecARFAQIHDDIERMPMGYDTLiGELGEGLSGGQKQRIFIARAIYKKPSILFMDEAT 657
Cdd:COG4167 104 LNIGQILEEPLRLNTDLTAE-----EREERIFATLRLVGLLPEHA-NFYPHMLSSGQKQRVALARALILQPKIIIADEAL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1533513286 658 SSLDHT-NEQYIN---DAIKSLNITRIVIAHRKSTINS-ADRIIALQE 700
Cdd:COG4167 178 AALDMSvRSQIINlmlELQEKLGISYIYVSQHLGIVKHiSDKVLVMHQ 225
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
506-661 |
4.07e-13 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 69.23 E-value: 4.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 506 SYTLRHL----NIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNnyQKLIACVLQDDRLFSG 581
Cdd:PRK10771 8 TWLYHHLpmrfDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFSH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 582 -TLRDNIcsfSTQIDDNWLIECARFAQIHDDIERmpMGYDTLIGELGEGLSGGQKQRIFIARAIYKKPSILFMDEATSSL 660
Cdd:PRK10771 86 lTVAQNI---GLGLNPGLKLNAAQREKLHAIARQ--MGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSAL 160
|
.
gi 1533513286 661 D 661
Cdd:PRK10771 161 D 161
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
492-660 |
4.25e-13 |
|
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: 69.00 E-value: 4.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISYKYDsyASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKelGVNNYQKL--- 568
Cdd:cd03224 1 LEVENLNAGYG--KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDIT--GLPPHERArag 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 569 IACVLQDDRLFSG-TLRDNI---CSFSTQIDDNWLIE--CARFAQIHDDIER----MPMGydtligelgeglsggQKQRI 638
Cdd:cd03224 77 IGYVPEGRRIFPElTVEENLllgAYARRRAKRKARLErvYELFPRLKERRKQlagtLSGG---------------EQQML 141
|
170 180
....*....|....*....|..
gi 1533513286 639 FIARAIYKKPSILFMDEATSSL 660
Cdd:cd03224 142 AIARALMSRPKLLLLDEPSEGL 163
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
512-687 |
5.07e-13 |
|
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: 72.47 E-value: 5.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 512 LNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPA--------SEGNIFVdgidikelgvnnyqkliacVLQDDRLFSGTL 583
Cdd:TIGR00954 471 LSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVyggrltkpAKGKLFY-------------------VPQRPYMTLGTL 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 584 RDNIC-------SFSTQIDDNWLIECARFAQIHDDIERmPMGYDTlIGELGEGLSGGQKQRIFIARAIYKKPSILFMDEA 656
Cdd:TIGR00954 532 RDQIIypdssedMKRRGLSDKDLEQILDNVQLTHILER-EGGWSA-VQDWMDVLSGGEKQRIAMARLFYHKPQFAILDEC 609
|
170 180 190
....*....|....*....|....*....|.
gi 1533513286 657 TSSLDHTNEQYINDAIKSLNITRIVIAHRKS 687
Cdd:TIGR00954 610 TSAVSVDVEGYMYRLCREFGITLFSVSHRKS 640
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
491-698 |
5.47e-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: 72.67 E-value: 5.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 491 SLSAKNISYKYDSYASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIdikelgvnnyqklIA 570
Cdd:TIGR00957 636 SITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-------------VA 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 571 CVLQDDRLFSGTLRDNICsFSTQIDDNWLIECARFAQIHDDIERMPMGYDTLIGELGEGLSGGQKQRIFIARAIYKKPSI 650
Cdd:TIGR00957 703 YVPQQAWIQNDSLRENIL-FGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADI 781
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1533513286 651 LFMDEATSSLD-----HTNEQYINDAIKSLNITRIVIAHRKSTINSADRIIAL 698
Cdd:TIGR00957 782 YLFDDPLSAVDahvgkHIFEHVIGPEGVLKNKTRILVTHGISYLPQVDVIIVM 834
|
|
| C39G |
COG3271 |
Predicted double-glycine leader peptidase, C39-like (CLD) domain [Intracellular trafficking, ... |
20-143 |
5.85e-13 |
|
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: 67.71 E-value: 5.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 20 RFPMIHQTESSECGLACLAMICGY-YGKNID---IFTLRQKFKLSSR-GTDLASLNDIAVKMHMSTRAVSVELDELHSVK 94
Cdd:COG3271 42 FRNVVRQQYDYSCGAAALATLLNYhYGRPVSeaeVLEGMLTHGDQRRrGFSLLDMKRYLEALGLRADGYRLTLDDLAQLG 121
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1533513286 95 LPCILHWD---FNHFVVLTKIKNGKFTVHDPSVGIVKVAKSELSKKFTGIVL 143
Cdd:COG3271 122 IPAIVLINlggYKHFVVVKGVDDGRVLLADPALGNRSLSREEFEKMWDGNVL 173
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
509-661 |
6.19e-13 |
|
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: 69.59 E-value: 6.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 509 LRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKL----IACVLQDDRLFSG-TL 583
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrrkkISMVFQSFALLPHrTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 584 RDNIcSFSTQIDDNWLIECARFAQ-------IHDDIERMPmgyDTLigelgeglSGGQKQRIFIARAIYKKPSILFMDEA 656
Cdd:cd03294 120 LENV-AFGLEVQGVPRAEREERAAealelvgLEGWEHKYP---DEL--------SGGMQQRVGLARALAVDPDILLMDEA 187
|
....*
gi 1533513286 657 TSSLD 661
Cdd:cd03294 188 FSALD 192
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
509-661 |
6.32e-13 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 68.75 E-value: 6.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 509 LRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELG---VNNYQKLIACVLQDDRLFsgtlrd 585
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKnreVPFLRRQIGMIFQDHHLL------ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 586 nicsFSTQIDDNWLIECARFAQIHDDIER-MPMGYDTLIGELGEGLSGGQ-----KQRIFIARAIYKKPSILFMDEATSS 659
Cdd:PRK10908 92 ----MDRTVYDNVAIPLIIAGASGDDIRRrVSAALDKVGLLDKAKNFPIQlsggeQQRVGIARAVVNKPAVLLADEPTGN 167
|
..
gi 1533513286 660 LD 661
Cdd:PRK10908 168 LD 169
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
492-699 |
7.11e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 69.74 E-value: 7.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISYKYDSYASYT-LRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKLIA 570
Cdd:PRK13642 5 LEVENLVFKYEKESDVNqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 571 CVLQ--DDRLFSGTLRDNIcSFSTQ---IDDNWLI----ECARFAQIHDDIERMPmgydtligelgEGLSGGQKQRIFIA 641
Cdd:PRK13642 85 MVFQnpDNQFVGATVEDDV-AFGMEnqgIPREEMIkrvdEALLAVNMLDFKTREP-----------ARLSGGQKQRVAVA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1533513286 642 RAIYKKPSILFMDEATSSLDHTNEQYINDAIKSL----NITRIVIAHRKSTINSADRIIALQ 699
Cdd:PRK13642 153 GIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIkekyQLTVLSITHDLDEAASSDRILVMK 214
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
492-699 |
9.10e-13 |
|
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: 68.23 E-value: 9.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISYKYDSYAS--YTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGvnnyqkli 569
Cdd:COG4181 9 IELRGLTKTVGTGAGelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALD-------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 570 acvlQDDRLfsgTLRDNICSF---STQiddnwLI-------------ECAR----FAQIHDDIERMPMG-----YDTlig 624
Cdd:COG4181 81 ----EDARA---RLRARHVGFvfqSFQ-----LLptltalenvmlplELAGrrdaRARARALLERVGLGhrldhYPA--- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 625 elgeglsggQ-----KQRIFIARAIYKKPSILFMDEATSSLDHTNEQYINDAIKSLNITR----IVIAHRKSTINSADRI 695
Cdd:COG4181 146 ---------QlsggeQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERgttlVLVTHDPALAARCDRV 216
|
....
gi 1533513286 696 IALQ 699
Cdd:COG4181 217 LRLR 220
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
178-452 |
1.04e-12 |
|
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: 69.40 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 178 KIFFL----SIIIESINLVMPVATQLVMDHAIPANDSGLLTLICFGLVFFVALRTITGLIRSWTVLIMSSFINA------ 247
Cdd:cd18549 2 KLFFLdlfcAVLIAALDLVFPLIVRYIIDDLLPSKNLRLILIIGAILLALYILRTLLNYFVTYWGHVMGARIETdmrrdl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 248 --QWQKgllqhllkLPLEYFERRKIGDIQSRFGS-LNTLQETFTTSVVGAIIDSIMIIGLLIMLVLYGGWLTWFVILFTC 324
Cdd:cd18549 82 feHLQK--------LSFSFFDNNKTGQLMSRITNdLFDISELAHHGPEDLFISIITIIGSFIILLTINVPLTLIVFALLP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 325 LYVFIRVLTYNRYRQLSEESLIKDARANSFFMETLYGIATVKVQGlNKRREENWFnlevDSINTGIKVSRLN------LF 398
Cdd:cd18549 154 LMIIFTIYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFA-NEEYEIEKF----DEGNDRFLESKKKaykamaYF 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1533513286 399 FGGINTLIATMeQILILWLGASLVISGNMTIGMFVAFSSYRGQFSDRIASFIDF 452
Cdd:cd18549 229 FSGMNFFTNLL-NLVVLVAGGYFIIKGEITLGDLVAFLLYVNVFIKPIRRLVNF 281
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
191-438 |
1.40e-12 |
|
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: 68.66 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 191 LVMPVATQLVMDHAIPANDSGLLTLICFGLVFFVALRTITGLIRSWTVLIMSSFINAQWQKGLLQHLLKLPLEYFERRKI 270
Cdd:cd18543 16 LAIPLLTRRAIDGPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFAHLQRLDGAFHDRWQS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 271 GDIQSRFGS-LNTLQE--TFTTSVVGAIIdsIMIIGLLIMLVLYgGWLTwfvILFTCLYVFIRVLTY---NRYRQLSEES 344
Cdd:cd18543 96 GQLLSRATSdLSLVQRflAFGPFLLGNLL--TLVVGLVVMLVLS-PPLA---LVALASLPPLVLVARrfrRRYFPASRRA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 345 LIKDARANSFFMETLYGIATVKVQGlNKRREENWFNLEVDSI-NTGIKVSRLNLFFGGINTLIATMEQILILWLGASLVI 423
Cdd:cd18543 170 QDQAGDLATVVEESVTGIRVVKAFG-RERRELDRFEAAARRLrATRLRAARLRARFWPLLEALPELGLAAVLALGGWLVA 248
|
250
....*....|....*
gi 1533513286 424 SGNMTIGMFVAFSSY 438
Cdd:cd18543 249 NGSLTLGTLVAFSAY 263
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
509-700 |
1.72e-12 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 67.12 E-value: 1.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 509 LRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPA---SEGNIFVDGIDIKELGVnnYQKLIACVLQDDRLFSG-TLR 584
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPA--EQRRIGILFQDDLLFPHlSVG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 585 DNICsFST--QIDDNwliecARFAQIHDDIERMPMGY------DTLigelgeglSGGQKQRIFIARAIYKKPSILFMDEA 656
Cdd:COG4136 95 ENLA-FALppTIGRA-----QRRARVEQALEEAGLAGfadrdpATL--------SGGQRARVALLRALLAEPRALLLDEP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1533513286 657 TSSLDHTNEQYIN----DAIKSLNITRIVIAHRKSTINSADRIIALQE 700
Cdd:COG4136 161 FSKLDAALRAQFRefvfEQIRQRGIPALLVTHDEEDAPAAGRVLDLGN 208
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
492-661 |
3.06e-12 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 68.71 E-value: 3.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISYKYDsyASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKElgVNNYQKLIAC 571
Cdd:PRK11607 20 LEIRNLTKSFD--GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSH--VPPYQRPINM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 572 VLQDDRLFSG-TLRDNIcSFSTQIDdnwliECARfAQIHDDIERMPmgydTLIGELGEGLSG------GQKQRIFIARAI 644
Cdd:PRK11607 96 MFQSYALFPHmTVEQNI-AFGLKQD-----KLPK-AEIASRVNEML----GLVHMQEFAKRKphqlsgGQRQRVALARSL 164
|
170
....*....|....*..
gi 1533513286 645 YKKPSILFMDEATSSLD 661
Cdd:PRK11607 165 AKRPKLLLLDEPMGALD 181
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
491-684 |
3.47e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 67.37 E-value: 3.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 491 SLSAKNISYKYDSyaSYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLcGLFPASEGNIFVDG--------IDIKELGV 562
Cdd:PRK14258 7 AIKVNNLSFYYDT--QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEGrveffnqnIYERRVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 563 NNYQKLIACVLQDDRLFSGTLRDN------ICSFSTQIDDNWLIECA-RFAQIHDDIERMpmgydtlIGELGEGLSGGQK 635
Cdd:PRK14258 84 NRLRRQVSMVHPKPNLFPMSVYDNvaygvkIVGWRPKLEIDDIVESAlKDADLWDEIKHK-------IHKSALDLSGGQQ 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1533513286 636 QRIFIARAIYKKPSILFMDEATSSLDHTNEQYINDAIKSLN----ITRIVIAH 684
Cdd:PRK14258 157 QRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrseLTMVIVSH 209
|
|
| ABC_6TM_LapB_like |
cd18587 |
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ... |
179-434 |
3.80e-12 |
|
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: 67.46 E-value: 3.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 179 IFFLSIIIESINLVMPVATQLVMDHAIPANdsGLLTL------ICFGLVFFVALRtitgLIRSWTV--------LIMSSF 244
Cdd:cd18587 7 VLLAALLINLFALASPLFVMNVYDRVVPNN--AIETLwvlaigVLIALLFDFILK----LLRAYFIdvagkradVILSSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 245 InaqwqkgllqhllklpleyFER----------RKIGDIQSRFGSLNTLQETFTTSVVGAIIDSIMIIGLLIMLVLYGGW 314
Cdd:cd18587 81 L-------------------FERvlglrlearpASVGSFANNLREFESVRDFFTSATLTALIDLPFVLLFLAVIALIGGP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 315 LTWFVILFTCLYVFIRVLTYNRYRQLSEESLIKDARANSFFMETLYGIATVKVQGLNKRREENWFNLEVDSINTGIKVSR 394
Cdd:cd18587 142 LALVPLVAIPLVLLYGLLLQKPLRRLVEESMRESAQKNALLVESLSGLETIKALGAEGRMQRRWEEAVAALARSSLKSRL 221
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1533513286 395 LNLFFGGINTLIATMEQILILWLGASLVISGNMTIGMFVA 434
Cdd:cd18587 222 LSSSATNFAQFVQQLVTVAIVIVGVYLISDGELTMGGLIA 261
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
504-700 |
4.33e-12 |
|
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: 68.21 E-value: 4.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 504 YASYTLRhLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDI----KELGVNNYQKLIACVLQDDRLF 579
Cdd:TIGR02142 9 LGDFSLD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfdsrKGIFLPPEKRRIGYVFQEARLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 580 SG-TLRDNI---CSFSTQIDDNwliecARFAQIHDdiermPMGYDTLIGELGEGLSGGQKQRIFIARAIYKKPSILFMDE 655
Cdd:TIGR02142 88 PHlSVRGNLrygMKRARPSERR-----ISFERVIE-----LLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1533513286 656 ATSSLDHTNEQ----YINDAIKSLNITRIVIAHRKSTINS-ADRIIALQE 700
Cdd:TIGR02142 158 PLAALDDPRKYeilpYLERLHAEFGIPILYVSHSLQEVLRlADRVVVLED 207
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
492-684 |
4.75e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 67.02 E-value: 4.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISYKYDSyASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDG--IDIKELGVNNYQKLI 569
Cdd:PRK13639 2 LETRDLKYSYPD-GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepIKYDKKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 570 ACVLQ--DDRLFSGTLRDNICSFSTQIDdnwLIECARFAQIHDDIERMPM-GYDtliGELGEGLSGGQKQRIFIARAIYK 646
Cdd:PRK13639 81 GIVFQnpDDQLFAPTVEEDVAFGPLNLG---LSKEEVEKRVKEALKAVGMeGFE---NKPPHHLSGGQKKRVAIAGILAM 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1533513286 647 KPSILFMDEATSSLDHTNEQYINDAIKSLN---ITRIVIAH 684
Cdd:PRK13639 155 KPEIIVLDEPTSGLDPMGASQIMKLLYDLNkegITIIISTH 195
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
495-700 |
5.49e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 66.93 E-value: 5.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 495 KNISYKYDSyASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELG-VNNYQKLIACVL 573
Cdd:PRK13644 5 ENVSYSYPD-GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVGIVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 574 QD-DRLFSG-TLR-------DNICSFSTQID---DNWLIECARFAQIHDDIERMPMGydtligelgeglsggQKQRIFIA 641
Cdd:PRK13644 84 QNpETQFVGrTVEedlafgpENLCLPPIEIRkrvDRALAEIGLEKYRHRSPKTLSGG---------------QGQCVALA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1533513286 642 RAIYKKPSILFMDEATSSLDHTNEQYINDAIKSLN---ITRIVIAHRKSTINSADRIIALQE 700
Cdd:PRK13644 149 GILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHekgKTIVYITHNLEELHDADRIIVMDR 210
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
523-662 |
5.86e-12 |
|
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: 67.82 E-value: 5.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 523 AITGASGTGKTTLLKVLCGLFPASEGNIFVDG---IDiKELGVN--NYQKLIACVLQDDRLFSG-TLRDNI---CSFSTQ 593
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlQD-SARGIFlpPHRRRIGYVFQEARLFPHlSVRGNLlygRKRAPR 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1533513286 594 IDDNwliecARFAQIHD--DIE----RMPM----GydtligelgeglsggQKQRIFIARAIYKKPSILFMDEATSSLDH 662
Cdd:COG4148 108 AERR-----ISFDEVVEllGIGhlldRRPAtlsgG---------------ERQRVAIGRALLSSPRLLLMDEPLAALDL 166
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
263-438 |
7.26e-12 |
|
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: 66.77 E-value: 7.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 263 EYFERRKIGDIQSRFGS-LNTLQETFTTSVVGAIIDSIMIIGLLIMLVLYGGWLTwFVILFTCLYVFIRVLTYNRY-RQL 340
Cdd:cd18573 90 AFFDKNKTGELVSRLSSdTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLT-LVMLLVVPPIAVGAVFYGRYvRKL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 341 SEESLIKDARANSFFMETLYGIATVKVQGlNKRREENWFNLEVDSI-NTGIKVSRLN-LFFGGINtLIATMEQILILWLG 418
Cdd:cd18573 169 SKQVQDALADATKVAEERLSNIRTVRAFA-AERKEVERYAKKVDEVfDLAKKEALASgLFFGSTG-FSGNLSLLSVLYYG 246
|
170 180
....*....|....*....|
gi 1533513286 419 ASLVISGNMTIGMFVAFSSY 438
Cdd:cd18573 247 GSLVASGELTVGDLTSFLMY 266
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
491-661 |
8.59e-12 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 67.09 E-value: 8.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 491 SLSAKNISYKYDSYAsyTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDI------KELGVnn 564
Cdd:COG1118 2 SIEVRNISKRFGSFT--LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLftnlppRERRV-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 565 yqkliACVLQDDRLFSG-TLRDNIC-------SFSTQID---DNWLiecaRFAQIHDDIERMPM----Gydtligelgeg 629
Cdd:COG1118 78 -----GFVFQHYALFPHmTVAENIAfglrvrpPSKAEIRarvEELL----ELVQLEGLADRYPSqlsgG----------- 137
|
170 180 190
....*....|....*....|....*....|..
gi 1533513286 630 lsggQKQRIFIARAIYKKPSILFMDEATSSLD 661
Cdd:COG1118 138 ----QRQRVALARALAVEPEVLLLDEPFGALD 165
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
489-682 |
8.88e-12 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 65.83 E-value: 8.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 489 PVSLSAKNISYKYDSYASytLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCG---LFPAS--EGNIFVDGIDIKELGVN 563
Cdd:COG1117 9 EPKIEVRNLNVYYGDKQA--LKDINLDIPENKVTALIGPSGCGKSTLLRCLNRmndLIPGArvEGEILLDGEDIYDPDVD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 564 NYQ--KLIACVLQDDRLFSGTLRDNIcSF---------STQIDDnwLIE-----CARFAQIHDDIERMPM----Gydtli 623
Cdd:COG1117 87 VVElrRRVGMVFQKPNPFPKSIYDNV-AYglrlhgiksKSELDE--IVEeslrkAALWDEVKDRLKKSALglsgG----- 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1533513286 624 gelgeglsggQKQRIFIARAIYKKPSILFMDEATSSLDHTNEQYINDAIKSL--NITrIVI 682
Cdd:COG1117 159 ----------QQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELkkDYT-IVI 208
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
492-685 |
1.16e-11 |
|
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: 67.54 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISYKYDSYASytLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPAS--EGNIFVDGIDIKELGVNNYQ-KL 568
Cdd:TIGR02633 2 LEMKGIVKTFGGVKA--LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPLKASNIRDTErAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 569 IACVLQD----------DRLFSGtlrDNICSFSTQIDDNWLI----ECARFAQIHDDIERMPMGydtligelgeGLSGGQ 634
Cdd:TIGR02633 80 IVIIHQEltlvpelsvaENIFLG---NEITLPGGRMAYNAMYlrakNLLRELQLDADNVTRPVG----------DYGGGQ 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1533513286 635 KQRIFIARAIYKKPSILFMDEATSSLDHTNEQYINDAIKSL---NITRIVIAHR 685
Cdd:TIGR02633 147 QQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLkahGVACVYISHK 200
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
487-675 |
1.16e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 65.29 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 487 MCPVSLSAKNISYKYDSYASytLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNN-Y 565
Cdd:PRK11614 1 MEKVMLSFDKVSAHYGKIQA--LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 566 QKLIACVLQDDRLFSG-TLRDNICSFSTQIDDNWLIEcaRFAQIHDDIERMpmgYDTLIGELGEGLSGGQkQRIFIARAI 644
Cdd:PRK11614 79 REAVAIVPEGRRVFSRmTVEENLAMGGFFAERDQFQE--RIKWVYELFPRL---HERRIQRAGTMSGGEQ-QMLAIGRAL 152
|
170 180 190
....*....|....*....|....*....|.
gi 1533513286 645 YKKPSILFMDEATSSLDHTNEQYINDAIKSL 675
Cdd:PRK11614 153 MSQPRLLLLDEPSLGLAPIIIQQIFDTIEQL 183
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
511-698 |
1.73e-11 |
|
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: 64.05 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 511 HLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNnyQKLIACVLQDDRLFSG-TLRDNI-C 588
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFAHlTVEQNVgL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 589 SFSTQIDdnwLIECARFAqIHDDIERMpmGYDTLIGELGEGLSGGQKQRIFIARAIYKKPSILFMDEATSSLD----HTN 664
Cdd:cd03298 94 GLSPGLK---LTAEDRQA-IEVALARV--GLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDpalrAEM 167
|
170 180 190
....*....|....*....|....*....|....*
gi 1533513286 665 EQYINDAIKSLNITRIVIAHRKSTINS-ADRIIAL 698
Cdd:cd03298 168 LDLVLDLHAETKMTVLMVTHQPEDAKRlAQRVVFL 202
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
180-449 |
1.91e-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: 350051 [Multi-domain] Cd Length: 293 Bit Score: 65.64 E-value: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 180 FFLSIIIESINLVMPVATQLVMDHA-IPANDSGLLTLICFGLVFFVALRTITGLIRSW--------TVLIMSSFINAQWQ 250
Cdd:cd18778 5 LLCALLSTLLGLVPPWLIRELVDLVtIGSKSLGLLLGLALLLLGAYLLRALLNFLRIYlnhvaeqkVVADLRSDLYDKLQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 251 KgllqhllkLPLEYFERRKIGDIQSRF-GSLNTLQETFTTSVVGAIIDSIMIIGLLIMLVlyggWLTWFVILFTCLYV-F 328
Cdd:cd18778 85 R--------LSLRYFDDRQTGDLMSRViNDVANVERLIADGIPQGITNVLTLVGVAIILF----SINPKLALLTLIPIpF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 329 IRVLT-------YNRYRQLSEESlikdARANSFFMETLYGIATVKVQGLNKRREENWFNLEVDSINTGIKVSRLNLFFGG 401
Cdd:cd18778 153 LALGAwlyskkvRPRYRKVREAL----GELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHP 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1533513286 402 INTLIATMEQILILWLGASLVISGNMTIGMFVAFSSYRGQFSDRIASF 449
Cdd:cd18778 229 LMEFLTSLGTVLVLGFGGRLVLAGELTIGDLVAFLLYLGLFYEPITSL 276
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
492-684 |
2.34e-11 |
|
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: 65.46 E-value: 2.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISYKYDSYASYT--LRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPA---SEGNIFVDGIDIKELGVNNYQ 566
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVkaVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 567 KL----IACVLQD-----DRLFsgTLRDnicsfstQIDDNWL--------------IECARFAQIHDDIERMPM------ 617
Cdd:COG0444 82 KIrgreIQMIFQDpmtslNPVM--TVGD-------QIAEPLRihgglskaeareraIELLERVGLPDPERRLDRyphels 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1533513286 618 -GydtligelgeglsggQKQRIFIARAIYKKPSILFMDEATSSLDHTNEQYI----NDAIKSLNITRIVIAH 684
Cdd:COG0444 153 gG---------------MRQRVMIARALALEPKLLIADEPTTALDVTIQAQIlnllKDLQRELGLAILFITH 209
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
510-568 |
2.44e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 63.67 E-value: 2.44e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1533513286 510 RHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKL 568
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDL 76
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
492-599 |
2.70e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 66.53 E-value: 2.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISYKYDSyASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKLIAC 571
Cdd:PRK10522 323 LELRNVTFAYQD-NGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSA 401
|
90 100
....*....|....*....|....*...
gi 1533513286 572 VLQDDRLFSGTLRDNICSFSTQIDDNWL 599
Cdd:PRK10522 402 VFTDFHLFDQLLGPEGKPANPALVEKWL 429
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
492-684 |
3.00e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 64.07 E-value: 3.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISYKYD--SYASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKL- 568
Cdd:PRK11629 6 LQCDNLCKRYQegSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 569 ---IACVLQddrlFSGTLRDnicsFST--QIDDNWLIECARFAQIHDDIERM--PMGYDTLIGELGEGLSGGQKQRIFIA 641
Cdd:PRK11629 86 nqkLGFIYQ----FHHLLPD----FTAleNVAMPLLIGKKKPAEINSRALEMlaAVGLEHRANHRPSELSGGERQRVAIA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1533513286 642 RAIYKKPSILFMDEATSSLDHTNEQYINDAIKSLNITR----IVIAH 684
Cdd:PRK11629 158 RALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQgtafLVVTH 204
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
490-560 |
3.68e-11 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 64.02 E-value: 3.68e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1533513286 490 VSLSAKNISYKYDSYAsyTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKEL 560
Cdd:PRK13548 1 AMLEARNLSVRLGGRT--LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADW 69
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
487-685 |
6.56e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 65.34 E-value: 6.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 487 MCPVSLSAKNISYKYDSYASytLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPAS--EGNIFVDGIDIKELGV-N 563
Cdd:PRK13549 1 MMEYLLEMKNITKTFGGVKA--LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGEELQASNIrD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 564 NYQKLIACVLQDDRLFSG-TLRDNIcsF-------STQIDDNWL-IECAR-FAQIHDDIE-RMPMGYDTLigelgeglsg 632
Cdd:PRK13549 79 TERAGIAIIHQELALVKElSVLENI--FlgneitpGGIMDYDAMyLRAQKlLAQLKLDINpATPVGNLGL---------- 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1533513286 633 GQKQRIFIARAIYKKPSILFMDEATSSLDHTNEQYINDAIKSL---NITRIVIAHR 685
Cdd:PRK13549 147 GQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLkahGIACIYISHK 202
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
489-661 |
7.30e-11 |
|
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: 61.88 E-value: 7.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 489 PVSLSAKNISYKYDSYASyTLRHL-NIE--IQPGEHVAITGASGTGKTTLLKVLCGLFPAS--EGNIFVDGIDIKElgvn 563
Cdd:cd03232 1 GSVLTWKNLNYTVPVKGG-KRQLLnNISgyVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLDK---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 564 NYQKLIACVLQDDRLFsgtlrdnicSFSTqiddnwLIECARFAQIHDDIermpmgydtligelgeglSGGQKQRIFIARA 643
Cdd:cd03232 76 NFQRSTGYVEQQDVHS---------PNLT------VREALRFSALLRGL------------------SVEQRKRLTIGVE 122
|
170
....*....|....*...
gi 1533513286 644 IYKKPSILFMDEATSSLD 661
Cdd:cd03232 123 LAAKPSILFLDEPTSGLD 140
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
509-698 |
8.21e-11 |
|
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: 63.13 E-value: 8.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 509 LRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKL-IACVLQDDRLFSG-TLRDN 586
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLgIARTFQNPRLFPElTVLEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 587 I---------CSFSTQIDDNWLI------------ECARFAQIHDDIER----MPMGydtligelgeglsggQKQRIFIA 641
Cdd:COG0411 100 VlvaaharlgRGLLAALLRLPRArreereareraeELLERVGLADRADEpagnLSYG---------------QQRRLEIA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1533513286 642 RAIYKKPSILFMDEATSSLDHTNEQYINDAIKSLN----ITRIVIAHRKSTINS-ADRIIAL 698
Cdd:COG0411 165 RALATEPKLLLLDEPAAGLNPEETEELAELIRRLRdergITILLIEHDMDLVMGlADRIVVL 226
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
180-438 |
1.44e-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: 62.82 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 180 FFLSIIIESINLVMPVATQLVMD-----HAIPAND--SGLLTLICFGLVFFVALRTITGLIRSWTVLIMSSFINAQWQKG 252
Cdd:cd18554 5 IVIGLVRFGIPLLLPLILKYIVDdviqgSSLTLDEkvYKLFTIIGIMFFIFLILRPPVEYYRQYFAQWIANKILYDIRKD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 253 LLQHLLKLPLEYFERRKIGDIQSRFgsLNTLQET---FTTSVVGAIIDSIM-IIGLLIMLVLYGGwLTWFVILFTCLYVF 328
Cdd:cd18554 85 LFDHLQKLSLRYYANNRSGEIISRV--INDVEQTkdfITTGLMNIWLDMITiIIAICIMLVLNPK-LTFVSLVIFPFYIL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 329 IRVLTYNRYRQLSEESLIKDARANSFFMETLYGIATVKVQGLNKRREENWFNLEVDSINTGIKVSRLN-LFFGGINTLIa 407
Cdd:cd18554 162 AVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTRWNaKTFSAVNTIT- 240
|
250 260 270
....*....|....*....|....*....|.
gi 1533513286 408 TMEQILILWLGASLVISGNMTIGMFVAFSSY 438
Cdd:cd18554 241 DLAPLLVIGFAAYLVIEGNLTVGTLVAFVGY 271
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
494-661 |
1.57e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 63.93 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 494 AKNISYkydSYASYTL-RHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGiDIKelgvnnyqklIACV 572
Cdd:COG0488 1 LENLSK---SFGGRPLlDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-GLR----------IGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 573 LQDDRLFSG-TLRDNICS--------------FSTQIDDNwLIECARFAQIHDDIERMPmGYD------TLIGELGEGLS 631
Cdd:COG0488 67 PQEPPLDDDlTVLDTVLDgdaelraleaeleeLEAKLAEP-DEDLERLAELQEEFEALG-GWEaearaeEILSGLGFPEE 144
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1533513286 632 GG----------QKQRIFIARAIYKKPSILFMDEATSSLD 661
Cdd:COG0488 145 DLdrpvselsggWRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
492-698 |
1.63e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 62.51 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISYKYDSYASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLF---PASEGNIFVDGIDIKELGVNNYQKL 568
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 569 IACVLQ--DDRLFSGTLRDNIcSF---STQIDDNWLIECarfaqIHDDIERMPMGydTLIGELGEGLSGGQKQRIFIARA 643
Cdd:PRK13640 86 VGIVFQnpDNQFVGATVGDDV-AFgleNRAVPRPEMIKI-----VRDVLADVGML--DYIDSEPANLSGGQKQRVAIAGI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1533513286 644 IYKKPSILFMDEATSSLDHTNEQYINDAIKSL----NITRIVIAHRKSTINSADRIIAL 698
Cdd:PRK13640 158 LAVEPKIIILDESTSMLDPAGKEQILKLIRKLkkknNLTVISITHDIDEANMADQVLVL 216
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
492-661 |
1.99e-10 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 62.01 E-value: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISYKYDSY-------ASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKEL---G 561
Cdd:PRK10419 4 LNVSGLSHHYAHGglsgkhqHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 562 VNNYQKLIACVLQDdrlfsgtlrdNICSFSTQIDDNWLI-----------ECARFAQIHDDIERMPMGyDTLIGELGEGL 630
Cdd:PRK10419 84 RKAFRRDIQMVFQD----------SISAVNPRKTVREIIreplrhllsldKAERLARASEMLRAVDLD-DSVLDKRPPQL 152
|
170 180 190
....*....|....*....|....*....|.
gi 1533513286 631 SGGQKQRIFIARAIYKKPSILFMDEATSSLD 661
Cdd:PRK10419 153 SGGQLQRVCLARALAVEPKLLILDEAVSNLD 183
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
509-684 |
2.13e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 61.99 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 509 LRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGI------DIKELGVNNYQKLIACVLQDDRLFSG- 581
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNPFPHl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 582 TLRDNICS--FSTQIDDNWLI-----ECARFAQIHDDIermpmgYDTLiGELGEGLSGGQKQRIFIARAIYKKPSILFMD 654
Cdd:PRK14246 106 SIYDNIAYplKSHGIKEKREIkkiveECLRKVGLWKEV------YDRL-NSPASQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190
....*....|....*....|....*....|..
gi 1533513286 655 EATSSLDHTNEQYINDAIKSLN--ITRIVIAH 684
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLITELKneIAIVIVSH 210
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
516-679 |
2.23e-10 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 63.32 E-value: 2.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 516 IQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKLIACVLQDDRL-FSGTLRDNI------- 587
Cdd:PRK09536 26 VREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFEFDVRQVVemgrtph 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 588 -CSFSTQIDDNwliecarFAQIHDDIERMpmGYDTLIGELGEGLSGGQKQRIFIARAIYKKPSILFMDEATSSLDhtneq 666
Cdd:PRK09536 106 rSRFDTWTETD-------RAAVERAMERT--GVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLD----- 171
|
170
....*....|...
gi 1533513286 667 yINDAIKSLNITR 679
Cdd:PRK09536 172 -INHQVRTLELVR 183
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
190-438 |
2.95e-10 |
|
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: 61.88 E-value: 2.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 190 NLVMPVATQLVMDHAIPANDSG------LLTLICFGLVFFVALRTITGLIRSWTVLIMSSFINAQWQKGLLQHLLKLPLE 263
Cdd:cd18780 12 NLALPYFFGQVIDAVTNHSGSGgeealrALNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKRLFSAIIAQEIA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 264 YFERRKIGDIQSRFGS-LNTLQETFTTSVVGAIIDSIMIIGLLIMLvLYGGW-LTwfVILFTCL-YVFIRVLTYNRY-RQ 339
Cdd:cd18780 92 FFDVTRTGELLNRLSSdTQVLQNAVTVNLSMLLRYLVQIIGGLVFM-FTTSWkLT--LVMLSVVpPLSIGAVIYGKYvRK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 340 LSEESLIKDARANSFFMETLYGIATVKVQGlNKRREENWFNLEVD-SINTGIKVSRLNLFFGGINTLIATMEQILILWLG 418
Cdd:cd18780 169 LSKKFQDALAAASTVAEESISNIRTVRSFA-KETKEVSRYSEKINeSYLLGKKLARASGGFNGFMGAAAQLAIVLVLWYG 247
|
250 260
....*....|....*....|
gi 1533513286 419 ASLVISGNMTIGMFVAFSSY 438
Cdd:cd18780 248 GRLVIDGELTTGLLTSFLLY 267
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
511-661 |
3.36e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 62.20 E-value: 3.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 511 HLNIEIQ-PGEHV-AITGASGTGKTTLLKVLCGLFPASEGNIFVDG---IDIkELGVN--NYQKLIACVLQDDRLFSG-T 582
Cdd:PRK11144 14 CLTVNLTlPAQGItAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlFDA-EKGIClpPEKRRIGYVFQDARLFPHyK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 583 LRDNICSFSTQIDDnwliecARFAQIHD--DIE----RMPMgydTLigelgeglSGGQKQRIFIARAIYKKPSILFMDEA 656
Cdd:PRK11144 93 VRGNLRYGMAKSMV------AQFDKIVAllGIEplldRYPG---SL--------SGGEKQRVAIGRALLTAPELLLMDEP 155
|
....*
gi 1533513286 657 TSSLD 661
Cdd:PRK11144 156 LASLD 160
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
509-554 |
3.41e-10 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 60.87 E-value: 3.41e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1533513286 509 LRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDG 554
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG 87
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
492-699 |
4.32e-10 |
|
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: 59.99 E-value: 4.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISykyDSYASYT-LRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNN------ 564
Cdd:cd03269 1 LEVENVT---KRFGRVTaLDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRigylpe 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 565 ----YQKLiacVLQDDRLFSGTLRD-NICSFSTQIDDnWL--IECARFAQIHddIERMPMGydtligelgeglsggQKQR 637
Cdd:cd03269 78 erglYPKM---KVIDQLVYLAQLKGlKKEEARRRIDE-WLerLELSEYANKR--VEELSKG---------------NQQK 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1533513286 638 IFIARAIYKKPSILFMDEATSSLDHTNEQYINDAIKSL---NITRIVIAHRKSTINS-ADRIIALQ 699
Cdd:cd03269 137 VQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELaraGKTVILSTHQMELVEElCDRVLLLN 202
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
492-657 |
6.08e-10 |
|
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: 59.85 E-value: 6.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISYKYDsyASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELgvNNYQKL--- 568
Cdd:TIGR03410 1 LEVSNLNVYYG--QSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKL--PPHERArag 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 569 IACVLQDDRLFSG-TLRDNI-------CSFSTQIDDNWLiecARFAQIHDDIERMpmGYDtligelgegLSGGQKQRIFI 640
Cdd:TIGR03410 77 IAYVPQGREIFPRlTVEENLltglaalPRRSRKIPDEIY---ELFPVLKEMLGRR--GGD---------LSGGQQQQLAI 142
|
170
....*....|....*..
gi 1533513286 641 ARAIYKKPSILFMDEAT 657
Cdd:TIGR03410 143 ARALVTRPKLLLLDEPT 159
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
495-684 |
6.94e-10 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 60.11 E-value: 6.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 495 KNISYKYDsyASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNnyQKLI----A 570
Cdd:PRK09493 5 KNVSKHFG--PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVD--ERLIrqeaG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 571 CVLQDDRLFSG-TLRDNICsfstqiddnwliecarFAQIH------DDIERMPM------GYDTLIGELGEGLSGGQKQR 637
Cdd:PRK09493 81 MVFQQFYLFPHlTALENVM----------------FGPLRvrgaskEEAEKQARellakvGLAERAHHYPSELSGGQQQR 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1533513286 638 IFIARAIYKKPSILFMDEATSSLDHTNEQYINDAIKSL---NITRIVIAH 684
Cdd:PRK09493 145 VAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLaeeGMTMVIVTH 194
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
509-661 |
9.66e-10 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 60.87 E-value: 9.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 509 LRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQklIACVLQDDRLFSG-TLRDNI 587
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRK--VGFVFQHYALFRHmTVFDNI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 588 cSFS-------------------TQIDDnwLIECARFAqihddiERMPmgydtligelgEGLSGGQKQRIFIARAIYKKP 648
Cdd:PRK10851 96 -AFGltvlprrerpnaaaikakvTQLLE--MVQLAHLA------DRYP-----------AQLSGGQKQRVALARALAVEP 155
|
170
....*....|...
gi 1533513286 649 SILFMDEATSSLD 661
Cdd:PRK10851 156 QILLLDEPFGALD 168
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
509-661 |
1.28e-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: 59.02 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 509 LRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNyqkliACVLQDDRLFSG-TLRDNI 587
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDR-----MVVFQNYSLLPWlTVRENI 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1533513286 588 CSFSTQIDDNwLIECARFAQIHDDIERMpmGYDTLIGELGEGLSGGQKQRIFIARAIYKKPSILFMDEATSSLD 661
Cdd:TIGR01184 76 ALAVDRVLPD-LSKSERRAIVEEHIALV--GLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALD 146
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
509-689 |
1.34e-09 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 58.82 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 509 LRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFP---ASEGNIFVDGidiKELGVNNYQKLIACVLQDDRLFSG-TLR 584
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNG---QPRKPDQFQKCVAYVRQDDILLPGlTVR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 585 DNIcSFSTQIDdnwLIECARFAQIH--DDIERMPMGYDTLIGELGEGLSGG-QKQRIFIARAIYKKPSILFMDEATSSLd 661
Cdd:cd03234 100 ETL-TYTAILR---LPRKSSDAIRKkrVEDVLLRDLALTRIGGNLVKGISGgERRRVSIAVQLLWDPKVLILDEPTSGL- 174
|
170 180 190
....*....|....*....|....*....|
gi 1533513286 662 htneqyinDAIKSLNITRIV--IAHRKSTI 689
Cdd:cd03234 175 --------DSFTALNLVSTLsqLARRNRIV 196
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
510-675 |
1.37e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 61.22 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 510 RHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKLIACVLQDDRLFSG-----TLR 584
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVYLPEDRQSSGlyldaPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 585 DNICSFSTQIDDNWL---IECARFAQIHDDI------ERMPMGydTLigelgeglSGGQKQRIFIARAIYKKPSILFMDE 655
Cdd:PRK15439 360 WNVCALTHNRRGFWIkpaRENAVLERYRRALnikfnhAEQAAR--TL--------SGGNQQKVLIAKCLEASPQLLIVDE 429
|
170 180
....*....|....*....|
gi 1533513286 656 ATSSLDHTNEQYINDAIKSL 675
Cdd:PRK15439 430 PTRGVDVSARNDIYQLIRSI 449
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
504-666 |
1.50e-09 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 59.33 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 504 YASY----TLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIK----ELGVnnyqkliacVLQD 575
Cdd:PRK11248 8 YADYggkpALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEgpgaERGV---------VFQN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 576 DRLFS-GTLRDNIcSFSTQ---IDDNWLIECARFAQIHDDIErmpmGYDtliGELGEGLSGGQKQRIFIARAIYKKPSIL 651
Cdd:PRK11248 79 EGLLPwRNVQDNV-AFGLQlagVEKMQRLEIAHQMLKKVGLE----GAE---KRYIWQLSGGQRQRVGIARALAANPQLL 150
|
170
....*....|....*.
gi 1533513286 652 FMDEATSSLD-HTNEQ 666
Cdd:PRK11248 151 LLDEPFGALDaFTREQ 166
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
456-684 |
1.54e-09 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 60.97 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 456 LQIMSLHNERVSDIALTEVTPFKDDIpvkndmcpvsLSAKNISYKYDSYASYTLR---HLNIEIQPGEHVAITGASGTGK 532
Cdd:TIGR03269 254 DEVVAVFMEGVSEVEKECEVEVGEPI----------IKVRNVSKRYISVDRGVVKavdNVSLEVKEGEIFGIVGTSGAGK 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 533 TTLLKVLCGLFPASEGNIFV----DGIDIKELGVNN---YQKLIACVLQDDRLFS-GTLRDNIC-SFSTQIDDnwliECA 603
Cdd:TIGR03269 324 TTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPDGrgrAKRYIGILHQEYDLYPhRTVLDNLTeAIGLELPD----ELA 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 604 RFAQIH-------DD------IERMPmgyDTLigelgeglSGGQKQRIFIARAIYKKPSILFMDEATSSLDHTNEQYIND 670
Cdd:TIGR03269 400 RMKAVItlkmvgfDEekaeeiLDKYP---DEL--------SEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTH 468
|
250
....*....|....*...
gi 1533513286 671 AI----KSLNITRIVIAH 684
Cdd:TIGR03269 469 SIlkarEEMEQTFIIVSH 486
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
490-684 |
1.60e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 59.41 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 490 VSLSAKNISYKYDSYASytLRHLNIEIQPGEHVAITGASGTGKTTLLKV---LCGLFPA--SEGNIFVDGIDIKELGVN- 563
Cdd:PRK14243 9 TVLRTENLNVYYGSFLA--VKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIPGfrVEGKVTFHGKNLYAPDVDp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 564 -NYQKLIACVLQDDRLFSGTLRDNIcSFSTQI-----DDNWLIECA-RFAQIHDDIErmpmgyDTLiGELGEGLSGGQKQ 636
Cdd:PRK14243 87 vEVRRRIGMVFQKPNPFPKSIYDNI-AYGARIngykgDMDELVERSlRQAALWDEVK------DKL-KQSGLSLSGGQQQ 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1533513286 637 RIFIARAIYKKPSILFMDEATSSLDHTNEQYINDAIKSL--NITRIVIAH 684
Cdd:PRK14243 159 RLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELkeQYTIIIVTH 208
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
491-684 |
1.61e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 59.37 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 491 SLSAKNISYKYDS---YASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVN---- 563
Cdd:PRK13649 2 GINLQNVSYTYQAgtpFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNkdik 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 564 NYQKLIACVLQ--DDRLFSGTLRDNIcSFSTQiddNWLIECARFAQIHDDIERMPMGYDTLIGELGEGLSGGQKQRIFIA 641
Cdd:PRK13649 82 QIRKKVGLVFQfpESQLFEETVLKDV-AFGPQ---NFGVSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1533513286 642 RAIYKKPSILFMDEATSSLDHTNEQYINDAIKSLN---ITRIVIAH 684
Cdd:PRK13649 158 GILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHqsgMTIVLVTH 203
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
489-700 |
2.13e-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: 57.44 E-value: 2.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 489 PVSLSAKNISykydsyASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKL 568
Cdd:cd03215 2 EPVLEVRGLS------VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 569 -IACVLqDDRLFSG-----TLRDNI---CSFS--TQiddnwliecarfaqihddiermpmgydtligelgeglsggqkQR 637
Cdd:cd03215 76 gIAYVP-EDRKREGlvldlSVAENIalsSLLSggNQ------------------------------------------QK 112
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1533513286 638 IFIARAIYKKPSILFMDEATSSLDHTNEQYINDAIKSL---NITRIVIahrkST-----INSADRIIALQE 700
Cdd:cd03215 113 VVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELadaGKAVLLI----SSeldelLGLCDRILVMYE 179
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
509-684 |
2.27e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 58.77 E-value: 2.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 509 LRHLNIEIQPGEHVAITGASGTGKTTLLKV---LCGLFPAS--EGNIFVDGIDIKELGVNNYQKLIACVLQ-DDRLFSGT 582
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVfnrLIELYPEArvSGEVYLDGQDIFKMDVIELRRRVQMVFQiPNPIPNLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 583 LRDNIcsfSTQIDDNWLIECAR--FAQIHDDIERMPMgYDTL---IGELGEGLSGGQKQRIFIARAIYKKPSILFMDEAT 657
Cdd:PRK14247 99 IFENV---ALGLKLNRLVKSKKelQERVRWALEKAQL-WDEVkdrLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPT 174
|
170 180
....*....|....*....|....*....
gi 1533513286 658 SSLDHTNEQYINDAIKSL--NITRIVIAH 684
Cdd:PRK14247 175 ANLDPENTAKIESLFLELkkDMTIVLVTH 203
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
509-700 |
2.35e-09 |
|
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: 60.47 E-value: 2.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 509 LRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPaSEGNIFVDGIDIKELGVNNYQKL---IACVLQDDrlFSgtlrd 585
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRALRPLrrrMQVVFQDP--FG----- 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 586 nicSFS-----TQIddnwLIECARFAQIH---------------------DDIERMPM----GydtligelgeglsggQK 635
Cdd:COG4172 374 ---SLSprmtvGQI----IAEGLRVHGPGlsaaerrarvaealeevgldpAARHRYPHefsgG---------------QR 431
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 636 QRIFIARAIYKKPSILFMDEATSSLDHTNEQYINDAIKSL----NITRIVIAHRKSTINS-ADRIIALQE 700
Cdd:COG4172 432 QRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLqrehGLAYLFISHDLAVVRAlAHRVMVMKD 501
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
509-700 |
2.73e-09 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 58.49 E-value: 2.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 509 LRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLF---PASEGNIFVDGIDIKELG-----VNNYQKLIACVLQDDRLFS 580
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQREGrlardIRKSRANTGYIFQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 581 G-TLRDNICSFSTQIDDNWLIECARFAQIHDD-----IERMPMGYdtLIGELGEGLSGGQKQRIFIARAIYKKPSILFMD 654
Cdd:PRK09984 100 RlSVLENVLIGALGSTPFWRTCFSWFTREQKQralqaLTRVGMVH--FAHQRVSTLSGGQQQRVAIARALMQQAKVILAD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1533513286 655 EATSSLDHTNEQYINDAIKSLN----ITRIVIAHR-KSTINSADRIIALQE 700
Cdd:PRK09984 178 EPIASLDPESARIVMDTLRDINqndgITVVVTLHQvDYALRYCERIVALRQ 228
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
495-700 |
3.22e-09 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 58.17 E-value: 3.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 495 KNISYKYDSYAsyTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKLIACVLQ 574
Cdd:COG4604 5 KNVSKRYGGKV--VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 575 DD----RLfsgTLRDnicsfstqiddnwLIECARF------------AQIHDDIERMPMG-----Y-DTLigelgeglSG 632
Cdd:COG4604 83 ENhinsRL---TVRE-------------LVAFGRFpyskgrltaedrEIIDEAIAYLDLEdladrYlDEL--------SG 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1533513286 633 GQKQRIFIARAIYKKPSILFMDEATSSLD--HTNE--QYINDAIKSLNITRIVIAHrksTINSA----DRIIALQE 700
Cdd:COG4604 139 GQRQRAFIAMVLAQDTDYVLLDEPLNNLDmkHSVQmmKLLRRLADELGKTVVIVLH---DINFAscyaDHIVAMKD 211
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
181-438 |
3.24e-09 |
|
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: 58.56 E-value: 3.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 181 FLSIIIESI-NLVMPVATQLVMDHAIPANDSGLLTLICFGLVFFVALRTITGLIRSWTVLIMSSFI-----NAQWQKgll 254
Cdd:cd18548 5 PLFKLLEVLlELLLPTLMADIIDEGIANGDLSYILRTGLLMLLLALLGLIAGILAGYFAAKASQGFgrdlrKDLFEK--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 255 qhllklpLEYFERRKIGDIQSrfGSL--------NTLQETFTTSVVGAIIDSIMIIGLLIMLVLYGGWLTW-----FVIL 321
Cdd:cd18548 82 -------IQSFSFAEIDKFGT--SSLitrltndvTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALillvaIPIL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 322 FTCLYVFIRvLTYNRYRQLsEESLikDaRANSFFMETLYGIATVKVqgLNK-RREENWFNLEVDSI-NTGIKVSRLNLFF 399
Cdd:cd18548 153 ALVVFLIMK-KAIPLFKKV-QKKL--D-RLNRVVRENLTGIRVIRA--FNReDYEEERFDKANDDLtDTSLKAGRLMALL 225
|
250 260 270
....*....|....*....|....*....|....*....
gi 1533513286 400 GGINTLIATMEQILILWLGASLVISGNMTIGMFVAFSSY 438
Cdd:cd18548 226 NPLMMLIMNLAIVAILWFGGHLINAGSLQVGDLVAFINY 264
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
492-699 |
3.28e-09 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 59.82 E-value: 3.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISYKYDSYAsyTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGL--FPASEGNIF------------------ 551
Cdd:TIGR03269 1 IEVKNLTKKFDGKE--VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpskv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 552 ---------------VDGIDIKELGVNNYQKLIACVLQddRLFS----GTLRDNICSFSTQIDDNWLIECARFAQIhddI 612
Cdd:TIGR03269 79 gepcpvcggtlepeeVDFWNLSDKLRRRIRKRIAIMLQ--RTFAlygdDTVLDNVLEALEEIGYEGKEAVGRAVDL---I 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 613 ERMPMGYDtlIGELGEGLSGGQKQRIFIARAIYKKPSILFMDEATSSLDHTNEQYINDAIKSL----NITRIVIAHRKST 688
Cdd:TIGR03269 154 EMVQLSHR--ITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvkasGISMVLTSHWPEV 231
|
250
....*....|..
gi 1533513286 689 INS-ADRIIALQ 699
Cdd:TIGR03269 232 IEDlSDKAIWLE 243
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
490-700 |
3.53e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 58.64 E-value: 3.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 490 VSLSAKNISYKYDS---YASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDI----KELGV 562
Cdd:PRK13646 1 MTIRFDNVSYTYQKgtpYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 563 NNYQKLIACVLQ--DDRLFSGTLRDNIC----SFSTQIDdnwliecarfaQIHDDIER--MPMGYD-TLIGELGEGLSGG 633
Cdd:PRK13646 81 RPVRKRIGMVFQfpESQLFEDTVEREIIfgpkNFKMNLD-----------EVKNYAHRllMDLGFSrDVMSQSPFQMSGG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1533513286 634 QKQRIFIARAIYKKPSILFMDEATSSLDHTNEQYINDAIKSL----NITRIVIAHRKSTINS-ADRIIALQE 700
Cdd:PRK13646 150 QMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLqtdeNKTIILVSHDMNEVARyADEVIVMKE 221
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
492-701 |
3.63e-09 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 59.69 E-value: 3.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISYKYDSYAsyTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIfvdgidikELGVN---NY--Q 566
Cdd:COG0488 316 LELEGLSKSYGDKT--LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV--------KLGETvkiGYfdQ 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 567 KLIAcvLQDDRlfsgTLRDNICSFSTQIDD----NWLiecARF----AQIHDDIERMPMGydtligelgeglsggQKQRI 638
Cdd:COG0488 386 HQEE--LDPDK----TVLDELRDGAPGGTEqevrGYL---GRFlfsgDDAFKPVGVLSGG---------------EKARL 441
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1533513286 639 FIARAIYKKPSILFMDEATSSLD-HTNEQyINDAIKSLNITRIVIAHRKSTINS-ADRIIALQEN 701
Cdd:COG0488 442 ALAKLLLSPPNVLLLDEPTNHLDiETLEA-LEEALDDFPGTVLLVSHDRYFLDRvATRILEFEDG 505
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
495-700 |
4.25e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 58.21 E-value: 4.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 495 KNISYKYDSyASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKLIACVLQ 574
Cdd:PRK13647 8 EDLHFRYKD-GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 575 --DDRLFSGTLRDNIC------SFSTQIDDNWLIECARFAQIHDDIERMP--MGYDtligelgeglsggQKQRIFIARAI 644
Cdd:PRK13647 87 dpDDQVFSSTVWDDVAfgpvnmGLDKDEVERRVEEALKAVRMWDFRDKPPyhLSYG-------------QKKRVAIAGVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 645 YKKPSILFMDEATSSLDHTNEQYINDAIKSLN---ITRIVIAHRKSTINS-ADRIIALQE 700
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDPRGQETLMEILDRLHnqgKTVIVATHDVDLAAEwADQVIVLKE 213
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
482-700 |
4.28e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 58.71 E-value: 4.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 482 PVKNDmcpVSLSAKNISYKYDSYASYTLRHLN---IEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNI----FVDG 554
Cdd:PRK13631 15 PLSDD---IILRVKNLYCVFDEKQENELVALNnisYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 555 IDIKELGVNNY------------QKLIACVLQ--DDRLFSGTLRDNIcSFSTQIDDNWLIECARFAQIHddIERMPMGYD 620
Cdd:PRK13631 92 DKKNNHELITNpyskkiknfkelRRRVSMVFQfpEYQLFKDTIEKDI-MFGPVALGVKKSEAKKLAKFY--LNKMGLDDS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 621 TLiGELGEGLSGGQKQRIFIARAIYKKPSILFMDEATSSLDHTNEQYINDAI---KSLNITRIVIAHR-KSTINSADRII 696
Cdd:PRK13631 169 YL-ERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLIldaKANNKTVFVITHTmEHVLEVADEVI 247
|
....
gi 1533513286 697 ALQE 700
Cdd:PRK13631 248 VMDK 251
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
509-696 |
4.39e-09 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 57.84 E-value: 4.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 509 LRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDI---KELG-----VNNYQKLIACVLQDDRLFS 580
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtaRSLSqqkglIRQLRQHVGFVFQNFNLFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 581 G-TLRDNICSFSTQI---DDNWLIECAR--FAQI-----HDDIERMPMGydtligelgeglsgGQKQRIFIARAIYKKPS 649
Cdd:PRK11264 99 HrTVLENIIEGPVIVkgePKEEATARARelLAKVglagkETSYPRRLSG--------------GQQQRVAIARALAMRPE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1533513286 650 ILFMDEATSSLDHTNEQYINDAIKSL---NITRIVIAHRKS-TINSADRII 696
Cdd:PRK11264 165 VILFDEPTSALDPELVGEVLNTIRQLaqeKRTMVIVTHEMSfARDVADRAI 215
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
492-676 |
4.63e-09 |
|
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: 57.55 E-value: 4.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISYKYDSyaSYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKLIAC 571
Cdd:cd03218 1 LRAENLSKRYGK--RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 572 VL-QDDRLFSG-TLRDNI-CSFSTQIDDNwliecarfAQIHDDIERM--PMGYDTLIGELGEGLSGGQKQRIFIARAIYK 646
Cdd:cd03218 79 YLpQEASIFRKlTVEENIlAVLEIRGLSK--------KEREEKLEELleEFHITHLRKSKASSLSGGERRRVEIARALAT 150
|
170 180 190
....*....|....*....|....*....|
gi 1533513286 647 KPSILFMDEATSSLDHTNEQYINDAIKSLN 676
Cdd:cd03218 151 NPKFLLLDEPFAGVDPIAVQDIQKIIKILK 180
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
492-695 |
6.41e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 57.51 E-value: 6.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISYKYDSyASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKLIAC 571
Cdd:PRK13652 4 IETRDLCYSYSG-SKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 572 VLQ--DDRLFSGTLRDNICSFSTqiddNWLIECARFAQIHDDIERMpMGYDTLIGELGEGLSGGQKQRIFIARAIYKKPS 649
Cdd:PRK13652 83 VFQnpDDQIFSPTVEQDIAFGPI----NLGLDEETVAHRVSSALHM-LGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1533513286 650 ILFMDEATSSLDHTNEQ----YINDAIKSLNITRIVIAHRKSTINS-ADRI 695
Cdd:PRK13652 158 VLVLDEPTAGLDPQGVKelidFLNDLPETYGMTVIFSTHQLDLVPEmADYI 208
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
515-682 |
1.00e-08 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 58.52 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 515 EIQPGEHVAITGASGTGKTTLLKVLCGLFPAS---EGNIFVDG--IDIKElgvnnyQKLIACVLQDDRLFSGTL--RDNI 587
Cdd:TIGR00955 47 VAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGmpIDAKE------MRAISAYVQQDDLFIPTLtvREHL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 588 cSFSTQID-DNWLIECARFAQIHDDIERMPMG--YDTLIGELGEGLSGG--QKQRIFIARAIYKKPSILFMDEATSSLDH 662
Cdd:TIGR00955 121 -MFQAHLRmPRRVTKKEKRERVDEVLQALGLRkcANTRIGVPGRVKGLSggERKRLAFASELLTDPPLLFCDEPTSGLDS 199
|
170 180
....*....|....*....|.
gi 1533513286 663 TNEQYINDAIKSL-NITRIVI 682
Cdd:TIGR00955 200 FMAYSVVQVLKGLaQKGKTII 220
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
506-699 |
1.24e-08 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 57.74 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 506 SYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNY----QKLIACVLQDDRLFSG 581
Cdd:PRK10070 41 SLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrRKKIAMVFQSFALMPH 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 582 -TLRDNIcSFSTQIDDnwlIECARFAQIHDDIERMpMGYDTLIGELGEGLSGGQKQRIFIARAIYKKPSILFMDEATSSL 660
Cdd:PRK10070 121 mTVLDNT-AFGMELAG---INAEERREKALDALRQ-VGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSAL 195
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1533513286 661 DHTNEQYINDAIKSLNI----TRIVIAHR-KSTINSADRIIALQ 699
Cdd:PRK10070 196 DPLIRTEMQDELVKLQAkhqrTIVFISHDlDEAMRIGDRIAIMQ 239
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
507-684 |
1.26e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 58.18 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 507 YTLRHLNIEIQPGEHVAITGASGTGKTT----LLKVLcglfpASEGNIFVDGIDIKELGVNN---YQKLIACVLQDDrlf 579
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRRQllpVRHRIQVVFQDP--- 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 580 SGTL--RDN---ICSFSTQIDDNWLIECARFAQIHDDIERMPMGYDTLiGELGEGLSGGQKQRIFIARAIYKKPSILFMD 654
Cdd:PRK15134 372 NSSLnpRLNvlqIIEEGLRVHQPTLSAAQREQQVIAVMEEVGLDPETR-HRYPAEFSGGQRQRIAIARALILKPSLIILD 450
|
170 180 190
....*....|....*....|....*....|....
gi 1533513286 655 EATSSLDHTNEQYINDAIKSLNITR----IVIAH 684
Cdd:PRK15134 451 EPTSSLDKTVQAQILALLKSLQQKHqlayLFISH 484
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
491-684 |
1.37e-08 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 56.17 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 491 SLSAKNISYKYDSYASytLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNI--------FVDGIDIKElgV 562
Cdd:COG4161 2 SIQLKNINCFYGSHQA--LFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLniaghqfdFSQKPSEKA--I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 563 NNYQKLIACVLQDDRLFSG-TLRDNicsfstqiddnwLIEC-----------ARFA--------QIHDDIERMPMgydtl 622
Cdd:COG4161 78 RLLRQKVGMVFQQYNLWPHlTVMEN------------LIEApckvlglskeqAREKamkllarlRLTDKADRFPL----- 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1533513286 623 igelgeGLSGGQKQRIFIARAIYKKPSILFMDEATSSLDH--TNEqyINDAIKSLN---ITRIVIAH 684
Cdd:COG4161 141 ------HLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPeiTAQ--VVEIIRELSqtgITQVIVTH 199
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
211-450 |
1.47e-08 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); 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: 350034 [Multi-domain] Cd Length: 289 Bit Score: 56.58 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 211 GLLTLICFGLVFFVALR------TITGLIRSWTVLIMSSFINAQwqkgllqhllklpLEYFERRKIGDIQSRFGSLNTLQ 284
Cdd:cd18590 40 GLMCLFSLGSSLSAGLRgglfmcTLSRLNLRLRHQLFSSLVQQD-------------IGFFEKTKTGDLTSRLSTDTTLM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 285 ETFTTSVVGAIIDS-IMIIGLLIMLVlyggWLTWFVILFTCLYVFIRVLT---YN-RYRQLSEESLIKDARANSFFMETL 359
Cdd:cd18590 107 SRSVALNANVLLRSlVKTLGMLGFML----SLSWQLTLLTLIEMPLTAIAqkvYNtYHQKLSQAVQDSIAKAGELAREAV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 360 YGIATVKVQGLNKRREENWFNLEVDSINTGIKVSRLNLFFGGINTLIATMEQILILWLGASLVISGNMTIGMFVAFSSYR 439
Cdd:cd18590 183 SSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLYCGRQLIQSGHLTTGSLVSFILYQ 262
|
250
....*....|.
gi 1533513286 440 GQFSDRIASFI 450
Cdd:cd18590 263 KNLGSYVRTLV 273
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
509-658 |
1.55e-08 |
|
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: 55.62 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 509 LRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGID--IKELGVNnyqkliacvLQDDrlFSGtlRDN 586
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVssLLGLGGG---------FNPE--LTG--REN 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1533513286 587 I---CSF---STQIDDNWLIECARFAQIHDDIErMPMG-YDTligelgeglsgGQKQRIFIARAIYKKPSILFMDEATS 658
Cdd:cd03220 105 IylnGRLlglSRKEIDEKIDEIIEFSELGDFID-LPVKtYSS-----------GMKARLAFAIATALEPDILLIDEVLA 171
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
489-587 |
2.53e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 56.96 E-value: 2.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 489 PVSLSAKNISYKyDSYASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKL 568
Cdd:COG3845 255 EVVLEVENLSVR-DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRL 333
|
90 100
....*....|....*....|....*
gi 1533513286 569 -IACVlQDDRLFSG-----TLRDNI 587
Cdd:COG3845 334 gVAYI-PEDRLGRGlvpdmSVAENL 357
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
509-557 |
2.62e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 54.88 E-value: 2.62e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1533513286 509 LRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDI 557
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI 66
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
487-660 |
2.76e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 56.96 E-value: 2.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 487 MCPVSLSAKNISYKYDS-YAsytLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDG--IDIK----- 558
Cdd:COG3845 1 MMPPALELRGITKRFGGvVA---NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpVRIRsprda 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 559 -ELGvnnyqklIACVLQDDRLFSG-TLRDNIC-----SFSTQIDDNWLIE-----CARF-------AQIHDdierMPMGy 619
Cdd:COG3845 78 iALG-------IGMVHQHFMLVPNlTVAENIVlglepTKGGRLDRKAARArirelSERYgldvdpdAKVED----LSVG- 145
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1533513286 620 dtligelgeglsggQKQRIFIARAIYKKPSILFMDEATSSL 660
Cdd:COG3845 146 --------------EQQRVEILKALYRGARILILDEPTAVL 172
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
509-563 |
2.79e-08 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 54.46 E-value: 2.79e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1533513286 509 LRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGlFPASE---GNIFVDGIDIKELGVN 563
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG-HPKYEvteGEILFKGEDITDLPPE 72
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
487-699 |
2.84e-08 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 56.19 E-value: 2.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 487 MCPVSLsaKNISYKYDSYAsyTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKElgVNNYQ 566
Cdd:PRK11000 1 MASVTL--RNVTKAYGDVV--ISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMND--VPPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 567 KLIACVLQDDRLFSG-TLRDNIcSF--------STQIDDNwLIECARFAQIHDDIERMPmgydtligelgEGLSGGQKQR 637
Cdd:PRK11000 75 RGVGMVFQSYALYPHlSVAENM-SFglklagakKEEINQR-VNQVAEVLQLAHLLDRKP-----------KALSGGQRQR 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1533513286 638 IFIARAIYKKPSILFMDEATSSLDHTNEQYINDAI----KSLNITRIVIAHRK-STINSADRIIALQ 699
Cdd:PRK11000 142 VAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEIsrlhKRLGRTMIYVTHDQvEAMTLADKIVVLD 208
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
492-700 |
3.29e-08 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 55.07 E-value: 3.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISYKYDSYAsyTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELgvnnyQKLIAC 571
Cdd:PRK11247 13 LLLNAVSKRYGERT--VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA-----REDTRL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 572 VLQDDRLFS-GTLRDNIcsfSTQIDDNWLiecarfAQIHDDIErmPMGYDTLIGELGEGLSGGQKQRIFIARAIYKKPSI 650
Cdd:PRK11247 86 MFQDARLLPwKKVIDNV---GLGLKGQWR------DAALQALA--AVGLADRANEWPAALSGGQKQRVALARALIHRPGL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1533513286 651 LFMDEATSSLDHTNEQYINDAIKSL----NITRIVIAHRKS-TINSADRIIALQE 700
Cdd:PRK11247 155 LLLDEPLGALDALTRIEMQDLIESLwqqhGFTVLLVTHDVSeAVAMADRVLLIEE 209
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
518-689 |
3.51e-08 |
|
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: 53.15 E-value: 3.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 518 PGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVdgidikelgvnnyqkliacvlqddrlfsgtlrdnicsfstqIDDN 597
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY-----------------------------------------IDGE 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 598 WLIECARFAQIHDDIERMPMGYDTligelgeglsgGQKQRIFIARAIYKKPSILFMDEATSSLDHTNEQYINDAIKSLNI 677
Cdd:smart00382 40 DILEEVLDQLLLIIVGGKKASGSG-----------ELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLL 108
|
170
....*....|..
gi 1533513286 678 TRIVIAHRKSTI 689
Cdd:smart00382 109 LLLKSEKNLTVI 120
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
509-696 |
3.58e-08 |
|
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: 54.65 E-value: 3.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 509 LRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGvNNYQKLIACVL-QDDRL-FSGTLRDn 586
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRR-KKFLRRIGVVFgQKTQLwWDLPVID- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 587 icSFSTqIDDNWLIECARFAQIHDDIERMpMGYDTLIGELGEGLSGGQKQRIFIARAIYKKPSILFMDEATSSLDHTNEQ 666
Cdd:cd03267 115 --SFYL-LAAIYDLPPARFKKRLDELSEL-LDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQE 190
|
170 180 190
....*....|....*....|....*....|....*
gi 1533513286 667 YINDAIKSLN----ITRIVIAHRKSTINS-ADRII 696
Cdd:cd03267 191 NIRNFLKEYNrergTTVLLTSHYMKDIEAlARRVL 225
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
496-661 |
4.13e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 55.12 E-value: 4.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 496 NISYKYDS-YASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDI----KELGVNNYQKLIA 570
Cdd:PRK13643 8 NYTYQPNSpFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVsstsKQKEIKPVRKKVG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 571 CVLQ--DDRLFSGTLRDNIcSFSTQiddNWLIECARFAQIHDDIERMPMGYDTLIGELGEGLSGGQKQRIFIARAIYKKP 648
Cdd:PRK13643 88 VVFQfpESQLFEETVLKDV-AFGPQ---NFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEP 163
|
170
....*....|...
gi 1533513286 649 SILFMDEATSSLD 661
Cdd:PRK13643 164 EVLVLDEPTAGLD 176
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
491-684 |
4.35e-08 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 54.64 E-value: 4.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 491 SLSAKNISYKYDSyaSYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNI--------FVDGIDIKElgV 562
Cdd:PRK11124 2 SIQLNGINCFYGA--HQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLniagnhfdFSKTPSDKA--I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 563 NNYQKLIACVLQDDRLFSG-TLRDN-------ICSFSTQIDDNWLIECARFAQIHDDIERMPMgydtligelgeGLSGGQ 634
Cdd:PRK11124 78 RELRRNVGMVFQQYNLWPHlTVQQNlieapcrVLGLSKDQALARAEKLLERLRLKPYADRFPL-----------HLSGGQ 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1533513286 635 KQRIFIARAIYKKPSILFMDEATSSLDHTNEQYINDAIKSL---NITRIVIAH 684
Cdd:PRK11124 147 QQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELaetGITQVIVTH 199
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
492-700 |
4.49e-08 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 56.27 E-value: 4.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISYKYDSYASYT--LRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKL- 568
Cdd:PRK10535 5 LELKDIRRSYPSGEEQVevLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 569 ---IACVLQDDRLFSG-TLRDN--ICSFSTQIDDNwliecARFAQIHDDIERmpMGYDTLIGELGEGLSGGQKQRIFIAR 642
Cdd:PRK10535 85 rehFGFIFQRYHLLSHlTAAQNveVPAVYAGLERK-----QRLLRAQELLQR--LGLEDRVEYQPSQLSGGQQQRVSIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1533513286 643 AIYKKPSILFMDEATSSLD-HTNEQYINdAIKSLNI---TRIVIAHRKSTINSADRIIALQE 700
Cdd:PRK10535 158 ALMNGGQVILADEPTGALDsHSGEEVMA-ILHQLRDrghTVIIVTHDPQVAAQAERVIEIRD 218
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
504-700 |
5.00e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 54.61 E-value: 5.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 504 YASYTLRH-LNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKLIACVLQDdrlfsgt 582
Cdd:PRK10253 17 YGKYTVAEnLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQN------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 583 lrdniCSFSTQIDDNWLIECARF----------AQIHDDIERM--PMGYDTLIGELGEGLSGGQKQRIFIARAIYKKPSI 650
Cdd:PRK10253 90 -----ATTPGDITVQELVARGRYphqplftrwrKEDEEAVTKAmqATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAI 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1533513286 651 LFMDEATSSLDHTNEQYINDAIKSLNITR-IVIAHRKSTINSADR----IIALQE 700
Cdd:PRK10253 165 MLLDEPTTWLDISHQIDLLELLSELNREKgYTLAAVLHDLNQACRyashLIALRE 219
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
509-700 |
5.64e-08 |
|
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: 53.98 E-value: 5.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 509 LRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVD----GIDIKELGVnnyQKLIAcvlqddrlfsgtLR 584
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLAQASP---REILA------------LR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 585 DNICSFSTQ------------------IDDNWLIECARfAQIHDDIERM----------PM----Gydtligelgeglsg 632
Cdd:COG4778 92 RRTIGYVSQflrviprvsaldvvaeplLERGVDREEAR-ARARELLARLnlperlwdlpPAtfsgG-------------- 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1533513286 633 gQKQRIFIARAIYKKPSILFMDEATSSLDHTNEQYINDAI---KSLNITRIVIAHRKSTINS-ADRIIALQE 700
Cdd:COG4778 157 -EQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIeeaKARGTAIIGIFHDEEVREAvADRVVDVTP 227
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
506-669 |
5.73e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 54.80 E-value: 5.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 506 SYTLRhlnieiqPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGidiKELGVNNY---QKLIACVLQDD------ 576
Cdd:PRK15112 33 SFTLR-------EGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDD---HPLHFGDYsyrSQRIRMIFQDPstslnp 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 577 RLFSGTLRDNICSFSTQIDDNwliecARFAQIHDDIERMPMGYDTlIGELGEGLSGGQKQRIFIARAIYKKPSILFMDEA 656
Cdd:PRK15112 103 RQRISQILDFPLRLNTDLEPE-----QREKQIIETLRQVGLLPDH-ASYYPHMLAPGQKQRLGLARALILRPKVIIADEA 176
|
170
....*....|....
gi 1533513286 657 TSSLDHT-NEQYIN 669
Cdd:PRK15112 177 LASLDMSmRSQLIN 190
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
516-700 |
5.97e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 54.01 E-value: 5.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 516 IQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKL----IACVLQDDRLFSgTL--RDNIcs 589
Cdd:PRK10584 33 VKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLrakhVGFVFQSFMLIP-TLnaLENV-- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 590 fstQIDDnwLIECARFAQIHDDIERM--PMGYDTLIGELGEGLSGGQKQRIFIARAIYKKPSILFMDEATSSLDHTNEQY 667
Cdd:PRK10584 110 ---ELPA--LLRGESSRQSRNGAKALleQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDK 184
|
170 180 190
....*....|....*....|....*....|....*..
gi 1533513286 668 INDAIKSLN----ITRIVIAHRKSTINSADRIIALQE 700
Cdd:PRK10584 185 IADLLFSLNrehgTTLILVTHDLQLAARCDRRLRLVN 221
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
492-661 |
8.09e-08 |
|
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: 53.04 E-value: 8.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISYKYDSYAS--YTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPAS---EGNIFVDGIDIKELGvNNYQ 566
Cdd:cd03233 4 LSWRNISFTTGKGRSkiPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFA-EKYP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 567 KLIACVLQDDRLFSG-TLRDnicsfstqiddnwLIECARFAQIHDDIERMPMGydtligelgeglsggQKQRIFIARAIY 645
Cdd:cd03233 83 GEIIYVSEEDVHFPTlTVRE-------------TLDFALRCKGNEFVRGISGG---------------ERKRVSIAEALV 134
|
170
....*....|....*.
gi 1533513286 646 KKPSILFMDEATSSLD 661
Cdd:cd03233 135 SRASVLCWDNSTRGLD 150
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
492-661 |
1.12e-07 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 53.78 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISYKYDSYASytLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDG-----IDIKELGVNNYQ 566
Cdd:PRK11701 7 LSVRGLTKLYGPRKG--CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlRDLYALSEAERR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 567 KLI----ACVLQD----------------DRLFS------GTLRDnicsfsTQIDdnWL----IECARFaqihDDIERMP 616
Cdd:PRK11701 85 RLLrtewGFVHQHprdglrmqvsaggnigERLMAvgarhyGDIRA------TAGD--WLerveIDAARI----DDLPTTF 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1533513286 617 MGydtligelgeglsgGQKQRIFIARAIYKKPSILFMDEATSSLD 661
Cdd:PRK11701 153 SG--------------GMQQRLQIARNLVTHPRLVFMDEPTGGLD 183
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
509-700 |
1.28e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 54.79 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 509 LRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIK--------ELGVN-NYQKL--IACVLQDDR 577
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNkldhklaaQLGIGiIYQELsvIDELTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 578 LFSGTL-RDNICSFSTqIDdnWliecaRFAQIHDDIERMPMGYDTLIGELGEGLSGGQKQRIFIARAIYKKPSILFMDEA 656
Cdd:PRK09700 101 LYIGRHlTKKVCGVNI-ID--W-----REMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1533513286 657 TSSLDHTNEQY---INDAIKSLNITRIVIAHRKSTINS-ADRIIALQE 700
Cdd:PRK09700 173 TSSLTNKEVDYlflIMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKD 220
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
176-466 |
1.55e-07 |
|
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: 53.64 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 176 LTKIFFLSIIIESINLVMPVATQLVMDHAIPANDSGLLTLICFGLVFFVALRTITGLIRSWTVLIMSSFINAQWQKGLLQ 255
Cdd:cd18540 4 LILLIILMLLVALLDAVFPLLTKYAIDHFITPGTLDGLTGFILLYLGLILIQALSVFLFIRLAGKIEMGVSYDLRKKAFE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 256 HLLKLPLEYFERRKIGDIQSRFGS-LNTLQETFTTSVVGAIIDSIMIIGLLIMLVLYGGWLTWFVILFTCLYVFI----- 329
Cdd:cd18540 84 HLQTLSFSYFDKTPVGWIMARVTSdTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPVLAVVsiyfq 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 330 -RVLTYNR-YRQLSeeSLIKDAransfFMETLYGIATVKVQGLNKRREENWFNLEVDSINTGIKVSRLNLFFGGINTLIA 407
Cdd:cd18540 164 kKILKAYRkVRKIN--SRITGA-----FNEGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFLPIVLFLG 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1533513286 408 TMEQILILWLGASLVISGNMTIGMFVAFSSYRGQFSDRIASFIDFLLRLQIMSLHNERV 466
Cdd:cd18540 237 SIATALVLWYGGILVLAGAITIGTLVAFISYATQFFEPIQQLARVLAELQSAQASAERV 295
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
265-433 |
1.73e-07 |
|
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: 53.25 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 265 FERRKIGDIQSRF-GSLNTLQETFTTSVVGAIIDSIMIIGLLIMLVLYGGWLT-WFVILFTCLYVFIRVLTYNRYRQLSE 342
Cdd:cd18585 86 LQKYRSGDLLNRIvADIDTLDNLYLRVLSPPVVALLVILATILFLAFFSPALAlILLAGLLLAGVVIPLLFYRLGKKIGQ 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 343 ESLIKDARANSFFMETLYGIATVKVQGLNKRREENWFNLEVDSINTGIKVSRLNLFFGGINTLIATMEQILILWLGASLV 422
Cdd:cd18585 166 QLVQLRAELRTELVDGLQGMAELLIFGALERQRQQLEQLSDALIKEQRRLARLSGLSQALMILLSGLTVWLVLWLGAPLV 245
|
170
....*....|....
gi 1533513286 423 ISGNMT---IGMFV 433
Cdd:cd18585 246 QNGALDgalLAMLV 259
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
492-695 |
1.90e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 52.86 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISYKYDSyaSYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVL------------CGLFPASEGNIFVDGIDIKE 559
Cdd:PRK14239 6 LQVSDLSVYYNK--KKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmndlnpevtiTGSIVYNGHNIYSPRTDTVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 560 LgvnnyQKLIACVLQDDRLFSGTLRDNIC-------SFSTQIDDNWLIECARFAQIHDDI-ERMpmgYDTLIgelgeGLS 631
Cdd:PRK14239 84 L-----RKEIGMVFQQPNPFPMSIYENVVyglrlkgIKDKQVLDEAVEKSLKGASIWDEVkDRL---HDSAL-----GLS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1533513286 632 GGQKQRIFIARAIYKKPSILFMDEATSSLDHTNEQYINDAIKSL--NITRIVIAHrksTINSADRI 695
Cdd:PRK14239 151 GGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLkdDYTMLLVTR---SMQQASRI 213
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
515-684 |
3.09e-07 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 52.81 E-value: 3.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 515 EIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKL---IACVLQDD------RLfsgTLRD 585
Cdd:COG4608 40 DIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLrrrMQMVFQDPyaslnpRM---TVGD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 586 nicsfstQIDDNWLI-----ECARFAQIH----------DDIERMPM----GydtligelgeglsggQKQRIFIARAIYK 646
Cdd:COG4608 117 -------IIAEPLRIhglasKAERRERVAellelvglrpEHADRYPHefsgG---------------QRQRIGIARALAL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1533513286 647 KPSILFMDEATSSLDHTNE-QYIN---DAIKSLNITRIVIAH 684
Cdd:COG4608 175 NPKLIVCDEPVSALDVSIQaQVLNlleDLQDELGLTYLFISH 216
|
|
| Peptidase_C39_likeA |
cd02417 |
A sub-family of peptidase C39 which contains Cyclolysin and Hemolysin processing peptidases. ... |
33-143 |
3.26e-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: 49.55 E-value: 3.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 33 GLACLAMICGYYGKNIDIFTLRQKFKLSSRGTDLASLNDIAVKMHMSTRAVSVELDELHSVKLPCILHWDFNHFVVLTKI 112
Cdd:cd02417 8 GLLALVLLARYHGIAADPEQLRHEFGLAGEPFNSTELLLAAKSLGLKAKAVRQPVERLARLPLPALAWDDDGGHFILAKL 87
|
90 100 110
....*....|....*....|....*....|..
gi 1533513286 113 KNGKFTVHDPSVG-IVKVAKSELSKKFTGIVL 143
Cdd:cd02417 88 DGQKYLIQDPISQrPEVLSREEFEARWSGELI 119
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
509-661 |
3.58e-07 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 52.28 E-value: 3.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 509 LRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIK-------ELGVNNYQKL------IACVLQD 575
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgQLKVADKNQLrllrtrLTMVFQH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 576 DRLFSG-TLRDNICSFSTQIDDNWLIECARFAQIHDD----IERMPMGYDTLIGELgeglsggQKQRIFIARAIYKKPSI 650
Cdd:PRK10619 101 FNLWSHmTVLENVMEAPIQVLGLSKQEARERAVKYLAkvgiDERAQGKYPVHLSGG-------QQQRVSIARALAMEPEV 173
|
170
....*....|.
gi 1533513286 651 LFMDEATSSLD 661
Cdd:PRK10619 174 LLFDEPTSALD 184
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
489-660 |
4.50e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 53.13 E-value: 4.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 489 PVSLSAKNISYKYDSYAsyTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKL 568
Cdd:PRK15439 9 PPLLCARSISKQYSGVE--VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 569 -IACVLQDDRLFSG-TLRDNICsF---STQIDDNWLIECARFAQIHDDIErMPMGydTLigelgeglSGGQKQRIFIARA 643
Cdd:PRK15439 87 gIYLVPQEPLLFPNlSVKENIL-FglpKRQASMQKMKQLLAALGCQLDLD-SSAG--SL--------EVADRQIVEILRG 154
|
170
....*....|....*..
gi 1533513286 644 IYKKPSILFMDEATSSL 660
Cdd:PRK15439 155 LMRDSRILILDEPTASL 171
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
264-438 |
7.16e-07 |
|
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: 51.54 E-value: 7.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 264 YFERRKIGDIQSRFGS-LNTLQETFTTSVVGAIIDSIMIIGLLIMLVLyggwLTWFVILFTCL---YVFIRVLTY-NRYR 338
Cdd:cd18784 86 FFDTVKTGDITSRLTSdTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFK----LSWQLSLVTLIglpLIAIVSKVYgDYYK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 339 QLSEESLIKDARANSFFMETLYGIATVKvqglNKRREENWFNLEVDSINTGIKVSRLN-LFFGG---INTLIATMEQILI 414
Cdd:cd18784 162 KLSKAVQDSLAKANEVAEETISSIRTVR----SFANEDGEANRYSEKLKDTYKLKIKEaLAYGGyvwSNELTELALTVST 237
|
170 180
....*....|....*....|....
gi 1533513286 415 LWLGASLVISGNMTIGMFVAFSSY 438
Cdd:cd18784 238 LYYGGHLVITGQISGGNLISFILY 261
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
492-661 |
7.90e-07 |
|
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: 50.05 E-value: 7.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISYKYDsyASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKElGVNNYQKLIAC 571
Cdd:TIGR01189 1 LAARNLACSRG--ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAE-QRDEPHENILY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 572 VLQDDRLfSGTL--RDNIcSFstqiddnwliecarFAQIHDDIERMP------MGYDTLIGELGEGLSGGQKQRIFIARA 643
Cdd:TIGR01189 78 LGHLPGL-KPELsaLENL-HF--------------WAAIHGGAQRTIedalaaVGLTGFEDLPAAQLSAGQQRRLALARL 141
|
170
....*....|....*...
gi 1533513286 644 IYKKPSILFMDEATSSLD 661
Cdd:TIGR01189 142 WLSRRPLWILDEPTTALD 159
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
511-675 |
1.42e-06 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 50.57 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 511 HLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKlIACVLQDDRL---FsgTLRDNI 587
Cdd:PRK13537 25 GLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQR-VGVVPQFDNLdpdF--TVRENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 588 CSF-------STQIDDNW--LIECARFAQIHDDIERMPMGydtligelgeglsgGQKQRIFIARAIYKKPSILFMDEATS 658
Cdd:PRK13537 102 LVFgryfglsAAAARALVppLLEFAKLENKADAKVGELSG--------------GMKRRLTLARALVNDPDVLVLDEPTT 167
|
170
....*....|....*..
gi 1533513286 659 SLDHTNEQYINDAIKSL 675
Cdd:PRK13537 168 GLDPQARHLMWERLRSL 184
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
492-693 |
1.51e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 50.39 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISYKYDSyaSYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDG--IDIKELGVNNYQKLI 569
Cdd:PRK13638 2 LATSDLWFRYQD--EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 570 ACVLQD-DRLFSGTLRDNICSFS------------TQIDDNW-LIECARFAqiHDDIERMPMGydtligelgeglsggQK 635
Cdd:PRK13638 80 ATVFQDpEQQIFYTDIDSDIAFSlrnlgvpeaeitRRVDEALtLVDAQHFR--HQPIQCLSHG---------------QK 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1533513286 636 QRIFIARAIYKKPSILFMDEATSSLDHTNE-QYIndAIkslnITRIVIAHRKSTINSAD 693
Cdd:PRK13638 143 KRVAIAGALVLQARYLLLDEPTAGLDPAGRtQMI--AI----IRRIVAQGNHVIISSHD 195
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
511-696 |
1.96e-06 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 50.48 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 511 HLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNY---QKLIACVLQDDrLFSGTLRDNI 587
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravRSDIQMIFQDP-LASLNPRMTI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 588 CSFSTQIDDNWLIECARfAQIHDDIERMPMG---YDTLIGELGEGLSGGQKQRIFIARAIYKKPSILFMDEATSSLD-HT 663
Cdd:PRK15079 118 GEIIAEPLRTYHPKLSR-QEVKDRVKAMMLKvglLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDvSI 196
|
170 180 190
....*....|....*....|....*....|....*..
gi 1533513286 664 NEQYIN---DAIKSLNITRIVIAHRKSTINS-ADRII 696
Cdd:PRK15079 197 QAQVVNllqQLQREMGLSLIFIAHDLAVVKHiSDRVL 233
|
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
263-457 |
2.01e-06 |
|
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: 50.22 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 263 EYFERRKIGDIQS---RFGSLNTLQETFTTSVVGAIIDsiMIIGLLIMLVLYGGWLTWFVILFTCLYVFIRVLTYNRYRQ 339
Cdd:cd18583 86 DFHDSKKSGEVLKaieQGSSINDLLEQILFQIVPMIID--LVIAIVYLYYLFDPYMGLIVAVVMVLYVWSTIKLTSWRTK 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 340 LSEESLIKDARANSFFMETLYGIATVKVQGlNKRREENWFNLEVDSINTgikvSRLNLFFGginTLIATMEQILIL---- 415
Cdd:cd18583 164 LRRDMIDADREERSILTESLLNWETVKYFN-REPYEKERYREAVKNYQK----AERKYLFS---LNLLNAVQSLILtlgl 235
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1533513286 416 ----WLGASLVISGNMTIGMFVAFSSYRGQFSDRIASFIDFLLRLQ 457
Cdd:cd18583 236 lagcFLAAYQVSQGQATVGDFVTLLTYWAQLSGPLNFFATLYRSIQ 281
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
462-668 |
2.69e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.40 E-value: 2.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 462 HNERVSDIALtevtPFKDDIPVKN----DMCPVSLSAKNISYKydsyASYTLRHLNIEIQPGEHVAITGASGTGKTTLLK 537
Cdd:PRK10938 233 HSEQLEGVQL----PEPDEPSARHalpaNEPRIVLNNGVVSYN----DRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLS 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 538 VLCGLFPASEGNIFV---------DGI-DIKelgvnnyqKLIACV---LQDDRLFSGTLRDNICS--FST---------- 592
Cdd:PRK10938 305 LITGDHPQGYSNDLTlfgrrrgsgETIwDIK--------KHIGYVsssLHLDYRVSTSVRNVILSgfFDSigiyqavsdr 376
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1533513286 593 --QIDDNWLiecarfaqihdDIermpMGYDTLIGELGEGLSGGQKQR-IFIARAIYKKPSILFMDEATSSLDHTNEQYI 668
Cdd:PRK10938 377 qqKLAQQWL-----------DI----LGIDKRTADAPFHSLSWGQQRlALIVRALVKHPTLLILDEPLQGLDPLNRQLV 440
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
509-696 |
2.77e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 48.09 E-value: 2.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 509 LRHLNIEIQPGEHVAITGASGTGKTTLlkVLCGLFPASEGNIfvdgidIKELGVNNYQKLIAcvlqddrlfsgtlrdnIC 588
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTL--VNEGLYASGKARL------ISFLPKFSRNKLIF----------------ID 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 589 SFSTQIDdnwliecarfaqihddierMPMGYDTLiGELGEGLSGGQKQRIFIARAIYK--KPSILFMDEATSSLDHTNEQ 666
Cdd:cd03238 67 QLQFLID-------------------VGLGYLTL-GQKLSTLSGGELQRVKLASELFSepPGTLFILDEPSTGLHQQDIN 126
|
170 180 190
....*....|....*....|....*....|...
gi 1533513286 667 YINDAIKSL---NITRIVIAHRKSTINSADRII 696
Cdd:cd03238 127 QLLEVIKGLidlGNTVILIEHNLDVLSSADWII 159
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
509-556 |
3.41e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 49.70 E-value: 3.41e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1533513286 509 LRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGID 556
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYV 85
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
507-684 |
3.67e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 50.24 E-value: 3.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 507 YTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKL---IACVLQDD------R 577
Cdd:PRK10261 338 HAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALrrdIQFIFQDPyasldpR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 578 LFSG-----TLRDN--ICSFSTQIDDNWLIEcaRFAQIHDDIERMPMGYDTligelgeglsgGQKQRIFIARAIYKKPSI 650
Cdd:PRK10261 418 QTVGdsimePLRVHglLPGKAAAARVAWLLE--RVGLLPEHAWRYPHEFSG-----------GQRQRICIARALALNPKV 484
|
170 180 190
....*....|....*....|....*....|....*...
gi 1533513286 651 LFMDEATSSLD-HTNEQYIN---DAIKSLNITRIVIAH 684
Cdd:PRK10261 485 IIADEAVSALDvSIRGQIINlllDLQRDFGIAYLFISH 522
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
300-443 |
3.82e-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: 49.42 E-value: 3.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 300 MIIGLLIMLVLYGGWLtwFVILFTC--LYVFIRVLTYNRYRQLSEESLIKDARANSFFMETLYGIATVKVQGlNKRREEN 377
Cdd:cd18582 126 LLLVCGILWYLYGWSY--ALITLVTvaLYVAFTIKVTEWRTKFRREMNEADNEANAKAVDSLLNYETVKYFN-NEEYEAE 202
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1533513286 378 WFN-----LEVDSINTGIKVSRLNLffgGINTLIATMeQILILWLGASLVISGNMTIGMFVAFSSYRGQFS 443
Cdd:cd18582 203 RYDkalakYEKAAVKSQTSLALLNI---GQALIISLG-LTAIMLLAAQGVVAGTLTVGDFVLVNTYLLQLY 269
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
476-698 |
4.03e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 50.24 E-value: 4.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 476 PFKDDIPVkNDMcpVSLSAKNISYKYDSYASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDG- 554
Cdd:PRK10261 2 PHSDELDA-RDV--LAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKm 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 555 ---------IDIKELGVNNYQKL----IACVLQDDRlfsgTLRDNICSFSTQIDDNWLI-------ECARFAQIHDDIER 614
Cdd:PRK10261 79 llrrrsrqvIELSEQSAAQMRHVrgadMAMIFQEPM----TSLNPVFTVGEQIAESIRLhqgasreEAMVEAKRMLDQVR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 615 MPMGyDTLIGELGEGLSGGQKQRIFIARAIYKKPSILFMDEATSSLDHTNEQYINDAIKSL----NITRIVIAHRKSTI- 689
Cdd:PRK10261 155 IPEA-QTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLqkemSMGVIFITHDMGVVa 233
|
....*....
gi 1533513286 690 NSADRIIAL 698
Cdd:PRK10261 234 EIADRVLVM 242
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
487-698 |
5.46e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.56 E-value: 5.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 487 MCPVSLSAKNISYkydSYASYtLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFP---------------------- 544
Cdd:PRK11147 1 MSLISIHGAWLSF---SDAPL-LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLlddgriiyeqdlivarlqqdpp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 545 -ASEGNIFvDGID--IKELG--VNNYQKLIACVLQD--DRLFS--GTLRDnicsfstQID--DNWLIEcarfAQIHDDIE 613
Cdd:PRK11147 77 rNVEGTVY-DFVAegIEEQAeyLKRYHDISHLVETDpsEKNLNelAKLQE-------QLDhhNLWQLE----NRINEVLA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 614 RMPMGYDTLIGELGEGLSggqkQRIFIARAIYKKPSILFMDEATSSLDHTNEQYINDAIKSLNITRIVIAHRKSTINS-A 692
Cdd:PRK11147 145 QLGLDPDAALSSLSGGWL----RKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNmA 220
|
....*.
gi 1533513286 693 DRIIAL 698
Cdd:PRK11147 221 TRIVDL 226
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
509-560 |
8.54e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 47.71 E-value: 8.54e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1533513286 509 LRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGlFPA---SEGNIFVDGIDIKEL 560
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG-HPAykiLEGDILFKGESILDL 76
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
489-554 |
8.61e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 47.54 E-value: 8.61e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1533513286 489 PVSLSAKNISYKYDsyASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDG 554
Cdd:PRK13543 9 PPLLAAHALAFSRN--EEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDG 72
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
477-675 |
8.88e-06 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 48.29 E-value: 8.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 477 FKDDIPVKNDMCPVSLSAKNISYKYDSYAsyTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGID 556
Cdd:PRK13536 27 SEAKASIPGSMSTVAIDLAGVSKSYGDKA--VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 557 IKElGVNNYQKLIACVLQDDRL-FSGTLRDNI------CSFSTQIDDNWLIECARFAqihddieRMPMGYDTLIGELGEG 629
Cdd:PRK13536 105 VPA-RARLARARIGVVPQFDNLdLEFTVRENLlvfgryFGMSTREIEAVIPSLLEFA-------RLESKADARVSDLSGG 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1533513286 630 LsggqKQRIFIARAIYKKPSILFMDEATSSLDHTNEQYINDAIKSL 675
Cdd:PRK13536 177 M----KRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSL 218
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
509-675 |
9.03e-06 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 47.96 E-value: 9.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 509 LRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELgvnNYQKLIACVLQDDRLfsgtlrdnIC 588
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQA---LQKNLVAYVPQSEEV--------DW 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 589 SFSTQIDDnwLIECARFAqiHDDIERMPMGYDTLIGELGEGLSGG--------------QKQRIFIARAIYKKPSILFMD 654
Cdd:PRK15056 92 SFPVLVED--VVMMGRYG--HMGWLRRAKKRDRQIVTAALARVDMvefrhrqigelsggQKKRVFLARAIAQQGQVILLD 167
|
170 180
....*....|....*....|.
gi 1533513286 655 EATSSLDHTNEQYINDAIKSL 675
Cdd:PRK15056 168 EPFTGVDVKTEARIISLLREL 188
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
490-661 |
9.53e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 47.90 E-value: 9.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 490 VSLSAKNISYKYD---SYASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIK-ELGVNNY 565
Cdd:PRK13641 1 MSIKFENVDYIYSpgtPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpETGNKNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 566 QKL---IACVLQ--DDRLFSGTLRDNI------CSFSTQIDDNWLIECARFAQIHDD-IERMPMgydtligelgeGLSGG 633
Cdd:PRK13641 81 KKLrkkVSLVFQfpEAQLFENTVLKDVefgpknFGFSEDEAKEKALKWLKKVGLSEDlISKSPF-----------ELSGG 149
|
170 180
....*....|....*....|....*...
gi 1533513286 634 QKQRIFIARAIYKKPSILFMDEATSSLD 661
Cdd:PRK13641 150 QMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
489-657 |
9.64e-06 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 48.86 E-value: 9.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 489 PVSLSAKNISykydsyASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGidiKELGVNNYQKL 568
Cdd:COG1129 254 EVVLEVEGLS------VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDG---KPVRIRSPRDA 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 569 IA---CVLQDDRLFSG-----TLRDNIC-----SFSTQ--IDDNWLIECARfAQIHD-DIeRMPmGYDTLIgelgeglsg 632
Cdd:COG1129 325 IRagiAYVPEDRKGEGlvldlSIRENITlasldRLSRGglLDRRRERALAE-EYIKRlRI-KTP-SPEQPV--------- 392
|
170 180 190
....*....|....*....|....*....|.
gi 1533513286 633 gQK------QRIFIARAIYKKPSILFMDEAT 657
Cdd:COG1129 393 -GNlsggnqQKVVLAKWLATDPKVLILDEPT 422
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
494-550 |
9.90e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 48.16 E-value: 9.90e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 494 AKNISYKYDSYASYTLRHLN---IEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNI 550
Cdd:PRK13651 5 VKNIVKIFNKKLPTELKALDnvsVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTI 64
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
492-701 |
1.32e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 48.35 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISYKYDSYAsyTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNI-FVDGIDIKELGVNNYQKlia 570
Cdd:PRK15064 320 LEVENLTKGFDNGP--LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkWSENANIGYYAQDHAYD--- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 571 cvLQDDRlfsgTLRDNICSFSTQIDDNWLIECA--R--FAQihDDIERmpmgydtligeLGEGLSGGQKQRIFIARAIYK 646
Cdd:PRK15064 395 --FENDL----TLFDWMSQWRQEGDDEQAVRGTlgRllFSQ--DDIKK-----------SVKVLSGGEKGRMLFGKLMMQ 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1533513286 647 KPSILFMDEATSSLDHtneqyinDAIKSLNI-------TRIVIAHRKSTINS-ADRIIALQEN 701
Cdd:PRK15064 456 KPNVLVMDEPTNHMDM-------ESIESLNMalekyegTLIFVSHDREFVSSlATRIIEITPD 511
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
499-696 |
1.57e-05 |
|
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: 47.02 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 499 YKYdSYASYTLR--HLNIE---IQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIkelgvnNY--QKLIAc 571
Cdd:cd03237 1 YTY-PTMKKTLGefTLEVEggsISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV------SYkpQYIKA- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 572 vlqddrLFSGTLRDnicsFSTQIDDNWLIEcarfAQIHDDIERmPMGYDTLIGELGEGLSGGQKQRIFIARAIYKKPSIL 651
Cdd:cd03237 73 ------DYEGTVRD----LLSSITKDFYTH----PYFKTEIAK-PLQIEQILDREVPELSGGELQRVAIAACLSKDADIY 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1533513286 652 FMDEATSSLDHTNEQYINDAIKSL----NITRIVIAHRKSTINS-ADRII 696
Cdd:cd03237 138 LLDEPSAYLDVEQRLMASKVIRRFaennEKTAFVVEHDIIMIDYlADRLI 187
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
263-437 |
1.67e-05 |
|
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: 47.47 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 263 EYFERRKIGDIQSRFGS-LNTLQETFTTSVVGAIIDSIMIIGLLImLVLYGGW-LTwFVILFTCLYVFIRVLTYNRY-RQ 339
Cdd:cd18577 96 AWFDKNGAGELTSRLTSdTNLIQDGIGEKLGLLIQSLSTFIAGFI-IAFIYSWkLT-LVLLATLPLIAIVGGIMGKLlSK 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 340 LSEESLIKDARANSFFMETLYGIATVKVQGLNKRREENWFNLEVDSINTGIKVSRLN-LFFGGINTLIATMeQILILWLG 418
Cdd:cd18577 174 YTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSgLGLGLLFFIIFAM-YALAFWYG 252
|
170 180
....*....|....*....|
gi 1533513286 419 ASLVISGNMTIG-MFVAFSS 437
Cdd:cd18577 253 SRLVRDGEISPGdVLTVFFA 272
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
496-700 |
1.70e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 47.31 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 496 NISYKYDSYASYTLRHLN---IEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVD------GID-IKElgVNNY 565
Cdd:PRK13645 11 NVSYTYAKKTPFEFKALNntsLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGdyaipaNLKkIKE--VKRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 566 QKLIACVLQ--DDRLFSGTLRDNICSFSTQIDDNWLIECARFAQIHDDIErMPMGYdtlIGELGEGLSGGQKQRIFIARA 643
Cdd:PRK13645 89 RKEIGLVFQfpEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQ-LPEDY---VKRSPFELSGGQKRRVALAGI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1533513286 644 IYKKPSILFMDEATSSLDHTNEQYINDAIKSLNITR----IVIAHR-KSTINSADRIIALQE 700
Cdd:PRK13645 165 IAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYkkriIMVTHNmDQVLRIADEVIVMHE 226
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
509-698 |
2.23e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 46.74 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 509 LRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPAS--------EGNIFVDGIDIKELGVNNYQKLIACVLQ-DDRLF 579
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPRLARLRAVLPQaAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 580 SGTLRDNIC---------SFSTQIDDNWLIECArfaqihddIERmpMGYDTLIGELGEGLSGGQKQRIFIARAIYK---- 646
Cdd:PRK13547 97 AFSAREIVLlgrypharrAGALTHRDGEIAWQA--------LAL--AGATALVGRDVTTLSGGELARVQFARVLAQlwpp 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1533513286 647 -----KPSILFMDEATSSLDHTNEQYINDAIKSL----NITRIVIAHRKS-TINSADRIIAL 698
Cdd:PRK13547 167 hdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLardwNLGVLAIVHDPNlAARHADRIAML 228
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
509-661 |
2.82e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 47.80 E-value: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 509 LRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPA---SEGNIFVDGIDIKElgvnNYQKLIACVLQDD-RLFSGTLR 584
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPLDS----SFQRSIGYVQQQDlHLPTSTVR 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 585 DNIcSFST---QIDDNWLIECARFAQIHDDIERMPMGYDTLIGELGEGLSGGQKQRIFIARAIYKKP-SILFMDEATSSL 660
Cdd:TIGR00956 855 ESL-RFSAylrQPKSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGEGLNVEQRKRLTIGVELVAKPkLLLFLDEPTSGL 933
|
.
gi 1533513286 661 D 661
Cdd:TIGR00956 934 D 934
|
|
| Peptidase_C39_likeD |
cd02421 |
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
34-143 |
3.34e-05 |
|
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: 43.77 E-value: 3.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 34 LACLAMICGYYGKNIDIFTLRQKFKLSSRGTDLASLNDIAVKMHMSTRAVSVELDELHSVKLPCILHWDFNHFVVLTKIK 113
Cdd:cd02421 9 LDCLVLLARQFGKPASRDSLVAGLPLDDGRLSPALFPRAAARAGLSARVVRRPLDAIPTLLLPAILLLKNGRACVLLGVD 88
|
90 100 110
....*....|....*....|....*....|..
gi 1533513286 114 NGKFTVHDPSV--GIVKVAKSELSKKFTGIVL 143
Cdd:cd02421 89 DGHARILDPESggGEVEISLEELEEEYSGYAI 120
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
509-684 |
3.66e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 45.99 E-value: 3.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 509 LRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPAS-----EGNIFVDGIDIKELGVN--NYQKLIACVLQDDRLFSG 581
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDVDpiEVRREVGMVFQYPNPFPH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 582 -TLRDNIC---------SFSTQIDD--NW-LIECARFAQIHDDIERMPmgydtligelgEGLSGGQKQRIFIARAIYKKP 648
Cdd:PRK14267 100 lTIYDNVAigvklnglvKSKKELDErvEWaLKKAALWDEVKDRLNDYP-----------SNLSGGQRQRLVIARALAMKP 168
|
170 180 190
....*....|....*....|....*....|....*...
gi 1533513286 649 SILFMDEATSSLDHTNEQYINDAIKSL--NITRIVIAH 684
Cdd:PRK14267 169 KILLMDEPTANIDPVGTAKIEELLFELkkEYTIVLVTH 206
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
491-681 |
3.81e-05 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 45.65 E-value: 3.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 491 SLSAKNISYKYDsyASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVN-NYQKLI 569
Cdd:PRK10895 3 TLTAKNLAKAYK--GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHaRARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 570 ACVLQDDRLFSG-----------TLRDNICSFSTQIDDNWLIECARFAQIHDDIERMPMGydtligelgeglsgGQKQRI 638
Cdd:PRK10895 81 GYLPQEASIFRRlsvydnlmavlQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSG--------------GERRRV 146
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1533513286 639 FIARAIYKKPSILFMDEATSSLdhtneqyinDAIKSLNITRIV 681
Cdd:PRK10895 147 EIARALAANPKFILLDEPFAGV---------DPISVIDIKRII 180
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
495-700 |
3.91e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 46.17 E-value: 3.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 495 KNISYKYDS---YASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVdGIDIKELGVNNYQ----- 566
Cdd:PRK13634 6 QKVEHRYQYktpFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGKKNKKlkplr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 567 KLIACVLQ--DDRLFSGTLRDNIC----SFSTQIDD-----NWLIECARFAqiHDDIERMPMgydtligelgeGLSGGQK 635
Cdd:PRK13634 85 KKVGIVFQfpEHQLFEETVEKDICfgpmNFGVSEEDakqkaREMIELVGLP--EELLARSPF-----------ELSGGQM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 636 QRIFIARAIYKKPSILFMDEATSSLDHTNEQYINDAIKSL----NITRIVIAHR-KSTINSADRIIALQE 700
Cdd:PRK13634 152 RRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLhkekGLTTVLVTHSmEDAARYADQIVVMHK 221
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
491-694 |
3.93e-05 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 45.78 E-value: 3.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 491 SLSAKNISYKYDsyASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKLIA 570
Cdd:PRK11231 2 TLRTENLTVGYG--TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 571 CVLQDDRLFSG-TLRDNICSFSTQiddnWLIECARFAQihDDIERMP-----MGYDTLIGELGEGLSGGQKQRIFIARAI 644
Cdd:PRK11231 80 LLPQHHLTPEGiTVRELVAYGRSP----WLSLWGRLSA--EDNARVNqameqTRINHLADRRLTDLSGGQRQRAFLAMVL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1533513286 645 YKKPSILFMDEATSSLD--HTNE-----QYINDAIKslniTRIVIAHrksTINSADR 694
Cdd:PRK11231 154 AQDTPVVLLDEPTTYLDinHQVElmrlmRELNTQGK----TVVTVLH---DLNQASR 203
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
481-661 |
5.71e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 46.76 E-value: 5.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 481 IPVKNDMC----PVSLSAKNISYKYDSYASYT-----------LRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPA 545
Cdd:PLN03140 853 VAPKRGMVlpftPLAMSFDDVNYFVDMPAEMKeqgvtedrlqlLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTG 932
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 546 S--EGNIFVDGIDIKElgvNNYQKLIACVLQDD-----------RLFSGTLR-------DNICSFSTQIddnwlIECARF 605
Cdd:PLN03140 933 GyiEGDIRISGFPKKQ---ETFARISGYCEQNDihspqvtvresLIYSAFLRlpkevskEEKMMFVDEV-----MELVEL 1004
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1533513286 606 AQIHDDIERMP--MGYDTligelgeglsgGQKQRIFIARAIYKKPSILFMDEATSSLD 661
Cdd:PLN03140 1005 DNLKDAIVGLPgvTGLST-----------EQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
497-693 |
7.94e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 44.17 E-value: 7.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 497 ISYKYDSYASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKElGVNNYQKLIACVLQDD 576
Cdd:PRK13540 5 IELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFVGHRS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 577 RLFSG-TLRDNiCSF-----STQIDDNWLIECARFAQIHDdierMPMGydtligelgeGLSGGQKQRIFIARAIYKKPSI 650
Cdd:PRK13540 84 GINPYlTLREN-CLYdihfsPGAVGITELCRLFSLEHLID----YPCG----------LLSSGQKRQVALLRLWMSKAKL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1533513286 651 LFMDEATSSLDhtnEQYINDAIKSLNITR------IVIAHRKSTINSAD 693
Cdd:PRK13540 149 WLLDEPLVALD---ELSLLTIITKIQEHRakggavLLTSHQDLPLNKAD 194
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
509-660 |
8.18e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.88 E-value: 8.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 509 LRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIK--------ELGVNNYQKLIACVLQDdrlfs 580
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfksskealENGISMVHQELNLVLQR----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 581 gTLRDNIcsfstqiddnWLiecARF---------AQIHDDIERM--PMGYDTLIGELGEGLSGGQKQRIFIARAIYKKPS 649
Cdd:PRK10982 89 -SVMDNM----------WL---GRYptkgmfvdqDKMYRDTKAIfdELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAK 154
|
170
....*....|.
gi 1533513286 650 ILFMDEATSSL 660
Cdd:PRK10982 155 IVIMDEPTSSL 165
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
519-661 |
9.59e-05 |
|
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: 44.02 E-value: 9.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 519 GEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKLIACVLQDDRLFSGTLRDNIcSFstqiddnW 598
Cdd:cd03231 26 GEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENL-RF-------W 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1533513286 599 LIECARfAQIHDDIERMPM-GYDTLIgelGEGLSGGQKQRIFIARAIYKKPSILFMDEATSSLD 661
Cdd:cd03231 98 HADHSD-EQVEEALARVGLnGFEDRP---VAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
495-558 |
1.03e-04 |
|
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: 45.77 E-value: 1.03e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1533513286 495 KNISYKYDSYASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIK 558
Cdd:TIGR01257 932 KNLVKIFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIE 995
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
509-554 |
1.20e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.17 E-value: 1.20e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1533513286 509 LRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPAS--EGNIFVDG 554
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGsyEGEILFDG 64
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
509-662 |
1.33e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 44.90 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 509 LRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGidiKELGVNNYQKL----IACVLQDDRLFSG-TL 583
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDG---QEMRFASTTAAlaagVAIIYQELHLVPEmTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 584 RDNIC--SFSTQ---IDDNWLIECAR--FAQIHDDIE-RMPMGYDTLigelgeglsgGQKQRIFIARAIYKKPSILFMDE 655
Cdd:PRK11288 97 AENLYlgQLPHKggiVNRRLLNYEAReqLEHLGVDIDpDTPLKYLSI----------GQRQMVEIAKALARNARVIAFDE 166
|
....*..
gi 1533513286 656 ATSSLDH 662
Cdd:PRK11288 167 PTSSLSA 173
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
518-691 |
1.34e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.16 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 518 PGEHVAITGASGTGKTTLLKVLCGLFPASEGNI-FVDGIDIKELGVNNYQKLIA--CVLQD-----DRLFSGTLRDNICS 589
Cdd:PRK10636 337 PGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYFAQHQLEFLRAdeSPLQHlarlaPQELEQKLRDYLGG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 590 FSTQIDdnwliecarfaQIHDDIERMPMGydtligelgeglsggQKQRIFIARAIYKKPSILFMDEATSSLDHTNEQYIN 669
Cdd:PRK10636 417 FGFQGD-----------KVTEETRRFSGG---------------EKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALT 470
|
170 180
....*....|....*....|..
gi 1533513286 670 DAIKSLNITRIVIAHRKSTINS 691
Cdd:PRK10636 471 EALIDFEGALVVVSHDRHLLRS 492
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
509-661 |
1.34e-04 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 44.83 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 509 LRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDG-----IDIKELGvnnyqklIACVLQDDRLFSG-T 582
Cdd:PRK11650 20 IKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGrvvneLEPADRD-------IAMVFQNYALYPHmS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 583 LRDN------ICSFS-TQIDDNwLIECARFAQIHDDIERMPM----GydtligelgeglsggQKQRIFIARAIYKKPSIL 651
Cdd:PRK11650 93 VRENmayglkIRGMPkAEIEER-VAEAARILELEPLLDRKPRelsgG---------------QRQRVAMGRAIVREPAVF 156
|
170
....*....|
gi 1533513286 652 FMDEATSSLD 661
Cdd:PRK11650 157 LFDEPLSNLD 166
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
510-661 |
1.51e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 45.24 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 510 RHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIF--------------VDGIDikeLGVNNYQKLIACvlqd 575
Cdd:PLN03073 526 KNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFrsakvrmavfsqhhVDGLD---LSSNPLLYMMRC---- 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 576 drlFSGT----LRDNICSFStqiddnwliecarfaqIHDDIERMPMgYdTLigelgeglSGGQKQRIFIARAIYKKPSIL 651
Cdd:PLN03073 599 ---FPGVpeqkLRAHLGSFG----------------VTGNLALQPM-Y-TL--------SGGQKSRVAFAKITFKKPHIL 649
|
170
....*....|
gi 1533513286 652 FMDEATSSLD 661
Cdd:PLN03073 650 LLDEPSNHLD 659
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
505-661 |
1.74e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 44.53 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 505 ASYTLRHlnieiqpGEHVAITGASGTGKTTLLKVLCGLFP-ASEGNIFVDGidiKELGVNNYQKLIA---CVLQDDRLFS 580
Cdd:PRK13549 281 VSFSLRR-------GEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDG---KPVKIRNPQQAIAqgiAMVPEDRKRD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 581 GTLRD-----NIC-------SFSTQIDDNwliecARFAQIHDDIERMPMGYDTLIGELGEGLSGGQkQRIFIARAIYKKP 648
Cdd:PRK13549 351 GIVPVmgvgkNITlaaldrfTGGSRIDDA-----AELKTILESIQRLKVKTASPELAIARLSGGNQ-QKAVLAKCLLLNP 424
|
170
....*....|...
gi 1533513286 649 SILFMDEATSSLD 661
Cdd:PRK13549 425 KILILDEPTRGID 437
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
511-695 |
2.08e-04 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 43.44 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 511 HLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKEL-GVNNYQKLIACVLQDDRLF-SGTLRDN-I 587
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLpGHQIARMGVVRTFQHVRLFrEMTVIENlL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 588 CSFSTQIDDNW---LIECARFAQIHDD-IERMP-----MGYDTLIGELGEGLSGGQKQRIFIARAIYKKPSILFMDEATS 658
Cdd:PRK11300 103 VAQHQQLKTGLfsgLLKTPAFRRAESEaLDRAAtwlerVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAA 182
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1533513286 659 SLDHTNEQYINDAIKSL----NITRIVIAHRKSTINS-ADRI 695
Cdd:PRK11300 183 GLNPKETKELDELIAELrnehNVTVLLIEHDMKLVMGiSDRI 224
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
512-587 |
2.44e-04 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 43.60 E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 512 LNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKEL---GVNNYQKLIACVLQDDRLFSG-TLRDNI 587
Cdd:PRK11831 26 ISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMsrsRLYTVRKRMSMLFQSGALFTDmNVFDNV 105
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
492-560 |
4.52e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 42.47 E-value: 4.52e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1533513286 492 LSAKNISYKYDSYAsyTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGL--FPASEGNIFVDGIDIKEL 560
Cdd:PRK09580 2 LSIKDLHVSVEDKA--ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLEL 70
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
172-435 |
4.84e-04 |
|
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: 42.94 E-value: 4.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 172 LYSALTKIF------FLSIIIESINLVMPVATQLVMDHAIPANDSGLLTLIcFGLVFFV-ALRTITGLIRSWTV------ 238
Cdd:cd18565 6 LASILNRLFdlapplLIGVAIDAVFNGEASFLPLVPASLGPADPRGQLWLL-GGLTVAAfLLESLFQYLSGVLWrrfaqr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 239 ----LIMSSFINAQwqkgllqhllKLPLEYFERRKIGDIQSRFGS-LNTLQETFTTSVVGAIIDSIMIIGLLIMLVLYGG 313
Cdd:cd18565 85 vqhdLRTDTYDHVQ----------RLDMAFFEDRQTGDLMSVLNNdVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 314 WLTWFVILFT-----CLYVFIRVLTyNRYRQLSEESlikdARANSFFMETLYGIATVKVQGLNKR------------REE 376
Cdd:cd18565 155 QLALVALLPVpliiaGTYWFQRRIE-PRYRAVREAV----GDLNARLENNLSGIAVIKAFTAEDFerervadaseeyRDA 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1533513286 377 NWfnlevdsinTGIKVSrlNLFFGGINTLIATMEqILILWLGASLVISGN------MTIGMFVAF 435
Cdd:cd18565 230 NW---------RAIRLR--AAFFPVIRLVAGAGF-VATFVVGGYWVLDGPplftgtLTVGTLVTF 282
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
519-700 |
4.85e-04 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 43.27 E-value: 4.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 519 GEHVAITGASGTGKTTLLKVLCGLFP-ASEGNIFVDGidiKELGVNNYQKLIA---CVLQDDRLFSGTLRD-----NIC- 588
Cdd:TIGR02633 286 GEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFING---KPVDIRNPAQAIRagiAMVPEDRKRHGIVPIlgvgkNITl 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 589 ------SFSTQIDDnwlieCARFAQIHDDIERMPMGYDTLIGELGEGLSGGQkQRIFIARAIYKKPSILFMDEATSSLDH 662
Cdd:TIGR02633 363 svlksfCFKMRIDA-----AAELQIIGSAIQRLKVKTASPFLPIGRLSGGNQ-QKAVLAKMLLTNPRVLILDEPTRGVDV 436
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1533513286 663 TNEQYINDAIKSL---NITRIVIAHR-KSTINSADRIIALQE 700
Cdd:TIGR02633 437 GAKYEIYKLINQLaqeGVAIIVVSSElAEVLGLSDRVLVIGE 478
|
|
| HerA |
COG0433 |
Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase ... |
511-558 |
6.22e-04 |
|
Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase domains [Replication, recombination and repair];
Pssm-ID: 440202 [Multi-domain] Cd Length: 388 Bit Score: 42.67 E-value: 6.22e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1533513286 511 HLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVdgIDIK 558
Cdd:COG0433 39 YLDLDKLLNRHILILGATGSGKSNTLQVLLEELSRAGVPVLV--FDPH 84
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
263-441 |
6.61e-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: 42.21 E-value: 6.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 263 EYFERRKIGDIQSRF----GSLNTLQETFTTSVVGAIIDSIMIIGLLIMLvlYGGWLTWFVILFTCLYVFIRVLTYNRYR 338
Cdd:cd18560 87 DWHLSKKTGEVVRIMdrgtESANTLLSYLVFYLVPTLLELIVVSVVFAFH--FGAWLALIVFLSVLLYGVFTIKVTEWRT 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 339 QLSEESLIKDARANSFFMETLYGIATVKVQGlNKRREENWFNLEVD-----SINTGIKVSRLNLffggINTLIATMEQIL 413
Cdd:cd18560 165 KFRRAANKKDNEAHDIAVDSLLNFETVKYFT-NEKYEVDRYGEAVKeyqksSVKVQASLSLLNV----GQQLIIQLGLTL 239
|
170 180
....*....|....*....|....*...
gi 1533513286 414 ILWLGASLVISGNMTIGMFVAFSSYRGQ 441
Cdd:cd18560 240 GLLLAGYRVVDGGLSVGDFVAVNTYIFQ 267
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
523-684 |
7.44e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 42.01 E-value: 7.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 523 AITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKL------IACVLQDDRLFSGTLRDNICSFSTQ--- 593
Cdd:PRK14271 51 SLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNYRDVlefrrrVGMLFQRPNPFPMSIMDNVLAGVRAhkl 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 594 --------IDDNWLIECARFAQIHDDIERMPMgydtligelgeGLSGGQKQRIFIARAIYKKPSILFMDEATSSLDHTNE 665
Cdd:PRK14271 131 vprkefrgVAQARLTEVGLWDAVKDRLSDSPF-----------RLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTT 199
|
170 180
....*....|....*....|.
gi 1533513286 666 QYINDAIKSL--NITRIVIAH 684
Cdd:PRK14271 200 EKIEEFIRSLadRLTVIIVTH 220
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
509-557 |
7.90e-04 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 42.75 E-value: 7.90e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1533513286 509 LRHLNIEIQPGEHVAITGASGTGKT-TLLKVLcGLFPAS----EGNIFVDGIDI 557
Cdd:COG4172 26 VKGVSFDIAAGETLALVGESGSGKSvTALSIL-RLLPDPaahpSGSILFDGQDL 78
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
508-661 |
8.12e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 42.26 E-value: 8.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 508 TLRHLN---IEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKE---LGVNNYQKLIACVLQDDrlfSG 581
Cdd:PRK11308 27 LVKALDgvsFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKadpEAQKLLRQKIQIVFQNP---YG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 582 TL--RDNIcsfSTQIDDNWLIEC-----ARFAQIHDDIERM---PMGYDtligELGEGLSGGQKQRIFIARAIYKKPSIL 651
Cdd:PRK11308 104 SLnpRKKV---GQILEEPLLINTslsaaERREKALAMMAKVglrPEHYD----RYPHMFSGGQRQRIAIARALMLDPDVV 176
|
170
....*....|
gi 1533513286 652 FMDEATSSLD 661
Cdd:PRK11308 177 VADEPVSALD 186
|
|
| CpaF |
COG4962 |
Pilus assembly protein, ATPase of CpaF family [Intracellular trafficking, secretion, and ... |
524-547 |
8.31e-04 |
|
Pilus assembly protein, ATPase of CpaF family [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 443988 [Multi-domain] Cd Length: 386 Bit Score: 42.46 E-value: 8.31e-04
10 20
....*....|....*....|....
gi 1533513286 524 ITGASGTGKTTLLKVLCGLFPASE 547
Cdd:COG4962 187 VSGGTGSGKTTLLNALSGFIPPDE 210
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
516-689 |
8.34e-04 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 42.56 E-value: 8.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 516 IQPGEHVAITGASGTGKTTLLKVLCGLFPAS--EGNIFVDGIDIKElgvnNYQKLIACVLQDDRLFSG-TLRDNI--CSF 590
Cdd:PLN03211 91 ASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTK----QILKRTGFVTQDDILYPHlTVRETLvfCSL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 591 -----STQIDDNWLIECARFAQIH-DDIERMPMGyDTLIGELGEGlsggQKQRIFIARAIYKKPSILFMDEATSSLDHTn 664
Cdd:PLN03211 167 lrlpkSLTKQEKILVAESVISELGlTKCENTIIG-NSFIRGISGG----ERKRVSIAHEMLINPSLLILDEPTSGLDAT- 240
|
170 180
....*....|....*....|....*
gi 1533513286 665 eqyindAIKSLNITRIVIAHRKSTI 689
Cdd:PLN03211 241 ------AAYRLVLTLGSLAQKGKTI 259
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
286-437 |
9.75e-04 |
|
Six-transmembrane helical domain 2 (TMD2) 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: 350022 [Multi-domain] Cd Length: 317 Bit Score: 41.67 E-value: 9.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 286 TFTTSVVGAIIDSI--MIIGLLIMLVLygGW------LTWFVILFTCLYVFIRVLTynryrQLSEESLIKDARANSFFME 357
Cdd:cd18578 126 GLVGDRLGLILQAIvtLVAGLIIAFVY--GWklalvgLATVPLLLLAGYLRMRLLS-----GFEEKNKKAYEESSKIASE 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 358 TLYGIATVkvQGLNKrreENWF-----NLEVDSINTGIKVSRLNLFFGGINTLIATMEQILILWLGASLVISGNMTIG-M 431
Cdd:cd18578 199 AVSNIRTV--ASLTL---EDYFlekyeEALEEPLKKGLRRALISGLGFGLSQSLTFFAYALAFWYGGRLVANGEYTFEqF 273
|
....*.
gi 1533513286 432 FVAFSS 437
Cdd:cd18578 274 FIVFMA 279
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
490-699 |
1.10e-03 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 41.31 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 490 VSLSAKNISYkydSYASYTLRH-LNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKL 568
Cdd:PRK10575 10 TTFALRNVSF---RVPGRTLLHpLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 569 IACVLQDDRLFSG-TLRD--NICSFStqiddnWLIECARFAQihDDIERMP-----MGYDTLIGELGEGLSGGQKQRIFI 640
Cdd:PRK10575 87 VAYLPQQLPAAEGmTVRElvAIGRYP------WHGALGRFGA--ADREKVEeaislVGLKPLAHRLVDSLSGGERQRAWI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1533513286 641 ARAIYKKPSILFMDEATSSLDHTNEQYINDAIKSLN----ITRIVIAHrksTINSA----DRIIALQ 699
Cdd:PRK10575 159 AMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSqergLTVIAVLH---DINMAarycDYLVALR 222
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
503-696 |
1.16e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 42.10 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 503 SYASYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDgIDIkelgvnNY--QKliacvLQDDrlFS 580
Cdd:PRK13409 349 KLGDFSLEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKI------SYkpQY-----IKPD--YD 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 581 GTLRDNICSFSTQIDDNWL-IECARFAQIHDDIERMpmgYDTLigelgeglSGGQKQRIFIARAIYKKPSILFMDEATSS 659
Cdd:PRK13409 415 GTVEDLLRSITDDLGSSYYkSEIIKPLQLERLLDKN---VKDL--------SGGELQRVAIAACLSRDADLYLLDEPSAH 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1533513286 660 LDhtNEQYIN--DAIKSL----NITRIVIAHRKSTINS-ADRII 696
Cdd:PRK13409 484 LD--VEQRLAvaKAIRRIaeerEATALVVDHDIYMIDYiSDRLM 525
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
263-435 |
1.17e-03 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, 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. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 41.38 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 263 EYFERRKIGDIQSRFGS-LNTLQETFTTSVVGAIIDSIMIIGLLIMLVLYGGWLTwfVILFTCLYVFIRVLT-YNRY-RQ 339
Cdd:cd18574 91 AFFDTHRTGELVNRLTAdVQEFKSSFKQCVSQGLRSVTQTVGCVVSLYLISPKLT--LLLLVIVPVVVLVGTlYGSFlRK 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 340 LSEESLIKDARANSFFMETLYGIATVKVQGlNKRREENWFNLEVDsintgiKVSRLN--------LFFGGINTLIATMeq 411
Cdd:cd18574 169 LSRRAQAQVAKATGVADEALGNIRTVRAFA-MEDRELELYEEEVE------KAAKLNeklglgigIFQGLSNLALNGI-- 239
|
170 180
....*....|....*....|....*
gi 1533513286 412 ILI-LWLGASLVISGNMTIGMFVAF 435
Cdd:cd18574 240 VLGvLYYGGSLVSRGELTAGDLMSF 264
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
511-557 |
1.41e-03 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 40.25 E-value: 1.41e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1533513286 511 HLNIE---IQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDI 557
Cdd:cd03222 14 FLLVElgvVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITP 63
|
|
| PRK15177 |
PRK15177 |
Vi polysaccharide ABC transporter ATP-binding protein VexC; |
520-565 |
1.63e-03 |
|
Vi polysaccharide ABC transporter ATP-binding protein VexC;
Pssm-ID: 185099 [Multi-domain] Cd Length: 213 Bit Score: 40.43 E-value: 1.63e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1533513286 520 EHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNY 565
Cdd:PRK15177 14 EHIGILAAPGSGKTTLTRLLCGLDAPDEGDFIGLRGDALPLGANSF 59
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
492-675 |
1.78e-03 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 40.87 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 492 LSAKNISYKYDSyaSYTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIfvdgidikelgvnnyqkliac 571
Cdd:PRK09544 5 VSLENVSVSFGQ--RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI--------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 572 vLQDDRLFSGTLRDNIcsfstQIDDNWLIECARFAQIH-----DDI----ERMPMGYdtLIGELGEGLSGGQKQRIFIAR 642
Cdd:PRK09544 62 -KRNGKLRIGYVPQKL-----YLDTTLPLTVNRFLRLRpgtkkEDIlpalKRVQAGH--LIDAPMQKLSGGETQRVLLAR 133
|
170 180 190
....*....|....*....|....*....|...
gi 1533513286 643 AIYKKPSILFMDEATSSLDHTNEQYINDAIKSL 675
Cdd:PRK09544 134 ALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQL 166
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
512-692 |
1.92e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 40.24 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 512 LNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFvdgidIKELGVNNYQKLIaCVLQDDRL---FSGTLRDNIC 588
Cdd:PRK13541 19 LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIY-----YKNCNINNIAKPY-CTYIGHNLglkLEMTVFENLK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 589 SFSTQIDDNWLIECA-RFAQIHDdiermpmgydtLIGELGEGLSGGQKQRIFIARAIYKKPSILFMDEATSSLDHTNEQY 667
Cdd:PRK13541 93 FWSEIYNSAETLYAAiHYFKLHD-----------LLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDL 161
|
170 180
....*....|....*....|....*...
gi 1533513286 668 INDAI-KSLNITRIVI--AHRKSTINSA 692
Cdd:PRK13541 162 LNNLIvMKANSGGIVLlsSHLESSIKSA 189
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
512-554 |
2.28e-03 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 40.30 E-value: 2.28e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1533513286 512 LNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPaSEGNIFVDG 554
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAG 56
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
511-661 |
2.37e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 41.26 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 511 HLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGN--IF---VDGIDIK----------------ELGVnnYQKLi 569
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEawLFgqpVDAGDIAtrrrvgymsqafslygELTV--RQNL- 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 570 acVLQdDRLFsGTLRDNIcsfSTQIDDnwLIEcaRF--AQIHDDI-ERMPMGydtligelgeglsggQKQRIFIARAIYK 646
Cdd:NF033858 361 --ELH-ARLF-HLPAAEI---AARVAE--MLE--RFdlADVADALpDSLPLG---------------IRQRLSLAVAVIH 414
|
170
....*....|....*
gi 1533513286 647 KPSILFMDEATSSLD 661
Cdd:NF033858 415 KPELLILDEPTSGVD 429
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
508-689 |
2.40e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.15 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 508 TLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIKELGVNNYQKLIACVLQD---DRLFSG--- 581
Cdd:PRK10938 18 TLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSDEWQRnntDMLSPGedd 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 582 ---TLRDNIcsfSTQIDDNWLieCARFAQIhddiermpMGYDTLIGELGEGLSGGQKQRIFIARAIYKKPSILFMDEATS 658
Cdd:PRK10938 98 tgrTTAEII---QDEVKDPAR--CEQLAQQ--------FGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFD 164
|
170 180 190
....*....|....*....|....*....|....
gi 1533513286 659 SLDHTNEQYINDAIKSLN---ITRIVIAHRKSTI 689
Cdd:PRK10938 165 GLDVASRQQLAELLASLHqsgITLVLVLNRFDEI 198
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
489-558 |
2.60e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 40.76 E-value: 2.60e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 489 PVSLSAKNISYKYDSYASYTLRHlnieiqpGEHVAITGASGTGKTTLLKVLCGLFPASEGNIFVDGIDIK 558
Cdd:PRK10762 255 EVRLKVDNLSGPGVNDVSFTLRK-------GEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVV 317
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
494-550 |
4.28e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 40.32 E-value: 4.28e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1533513286 494 AKNISYKYDSYAsyTLRHLNIEIQPGEHVAITGASGTGKTTLLKVLCGLFPASEGNI 550
Cdd:PRK11147 322 MENVNYQIDGKQ--LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI 376
|
|
| T2SSE |
pfam00437 |
Type II/IV secretion system protein; This family contains components of both the Type II ... |
524-585 |
5.08e-03 |
|
Type II/IV secretion system protein; This family contains components of both the Type II protein secretion system (T2SS), including Type 4 pilus (T4P), and Type IV protein secretion system (T4SS) from Gram-negative bacteria. VirB11 ATPase is a subunit of the Agrobacterium tumefaciens transfer DNA (T-DNA) transfer system, a type IV secretion pathway required for delivery of T-DNA and effector proteins to plant cells during infection. The cytoplasmic T2S E ATPase is a Zn-containing protein thought to provide the mechanical force for the secretion process. T2S-E contains Walker A and B motifs, that are essential for secretion and ATPase activity. ATPase PulE and XcpR from Klebsiella oxytoca and Pseudomonas aeruginosa respectively are required for protein secretion via the T2SS. ATPase PilB is required for T4P extension.
Pssm-ID: 425681 [Multi-domain] Cd Length: 269 Bit Score: 39.58 E-value: 5.08e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1533513286 524 ITGASGTGKTTLLKVLCGLFPASEGNIFV--DGIDIKELGVN----------NYQKLI-ACVLQD-DRLFSGTLRD 585
Cdd:pfam00437 135 VTGPTGSGKTTTLYAALGELNTRDENIVTveDPVEIQLEGINqvqlnaragvTFADLLrAILRQDpDRIMVGEIRD 210
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
263-373 |
5.98e-03 |
|
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: 39.41 E-value: 5.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533513286 263 EYFERRKIGDIQSRFGS-LNTLQETFTTSVVGAIIDSIMIIGLLIMLVLYGGWLTWFVILFTCLYVFIRvltyNRYRQLS 341
Cdd:cd18580 88 SFFDTTPSGRILNRFSKdIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLLQ----RYYLRTS 163
|
90 100 110
....*....|....*....|....*....|....*.
gi 1533513286 342 EES--LIKDARA--NSFFMETLYGIATVKVQGLNKR 373
Cdd:cd18580 164 RQLrrLESESRSplYSHFSETLSGLSTIRAFGWQER 199
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
636-698 |
9.70e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 38.57 E-value: 9.70e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1533513286 636 QRIFIARAIYKKPSILFMDEATSSLDHTNEQYINDAIKSL----NITRIVIAHRKSTI-NSADRIIAL 698
Cdd:PRK11022 160 QRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqqkeNMALVLITHDLALVaEAAHKIIVM 227
|
|
| |
