|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
23-597 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 718.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 23 KNTKGTVKRIWNYMGYEKAALMFVIFLVFVTTLLGLLGPYFMGVIIDQYIVPKDLNGTARMCMLLIAIYGVTVLLTWLQT 102
Cdd:COG1132 3 KSPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 103 YVMINVALKTIQKIRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFSLNWI 182
Cdd:COG1132 83 YLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 183 LALVTLITVPIMFFVTKKLVAYSGKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRISATKADT 262
Cdd:COG1132 163 LALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAAR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 263 FSAFIFPSMNFINNLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERVFEIMDEVP 342
Cdd:COG1132 243 LSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 343 EIQNKKDAFIVQNIQGHVELENVSFGYVENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGK 422
Cdd:COG1132 323 EIPDPPGAVPLPPVRGEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGV 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 423 DIKDYDINSLRSKIGVVLQDTYLFAGTIMDNIRYGRLHASDEEVINAAKAASAHSFIKHLPKQYETEIASEGSNLSQGQK 502
Cdd:COG1132 403 DIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQR 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 503 QLLAIARAILADADILILDEATSNIDTRTELQIQAGLNNLMRGRTSFVIAHRLKTIEKADQILVIKDGSILERGNHESLM 582
Cdd:COG1132 483 QRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELL 562
|
570
....*....|....*
gi 447166293 583 EDRGFYFELYTSQFK 597
Cdd:COG1132 563 ARGGLYARLYRLQFG 577
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
21-595 |
5.16e-176 |
|
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: 515.54 E-value: 5.16e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 21 KVKNTKGTVKRIWNYMGYEKAALMFVIFLVFVTTLLGLLGPYFMGVIIDQYIVPKDLNGTARMCMLLIAIYGVTVLLTWL 100
Cdd:COG2274 136 KRGEKPFGLRWFLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVIDRVLPNQDLSTLWVLAIGLLLALLFEGLLRLL 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 101 QTYVMINVALKTIQKIRQDIFEKIQTLSLRFFDVRSQGDLMSRVtNDIDNLNQALTQSVVQIISSALTFIGVTIAMFSLN 180
Cdd:COG2274 216 RSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIREFLTGSLLTALLDLLFVLIFLIVLFFYS 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 181 WILALVTLITVPIM----FFVTKKLVAYSgknfAKRQKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRIS 256
Cdd:COG2274 295 PPLALVVLLLIPLYvllgLLFQPRLRRLS----REESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNA 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 257 ATKADTFSAFIFPSMNFINNLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERVFE 336
Cdd:COG2274 371 RFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDD 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 337 IMDEVPEIQNKKDAFIVQNIQGHVELENVSFGYVENKT-ILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQG 415
Cdd:COG2274 451 ILDLPPEREEGRSKLSLPRLKGDIELENVSFRYPGDSPpVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSG 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 416 QIHIDGKDIKDYDINSLRSKIGVVLQDTYLFAGTIMDNIRYGRLHASDEEVINAAKAASAHSFIKHLPKQYETEIASEGS 495
Cdd:COG2274 531 RILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGS 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 496 NLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQAGLNNLMRGRTSFVIAHRLKTIEKADQILVIKDGSILER 575
Cdd:COG2274 611 NLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVED 690
|
570 580
....*....|....*....|
gi 447166293 576 GNHESLMEDRGFYFELYTSQ 595
Cdd:COG2274 691 GTHEELLARKGLYAELVQQQ 710
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
28-597 |
3.85e-149 |
|
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: 441.85 E-value: 3.85e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 28 TVKRIWNYMGYEK-----AALMFVIFLVFVTTLLGLLGPyfmgvIIDQYIVPKDLNGTARMCMLLIAIYGVTVLLTWLQT 102
Cdd:TIGR02203 1 TFRRLWSYVRPYKaglvlAGVAMILVAATESTLAALLKP-----LLDDGFGGRDRSVLWWVPLVVIGLAVLRGICSFVST 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 103 YVMINVALKTIQKIRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFSLNWI 182
Cdd:TIGR02203 76 YLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 183 LALVTLITVPI----MFFVTKKLVAYSgknfAKRQKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRISAT 258
Cdd:TIGR02203 156 LTLIVVVMLPVlsilMRRVSKRLRRIS----KEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 259 KADTFSAFIFPSMNFINNLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERVFEIM 338
Cdd:TIGR02203 232 KMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 339 DEVPEIQNKKDAfiVQNIQGHVELENVSFGYV-ENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQI 417
Cdd:TIGR02203 312 DSPPEKDTGTRA--IERARGDVEFRNVTFRYPgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 418 HIDGKDIKDYDINSLRSKIGVVLQDTYLFAGTIMDNIRYGRLH-ASDEEVINAAKAASAHSFIKHLPKQYETEIASEGSN 496
Cdd:TIGR02203 390 LLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEqADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVL 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 497 LSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQAGLNNLMRGRTSFVIAHRLKTIEKADQILVIKDGSILERG 576
Cdd:TIGR02203 470 LSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERG 549
|
570 580
....*....|....*....|.
gi 447166293 577 NHESLMEDRGFYFELYTSQFK 597
Cdd:TIGR02203 550 THNELLARNGLYAQLHNMQFR 570
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
33-595 |
2.98e-132 |
|
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: 399.58 E-value: 2.98e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 33 WNYMGYEKAALMFVIFLVFVTTLLGLLGPYFMGVIIDQYIVPKDLNGTArmcMLLIAIYGV----TVLLTWLQTYVMINV 108
Cdd:COG5265 29 PPYLRRRRRALAALLLLLLAAALALVVPPLLKDAIDALLSGAAALLVVP---VGLLLAYGLlrllSVLFGELRDALFARV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 109 ALKTIQKIRQDIFEKIQTLSLRFFDVRSQGDL---MSRVTNDIDNLnqaLTQSVVQIISSALTFIGVTIAMFSL-NWILA 184
Cdd:COG5265 106 TQRAVRRLALEVFRHLHALSLRFHLERQTGGLsrdIERGTKGIEFL---LRFLLFNILPTLLEIALVAGILLVKyDWWFA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 185 LVTLITVpimffvtkklVAYSGKNFA---KRQKDLGELNGFIEEAITGAdVTTL--YgkekETVQNFNkiNE-------- 251
Cdd:COG5265 183 LITLVTV----------VLYIAFTVVvteWRTKFRREMNEADSEANTRA-VDSLlnY----ETVKYFG--NEarearryd 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 252 ----QLRISATKADTfsafifpSMNFINnLGMGLVIGTGSVMVLnGMTTVGVIA--------AFIN-YSRQFSRPLSQFA 318
Cdd:COG5265 246 ealaRYERAAVKSQT-------SLALLN-FGQALIIALGLTAMM-LMAAQGVVAgtmtvgdfVLVNaYLIQLYIPLNFLG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 319 TLMNTIQAAVAGGERVFEIMDEVPEIQNKKDAFIVQNIQGHVELENVSFGYVENKTILKEVSLKARPGETIALVGPTGSG 398
Cdd:COG5265 317 FVYREIRQALADMERMFDLLDQPPEVADAPDAPPLVVGGGEVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 399 KTTIINLLTRFYDIQQGQIHIDGKDIKDYDINSLRSKIGVVLQDTYLFAGTIMDNIRYGRLHASDEEVINAAKAASAHSF 478
Cdd:COG5265 397 KSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 479 IKHLPKQYETEIASEGSNLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQAGLNNLMRGRTSFVIAHRLKTI 558
Cdd:COG5265 477 IESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTI 556
|
570 580 590
....*....|....*....|....*....|....*..
gi 447166293 559 EKADQILVIKDGSILERGNHESLMEDRGFYFELYTSQ 595
Cdd:COG5265 557 VDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQ 593
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
43-334 |
2.15e-128 |
|
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: 378.67 E-value: 2.15e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 43 LMFVIFLVFVTTLLGLLGPYFMGVIIDQYIVPK------DLNGTARMCMLLIAIYGVTVLLTWLQTYVMINVALKTIQKI 116
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEGLgggggvDFSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 117 RQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFSLNWILALVTLITVPIMFF 196
Cdd:cd18547 81 RKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 197 VTKKLVAYSGKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRISATKADTFSAFIFPSMNFINN 276
Cdd:cd18547 161 VTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKAQFYSGLLMPIMNFINN 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 447166293 277 LGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18547 241 LGYVLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAERV 298
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
32-596 |
3.06e-128 |
|
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: 388.29 E-value: 3.06e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 32 IWNYMGYEKAALMFVIFLVFVTTLLGLLGPYFMGVIIDQYIVPKDLNGTARMCMLLIAIYGVTVLLTWLQTYVMINVALK 111
Cdd:TIGR02204 9 LWPFVRPYRGRVLAALVALLITAAATLSLPYAVRLMIDHGFSKDSSGLLNRYFAFLLVVALVLALGTAARFYLVTWLGER 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 112 TIQKIRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFSLNWILALVTLITV 191
Cdd:TIGR02204 89 VVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVLLAV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 192 PI----MFFVTKKLVAYSGKNfakrQKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRISATKADTFSAFI 267
Cdd:TIGR02204 169 PLvllpILLFGRRVRKLSRES----QDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQRIRTRALL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 268 FPSMNFINNLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERVFEIMDEVPEIQ-- 345
Cdd:TIGR02204 245 TAIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELLQAEPDIKap 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 346 -NKKDafIVQNIQGHVELENVSFGYVE--NKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGK 422
Cdd:TIGR02204 325 aHPKT--LPVPLRGEIEFEQVNFAYPArpDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGV 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 423 DIKDYDINSLRSKIGVVLQDTYLFAGTIMDNIRYGRLHASDEEVINAAKAASAHSFIKHLPKQYETEIASEGSNLSQGQK 502
Cdd:TIGR02204 403 DLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQR 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 503 QLLAIARAILADADILILDEATSNIDTRTELQIQAGLNNLMRGRTSFVIAHRLKTIEKADQILVIKDGSILERGNHESLM 582
Cdd:TIGR02204 483 QRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELI 562
|
570
....*....|....
gi 447166293 583 EDRGFYFELYTSQF 596
Cdd:TIGR02204 563 AKGGLYARLARLQF 576
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
30-586 |
1.07e-127 |
|
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: 386.42 E-value: 1.07e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 30 KRIWNYMGYEKAALMFVIFLVFVTTLLGLLGPYFMGVIIDQYIVPK-DLNGTARMCMLLIAIYGVTVLLTWLQTYVMINV 108
Cdd:COG4988 6 KRLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIIGGaPLSALLPLLGLLLAVLLLRALLAWLRERAAFRA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 109 ALKTIQKIRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFSLNWILALVTL 188
Cdd:COG4988 86 AARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLDWLSGLILL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 189 ITVPI----MFFVTKKLVAYSGKNFAKrqkdLGELNGFIEEAITGadVTTL--YGKEKETVQNFNKINEQLRISatkadT 262
Cdd:COG4988 166 VTAPLiplfMILVGKGAAKASRRQWRA----LARLSGHFLDRLRG--LTTLklFGRAKAEAERIAEASEDFRKR-----T 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 263 FS----AFIfpS---MNFINNLGMGLVIGTGSVMVLNG-MTTVGVIAAFInYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:COG4988 235 MKvlrvAFL--SsavLEFFASLSIALVAVYIGFRLLGGsLTLFAALFVLL-LAPEFFLPLRDLGSFYHARANGIAAAEKI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 335 FEIMDEVPEIQNKKDAFIVQNIQGHVELENVSFGYVENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQ 414
Cdd:COG4988 312 FALLDAPEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYS 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 415 GQIHIDGKDIKDYDINSLRSKIGVVLQDTYLFAGTIMDNIRYGRLHASDEEVINAAKAASAHSFIKHLPKQYETEIASEG 494
Cdd:COG4988 392 GSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGG 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 495 SNLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQAGLNNLMRGRTSFVIAHRLKTIEKADQILVIKDGSILE 574
Cdd:COG4988 472 RGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVE 551
|
570
....*....|..
gi 447166293 575 RGNHESLMEDRG 586
Cdd:COG4988 552 QGTHEELLAKNG 563
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
107-592 |
6.78e-122 |
|
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: 371.79 E-value: 6.78e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 107 NVALKTIQKIRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFSLNWILALV 186
Cdd:COG4987 81 DATLRLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRVLLPLLVALLVILAAVAFLAFFSPALALV 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 187 TLITVPIMFFVTKKLVAYSGKNFAKRQKDL-GELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRISATKADTFSA 265
Cdd:COG4987 161 LALGLLLAGLLLPLLAARLGRRAGRRLAAArAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLSA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 266 FIFPSMNFINNLGMGLVIGTGSVMVLNGMTTVGVIAAFInysrqFSrPLSQFATLMNTIQAAVAGG------ERVFEIMD 339
Cdd:COG4987 241 LAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLV-----LA-ALALFEALAPLPAAAQHLGrvraaaRRLNELLD 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 340 EVPEIQNKKDAFIVQNiQGHVELENVSFGYVEN-KTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIH 418
Cdd:COG4987 315 APPAVTEPAEPAPAPG-GPSLELEDVSFRYPGAgRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSIT 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 419 IDGKDIKDYDINSLRSKIGVVLQDTYLFAGTIMDNIRYGRLHASDEEVINAAKAASAHSFIKHLPKQYETEIASEGSNLS 498
Cdd:COG4987 394 LGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLS 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 499 QGQKQLLAIARAILADADILILDEATSNIDTRTELQIQAGLNNLMRGRTSFVIAHRLKTIEKADQILVIKDGSILERGNH 578
Cdd:COG4987 474 GGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTH 553
|
490
....*....|....
gi 447166293 579 ESLMEDRGFYFELY 592
Cdd:COG4987 554 EELLAQNGRYRQLY 567
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
28-596 |
6.57e-121 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 369.73 E-value: 6.57e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 28 TVKRIWNYMGYEKAALMF-VIFLVFV----TTLLGLLGPyfmgvIIDQYIVPKDLNGTARMCMLLIAIYGVTVLLTWLQT 102
Cdd:PRK11176 12 TFRRLWPTIAPFKAGLIVaGVALILNaasdTFMLSLLKP-----LLDDGFGKADRSVLKWMPLVVIGLMILRGITSFISS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 103 YVMINVALKTIQKIRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFSLNWI 182
Cdd:PRK11176 87 YCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 183 LALVTLITVPIMFFVTKkLVAYSGKNFAKR-QKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRISATKAD 261
Cdd:PRK11176 167 LSLILIVIAPIVSIAIR-VVSKRFRNISKNmQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQGMKMV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 262 TFSAFIFPSMNFINNLGMGLVIGTGSVMVLNGMTTVGVIAafINYSRQFS--RPLSQFATLMNTIQAAVAGGERVFEIMD 339
Cdd:PRK11176 246 SASSISDPIIQLIASLALAFVLYAASFPSVMDTLTAGTIT--VVFSSMIAlmRPLKSLTNVNAQFQRGMAACQTLFAILD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 340 EVPEIQNKKdaFIVQNIQGHVELENVSFGYVENKTI-LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIH 418
Cdd:PRK11176 324 LEQEKDEGK--RVIERAKGDIEFRNVTFTYPGKEVPaLRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEIL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 419 IDGKDIKDYDINSLRSKIGVVLQDTYLFAGTIMDNIRYGRL-HASDEEVINAAKAASAHSFIKHLPKQYETEIASEGSNL 497
Cdd:PRK11176 402 LDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTeQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLL 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 498 SQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQAGLNNLMRGRTSFVIAHRLKTIEKADQILVIKDGSILERGN 577
Cdd:PRK11176 482 SGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGT 561
|
570
....*....|....*....
gi 447166293 578 HESLMEDRGFYFELYTSQF 596
Cdd:PRK11176 562 HAELLAQNGVYAQLHKMQF 580
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
358-586 |
1.44e-120 |
|
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: 356.15 E-value: 1.44e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 358 GHVELENVSFGYVENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINSLRSKIG 437
Cdd:cd03254 1 GEIEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 438 VVLQDTYLFAGTIMDNIRYGRLHASDEEVINAAKAASAHSFIKHLPKQYETEIASEGSNLSQGQKQLLAIARAILADADI 517
Cdd:cd03254 81 VVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447166293 518 LILDEATSNIDTRTELQIQAGLNNLMRGRTSFVIAHRLKTIEKADQILVIKDGSILERGNHESLMEDRG 586
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
23-591 |
4.92e-120 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 371.75 E-value: 4.92e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 23 KNTKGTVKRIWNYMGYEKAALMFVIFLVFVTTLLGLLGPYFMGVIIDQYIVPKDLNGTAR----MCMLLIAIYGVTVLLT 98
Cdd:TIGR00958 143 SETADLLFRLLGLSGRDWPWLISAFVFLTLSSLGEMFIPFYTGRVIDTLGGDKGPPALASaiffMCLLSIASSVSAGLRG 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 99 WLQTYVMINVALKtiqkIRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFS 178
Cdd:TIGR00958 223 GSFNYTMARINLR----IREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLW 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 179 LNWILALVTLITVPIMFFVTKKLVAYSGKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKETVQNFN-KINEQLRISA 257
Cdd:TIGR00958 299 LSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKeALEETLQLNK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 258 TKADTFSAFIFpSMNFINNLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERVFEI 337
Cdd:TIGR00958 379 RKALAYAGYLW-TTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEY 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 338 MDEVPEIQNKkDAFIVQNIQGHVELENVSFGYVE--NKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQG 415
Cdd:TIGR00958 458 LDRKPNIPLT-GTLAPLNLEGLIEFQDVSFSYPNrpDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGG 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 416 QIHIDGKDIKDYDINSLRSKIGVVLQDTYLFAGTIMDNIRYGRLHASDEEVINAAKAASAHSFIKHLPKQYETEIASEGS 495
Cdd:TIGR00958 537 QVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGS 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 496 NLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQAGLNnlMRGRTSFVIAHRLKTIEKADQILVIKDGSILER 575
Cdd:TIGR00958 617 QLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRS--RASRTVLLIAHRLSTVERADQILVLKKGSVVEM 694
|
570
....*....|....*.
gi 447166293 576 GNHESLMEDRGFYFEL 591
Cdd:TIGR00958 695 GTHKQLMEDQGCYKHL 710
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
360-592 |
4.92e-119 |
|
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: 352.30 E-value: 4.92e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYVENKT-ILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINSLRSKIGV 438
Cdd:cd03251 1 VEFKNVTFRYPGDGPpVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 439 VLQDTYLFAGTIMDNIRYGRLHASDEEVINAAKAASAHSFIKHLPKQYETEIASEGSNLSQGQKQLLAIARAILADADIL 518
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447166293 519 ILDEATSNIDTRTELQIQAGLNNLMRGRTSFVIAHRLKTIEKADQILVIKDGSILERGNHESLMEDRGFYFELY 592
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
360-595 |
2.55e-111 |
|
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: 332.66 E-value: 2.55e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYVENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINSLRSKIGVV 439
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 440 LQDTYLFAGTIMDNIRYGRLHASDEEVINAAKAASAHSFIKHLPKQYETEIASEGSNLSQGQKQLLAIARAILADADILI 519
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447166293 520 LDEATSNIDTRTELQIQAGLNNLMRGRTSFVIAHRLKTIEKADQILVIKDGSILERGNHESLMEDRGFYFELYTSQ 595
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
360-595 |
1.04e-106 |
|
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: 321.03 E-value: 1.04e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYVE--NKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINSLRSKIG 437
Cdd:cd03249 1 IEFKNVSFRYPSrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 438 VVLQDTYLFAGTIMDNIRYGRLHASDEEVINAAKAASAHSFIKHLPKQYETEIASEGSNLSQGQKQLLAIARAILADADI 517
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447166293 518 LILDEATSNIDTRTELQIQAGLNNLMRGRTSFVIAHRLKTIEKADQILVIKDGSILERGNHESLMEDRGFYFELYTSQ 595
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
165-596 |
7.92e-106 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 330.77 E-value: 7.92e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 165 SALTFIGVTIAM-FSLNWILALVtLITVPIMFFVTKKLVAysgknfaKRQKDL--------GELNGFIEEAITGADVttl 235
Cdd:PRK13657 139 ATLVALVVLLPLaLFMNWRLSLV-LVVLGIVYTLITTLVM-------RKTKDGqaaveehyHDLFAHVSDAIGNVSV--- 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 236 ygkeketVQNFNKINEQLRISATKADTFSAFIFPSMNF------IN----NLGMGLVIGTGSVMVLNGMTTVGVIAAFIN 305
Cdd:PRK13657 208 -------VQSYNRIEAETQALRDIADNLLAAQMPVLSWwalasvLNraasTITMLAILVLGAALVQKGQLRVGEVVAFVG 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 306 YSRQFSRPLSQFATLMNTIQAAVAGGERVFEIMDEVPEIQNKKDAFIVQNIQGHVELENVSFGYVENKTILKEVSLKARP 385
Cdd:PRK13657 281 FATLLIGRLDQVVAFINQVFMAAPKLEEFFEVEDAVPDVRDPPGAIDLGRVKGAVEFDDVSFSYDNSRQGVEDVSFEAKP 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 386 GETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINSLRSKIGVVLQDTYLFAGTIMDNIRYGRLHASDEE 465
Cdd:PRK13657 361 GQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEE 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 466 VINAAKAASAHSFIKHLPKQYETEIASEGSNLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQAGLNNLMRG 545
Cdd:PRK13657 441 MRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKG 520
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 447166293 546 RTSFVIAHRLKTIEKADQILVIKDGSILERGNHESLMEDRGFYFELYTSQF 596
Cdd:PRK13657 521 RTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALLRAQG 571
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
28-595 |
4.76e-99 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 313.58 E-value: 4.76e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 28 TVKRIWNYMGYEKAALMFVIFLVFVTTLLGLLGPYFMGVIIDQyIVPKD---LNGTARMCMLLIAIYGVTVLLTWLQTYV 104
Cdd:PRK10790 10 TLKRLLAYGSPWRKPLGLAVLMLWVAAAAEVSGPLLISYFIDN-MVAKGnlpLGLVAGLAAAYVGLQLLAAGLHYAQSLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 105 MINVALKTIQKIRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQaLTQSVVQIISSALTFIGVT-IAMFSLNWIL 183
Cdd:PRK10790 89 FNRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRD-LYVTVVATVLRSAALIGAMlVAMFSLDWRM 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 184 ALVTLITVPIMFFVTKKLVAYSGKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEK---ETVQNFNKINEQLRISATKA 260
Cdd:PRK10790 168 ALVAIMIFPAVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQArfgERMGEASRSHYMARMQTLRL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 261 DTFsaFIFPSMNFINNL---GMGLVIGTGSVmvlnGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERVFEI 337
Cdd:PRK10790 248 DGF--LLRPLLSLFSALilcGLLMLFGFSAS----GTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERVFEL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 338 MDEvPEIQNKKDAFIVQniQGHVELENVSFGYVENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQI 417
Cdd:PRK10790 322 MDG-PRQQYGNDDRPLQ--SGRIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEI 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 418 HIDGKDIKDYDINSLRSKIGVVLQDTYLFAGTIMDNIRYGRlHASDEEVINAAKAASAHSFIKHLPKQYETEIASEGSNL 497
Cdd:PRK10790 399 RLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGR-DISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNL 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 498 SQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQAGLNNLMRGRTSFVIAHRLKTIEKADQILVIKDGSILERGN 577
Cdd:PRK10790 478 SVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGT 557
|
570
....*....|....*...
gi 447166293 578 HESLMEDRGFYFELYTSQ 595
Cdd:PRK10790 558 HQQLLAAQGRYWQMYQLQ 575
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
47-595 |
1.82e-91 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 292.77 E-value: 1.82e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 47 IFLVFVTTLLGLLGPYFMGVIIDQyIVPKDLngTARMCMLLIAIYGVTVLLTWLQTYV----MINVALKTIQKIRQDIFE 122
Cdd:PRK10789 1 VALLIIIAMLQLIPPKVVGIIVDG-VTEQHM--TTGQILMWIGTMVLIAVVVYLLRYVwrvlLFGASYQLAVELREDFYR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 123 KIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFS-LNWILALVTLITVPIMFFVTKKL 201
Cdd:PRK10789 78 QLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIVMSTqISWQLTLLALLPMPVMAIMIKRY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 202 VAYSGKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQ-----LRISATKAdTFSAFIFPSMNFINN 276
Cdd:PRK10789 158 GDQLHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDtgkknMRVARIDA-RFDPTIYIAIGMANL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 277 LGmglvIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERVFEIMDEVPEIQNKKDAFIVQni 356
Cdd:PRK10789 237 LA----IGGGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAEAPVVKDGSEPVPEG-- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 357 QGHVELENVSFGYVEN-KTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINSLRSK 435
Cdd:PRK10789 311 RGELDVNIRQFTYPQTdHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSR 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 436 IGVVLQDTYLFAGTIMDNIRYGRLHASDEEVINAAKAASAHSFIKHLPKQYETEIASEGSNLSQGQKQLLAIARAILADA 515
Cdd:PRK10789 391 LAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNA 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 516 DILILDEATSNIDTRTELQIQAGLNNLMRGRTSFVIAHRLKTIEKADQILVIKDGSILERGNHESLMEDRGFYFELYTSQ 595
Cdd:PRK10789 471 EILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQ 550
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
43-334 |
1.45e-88 |
|
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: 276.19 E-value: 1.45e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 43 LMFVIFLVFVTTLLGLLGPYFMGVIIDQYIVP--KDLNGTARMCMLLIAIYGVTVLLTWLQTYVMINVALKTIQKIRQDI 120
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIDDYIVPgqGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 121 FEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFSLNWILALVTLITVPIMFFVTKK 200
Cdd:cd18544 81 FSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 201 LVAYSGKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRISATKADTFSAFIFPSMNFINNLGMG 280
Cdd:cd18544 161 FRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 447166293 281 LVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18544 241 LVLWYGGGQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAEKFNILQSAMASAERI 294
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
40-567 |
7.44e-87 |
|
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: 279.56 E-value: 7.44e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 40 KAALMFVIFLVFVTTLLGLLGPYFMGVIIDQYIVPKDLNGTARM-CMLLIAIYGVTVLLTWLQTYVMINVALKTIQKIRQ 118
Cdd:TIGR02857 2 RRALALLALLGVLGALLIIAQAWLLARVVDGLISAGEPLAELLPaLGALALVLLLRALLGWLQERAAARAAAAVKSQLRE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 119 DIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFSLNWILALVTLITVP-IMFFV 197
Cdd:TIGR02857 82 RLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFARYLPQLVLAVIVPLAILAAVFPQDWISGLILLLTAPlIPIFM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 198 TkkLVAYSGKNFAKRQ-KDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRiSAT----KADTFSAFIfpsMN 272
Cdd:TIGR02857 162 I--LIGWAAQAAARKQwAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEYR-ERTmrvlRIAFLSSAV---LE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 273 FINNLGMGLVIGTGSVMVLNG-MTTVGVIAAFInYSRQFSRPLSQFATLMNTIQAAVAGGERVFEIMDEVPEI-QNKKDA 350
Cdd:TIGR02857 236 LFATLSVALVAVYIGFRLLAGdLDLATGLFVLL-LAPEFYLPLRQLGAQYHARADGVAAAEALFAVLDAAPRPlAGKAPV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 351 FIVQNIQghVELENVSFGYVENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDIN 430
Cdd:TIGR02857 315 TAAPASS--LEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADAD 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 431 SLRSKIGVVLQDTYLFAGTIMDNIRYGRLHASDEEVINAAKAASAHSFIKHLPKQYETEIASEGSNLSQGQKQLLAIARA 510
Cdd:TIGR02857 393 SWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARA 472
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 447166293 511 ILADADILILDEATSNIDTRTELQIQAGLNNLMRGRTSFVIAHRLKTIEKADQILVI 567
Cdd:TIGR02857 473 FLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
42-334 |
2.98e-85 |
|
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: 267.41 E-value: 2.98e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 42 ALMFVIFLVFVTTLLGLLGPYFMGVIIDQYIVPKDLNGTARMCMLLIAIYGVTVLLTWLQTYVMINVALKTIQKIRQDIF 121
Cdd:cd18545 1 KLLLALLLMLLSTAASLAGPYLIKIAIDEYIPNGDLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 122 EKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFSLNWILALVTLITVPIMFFVTKKL 201
Cdd:cd18545 81 SHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 202 VAYSGKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRISATKADTFSAFIFPSMNFINNLGMGL 281
Cdd:cd18545 161 RRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVELISALGTAL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 447166293 282 VIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18545 241 VYWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASAERI 293
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
31-591 |
2.94e-83 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 271.76 E-value: 2.94e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 31 RIWNYMGYEKAALMFVIFLVFVTTLLGLLGPYFMGVIIDQYIVPKDLNGTarmcMLLIAIYGVTVLLTwlqtYVMI---- 106
Cdd:TIGR01192 9 RALSYLNVHKNRVLLIVIANITLAAITIAEPILFGRIIDAISSKSDVLPT----LALWAGFGVFNTIA----YVLVarea 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 107 -NVALKTIQKIRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFSLNWILAL 185
Cdd:TIGR01192 81 dRLAHGRRATLLTEAFGRIISMPLSWHQQRGTSNALHTLLRATETLFGLWLEFMRQHLATFVALFLLIPTAFAMDWRLSI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 186 VtLITVPIMFFVTKKLVAYSGKNF-AKRQKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRISATKADTFS 264
Cdd:TIGR01192 161 V-LMVLGILYILIAKLVMQRTKNGqAAVEHHYHNVFKHVSDSISNVSVVHSYNRIEAETSALKQFTNNLLSAQYPVLDWW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 265 AFIFPSMNFINNLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERVFEIMDEVPEI 344
Cdd:TIGR01192 240 ALASGLNRMASTISMMCILVIGTVLVIKGELSVGEVIAFIGFANLLIGRLDQMSGFITQIFEARAKLEDFFDLEDSVFQR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 345 QNKKDAFIVQNIQGHVELENVSFGYVENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDI 424
Cdd:TIGR01192 320 EEPADAPELPNVKGAVEFRHITFEFANSSQGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 425 KDYDINSLRSKIGVVLQDTYLFAGTIMDNIRYGRLHASDEEVINAAKAASAHSFIKHLPKQYETEIASEGSNLSQGQKQL 504
Cdd:TIGR01192 400 NTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQR 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 505 LAIARAILADADILILDEATSNIDTRTELQIQAGLNNLMRGRTSFVIAHRLKTIEKADQILVIKDGSILERGNHESLMED 584
Cdd:TIGR01192 480 LAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQK 559
|
....*..
gi 447166293 585 RGFYFEL 591
Cdd:TIGR01192 560 DGRFYKL 566
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
39-593 |
1.30e-79 |
|
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: 265.45 E-value: 1.30e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 39 EKAALMFVIFLVFVTTLLGLLGPYFMGVIIDQYIvPKDLNGTARMCML-LIAIYGVTVLLTWLQTYVMI----NVALKTI 113
Cdd:TIGR01193 154 QKKLIVNIVIAAIIVTLISIAGSYYLQKIIDTYI-PHKMMGTLGIISIgLIIAYIIQQILSYIQIFLLNvlgqRLSIDII 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 114 QKIRQDIFEkiqtLSLRFFDVRSQGDLMSRVTnDIDNLNQALTQSVVQIISSALTFIGVTIAMFSLNWILALVTLITVPI 193
Cdd:TIGR01193 233 LSYIKHLFE----LPMSFFSTRRTGEIVSRFT-DASSIIDALASTILSLFLDMWILVIVGLFLVRQNMLLFLLSLLSIPV 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 194 MffvtkKLVAYSGKN-FAKRQKDLGE----LNGFIEEAITGADVTTLYGKEKETvqnFNKINEQL------RISATKADT 262
Cdd:TIGR01193 308 Y-----AVIIILFKRtFNKLNHDAMQanavLNSSIIEDLNGIETIKSLTSEAER---YSKIDSEFgdylnkSFKYQKADQ 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 263 FSAFIFPSMNFINNLgmgLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERVFEIMDEVP 342
Cdd:TIGR01193 380 GQQAIKAVTKLILNV---VILWTGAYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEVYLVDS 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 343 EIQNKKDAFIVQNIQGHVELENVSFGYVENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGK 422
Cdd:TIGR01193 457 EFINKKKRTELNNLNGDIVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGF 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 423 DIKDYDINSLRSKIGVVLQDTYLFAGTIMDNIRYG-RLHASDEEVINAAKAASAHSFIKHLPKQYETEIASEGSNLSQGQ 501
Cdd:TIGR01193 537 SLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGaKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQ 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 502 KQLLAIARAILADADILILDEATSNIDTRTELQIqagLNNL--MRGRTSFVIAHRLKTIEKADQILVIKDGSILERGNHE 579
Cdd:TIGR01193 617 KQRIALARALLTDSKVLILDESTSNLDTITEKKI---VNNLlnLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHD 693
|
570
....*....|....
gi 447166293 580 SLMEDRGFYFELYT 593
Cdd:TIGR01193 694 ELLDRNGFYASLIH 707
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
360-570 |
1.88e-78 |
|
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: 245.37 E-value: 1.88e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGY-VENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINSLRSKIGV 438
Cdd:cd03228 1 IEFKNVSFSYpGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 439 VLQDTYLFAGTIMDNIrygrlhasdeevinaakaasahsfikhlpkqyeteiasegsnLSQGQKQLLAIARAILADADIL 518
Cdd:cd03228 81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 447166293 519 ILDEATSNIDTRTELQIQAGLNNLMRGRTSFVIAHRLKTIEKADQILVIKDG 570
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
43-334 |
3.31e-78 |
|
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: 249.39 E-value: 3.31e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 43 LMFVIFLVFVTTLLGLLGPYFMGVIIDQYIVPKDLNGTARMCMLLIAIYGVTVLLTWLQTYVMINVALKTIQKIRQDIFE 122
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 123 KIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFSLNWILALVTLITVPIMFFVTKKLV 202
Cdd:cd07346 81 HLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 203 AYSGKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRISATKADTFSAFIFPSMNFINNLGMGLV 282
Cdd:cd07346 161 RRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 447166293 283 IGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd07346 241 LLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
354-572 |
6.74e-77 |
|
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: 243.53 E-value: 6.74e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 354 QNIQGHVELENVSFGYVE--NKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINS 431
Cdd:cd03248 6 DHLKGIVKFQNVTFAYPTrpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 432 LRSKIGVVLQDTYLFAGTIMDNIRYGRLHASDEEVINAAKAASAHSFIKHLPKQYETEIASEGSNLSQGQKQLLAIARAI 511
Cdd:cd03248 86 LHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447166293 512 LADADILILDEATSNIDTRTELQIQAGLNNLMRGRTSFVIAHRLKTIEKADQILVIKDGSI 572
Cdd:cd03248 166 IRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
360-595 |
4.22e-74 |
|
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: 236.61 E-value: 4.22e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGY-VENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINSLRSKIGV 438
Cdd:cd03252 1 ITFEHVRFRYkPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 439 VLQDTYLFAGTIMDNIRYGRLHASDEEVINAAKAASAHSFIKHLPKQYETEIASEGSNLSQGQKQLLAIARAILADADIL 518
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447166293 519 ILDEATSNIDTRTELQIQAGLNNLMRGRTSFVIAHRLKTIEKADQILVIKDGSILERGNHESLMEDRGFYFELYTSQ 595
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
358-577 |
6.42e-74 |
|
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: 235.47 E-value: 6.42e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 358 GHVELENVSFGYVEN-KTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINSLRSKI 436
Cdd:cd03244 1 GDIEFKNVSLRYRPNlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 437 GVVLQDTYLFAGTIMDNIR-YGRlhASDEEVINAAKAASAHSFIKHLPKQYETEIASEGSNLSQGQKQLLAIARAILADA 515
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDpFGE--YSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447166293 516 DILILDEATSNIDTRTELQIQAGLNNLMRGRTSFVIAHRLKTIEKADQILVIKDGSILERGN 577
Cdd:cd03244 159 KILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
111-592 |
5.93e-72 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 241.65 E-value: 5.93e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 111 KTIQKIRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFSLNWILA------ 184
Cdd:PRK11160 90 RVLTHLRVFTFSKLLPLSPAGLARYRQGDLLNRLVADVDTLDHLYLRLISPLVAALVVILVLTIGLSFFDLTLAltlggi 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 185 -LVTLITVPIMFFvtkklvaYSGKNFAKRQKDL-GELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLrisatkadt 262
Cdd:PRK11160 170 lLLLLLLLPLLFY-------RLGKKPGQDLTHLrAQYRVQLTEWLQGQAELTLFGAEDRYRQQLEQTEQQW--------- 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 263 fsafiFPSMNFINNLGmGLviGTGSVMVLNGMTTVGV--IAAFINYSRQFSRP---LSQFATL-----MNTIQAA----- 327
Cdd:PRK11160 234 -----LAAQRRQANLT-GL--SQALMILANGLTVVLMlwLAAGGVGGNAQPGAliaLFVFAALaafeaLMPVAGAfqhlg 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 328 --VAGGERVFEIMDEVPEIQNKKDAfIVQNIQGHVELENVSFGYVENKT-ILKEVSLKARPGETIALVGPTGSGKTTIIN 404
Cdd:PRK11160 306 qvIASARRINEITEQKPEVTFPTTS-TAAADQVSLTLNNVSFTYPDQPQpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQ 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 405 LLTRFYDIQQGQIHIDGKDIKDYDINSLRSKIGVVLQDTYLFAGTIMDNIRYGRLHASDEEVINAAKAASAHsfiKHL-- 482
Cdd:PRK11160 385 LLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLE---KLLed 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 483 PKQYETEIASEGSNLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQAGLNNLMRGRTSFVIAHRLKTIEKAD 562
Cdd:PRK11160 462 DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFD 541
|
490 500 510
....*....|....*....|....*....|
gi 447166293 563 QILVIKDGSILERGNHESLMEDRGFYFELY 592
Cdd:PRK11160 542 RICVMDNGQIIEQGTHQELLAQQGRYYQLK 571
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
43-334 |
1.48e-71 |
|
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: 232.04 E-value: 1.48e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 43 LMFVIFLVFVTTLLGLLGPYFMGVIIDQ-YIVPKDLNGTARMCMLLIAIYGVTVLLTWLQTYVMINVALKTIQKIRQDIF 121
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDLvTIGSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 122 EKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFSLNWILALVTLITVPIMFFVTKKL 201
Cdd:cd18778 81 DKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 202 VAYSGKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRISATKADTFSAFIFPSMNFINNLGMGL 281
Cdd:cd18778 161 SKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPLMEFLTSLGTVL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 447166293 282 VIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18778 241 VLGFGGRLVLAGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGAERV 293
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
85-555 |
1.13e-70 |
|
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: 236.87 E-value: 1.13e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 85 MLLIAIYGVTVL------LTWLQTYVMINVALKTIQKIRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQS 158
Cdd:TIGR02868 51 YLSVAAVAVRAFgigravFRYLERLVGHDAALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 159 VVQIISSALTFIGVTIAMFSLNWILALVTLITVPIMFFVTKKLVAYSGKNFAKRQKDL-GELNGFIEEAITGADVTTLYG 237
Cdd:TIGR02868 131 IVPAGVALVVGAAAVAAIAVLSVPAALILAAGLLLAGFVAPLVSLRAARAAEQALARLrGELAAQLTDALDGAAELVASG 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 238 KEKETVQNFNKINEQLRISATKADTFSAFIFPSMNFINNLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQF 317
Cdd:TIGR02868 211 ALPAALAQVEEADRELTRAERRAAAATALGAALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAAL 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 318 ATLMNTIQAAVAGGERVFEIMD---EVPEIQNKKDAFIVQNIQGhVELENVSFGYVENKTILKEVSLKARPGETIALVGP 394
Cdd:TIGR02868 291 PAAAQQLTRVRAAAERIVEVLDaagPVAEGSAPAAGAVGLGKPT-LELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGP 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 395 TGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINSLRSKIGVVLQDTYLFAGTIMDNIRYGRLHASDEEVINAAKAAS 474
Cdd:TIGR02868 370 SGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVG 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 475 AHSFIKHLPKQYETEIASEGSNLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQAGLNNLMRGRTSFVIAHR 554
Cdd:TIGR02868 450 LADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHH 529
|
.
gi 447166293 555 L 555
Cdd:TIGR02868 530 L 530
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
43-334 |
6.96e-69 |
|
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: 225.08 E-value: 6.96e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 43 LMFVIFLVFVTTLLGLLGPYFMGVIIDQYIVPKDLNGTARMCMLLI----AIYGVTVLLTWLQTYVMINVALKTIQKIRQ 118
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPYLTKILIDDVLIQLGPGGNTSLLLLLVlglaGAYVLSALLGILRGRLLARLGERITADLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 119 DIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFSLNWILALVTLITVPIMFFVT 198
Cdd:cd18563 81 DLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 199 KKLVAYSGKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRISATKADTFSAFIFPSMNFINNLG 278
Cdd:cd18563 161 YFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFLTSLG 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 447166293 279 MGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18563 241 TLIVWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
40-572 |
8.46e-69 |
|
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: 232.72 E-value: 8.46e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 40 KAALMFVIFLVFVTTLLGLLGPYFMGVIIDQYIvpkdlngTAR-------MCMLLIAIYGVTVLLTWLQTYVMINVALKT 112
Cdd:COG4618 19 RRAFLSVGLFSFFINLLMLTPPLYMLQVYDRVL-------TSRsvdtllmLTLLALGLYAVMGLLDAVRSRILVRVGARL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 113 IQKIRQDIFEKIQTLSLRFFDVRSQGDLmsrvtNDIDNLNQALTqsvvqiiSSALT----------FIGVtiaMFSLNWI 182
Cdd:COG4618 92 DRRLGPRVFDAAFRAALRGGGGAAAQAL-----RDLDTLRQFLT-------GPGLFalfdlpwapiFLAV---LFLFHPL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 183 LALVTLITVPIMF-------FVTKKLVAYSGKNFAKRqkdlgelNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRI 255
Cdd:COG4618 157 LGLLALVGALVLValallneRLTRKPLKEANEAAIRA-------NAFAEAALRNAEVIEAMGMLPALRRRWQRANARALA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 256 SATKADTFSAFIfpsMNFINNLGMGL---VIGTGSVMVLNGMTTVGV-IAAFINYSRQFSrPLSQFATLMNTIQAAVAGG 331
Cdd:COG4618 230 LQARASDRAGGF---SALSKFLRLLLqsaVLGLGAYLVIQGEITPGAmIAASILMGRALA-PIEQAIGGWKQFVSARQAY 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 332 ERVFEIMDEVPEiqnKKDAFIVQNIQGHVELENVSFGY-VENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFY 410
Cdd:COG4618 306 RRLNELLAAVPA---EPERMPLPRPKGRLSVENLTVVPpGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVW 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 411 DIQQGQIHIDGKDIKDYDINSLRSKIGVVLQDTYLFAGTIMDNI-RYGRlhASDEEVINAAKAASAHSFIKHLPKQYETE 489
Cdd:COG4618 383 PPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIaRFGD--ADPEKVVAAAKLAGVHEMILRLPDGYDTR 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 490 IASEGSNLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQAGLNNL-MRGRTSFVIAHRLKTIEKADQILVIK 568
Cdd:COG4618 461 IGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLAAVDKLLVLR 540
|
....
gi 447166293 569 DGSI 572
Cdd:COG4618 541 DGRV 544
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
358-572 |
2.94e-67 |
|
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: 218.23 E-value: 2.94e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 358 GHVELENVSFGYVENKT-ILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINSLRSKI 436
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIpALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 437 GVVLQDTYLFAGTIMDNIRYGRLHASDEEVINAAKAASAHSFIKHLPKQYETEIASEGSNLSQGQKQLLAIARAILADAD 516
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 447166293 517 ILILDEATSNIDTRTELQIQAGLNNLMRGRTSFVIAHRLKTIEKADQILVIKDGSI 572
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
43-334 |
2.25e-63 |
|
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: 210.37 E-value: 2.25e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 43 LMFVIFLVFVTTLLGLLGPYFMGVIIDQYIVPKDLNGTARMCMLLIAIYGVTVLLTWLQTYVMINVALKTIQKIRQDIFE 122
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 123 KIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFSLNWILALVTLITVPIMFFVTKKLV 202
Cdd:cd18542 81 HLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 203 AYSGKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRISATKADTFSAFIFPSMNFINNLGMGLV 282
Cdd:cd18542 161 KKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 447166293 283 IGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18542 241 LWVGGYLVINGEITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAERI 292
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
43-334 |
3.56e-60 |
|
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: 201.95 E-value: 3.56e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 43 LMFVIFLVFVTTLLGLLGPYFMGVIIDQYIVPKDLngtaRMCMLLIAIYGVTVLLTWLQTYVMINVALKTIQKI----RQ 118
Cdd:cd18546 1 LALALLLVVVDTAASLAGPLLVRYGIDSGVRAGDL----GVLLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLlydlRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 119 DIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFSLNWILALVTLITVPIMFFVT 198
Cdd:cd18546 77 RVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALAT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 199 KKLVAYSGKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRISATKADTFSAFIFPSMNFINNLG 278
Cdd:cd18546 157 RWFRRRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLA 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 447166293 279 MGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18546 237 TAAVLLVGAWRVAAGTLTVGVLVAFLLYLRRFFAPIQQLSQVFDSYQQARAALEKI 292
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
43-593 |
2.52e-59 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 208.16 E-value: 2.52e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 43 LMFVIFLVFVTTLLGLLGPYFM-----GVIIDQyiVPKDLNGTarMCMLLIAIYGVTVLLTWLQTYVMINVALKTIQKIR 117
Cdd:PRK11174 24 LNLSILLGFLSGLLLIAQAWLLatilqALIIEN--IPREALLP--PFILLILLFVLRALLAWLRERVGFKAGQHIRQQIR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 118 QDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFSLNWILALVTLITVPI---- 193
Cdd:PRK11174 100 QQVLDKLQQLGPAWIQGKPAGSWATLVLEQVEDMHDFYARYLPQMALAVLVPLLILIAVFPINWAAGLILLGTAPLiplf 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 194 MFFVTKKLVAYSGKNFakrqKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRISatkadTFS----AFI-- 267
Cdd:PRK11174 180 MALVGMGAADANRRNF----LALARLSGHFLDRLRGLETLRLFNRGEAETESIRSASEDFRQR-----TMEvlrmAFLss 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 268 -----FPS-----------MNFINNL-----GMGLVIGTGsVMVLngmttvgvIAAfinysRQFSRPLSQFATLMNTIQA 326
Cdd:PRK11174 251 avlefFASisialvavyfgFSYLGELnfghyGTGVTLFAG-FFVL--------ILA-----PEFYQPLRDLGTFYHAKAQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 327 AVAGGERVFEIMDEVPEIQNKKDAFIVQNIQGHVELENVSFGYVENKTILKEVSLKARPGETIALVGPTGSGKTTIINLL 406
Cdd:PRK11174 317 AVGAAESLVTFLETPLAHPQQGEKELASNDPVTIEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNAL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 407 TRF--YdiqQGQIHIDGKDIKDYDINSLRSKIGVVLQDTYLFAGTIMDNIRYGRLHASDEEVINAAKAASAHSFIKHLPK 484
Cdd:PRK11174 397 LGFlpY---QGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQ 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 485 QYETEIASEGSNLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQAGLNNLMRGRTSFVIAHRLKTIEKADQI 564
Cdd:PRK11174 474 GLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQI 553
|
570 580
....*....|....*....|....*....
gi 447166293 565 LVIKDGSILERGNHESLMEDRGFYFELYT 593
Cdd:PRK11174 554 WVMQDGQIVQQGDYAELSQAGGLFATLLA 582
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
43-334 |
8.47e-58 |
|
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: 195.72 E-value: 8.47e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 43 LMFVIFLVFVTTLLGLLGPYFMGVIIDQYIVPKDLNGTARMCMLLIAIYGVTVLLTWLQTYVMINVALKTIQKIRQDIFE 122
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 123 KIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFSLNWILALVTLITVPIMFFVTKKLV 202
Cdd:cd18552 81 KLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 203 AYSGKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRISATKADTFSAFIFPSMNFINNLGMGLV 282
Cdd:cd18552 161 KRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGAIAIALV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 447166293 283 IGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18552 241 LWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
43-334 |
4.46e-57 |
|
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: 194.27 E-value: 4.46e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 43 LMFVIFLVFVTTLLGLLGPYFMGVIIDQYIVPK---------DLNGTARM------CMLLIAIYGVTVLLTWLQTYVMIN 107
Cdd:cd18564 1 LALALLALLLETALRLLEPWPLKVVIDDVLGDKplpgllglaPLLGPDPLallllaAAALVGIALLRGLASYAGTYLTAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 108 VALKTIQKIRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFSLNWILALVT 187
Cdd:cd18564 81 VGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLALIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 188 LITVPIMFFVTKKlvaYSG--KNFAKRQ-KDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRISATKADTFS 264
Cdd:cd18564 161 LAVAPLLLLAARR---FSRriKEASREQrRREGALASVAQESLSAIRVVQAFGREEHEERRFARENRKSLRAGLRAARLQ 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 265 AFIFPSMNFINNLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18564 238 ALLSPVVDVLVAVGTALVLWFGAWLVLAGRLTPGDLLVFLAYLKNLYKPVRDLAKLTGRIAKASASAERV 307
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
40-334 |
5.92e-56 |
|
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: 190.77 E-value: 5.92e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 40 KAALMFVIFLVFVTTLLGLLGPYFMGVIIDQYIVPKDLNGTARmcmlLIAIYGVTVLLTWLQTYVMINVA----LKTIQK 115
Cdd:cd18540 1 KKLLILLIILMLLVALLDAVFPLLTKYAIDHFITPGTLDGLTG----FILLYLGLILIQALSVFLFIRLAgkieMGVSYD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 116 IRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFSLNWILALVTLITVPIMF 195
Cdd:cd18540 77 LRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPVLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 196 FVTkklvAYSGKNFAKRQKDLGELN----GFIEEAITGADVTTLYGKEKETVQNFNKINEQLRISATKADTFSAFIFPSM 271
Cdd:cd18540 157 VVS----IYFQKKILKAYRKVRKINsritGAFNEGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFLPIV 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447166293 272 NFINNLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18540 233 LFLGSIATALVLWYGGILVLAGAITIGTLVAFISYATQFFEPIQQLARVLAELQSAQASAERV 295
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
47-334 |
3.23e-55 |
|
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: 188.77 E-value: 3.23e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 47 IFLVFVTTLLGLLGPYFMGVIIDQYIVPK-DLNGTARMCMLLIAIYGVTVLLTWLQTYVMINVALKTIQKIRQDIFEKIQ 125
Cdd:cd18541 5 ILFLILVDLLQLLIPRIIGRAIDALTAGTlTASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFAHLL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 126 TLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFSLNWILALVTLITVPIMFFVTKKLVAYS 205
Cdd:cd18541 85 TLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRLGKKI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 206 GKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRISATKADTFSAFIFPSMNFINNLGMGLVIGT 285
Cdd:cd18541 165 HKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLIVLWY 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 447166293 286 GSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18541 245 GGRLVIRGTITLGDLVAFNSYLGMLIWPMMALGWVINLIQRGAASLKRI 293
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
23-591 |
3.72e-54 |
|
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: 199.40 E-value: 3.72e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 23 KNTKGTVKR--IWNYMGYEKAALMFVIFLVFVTTLLGLLGP-YFMGVIIDQYIVpkdlNGTARMCMLLIAIYGVTVLLTW 99
Cdd:TIGR00957 944 KAQTGQVELsvYWDYMKAIGLFITFLSIFLFVCNHVSALASnYWLSLWTDDPMV----NGTQNNTSLRLSVYGALGILQG 1019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 100 LQTYVM-INVALKTIQKIR---QDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIA 175
Cdd:TIGR00957 1020 FAVFGYsMAVSIGGIQASRvlhQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIV 1099
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 176 MFSLNWILALVTLITVPIMFFVTKKLVAYSGKnfAKRQKDLGE--LNGFIEEAITGADVttlygkeketVQNFNKINEQL 253
Cdd:TIGR00957 1100 ILLATPIAAVIIPPLGLLYFFVQRFYVASSRQ--LKRLESVSRspVYSHFNETLLGVSV----------IRAFEEQERFI 1167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 254 RISATKADTFSAFIFPSMNFINNLGMGLVIGTGSVMVLNGMTTV--------GVIAAFINYSRQFSRPLSQFATLMNTIQ 325
Cdd:TIGR00957 1168 HQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAVisrhslsaGLVGLSVSYSLQVTFYLNWLVRMSSEME 1247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 326 AAVAGGERVFEIMDevpeiQNKKDAFIVQNIQ--------GHVELENVSFGYVEN-KTILKEVSLKARPGETIALVGPTG 396
Cdd:TIGR00957 1248 TNIVAVERLKEYSE-----TEKEAPWQIQETAppsgwpprGRVEFRNYCLRYREDlDLVLRHINVTIHGGEKVGIVGRTG 1322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 397 SGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINSLRSKIGVVLQDTYLFAGTIMDNIR-YGRLhaSDEEVINAAKAASA 475
Cdd:TIGR00957 1323 AGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDpFSQY--SDEEVWWALELAHL 1400
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 476 HSFIKHLPKQYETEIASEGSNLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQAGLNNLMRGRTSFVIAHRL 555
Cdd:TIGR00957 1401 KTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRL 1480
|
570 580 590
....*....|....*....|....*....|....*.
gi 447166293 556 KTIEKADQILVIKDGSILERGNHESLMEDRGFYFEL 591
Cdd:TIGR00957 1481 NTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSM 1516
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
358-576 |
8.88e-53 |
|
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: 179.53 E-value: 8.88e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 358 GHVELENVSFGYVEN-KTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINSLRSKI 436
Cdd:cd03369 5 GEIEVENLSVRYAPDlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 437 GVVLQDTYLFAGTIMDNI-RYGrlHASDEEVINAAKaasahsfikhlpkqyeteIASEGSNLSQGQKQLLAIARAILADA 515
Cdd:cd03369 85 TIIPQDPTLFSGTIRSNLdPFD--EYSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLKRP 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447166293 516 DILILDEATSNIDTRTELQIQAGLNNLMRGRTSFVIAHRLKTIEKADQILVIKDGSILERG 576
Cdd:cd03369 145 RVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYD 205
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
43-314 |
4.66e-52 |
|
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: 179.76 E-value: 4.66e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 43 LMFVIFLVFVTTLLGLLGPYFMGVIIDQYIVPKDLN--GTARMCMLLIAIYGVTVLLTWLQTYVMINVALKTIQKIRQDI 120
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPEtqALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 121 FEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFSLNWILALVTLITVPIMFFVTKK 200
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 201 LVAYSGKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRISATKADTFSAFIFPSMNFINNLGMG 280
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
|
250 260 270
....*....|....*....|....*....|....
gi 447166293 281 LVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPL 314
Cdd:pfam00664 241 LALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
43-334 |
6.99e-52 |
|
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: 179.94 E-value: 6.99e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 43 LMFVIFLVFVTTLLGLLGPYFMGVIIDQYIVPKDLNGTArmcMLLIAIYGVTVLLTWLQTYVMINVALKTIQKIRQDIFE 122
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLIDALSAGGSSGGLL---ALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 123 KIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFSLNWILALVTLITVPIMFFVTKKLV 202
Cdd:cd18551 78 RLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 203 AYSGKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRISATKADTFSAFIFPSMNFINNLGMGLV 282
Cdd:cd18551 158 RRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLALLVV 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 447166293 283 IGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18551 238 LGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
45-334 |
7.88e-51 |
|
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: 177.21 E-value: 7.88e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 45 FVIFLVFVTTLLGLLGPYFMGVIIDQYIVPKDLNGTARMCMLLIAIYGVTVLLTWLQTYVMINVALKTIQKIRQDIFEKI 124
Cdd:cd18548 3 LAPLFKLLEVLLELLLPTLMADIIDEGIANGDLSYILRTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 125 QTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFSLNWILALVTLITVPIMFFVTKKLVAY 204
Cdd:cd18548 83 QSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIMKK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 205 SGKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRISATKADTFSAFIFPSMNFINNLGMGLVIG 284
Cdd:cd18548 163 AIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAILW 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 447166293 285 TGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18548 243 FGGHLINAGSLQVGDLVAFINYLMQILMSLMMLSMVFVMLPRASASAKRI 292
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
43-584 |
1.81e-50 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 188.31 E-value: 1.81e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 43 LMFVIFLVfvTTLLGLLGPYFM---GVIIDQYIVPKDLNGtarMCMLLIAIYGVTVLLTWLQTYVMINVALKTIQKIRQD 119
Cdd:PTZ00265 61 LLGVSFVC--ATISGGTLPFFVsvfGVIMKNMNLGENVND---IIFSLVLIGIFQFILSFISSFCMDVVTTKILKTLKLE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 120 IFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFSLNWILALVTLITVPIMFFVtk 199
Cdd:PTZ00265 136 FLKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLIYIC-- 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 200 KLVAYSGKNFAKRQKDLGELN--GFIEEAITGADVTTLYGKEKETVQNFNkINEQLrisatkadtFSAFIFPSmNFINNL 277
Cdd:PTZ00265 214 GVICNKKVKINKKTSLLYNNNtmSIIEEALVGIRTVVSYCGEKTILKKFN-LSEKL---------YSKYILKA-NFMESL 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 278 GMGLVIG-----------TGSVMVLN------------GMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAvaggERV 334
Cdd:PTZ00265 283 HIGMINGfilasyafgfwYGTRIIISdlsnqqpnndfhGGSVISILLGVLISMFMLTIILPNITEYMKSLEAT----NSL 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 335 FEIMDEVPEIQNKKDAFIVQNIQgHVELENVSFGYVENK--TILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDI 412
Cdd:PTZ00265 359 YEIINRKPLVENNDDGKKLKDIK-KIQFKNVRFHYDTRKdvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDP 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 413 QQGQIHI-DGKDIKDYDINSLRSKIGVVLQDTYLFAGTIMDNIRY----------------------------------- 456
Cdd:PTZ00265 438 TEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYslyslkdlealsnyynedgndsqenknkrnscrak 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 457 ---------------GRLHA-------SDEEVINAAKAASAHSFIKHLPKQYETEIASEGSNLSQGQKQLLAIARAILAD 514
Cdd:PTZ00265 518 cagdlndmsnttdsnELIEMrknyqtiKDSEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRN 597
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447166293 515 ADILILDEATSNIDTRTELQIQAGLNNLM--RGRTSFVIAHRLKTIEKADQILVIKDGSILERGNHESLMED 584
Cdd:PTZ00265 598 PKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLSNRERGSTVDVDIIGED 669
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
43-334 |
2.91e-50 |
|
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: 175.75 E-value: 2.91e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 43 LMFVIFLVFVTTLLGLLGPYFMGVIIDQYIVPKDLNGTARMCMLLIAIYGVTVLLTWLQTYVMINVALKTIQKIRQDIFE 122
Cdd:cd18550 1 LALVLLLILLSALLGLLPPLLLREIIDDALPQGDLGLLVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 123 KIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFSLNWILALVTLITVPIMFFVTKKLV 202
Cdd:cd18550 81 HLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPTRRVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 203 AYSGKNFAKRQKDLGELNGFIEE--AITGADVTTLYGKEKETVQNFNKINEQLRISATKADTFSAFIFPSMNFINNLGMG 280
Cdd:cd18550 161 RRRRKLTREQQEKLAELNSIMQEtlSVSGALLVKLFGREDDEAARFARRSRELRDLGVRQALAGRWFFAALGLFTAIGPA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 447166293 281 LVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18550 241 LVYWVGGLLVIGGGLTIGTLVAFTALLGRLYGPLTQLLNIQVDLMTSLALFERI 294
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
43-333 |
5.07e-50 |
|
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: 174.95 E-value: 5.07e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 43 LMFVIFLVFVTTLLGLLGPYFMGVIIDQYIVPKDLNGTARMCMLLIAIYGVTVLLTWLQTYVMINVALKTIQKIRQDIFE 122
Cdd:cd18549 4 FFLDLFCAVLIAALDLVFPLIVRYIIDDLLPSKNLRLILIIGAILLALYILRTLLNYFVTYWGHVMGARIETDMRRDLFE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 123 KIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFSLNWILALVTLITVPIMFFVT---- 198
Cdd:cd18549 84 HLQKLSFSFFDNNKTGQLMSRITNDLFDISELAHHGPEDLFISIITIIGSFIILLTINVPLTLIVFALLPLMIIFTiyfn 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 199 KKLVAYSGKNFAKrqkdLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRISATKADTFSAFIFPSMNFINNLG 278
Cdd:cd18549 164 KKMKKAFRRVREK----IGEINAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDRFLESKKKAYKAMAYFFSGMNFFTNLL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 447166293 279 MGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGER 333
Cdd:cd18549 240 NLVVLVAGGYFIIKGEITLGDLVAFLLYVNVFIKPIRRLVNFTEQYQKGMAGFER 294
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
51-334 |
5.32e-49 |
|
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: 172.75 E-value: 5.32e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 51 FVTTLLGLLGPYFMGVIID---------QYIVPKDLNGTARMCM------LLIAIYGVTVLLTWLQTYVMINVALKTIQK 115
Cdd:cd18565 9 ILNRLFDLAPPLLIGVAIDavfngeasfLPLVPASLGPADPRGQlwllggLTVAAFLLESLFQYLSGVLWRRFAQRVQHD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 116 IRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFSLNWILALVTLITVPIMF 195
Cdd:cd18565 89 LRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLII 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 196 FVTKKLVAYSGKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRISATKADTFSAFIFPSMNFIN 275
Cdd:cd18565 169 AGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERERVADASEEYRDANWRAIRLRAAFFPVIRLVA 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447166293 276 NLGMGLVIGTGSVMVLNGMT------TVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18565 249 GAGFVATFVVGGYWVLDGPPlftgtlTVGTLVTFLFYTQRLLWPLTRLGDLIDQYQRAMASAKRV 313
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
360-585 |
1.35e-47 |
|
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: 166.35 E-value: 1.35e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYVENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINSLRSKIGVV 439
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 440 LQ--DTYLFAGTIMDNIRYG--RLHASDEEVINAAKAASAHSFIKHLpKQYETeiasegSNLSQGQKQLLAIARAILADA 515
Cdd:COG1122 81 FQnpDDQLFAPTVEEDVAFGpeNLGLPREEIRERVEEALELVGLEHL-ADRPP------HELSGGQKQRVAIAGVLAMEP 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447166293 516 DILILDEATSNIDTRTELQIQAGLNNLMRGRTSFVIA-HRLKTIEK-ADQILVIKDGSILERGNHESLMEDR 585
Cdd:COG1122 154 EVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLDLVAElADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
47-334 |
3.95e-47 |
|
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: 166.89 E-value: 3.95e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 47 IFLVFVTTLLGLLGPYFMGVIIDQYIVPKDLNGTARMCMLLIAIYGVTVLLTWLQTYVMINVALKTIQKIRQDIFEKIQT 126
Cdd:cd18576 2 LILLLLSSAIGLVFPLLAGQLIDAALGGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 127 LSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFSLNWILALVTLITVPIMFFVTKklvaYSG 206
Cdd:cd18576 82 LPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAV----LFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 207 KNF----AKRQKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRISATKADTFSAFIFPSMNFINNLGMGLV 282
Cdd:cd18576 158 RRIrklsKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAV 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 447166293 283 IGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18576 238 LWYGGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
360-576 |
5.39e-47 |
|
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: 162.87 E-value: 5.39e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYVEN-KTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDiNSLRSKIGV 438
Cdd:cd03247 1 LSINNVSFSYPEQeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 439 VLQDTYLFAGTIMDNIrygrlhasdeevinaakaasahsfikhlpkqyeteiaseGSNLSQGQKQLLAIARAILADADIL 518
Cdd:cd03247 80 LNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447166293 519 ILDEATSNIDTRTELQIQAGLNNLMRGRTSFVIAHRLKTIEKADQILVIKDGSILERG 576
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
42-334 |
1.69e-45 |
|
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: 162.65 E-value: 1.69e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 42 ALMFVifLVFVTTLLGLLGPYFMGVIIDQYIVPKDLNGTARMCMLLIAIYGVTVLLTWLQTYVMINVALKTIQKIRQDIF 121
Cdd:cd18543 2 ILALL--AALLATLAGLAIPLLTRRAIDGPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 122 EKIQTLSLRFFD-VRSqGDLMSRVTNDIdNLNQALTQSVVQIISSALTFIGVTIAMFSLNWILALVTLITVPIMFFVTkk 200
Cdd:cd18543 80 AHLQRLDGAFHDrWQS-GQLLSRATSDL-SLVQRFLAFGPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVA-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 201 lVAYSGKNFA---KRQKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRISATKADTFSAFIFPSMNFINNL 277
Cdd:cd18543 156 -RRFRRRYFPasrRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEALPEL 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 447166293 278 GMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18543 235 GLAAVLALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
85-582 |
1.11e-44 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 170.98 E-value: 1.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 85 MLLIAIygVTVLLTWLQTYVMINVALKTIQKIRQDIFEKIQTLSLRFFDVRSQ--GDLMSRVTNDIDNLNQALTQSVVQI 162
Cdd:PTZ00265 872 ILVIAI--AMFISETLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDQDKHapGLLSAHINRDVHLLKTGLVNNIVIF 949
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 163 ISSALTFIGVTIAMFSLNWILALVTLITVPIMFFV-------------TKKLVAYSGKNFAKRQKD--LGELNGFIEEAI 227
Cdd:PTZ00265 950 THFIVLFLVSMVMSFYFCPIVAAVLTGTYFIFMRVfairarltankdvEKKEINQPGTVFAYNSDDeiFKDPSFLIQEAF 1029
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 228 TGADVTTLYGKEK------ETVQNFNKINEQLRISATKAdtFSAFIFPSMNFINNLGM---GLVIGTGSVMVLNGMTTVG 298
Cdd:PTZ00265 1030 YNMNTVIIYGLEDyfcnliEKAIDYSNKGQKRKTLVNSM--LWGFSQSAQLFINSFAYwfgSFLIRRGTILVDDFMKSLF 1107
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 299 VIAAFINYSrqfsrplSQFATLMNTIQAAVAGGERVFEIMDEVPEIQNKKDAFI-VQN---IQGHVELENVSFGYVE--N 372
Cdd:PTZ00265 1108 TFLFTGSYA-------GKLMSLKGDSENAKLSFEKYYPLIIRKSNIDVRDNGGIrIKNkndIKGKIEIMDVNFRYISrpN 1180
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 373 KTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQ-------------------------------------- 414
Cdd:PTZ00265 1181 VPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNdhhivfknehtndmtneqdyqgdeeqnvgmknvnefsl 1260
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 415 ----------------GQIHIDGKDIKDYDINSLRSKIGVVLQDTYLFAGTIMDNIRYGRLHASDEEVINAAKAASAHSF 478
Cdd:PTZ00265 1261 tkeggsgedstvfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEF 1340
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 479 IKHLPKQYETEIASEGSNLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQAGLNNL--MRGRTSFVIAHRLK 556
Cdd:PTZ00265 1341 IESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdKADKTIITIAHRIA 1420
|
570 580 590
....*....|....*....|....*....|.
gi 447166293 557 TIEKADQILVI----KDGSILE-RGNHESLM 582
Cdd:PTZ00265 1421 SIKRSDKIVVFnnpdRTGSFVQaHGTHEELL 1451
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
361-572 |
1.92e-44 |
|
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: 155.84 E-value: 1.92e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 361 ELENVSFGYVENKT-ILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINSLRSKIGVV 439
Cdd:cd03246 2 EVENVSFRYPGAEPpVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 440 LQDTYLFAGTIMDNIrygrlhasdeevinaakaasahsfikhlpkqyeteiasegsnLSQGQKQLLAIARAILADADILI 519
Cdd:cd03246 82 PQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 447166293 520 LDEATSNIDTRTELQIQAGLNNL-MRGRTSFVIAHRLKTIEKADQILVIKDGSI 572
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
361-570 |
2.44e-43 |
|
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: 154.16 E-value: 2.44e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 361 ELENVSFGY-VENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINSLRSKIGVV 439
Cdd:cd03225 1 ELKNLSFSYpDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 440 LQ--DTYLFAGTIMDNIRYG--RLHASDEEVINAAKAASAHSFIKHLPKQyetEIasegSNLSQGQKQLLAIARAILADA 515
Cdd:cd03225 81 FQnpDDQFFGPTVEEEVAFGleNLGLPEEEIEERVEEALELVGLEGLRDR---SP----FTLSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447166293 516 DILILDEATSNIDTRTELQIQAGLNNLMRGRTSFVIA-HRLKTI-EKADQILVIKDG 570
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVtHDLDLLlELADRVIVLEDG 210
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
47-334 |
9.34e-43 |
|
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: 155.03 E-value: 9.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 47 IFLVFVTTLLGLLGPYFMGVIIDQYIVPKDLNGTARMCMLLIAIYGVTVLLTWLQTYVMINVALKTIQKIRQDIFEKIQT 126
Cdd:cd18557 2 LLFLLISSAAQLLLPYLIGRLIDTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 127 LSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFSLNWILALVTLITVPIMFFVTKKLVAYSG 206
Cdd:cd18557 82 QEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 207 KNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRISATKADTFSAFIFPSMNFINNLGMGLVIGTG 286
Cdd:cd18557 162 KLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYG 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 447166293 287 SVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18557 242 GYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
40-334 |
3.11e-42 |
|
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: 153.76 E-value: 3.11e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 40 KAALMFVIFLVFVTTLLGLLGPYFMGVIIDQYIVPKDLNGTARMCMLLIAIYGVTVLLTWLQTYVMINVALKTIQKIRQD 119
Cdd:cd18570 1 KKLLILILLLSLLITLLGIAGSFFFQILIDDIIPSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 120 IFEKIQTLSLRFFDVRSQGDLMSRVtNDIDNLNQALTQSVVQIISSALTFIGVTIAMFSLNWILALVTLITVPIMFFVTK 199
Cdd:cd18570 81 YFKHLLKLPLSFFETRKTGEIISRF-NDANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLYILIIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 200 KLVaysgKNFAKRQKDL----GELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRISATKADTFSAFIFPSMNFIN 275
Cdd:cd18570 160 LFN----KPFKKKNREVmesnAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLIS 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 447166293 276 NLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18570 236 LIGSLLILWIGSYLVIKGQLSLGQLIAFNALLGYFLGPIENLINLQPKIQEAKVAADRL 294
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
360-576 |
4.34e-42 |
|
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: 151.18 E-value: 4.34e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYvENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQ-----GQIHIDGKDI--KDYDINSL 432
Cdd:cd03260 1 IELRDLNVYY-GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPgapdeGEVLLDGKDIydLDVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 433 RSKIGVVLQDTYLFAGTIMDNIRYG-RLHAS------DEEVINAAKAAsahsfikHLPKqyETEIASEGSNLSQGQKQLL 505
Cdd:cd03260 80 RRRVGMVFQKPNPFPGSIYDNVAYGlRLHGIklkeelDERVEEALRKA-------ALWD--EVKDRLHALGLSGGQQQRL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447166293 506 AIARAILADADILILDEATSNIDTRTELQIQAGLNNLMRGRTSFVIAHRLKTIEK-ADQILVIKDGSILERG 576
Cdd:cd03260 151 CLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFG 222
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
33-589 |
2.76e-41 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 160.91 E-value: 2.76e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 33 WN-YMGYEKAA----LMFVIFLVFVTT-LLGLLGPYFMGVIIDQYIVPKDLNGtarmcmLLIAIYGV----TVLLTWLQT 102
Cdd:PLN03232 898 WNvLMRYNKAVgglwVVMILLVCYLTTeVLRVSSSTWLSIWTDQSTPKSYSPG------FYIVVYALlgfgQVAVTFTNS 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 103 YVMINVALKTIQKIRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIIS------SALTFIGvTIAM 176
Cdd:PLN03232 972 FWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNqlwqllSTFALIG-TVST 1050
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 177 FSLNWILALVTLITVPIMFFvtkklvaysgKNFAKRQKDLgelngfieEAITGADVTTLYGKEK---ETVQNFNKINEQL 253
Cdd:PLN03232 1051 ISLWAIMPLLILFYAAYLYY----------QSTSREVRRL--------DSVTRSPIYAQFGEALnglSSIRAYKAYDRMA 1112
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 254 RISATKADTFSAFIFPSMNF-------INNLGMGLVIGTGSVMVL-NGMT--------TVGVIAAF-INYSRQFSRPLSQ 316
Cdd:PLN03232 1113 KINGKSMDNNIRFTLANTSSnrwltirLETLGGVMIWLTATFAVLrNGNAenqagfasTMGLLLSYtLNITTLLSGVLRQ 1192
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 317 FATLMNTIQAAvaggERVFEIMD---EVPEIQNKKDAFIVQNIQGHVELENVSFGY-VENKTILKEVSLKARPGETIALV 392
Cdd:PLN03232 1193 ASKAENSLNSV----ERVGNYIDlpsEATAIIENNRPVSGWPSRGSIKFEDVHLRYrPGLPPVLHGLSFFVSPSEKVGVV 1268
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 393 GPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINSLRSKIGVVLQDTYLFAGTIMDNIRYGRLHaSDEEVINAAKA 472
Cdd:PLN03232 1269 GRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEH-NDADLWEALER 1347
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 473 ASAHSFIKHLPKQYETEIASEGSNLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQAGLNNLMRGRTSFVIA 552
Cdd:PLN03232 1348 AHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIA 1427
|
570 580 590
....*....|....*....|....*....|....*..
gi 447166293 553 HRLKTIEKADQILVIKDGSILERGNHESLMEDRGFYF 589
Cdd:PLN03232 1428 HRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAF 1464
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
119-585 |
3.20e-41 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 160.71 E-value: 3.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 119 DIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISsalTFIGVTIAMFSLNWILALVTLITVPIMFFVT 198
Cdd:PTZ00243 1036 DLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLPMSYLYLLQ---CLFSICSSILVTSASQPFVLVALVPCGYLYY 1112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 199 KKLVAYSGKNFA-KRQKDLGE--LNGFIEEAITGADVTTLYGKEKETVQnfnkinEQLRisatKAD-TFSAFIFPSM--- 271
Cdd:PTZ00243 1113 RLMQFYNSANREiRRIKSVAKspVFTLLEEALQGSATITAYGKAHLVMQ------EALR----RLDvVYSCSYLENVanr 1182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 272 ------NFINNLGMGLV--IGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERVFEIMDEV-- 341
Cdd:PTZ00243 1183 wlgvrvEFLSNIVVTVIalIGVIGTMLRATSQEIGLVSLSLTMAMQTTATLNWLVRQVATVEADMNSVERLLYYTDEVph 1262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 342 ---PEIQNKKDAF---------------------------IVQniQGHVELENVSFGYVEN-KTILKEVSLKARPGETIA 390
Cdd:PTZ00243 1263 edmPELDEEVDALerrtgmaadvtgtvviepasptsaaphPVQ--AGSLVFEGVQMRYREGlPLVLRGVSFRIAPREKVG 1340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 391 LVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINSLRSKIGVVLQDTYLFAGTIMDNIRyGRLHASDEEVINAA 470
Cdd:PTZ00243 1341 IVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVD-PFLEASSAEVWAAL 1419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 471 KAASAHSFIKHLPKQYETEIASEGSNLSQGQKQLLAIARAILADADILIL-DEATSNIDTRTELQIQAGLNNLMRGRTSF 549
Cdd:PTZ00243 1420 ELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFILmDEATANIDPALDRQIQATVMSAFSAYTVI 1499
|
490 500 510
....*....|....*....|....*....|....*.
gi 447166293 550 VIAHRLKTIEKADQILVIKDGSILERGNHESLMEDR 585
Cdd:PTZ00243 1500 TIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNR 1535
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
358-582 |
8.75e-41 |
|
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: 148.90 E-value: 8.75e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 358 GHVELENVSFGYVEN-KTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINSLRSKI 436
Cdd:cd03288 18 GEIKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 437 GVVLQDTYLFAGTIMDNIRYGRlHASDEEVINAAKAASAHSFIKHLPKQYETEIASEGSNLSQGQKQLLAIARAILADAD 516
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPEC-KCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSS 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447166293 517 ILILDEATSNIDTRTELQIQAGLNNLMRGRTSFVIAHRLKTIEKADQILVIKDGSILERGNHESLM 582
Cdd:cd03288 177 ILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLL 242
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
376-525 |
4.18e-40 |
|
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: 143.17 E-value: 4.18e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 376 LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINSLRSKIGVVLQDTYLFAG-TIMDNI 454
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447166293 455 RYGRLhasDEEVINAAKAASAHSFIKHL--PKQYETEIASEGSNLSQGQKQLLAIARAILADADILILDEATS 525
Cdd:pfam00005 81 RLGLL---LKGLSKREKDARAEEALEKLglGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
361-586 |
4.90e-40 |
|
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: 146.16 E-value: 4.90e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 361 ELENVSFGYvENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDiNSLRSKIGVVL 440
Cdd:COG4555 3 EVENLSKKY-GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP-REARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 441 QDTYLFAG-TIMDNIRY-GRLHASDEEVINAAKAASAHSFI--KHLPKQYETeiasegsnLSQGQKQLLAIARAILADAD 516
Cdd:COG4555 81 DERGLYDRlTVRENIRYfAELYGLFDEELKKRIEELIELLGleEFLDRRVGE--------LSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447166293 517 ILILDEATSNIDTRTELQIQAGLNNLMRGRTSFVIA-HRLKTIEK-ADQILVIKDGSILERGNHESLMEDRG 586
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSsHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
360-584 |
2.57e-39 |
|
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: 150.82 E-value: 2.57e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYVENK----TILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDY---DINSL 432
Cdd:COG1123 261 LEVRNLSKRYPVRGkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLsrrSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 433 RSKIGVVLQDTY--LFAG-TIMDNIRYG-RLH--ASDEEVinAAKAASA-------HSFIKHLPKQyeteiasegsnLSQ 499
Cdd:COG1123 341 RRRVQMVFQDPYssLNPRmTVGDIIAEPlRLHglLSRAER--RERVAELlervglpPDLADRYPHE-----------LSG 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 500 GQKQLLAIARAILADADILILDEATSNIDTRTELQIqagLNNLMR-----GRTSFVIAHRLKTIEK-ADQILVIKDGSIL 573
Cdd:COG1123 408 GQRQRVAIARALALEPKLLILDEPTSALDVSVQAQI---LNLLRDlqrelGLTYLFISHDLAVVRYiADRVAVMYDGRIV 484
|
250
....*....|.
gi 447166293 574 ERGNHESLMED 584
Cdd:COG1123 485 EDGPTEEVFAN 495
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
358-589 |
1.18e-38 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 152.97 E-value: 1.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 358 GHVELENVSFGYVEN-KTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINSLRSKI 436
Cdd:PLN03130 1236 GSIKFEDVVLRYRPElPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVL 1315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 437 GVVLQDTYLFAGTIMDNIRYGRLHaSDEEVINAAKAASAHSFIKHLPKQYETEIASEGSNLSQGQKQLLAIARAILADAD 516
Cdd:PLN03130 1316 GIIPQAPVLFSGTVRFNLDPFNEH-NDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSK 1394
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447166293 517 ILILDEATSNIDTRTELQIQAGLNNLMRGRTSFVIAHRLKTIEKADQILVIKDGSILERGNHESLMEDRGFYF 589
Cdd:PLN03130 1395 ILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAF 1467
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
360-582 |
7.31e-38 |
|
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: 140.56 E-value: 7.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYvENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINSLRSKIGVV 439
Cdd:COG1120 2 LEAENLSVGY-GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 440 LQDTYL-FAGTIMDNIRYGRL-H--------ASDEEVINAAKAASAhsfIKHLPKQYETEiasegsnLSQGQKQLLAIAR 509
Cdd:COG1120 81 PQEPPApFGLTVRELVALGRYpHlglfgrpsAEDREAVEEALERTG---LEHLADRPVDE-------LSGGERQRVLIAR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 510 AILADADILILDEATSNIDTRTELQIQAGLNNL--MRGRTSFVIAH------RLktiekADQILVIKDGSILERGNHESL 581
Cdd:COG1120 151 ALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLarERGRTVVMVLHdlnlaaRY-----ADRLVLLKDGRIVAQGPPEEV 225
|
.
gi 447166293 582 M 582
Cdd:COG1120 226 L 226
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
361-570 |
7.32e-38 |
|
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: 137.38 E-value: 7.32e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 361 ELENVSFGYvENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINSLRSKIGVVL 440
Cdd:cd00267 1 EIENLSFRY-GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 441 QdtylfagtimdnirygrlhasdeevinaakaasahsfikhlpkqyeteiasegsnLSQGQKQLLAIARAILADADILIL 520
Cdd:cd00267 80 Q-------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 447166293 521 DEATSNIDTRTELQIQAGLNNLM-RGRTSFVIAHRLKTIEKA-DQILVIKDG 570
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAeEGRTVIIVTHDPELAELAaDRVIVLKDG 156
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
360-571 |
1.39e-36 |
|
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: 135.29 E-value: 1.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYVENKT----ILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKdikdydinslrsk 435
Cdd:cd03250 1 ISVEDASFTWDSGEQetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 436 IGVVLQDTYLFAGTIMDNIRYGRLHASD--EEVInaaKAASAHSFIKHLPKQYETEIASEGSNLSQGQKQLLAIARAILA 513
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKPFDEEryEKVI---KACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYS 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 514 DADILILDEATSNIDTRTELQI--QAGLNNLMRGRTSFVIAHRLKTIEKADQILVIKDGS 571
Cdd:cd03250 145 DADIYLLDDPLSAVDAHVGRHIfeNCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
360-572 |
1.93e-36 |
|
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: 134.06 E-value: 1.93e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYvENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDyDINSLRSKIGVV 439
Cdd:cd03230 1 IEVRNLSKRY-GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 440 LQDTYLFAG-TIMDNIRYgrlhasdeevinaakaasahsfikhlpkqyeteiasegsnlSQGQKQLLAIARAILADADIL 518
Cdd:cd03230 79 PEEPSLYENlTVRENLKL-----------------------------------------SGGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 447166293 519 ILDEATSNIDTRTELQIQAGLNNLM-RGRTSFVIAHRLKTIEK-ADQILVIKDGSI 572
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLRELKkEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
360-584 |
3.08e-36 |
|
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: 142.35 E-value: 3.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYVEN-KTILKEVSLKARPGETIALVGPTGSGKTTI---INLLTRFYDIQQGQIHIDGKDIKDYDINSLRSK 435
Cdd:COG1123 5 LEVRDLSVRYPGGdVPAVDGVSLTIAPGETVALVGESGSGKSTLalaLMGLLPHGGRISGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 436 IGVVLQD--TYLFAGTIMDNIRYG--RLHASDEEVINAAKAASAHSFIKHLPKQYETEiasegsnLSQGQKQLLAIARAI 511
Cdd:COG1123 85 IGMVFQDpmTQLNPVTVGDQIAEAleNLGLSRAEARARVLELLEAVGLERRLDRYPHQ-------LSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447166293 512 LADADILILDEATSNIDTRTELQIQAGLNNLMR--GRTSFVIAHRLKTI-EKADQILVIKDGSILERGNHESLMED 584
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
360-574 |
5.45e-36 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 134.40 E-value: 5.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYVENK---TILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINSL---- 432
Cdd:COG1136 5 LELRNLTKSYGTGEgevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 433 RSKIGVVLQDTYLFAG-TIMDNIRYGRLHASDEEVINAAKAASA------HSFIKHLPKQyeteiasegsnLSQGQKQLL 505
Cdd:COG1136 85 RRHIGFVFQFFNLLPElTALENVALPLLLAGVSRKERRERARELlervglGDRLDHRPSQ-----------LSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447166293 506 AIARAILADADILILDEATSNIDTRTELQIQAGLNNLMR--GRTSFVIAHRLKTIEKADQILVIKDGSILE 574
Cdd:COG1136 154 AIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRelGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
360-576 |
3.42e-35 |
|
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: 132.24 E-value: 3.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYVENK---TILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYD---INSLR 433
Cdd:cd03257 2 LEVKNLSVSFPTGGgsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 434 SKIGVVLQDTY-----LFagTIMDNIRYGRLHASDEEVINAAKAASAHSFIK-HLPKQYETEIASEgsnLSQGQKQLLAI 507
Cdd:cd03257 82 KEIQMVFQDPMsslnpRM--TIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGvGLPEEVLNRYPHE---LSGGQRQRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447166293 508 ARAILADADILILDEATSNIDTRTELQIQAGLNNL--MRGRTSFVIAHRLKTIEK-ADQILVIKDGSILERG 576
Cdd:cd03257 157 ARALALNPKLLIADEPTSALDVSVQAQILDLLKKLqeELGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
360-570 |
4.71e-35 |
|
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: 130.38 E-value: 4.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYVEnKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINS--LRSKIG 437
Cdd:cd03229 1 LELKNVSKRYGQ-KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 438 VVLQDTYLFAG-TIMDNIRYGrlhasdeevinaakaasahsfikhlpkqyeteiasegsnLSQGQKQLLAIARAILADAD 516
Cdd:cd03229 80 MVFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447166293 517 ILILDEATSNIDTRTELQIQAGLNNL--MRGRTSFVIAHRLKTIEK-ADQILVIKDG 570
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLqaQLGITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
360-574 |
2.22e-34 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 129.79 E-value: 2.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYVENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKD---IKDYDINSLRSKI 436
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDlsrLKRREIPYLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 437 GVVLQDTYLFAG-TIMDNIRY-----GRLHASDEEVINAA--------KAasahsfiKHLPKQyeteiasegsnLSQGQK 502
Cdd:COG2884 82 GVVFQDFRLLPDrTVYENVALplrvtGKSRKEIRRRVREVldlvglsdKA-------KALPHE-----------LSGGEQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447166293 503 QLLAIARAILADADILILDEATSNIDTRTELQIQAGLNNLMRGRTSFVIA-HRLKTIEKADQ-ILVIKDGSILE 574
Cdd:COG2884 144 QRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIAtHDLELVDRMPKrVLELEDGRLVR 217
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
360-584 |
2.75e-34 |
|
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: 130.31 E-value: 2.75e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGY---VENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINSLRSKI 436
Cdd:COG1124 2 LEVRNLSVSYgqgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 437 GVVLQDTYL-------FAGTIMDNIRYGRLHASDEEVINAAKAAsahsfikHLPKQYETEIASEgsnLSQGQKQLLAIAR 509
Cdd:COG1124 82 QMVFQDPYAslhprhtVDRILAEPLRIHGLPDREERIAELLEQV-------GLPPSFLDRYPHQ---LSGGQRQRVAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447166293 510 AILADADILILDEATSNIDTRTELQIQAGLNNLM--RGRTSFVIAHRLKTIEK-ADQILVIKDGSILERGNHESLMED 584
Cdd:COG1124 152 ALILEPELLLLDEPTSALDVSVQAEILNLLKDLReeRGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLAG 229
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
360-576 |
4.49e-34 |
|
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: 128.79 E-value: 4.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYvENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINslRSKIGVV 439
Cdd:cd03259 1 LELKGLSKTY-GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 440 LQDTYLFAG-TIMDNIRYG-RLHASDEEVINAAKAASAHSF-IKHLPKQYETEiasegsnLSQGQKQLLAIARAILADAD 516
Cdd:cd03259 78 FQDYALFPHlTVAENIAFGlKLRGVPKAEIRARVRELLELVgLEGLLNRYPHE-------LSGGQQQRVALARALAREPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447166293 517 ILILDEATSNIDTRTELQIQAGLNNLMR--GRTSFVIAHRL-KTIEKADQILVIKDGSILERG 576
Cdd:cd03259 151 LLLLDEPLSALDAKLREELREELKELQRelGITTIYVTHDQeEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
360-572 |
2.50e-33 |
|
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: 126.84 E-value: 2.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYVENKT---ILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINSL---- 432
Cdd:cd03255 1 IELKNLSKTYGGGGEkvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 433 RSKIGVVLQDTYLFAG-TIMDNIRYGRLHASDEEVINAAKAASA-------HSfIKHLPKQyeteiasegsnLSQGQKQL 504
Cdd:cd03255 81 RRHIGFVFQSFNLLPDlTALENVELPLLLAGVPKKERRERAEELlervglgDR-LNHYPSE-----------LSGGQQQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 505 LAIARAILADADILILDEATSNIDTRTELQIQAGLNNL--MRGRTSFVIAHRLKTIEKADQILVIKDGSI 572
Cdd:cd03255 149 VAIARALANDPKIILADEPTGNLDSETGKEVMELLRELnkEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
361-576 |
3.13e-32 |
|
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: 122.54 E-value: 3.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 361 ELENVSFGYvENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINSLRSKIGVVL 440
Cdd:cd03214 1 EVENLSVGY-GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 441 QdtylfagtIMDNIRygrlhasdeevinaakaasahsfIKHLPKQYETEiasegsnLSQGQKQLLAIARAILADADILIL 520
Cdd:cd03214 80 Q--------ALELLG-----------------------LAHLADRPFNE-------LSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 447166293 521 DEATSNIDTRTELQIQAGLNNLMR--GRTSFVIAHRLK-TIEKADQILVIKDGSILERG 576
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRRLARerGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
360-582 |
3.77e-32 |
|
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: 124.34 E-value: 3.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYVENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINSLRSKIGVV 439
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 440 LQDTYLFAG-TIMDNIR-YGRLHASDEEVInAAKAASAHSFIKHLPKQYETEIASEgsnLSQGQKQLLAIARAILADADI 517
Cdd:cd03295 81 IQQIGLFPHmTVEENIAlVPKLLKWPKEKI-RERADELLALVGLDPAEFADRYPHE---LSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447166293 518 LILDEATSNIDTRTELQIQAGLNNLMR--GRTSFVIAHRL-KTIEKADQILVIKDGSILERGNHESLM 582
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
360-567 |
4.11e-32 |
|
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: 123.35 E-value: 4.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGY---VENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKdikdyDINSLRSKI 436
Cdd:cd03293 1 LEVRNVSKTYgggGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGE-----PVTGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 437 GVVLQDTYLFA-GTIMDNIRYGRLHA------SDEEVINAAKAASAHSFIKHLPKQyeteiasegsnLSQGQKQLLAIAR 509
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLELQgvpkaeARERAEELLELVGLSGFENAYPHQ-----------LSGGMRQRVALAR 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447166293 510 AILADADILILDEATSNIDTRTELQIQAGLNNLMR--GRTSFVIAHrlkTIEKA----DQILVI 567
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRetGKTVLLVTH---DIDEAvflaDRVVVL 205
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
360-572 |
4.12e-32 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 124.05 E-value: 4.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYvENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDydinsLRSKIGVV 439
Cdd:COG1121 7 IELENLTVSY-GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR-----ARRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 440 LQDTYL---FAGTIMDNI---RYG------RLHASDEEVINAA-KAASAHSFIKHLpkqyeteIasegSNLSQGQKQLLA 506
Cdd:COG1121 81 PQRAEVdwdFPITVRDVVlmgRYGrrglfrRPSRADREAVDEAlERVGLEDLADRP-------I----GELSGGQQQRVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447166293 507 IARAILADADILILDEATSNIDTRTELQIQAGLNNL-MRGRTSFVIAHRLKTIEK-ADQILVIKDGSI 572
Cdd:COG1121 150 LARALAQDPDLLLLDEPFAGVDAATEEALYELLRELrREGKTILVVTHDLGAVREyFDRVLLLNRGLV 217
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
360-583 |
1.05e-31 |
|
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: 122.78 E-value: 1.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYvENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYD---INSLRSKI 436
Cdd:COG1127 6 IEVRNLTKSF-GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 437 GVVLQDTYLFAG-TIMDNI-----RYGRLhaSDEEVINAAKAASA----HSFIKHLPkqyeteiasegSNLSQGQKQLLA 506
Cdd:COG1127 85 GMLFQGGALFDSlTVFENVafplrEHTDL--SEAEIRELVLEKLElvglPGAADKMP-----------SELSGGMRKRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 507 IARAILADADILILDEATSNIDTRTELQIqaglNNLMR------GRTSFVIAHRLKTIEK-ADQILVIKDGSILERGNHE 579
Cdd:COG1127 152 LARALALDPEILLYDEPTAGLDPITSAVI----DELIRelrdelGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPE 227
|
....
gi 447166293 580 SLME 583
Cdd:COG1127 228 ELLA 231
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
47-334 |
1.46e-31 |
|
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: 123.81 E-value: 1.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 47 IFLVFVTTLLGLLGPYFMGVIIDQYIVPKDLNGTARMCMLLIAIYGVTVLLTWLQTYVMINVALKTIQKIRQDIFEKIQT 126
Cdd:cd18572 2 FVFLVVAALSELAIPHYTGAVIDAVVADGSREAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 127 LSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFSLNWILALVTLITVPIMFFVTKKLVAYSG 206
Cdd:cd18572 82 QDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYYR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 207 KNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKETVQNFN-KINEQLRISaTKADTFSAFIFPSMNFINNLGMGLVIGT 285
Cdd:cd18572 162 KLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYErALDKALKLS-VRQALAYAGYVAVNTLLQNGTQVLVLFY 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 447166293 286 GSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18572 241 GGHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGAAEKV 289
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
41-334 |
1.86e-31 |
|
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: 124.12 E-value: 1.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 41 AALMFVIFLVFVTTLLGLLGPYFMGVIIDQYIvpkdLNGTARMCMLLIAIYGVTVLLTWLQTYVMINVALKTIQKIRQDI 120
Cdd:cd18577 11 AGAALPLMTIVFGDLFDAFTDFGSGESSPDEF----LDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQARRIRKRY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 121 FEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFI-GVTIAmFSLNWILALVTLITVPIMFFVTK 199
Cdd:cd18577 87 LKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIaGFIIA-FIYSWKLTLVLLATLPLIAIVGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 200 KLVAYSGKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRISATKADTFSAFIFPSMNFINNLGM 279
Cdd:cd18577 166 IMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLFFIIFAMY 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447166293 280 GLVIGTGSVMVLNGMTTVG-VIAAFIN-----YSrqfsrpLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18577 246 ALAFWYGSRLVRDGEISPGdVLTVFFAvligaFS------LGQIAPNLQAFAKARAAAAKI 300
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
358-588 |
6.59e-31 |
|
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: 121.89 E-value: 6.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 358 GHVELENVSFGYVEN-KTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQqGQIHIDGKDIKDYDINSLRSKI 436
Cdd:cd03289 1 GQMTVKDLTAKYTEGgNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 437 GVVLQDTYLFAGTIMDNIR-YGRLhaSDEEVINAAKAASAHSFIKHLPKQYETEIASEGSNLSQGQKQLLAIARAILADA 515
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDpYGKW--SDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447166293 516 DILILDEATSNIDTRTELQIQAGLNNLMRGRTSFVIAHRLKTIEKADQILVIKDGSILERGNHESLMEDRGFY 588
Cdd:cd03289 158 KILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHF 230
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
361-568 |
7.40e-31 |
|
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: 119.56 E-value: 7.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 361 ELENVSFGYvENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDydinsLRSKIGVVL 440
Cdd:cd03235 1 EVEDLTVSY-GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK-----ERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 441 QDTYL---FAGTIMDNIRYGRLH----------ASDEEVINAAKAASAHSFIKHLpkqyeteIasegSNLSQGQKQLLAI 507
Cdd:cd03235 75 QRRSIdrdFPISVRDVVLMGLYGhkglfrrlskADKAKVDEALERVGLSELADRQ-------I----GELSGGQQQRVLL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447166293 508 ARAILADADILILDEATSNIDTRTELQIQAGLNNL-MRGRTSFVIAHRLKTIEK-ADQILVIK 568
Cdd:cd03235 144 ARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVLEyFDRVLLLN 206
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
361-572 |
1.87e-30 |
|
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: 118.51 E-value: 1.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 361 ELENVSFGYVENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDinsLRSKIGVVL 440
Cdd:cd03226 1 RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE---RRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 441 QDT--YLFAGTIMDNIRYG--RLHASDEEVINAAKAASAHSFIKHLPKqyeteiasegsNLSQGQKQLLAIARAILADAD 516
Cdd:cd03226 78 QDVdyQLFTDSVREELLLGlkELDAGNEQAETVLKDLDLYALKERHPL-----------SLSGGQKQRLAIAAALLSGKD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447166293 517 ILILDEATSNIDTRTELQIQAGLNNLM-RGRTSFVIAHRLKTIEK-ADQILVIKDGSI 572
Cdd:cd03226 147 LLIFDEPTSGLDYKNMERVGELIRELAaQGKAVIVITHDYEFLAKvCDRVLLLANGAI 204
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
47-307 |
3.74e-30 |
|
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: 119.93 E-value: 3.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 47 IFLVFVTTLLGLLGPYFMGVIIDQYIVPKDLNGTA-----RMCMLLIAIYGVTVLLTWLQTYVMINVALKTIQKIRQDIF 121
Cdd:cd18573 2 LALLLVSSAVTMSVPFAIGKLIDVASKESGDIEIFglslkTFALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRLF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 122 EKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFSLNWILALVTLITVP---IMFFVT 198
Cdd:cd18573 82 KSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPpiaVGAVFY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 199 KKLVaysgKNFAKR-QKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRISATKADTFSAFIFPSMNFINNL 277
Cdd:cd18573 162 GRYV----RKLSKQvQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNL 237
|
250 260 270
....*....|....*....|....*....|
gi 447166293 278 GMGLVIGTGSVMVLNGMTTVGVIAAFINYS 307
Cdd:cd18573 238 SLLSVLYYGGSLVASGELTVGDLTSFLMYA 267
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
360-576 |
5.00e-30 |
|
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: 117.99 E-value: 5.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYvENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDI---KDYDINSLRSKI 436
Cdd:cd03261 1 IELRGLTKSF-GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsglSEAELYRLRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 437 GVVLQDTYLFAG-TIMDNI-----RYGRLhasDEEVINAA-----KAASAHSFIKHLPkqyeteiasegSNLSQGQKQLL 505
Cdd:cd03261 80 GMLFQSGALFDSlTVFENVafplrEHTRL---SEEEIREIvleklEAVGLRGAEDLYP-----------AELSGGMKKRV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447166293 506 AIARAILADADILILDEATSNIDTrtelqIQAG-LNNLMR------GRTSFVIAHRLKTIEK-ADQILVIKDGSILERG 576
Cdd:cd03261 146 ALARALALDPELLLYDEPTAGLDP-----IASGvIDDLIRslkkelGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEG 219
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
359-534 |
1.13e-29 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 117.88 E-value: 1.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 359 HVELENVSFGYVENK---TILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDydinsLRSK 435
Cdd:COG1116 7 ALELRGVSKRFPTGGggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-----PGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 436 IGVVLQDTYLFA-GTIMDNIRYG--RLHASDEEVinAAKAASA------HSFIKHLPKQyeteiasegsnLSQGQKQLLA 506
Cdd:COG1116 82 RGVVFQEPALLPwLTVLDNVALGleLRGVPKAER--RERARELlelvglAGFEDAYPHQ-----------LSGGMRQRVA 148
|
170 180 190
....*....|....*....|....*....|
gi 447166293 507 IARAILADADILILDEATSNID--TRTELQ 534
Cdd:COG1116 149 IARALANDPEVLLMDEPFGALDalTRERLQ 178
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
361-585 |
3.80e-29 |
|
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: 115.74 E-value: 3.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 361 ELENVSFGYVENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDI---KDYDINSLRSKIG 437
Cdd:cd03256 2 EVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInklKGKALRQLRRQIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 438 VVLQDTYLFAG-TIMDNIRYGRLhasdeevinaakaaSAHSFIKHLPKQY---ETEIASE--------------GSNLSQ 499
Cdd:cd03256 82 MIFQQFNLIERlSVLENVLSGRL--------------GRRSTWRSLFGLFpkeEKQRALAalervglldkayqrADQLSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 500 GQKQLLAIARAILADADILILDEATSNIDTRTELQIQAGL--NNLMRGRTSFVIAHRLKTIEK-ADQILVIKDGSILERG 576
Cdd:cd03256 148 GQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLkrINREEGITVIVSLHQVDLAREyADRIVGLKDGRIVFDG 227
|
....*....
gi 447166293 577 NHESLMEDR 585
Cdd:cd03256 228 PPAELTDEV 236
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
47-334 |
4.86e-29 |
|
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: 117.13 E-value: 4.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 47 IFLVFVTTLLGLLGPYFMGVIIDQYIVPKDLNGTARMCMLLIAIYGVTVLLTWLQ-------TYVMINVALKTIQKIRQD 119
Cdd:cd18554 5 IVIGLVRFGIPLLLPLILKYIVDDVIQGSSLTLDEKVYKLFTIIGIMFFIFLILRppveyyrQYFAQWIANKILYDIRKD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 120 IFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFSLNWILALVTLITVPIMFFvtk 199
Cdd:cd18554 85 LFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYIL--- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 200 kLVAYSGKNFAK----RQKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRISATKADTFSAFIFPSMNFIN 275
Cdd:cd18554 162 -AVKYFFGRLRKltkeRSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTRWNAKTFSAVNTIT 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 447166293 276 NLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18554 241 DLAPLLVIGFAAYLVIEGNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDRV 299
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
360-576 |
5.18e-29 |
|
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: 114.66 E-value: 5.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYvENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINslRSKIGVV 439
Cdd:cd03301 1 VELENVTKRF-GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK--DRDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 440 LQDTYLFAG-TIMDNIRYG-RLHASDEEVIN-----AAKAASAHSFIKHLPKQyeteiasegsnLSQGQKQLLAIARAIL 512
Cdd:cd03301 78 FQNYALYPHmTVYDNIAFGlKLRKVPKDEIDervreVAELLQIEHLLDRKPKQ-----------LSGGQRQRVALGRAIV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447166293 513 ADADILILDEATSNIDTRTELQIQAGLNNLMR--GRTSFVIAH-RLKTIEKADQILVIKDGSILERG 576
Cdd:cd03301 147 REPKVFLMDEPLSNLDAKLRVQMRAELKRLQQrlGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
360-587 |
7.70e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 115.86 E-value: 7.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYVENKT-ILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINSLRSKIGV 438
Cdd:PRK13632 8 IKVENVSFSYPNSENnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 439 VLQ--DTYLFAGTIMDNIRYG----RLHASDEEVI--NAAKAASAHSFIKHLPkqyeteiasegSNLSQGQKQLLAIARA 510
Cdd:PRK13632 88 IFQnpDNQFIGATVEDDIAFGlenkKVPPKKMKDIidDLAKKVGMEDYLDKEP-----------QNLSGGQKQRVAIASV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447166293 511 ILADADILILDEATSNIDTRTELQIQAGLNNLMRGRTSFVIA--HRLKTIEKADQILVIKDGSILERGNHESLMEDRGF 587
Cdd:PRK13632 157 LALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISitHDMDEAILADKVIVFSEGKLIAQGKPKEILNNKEI 235
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
40-325 |
8.88e-29 |
|
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: 116.07 E-value: 8.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 40 KAALMFVIFLVFVTTLLGLLGPYFMGVIIDQYIVPKDLNGTARMCMLLIAIYGVTVLLTWLQTYVMINVALKTIQKIRQD 119
Cdd:cd18555 1 KKLLISILLLSLLLQLLTLLIPILTQYVIDNVIVPGNLNLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 120 IFEKIQTLSLRFFDVRSQGDLMSRVtNDIDNLNQALTQSVVQIISSALTFIGVTIAMFSLNWILALVTLITVPIMFFV-- 197
Cdd:cd18555 81 FFEHLLKLPYSFFENRSSGDLLFRA-NSNVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLll 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 198 --TKKLVAYSGKNFAKRQKdlgeLNGFIEEAITG-ADVTTLyGKEKETVQNF-NKINEQLRISaTKADTFSAFIFPSMNF 273
Cdd:cd18555 160 ltRKKIKKLNQEEIVAQTK----VQSYLTETLYGiETIKSL-GSEKNIYKKWeNLFKKQLKAF-KKKERLSNILNSISSS 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 447166293 274 INNLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQ 325
Cdd:cd18555 234 IQFIAPLLILWIGAYLVINGELTLGELIAFSSLAGSFLTPIVSLINSYNQFI 285
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
360-584 |
1.19e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 115.22 E-value: 1.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYVENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINSLRSKIGVV 439
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 440 LQ--DTYLFAGTIMDNIRYG----RLHASD-EEVINAAKAASAHSFIKHLPKQYeteiasegsnLSQGQKQLLAIARAIL 512
Cdd:PRK13647 85 FQdpDDQVFSSTVWDDVAFGpvnmGLDKDEvERRVEEALKAVRMWDFRDKPPYH----------LSYGQKKRVAIAGVLA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447166293 513 ADADILILDEATSNIDTR---TELQIQAGLNNlmRGRTSFVIAHRLK-TIEKADQILVIKDGSILERGNHESLMED 584
Cdd:PRK13647 155 MDPDVIVLDEPMAYLDPRgqeTLMEILDRLHN--QGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGDKSLLTDE 228
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
360-581 |
1.68e-28 |
|
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: 113.83 E-value: 1.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYVENK---TILKEVSLKARPGETIALVGPTGSGKTT---IINLLTRfYDiqQGQIHIDGKDIKDYDINSL- 432
Cdd:cd03258 2 IELKNVSKVFGDTGgkvTALKDVSLSVPKGEIFGIIGRSGAGKSTlirCINGLER-PT--SGSVLVDGTDLTLLSGKELr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 433 --RSKIGVVLQDTYLFAG-TIMDNIRYG-RLHASDEEVInAAKAASAHSFI--KHLPKQYEteiasegSNLSQGQKQLLA 506
Cdd:cd03258 79 kaRRRIGMIFQHFNLLSSrTVFENVALPlEIAGVPKAEI-EERVLELLELVglEDKADAYP-------AQLSGGQKQRVG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447166293 507 IARAILADADILILDEATSNIDTRTELQIQAGLNNLMR--GRTSFVIAHRLKTIEK-ADQILVIKDGSILERGNHESL 581
Cdd:cd03258 151 IARALANNPKVLLCDEATSALDPETTQSILALLRDINRelGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEV 228
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
112-588 |
1.72e-28 |
|
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: 121.56 E-value: 1.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 112 TIQKIRQDIFEKIQTLSLR----FFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGvTIAMFSLNWILALVT 187
Cdd:TIGR01271 952 TLLTVSKRLHEQMLHSVLQapmaVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLG-AIFVVSVLQPYIFIA 1030
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 188 LITVPIMFFVtkkLVAYsgknFAKRQKDLGELNGFIEEAITGADVTTL--------YGKEKETVQNFNK-IN-------- 250
Cdd:TIGR01271 1031 AIPVAVIFIM---LRAY----FLRTSQQLKQLESEARSPIFSHLITSLkglwtiraFGRQSYFETLFHKaLNlhtanwfl 1103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 251 --EQLRISATKADTFSAFIFPSMNFINNLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSrplsqfaTLMNTIqaav 328
Cdd:TIGR01271 1104 ylSTLRWFQMRIDIIFVFFFIAVTFIAIGTNQDGEGEVGIILTLAMNILSTLQWAVNSSIDVD-------GLMRSV---- 1172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 329 aggERVFEIMDEVPEI---------QNKKDAFIVQNI--------QGHVELENVSFGYVEN-KTILKEVSLKARPGETIA 390
Cdd:TIGR01271 1173 ---SRVFKFIDLPQEEprpsggggkYQLSTVLVIENPhaqkcwpsGGQMDVQGLTAKYTEAgRAVLQDLSFSVEGGQRVG 1249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 391 LVGPTGSGKTTIINLLTRFYDiQQGQIHIDGKDIKDYDINSLRSKIGVVLQDTYLFAGTIMDNIR-YGRLhaSDEEVINA 469
Cdd:TIGR01271 1250 LLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDpYEQW--SDEEIWKV 1326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 470 AKAASAHSFIKHLPKQYETEIASEGSNLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQAGLNNLMRGRTSF 549
Cdd:TIGR01271 1327 AEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVI 1406
|
490 500 510
....*....|....*....|....*....|....*....
gi 447166293 550 VIAHRLKTIEKADQILVIKDGSILERGNHESLMEDRGFY 588
Cdd:TIGR01271 1407 LSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLF 1445
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
360-572 |
2.31e-28 |
|
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: 112.62 E-value: 2.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENV--SFGyveNKTILKEVSLKARPGETIALVGPTGSGKTTI---INLLTRfydIQQGQIHIDGKDI--KDYDINSL 432
Cdd:cd03262 1 IEIKNLhkSFG---DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLlrcINLLEE---PDSGTIIIDGLKLtdDKKNINEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 433 RSKIGVVLQDTYLFAG-TIMDNIRYG---RLHASDEEVINAAKAASAHSFIKHLPKQYEteiasegSNLSQGQKQLLAIA 508
Cdd:cd03262 75 RQKVGMVFQQFNLFPHlTVLENITLApikVKGMSKAEAEERALELLEKVGLADKADAYP-------AQLSGGQQQRVAIA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447166293 509 RAILADADILILDEATSNIDTRTELQIQAGLNNLMR-GRTSFVIAHRLKTIEK-ADQILVIKDGSI 572
Cdd:cd03262 148 RALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEeGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
46-307 |
6.02e-28 |
|
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: 113.73 E-value: 6.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 46 VIFLVFVTTLLGLLgPYFMGVIIDQYIVPKDLNGTARMCMLLIAIYGVTVLLTWLQTYVMINVALKTIQKIRQDIFEKIQ 125
Cdd:cd18575 2 LIALLIAAAATLAL-GQGLRLLIDQGFAAGNTALLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 126 TLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFSLNWILALVTLITVPI----MFFVTKKL 201
Cdd:cd18575 81 RLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLvvlpIILFGRRV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 202 VAYSgknfAKRQKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRISATKADTFSAFIFPSMNFINNLGMGL 281
Cdd:cd18575 161 RRLS----RASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIVF 236
|
250 260
....*....|....*....|....*.
gi 447166293 282 VIGTGSVMVLNGMTTVGVIAAFINYS 307
Cdd:cd18575 237 VLWLGAHDVLAGRMSAGELSQFVFYA 262
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
360-573 |
1.36e-27 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 114.01 E-value: 1.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYvENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKdikdyDINSLRSK---I 436
Cdd:COG3839 4 LELENVSKSY-GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGR-----DVTDLPPKdrnI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 437 GVVLQDtylFA----GTIMDNIRYG-RLHASDEEVINA--AKAASA---HSFIKHLPKQyeteiasegsnLSQGQKQLLA 506
Cdd:COG3839 78 AMVFQS---YAlyphMTVYENIAFPlKLRKVPKAEIDRrvREAAELlglEDLLDRKPKQ-----------LSGGQRQRVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 507 IARAILADADILILDEATSNID------TRTEL-QIQAGLNnlmrgrTSFVIA-H------RLktiekADQILVIKDGSI 572
Cdd:COG3839 144 LGRALVREPKVFLLDEPLSNLDaklrveMRAEIkRLHRRLG------TTTIYVtHdqveamTL-----ADRIAVMNDGRI 212
|
.
gi 447166293 573 L 573
Cdd:COG3839 213 Q 213
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
360-528 |
1.67e-27 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 111.67 E-value: 1.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYVENKtILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQ-----QGQIHIDGKDI--KDYDINSL 432
Cdd:COG1117 12 IEVRNLNVYYGDKQ-ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIpgarvEGEILLDGEDIydPDVDVVEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 433 RSKIGVVLQDTYLFAGTIMDNIRYG-RLHAS------DEEVINAAKAAsahsfikHLPKQYETEIASEGSNLSQGQKQLL 505
Cdd:COG1117 91 RRRVGMVFQKPNPFPKSIYDNVAYGlRLHGIkskselDEIVEESLRKA-------ALWDEVKDRLKKSALGLSGGQQQRL 163
|
170 180
....*....|....*....|...
gi 447166293 506 AIARAILADADILILDEATSNID 528
Cdd:COG1117 164 CIARALAVEPEVLLMDEPTSALD 186
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
360-576 |
3.80e-27 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 112.88 E-value: 3.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYvENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKdikdyDINSL---RSKI 436
Cdd:COG3842 6 LELENVSKRY-GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGR-----DVTGLppeKRNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 437 GVVLQDtY-LFAG-TIMDNIRYG-RLHASDEEVInAAKAASA------HSFIKHLPKQyeteiasegsnLSQGQKQLLAI 507
Cdd:COG3842 80 GMVFQD-YaLFPHlTVAENVAFGlRMRGVPKAEI-RARVAELlelvglEGLADRYPHQ-----------LSGGQQQRVAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447166293 508 ARAILADADILILDEATSNID--TRTELQIQagLNNLMR--GRTSFVIAH------RLktiekADQILVIKDGSILERG 576
Cdd:COG3842 147 ARALAPEPRVLLLDEPLSALDakLREEMREE--LRRLQRelGITFIYVTHdqeealAL-----ADRIAVMNDGRIEQVG 218
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
360-576 |
4.62e-27 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 110.88 E-value: 4.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYVENKTI-LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINSLRSKIGV 438
Cdd:PRK13635 6 IRVEHISFRYPDAATYaLKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 439 VLQ--DTYLFAGTIMDNIRYG-------------RLHASDEEVinaakaaSAHSFIKHLPkqyeteiasegSNLSQGQKQ 503
Cdd:PRK13635 86 VFQnpDNQFVGATVQDDVAFGlenigvpreemveRVDQALRQV-------GMEDFLNREP-----------HRLSGGQKQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447166293 504 LLAIARAILADADILILDEATSNIDTRTELQIQAGLNNLMR--GRTSFVIAHRLKTIEKADQILVIKDGSILERG 576
Cdd:PRK13635 148 RVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEqkGITVLSITHDLDEAAQADRVIVMNKGEILEEG 222
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
40-334 |
7.65e-27 |
|
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: 110.76 E-value: 7.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 40 KAALMFVIFLVFVTTLLGLLGPYFMGVIIDQYIVPKDLNGTARMCMLLIAIYGVTVLLTWLQTYVMINVALKTIQKIRQD 119
Cdd:cd18782 1 RRALIEVLALSFVVQLLGLANPLLFQVIIDKVLVQQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 120 IFEKIQTLSLRFFDVRSQGDLMSRVtNDIDNLNQALTQSVVQIISSALTFIGVTIAMFSLNWILALVTLITVPIMFFVTk 199
Cdd:cd18782 81 IIDHLLRLPLGFFDKRPVGELSTRI-SELDTIRGFLTGTALTTLLDVLFSVIYIAVLFSYSPLLTLVVLATVPLQLLLT- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 200 KLVAYSGKNFAKRQKDL-GELNGFIEEAITGADVTTLYGKEKETVQNF-----NKINEQLRISATKAdTFSAFIFpsmnF 273
Cdd:cd18782 159 FLFGPILRRQIRRRAEAsAKTQSYLVESLTGIQTVKAQNAELKARWRWqnryaRSLGEGFKLTVLGT-TSGSLSQ----F 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447166293 274 INNLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18782 234 LNKLSSLLVLWVGAYLVLRGELTLGQLIAFRILSGYVTGPILRLSTLWQQFQELRVSLERL 294
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
45-581 |
1.26e-26 |
|
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: 114.12 E-value: 1.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 45 FVIFLVFVTTLLGLLGPYFMGVIIDQyivpkdLNGTARMCMLLIAIYGVTVLLTWLQTYV----MINVALKTIQKIRQDI 120
Cdd:COG4615 14 LLLLALLLGLLSGLANAGLIALINQA------LNATGAALARLLLLFAGLLVLLLLSRLAsqllLTRLGQHAVARLRLRL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 121 FEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALtQSVVQIISSALTFIGVTIAMFSLNWILALVTLITVPIMFFVTKK 200
Cdd:COG4615 88 SRRILAAPLERLERIGAARLLAALTEDVRTISQAF-VRLPELLQSVALVLGCLAYLAWLSPPLFLLTLVLLGLGVAGYRL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 201 LVAYSGKNFAK-RQKDlGELNGFIEEAITGAdvttlygkeKETvqnfnKIN----------------EQLRISATKADTF 263
Cdd:COG4615 167 LVRRARRHLRRaREAE-DRLFKHFRALLEGF---------KEL-----KLNrrrrraffdedlqptaERYRDLRIRADTI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 264 SAFIFPSMNFINNLGMGLVIGtgsVMVLNGMTTVGVIAAF---INYSRQfsrPLSQFATLMNTI-QAAVAGG--ERVFEI 337
Cdd:COG4615 232 FALANNWGNLLFFALIGLILF---LLPALGWADPAVLSGFvlvLLFLRG---PLSQLVGALPTLsRANVALRkiEELELA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 338 MDEVPEIQNKKDAFIVQNIQGHVELENVSFGYVENKT----ILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQ 413
Cdd:COG4615 306 LAAAEPAAADAAAPPAPADFQTLELRGVTYRYPGEDGdegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 414 QGQIHIDGKDIKDYDINSLRSKIGVVLQDTYLFAgtimdnirygRLHASDEEVINAAkaasAHSFIKHLPKQYETEIAsE 493
Cdd:COG4615 386 SGEILLDGQPVTADNREAYRQLFSAVFSDFHLFD----------RLLGLDGEADPAR----ARELLERLELDHKVSVE-D 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 494 GS----NLSQGQKQLLAIARAILADADILILDEATSNIDTR------TEL--QIQAglnnlmRGRTSFVIAHRLKTIEKA 561
Cdd:COG4615 451 GRfsttDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEfrrvfyTELlpELKA------RGKTVIAISHDDRYFDLA 524
|
570 580
....*....|....*....|
gi 447166293 562 DQILVIKDGSILERGNHESL 581
Cdd:COG4615 525 DRVLKMDYGKLVELTGPAAL 544
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
360-583 |
1.56e-26 |
|
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: 108.19 E-value: 1.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYVENKtiLKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKdyDINSLRSKIGVV 439
Cdd:cd03299 1 LKVENLSKDWKEFK--LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT--NLPPEKRDISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 440 LQDTYLFAG-TIMDNIRYGRLHAS------DEEVINAAKAASahsfIKHLPKQYETeiasegsNLSQGQKQLLAIARAIL 512
Cdd:cd03299 77 PQNYALFPHmTVYKNIAYGLKKRKvdkkeiERKVLEIAEMLG----IDHLLNRKPE-------TLSGGEQQRVAIARALV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447166293 513 ADADILILDEATSNIDTRTELQIQAGLNNLMR--GRTSFVIAHRLKTIEK-ADQILVIKDGSILERGNHESLME 583
Cdd:cd03299 146 VNPKILLLDEPFSALDVRTKEKLREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFK 219
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
361-576 |
1.73e-26 |
|
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: 108.59 E-value: 1.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 361 ELENVS--FGYVenkTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDI---KDYDINSLrsk 435
Cdd:COG0411 6 EVRGLTkrFGGL---VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDItglPPHRIARL--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 436 iGVV--LQDTYLFAG-TIMDNIRYGRLHASDEEVINAakaasahsfIKHLPKQYETEIASEG------------------ 494
Cdd:COG0411 80 -GIArtFQNPRLFPElTVLENVLVAAHARLGRGLLAA---------LLRLPRARREEREAREraeellervgladradep 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 495 -SNLSQGQKQLLAIARAILADADILILDEATsnidtrtelqiqAGLN-----NLM---------RGRTSFVIAHRLKTIE 559
Cdd:COG0411 150 aGNLSYGQQRRLEIARALATEPKLLLLDEPA------------AGLNpeeteELAelirrlrdeRGITILLIEHDMDLVM 217
|
250
....*....|....*...
gi 447166293 560 K-ADQILVIKDGSILERG 576
Cdd:COG0411 218 GlADRIVVLDFGRVIAEG 235
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
360-583 |
1.83e-26 |
|
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: 107.71 E-value: 1.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYvENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINslRSKIGVV 439
Cdd:cd03300 1 IELENVSKFY-GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 440 LQDTYLFAG-TIMDNIRYG-RLHASDEEVINaAKAASAHSFIKHlpKQYETEIASEgsnLSQGQKQLLAIARAILADADI 517
Cdd:cd03300 78 FQNYALFPHlTVFENIAFGlRLKKLPKAEIK-ERVAEALDLVQL--EGYANRKPSQ---LSGGQQQRVAIARALVNEPKV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447166293 518 LILDEATSNIDTRTELQIQAGLNNLMR--GRTSFVIAH-RLKTIEKADQILVIKDGSILERGNHESLME 583
Cdd:cd03300 152 LLLDEPLGALDLKLRKDMQLELKRLQKelGITFVFVTHdQEEALTMSDRIAVMNKGKIQQIGTPEEIYE 220
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
373-573 |
2.07e-26 |
|
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: 107.21 E-value: 2.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 373 KTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKdYDINSLRSKIGVVLQDTYLFAG-TIM 451
Cdd:cd03263 15 KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR-TDRKAARQSLGYCPQFDALFDElTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 452 DNIR-YGRLHASDEEVINAAKAASAHSFikHLPKQYETEIasegSNLSQGQKQLLAIARAILADADILILDEATSNIDTR 530
Cdd:cd03263 94 EHLRfYARLKGLPKSEIKEEVELLLRVL--GLTDKANKRA----RTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 447166293 531 TELQIQAGLNNLMRGRTSFVIAHRLKTIEK-ADQILVIKDGSIL 573
Cdd:cd03263 168 SRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLR 211
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
360-570 |
6.21e-26 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 111.65 E-value: 6.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVS--FGYVenkTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDIN-SLRSKI 436
Cdd:COG1129 5 LEMRGISksFGGV---KALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRdAQAAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 437 GVVLQDTYLFAG-TIMDNI-------RYGRLHasDEEVINAAKAAsahsfikhLpKQYETEI--ASEGSNLSQGQKQLLA 506
Cdd:COG1129 82 AIIHQELNLVPNlSVAENIflgreprRGGLID--WRAMRRRAREL--------L-ARLGLDIdpDTPVGDLSVAQQQLVE 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 507 IARAILADADILILDEATSNIdTRTELQIqagLNNLMR-----GRTSFVIAHRLKTIEK-ADQILVIKDG 570
Cdd:COG1129 151 IARALSRDARVLILDEPTASL-TEREVER---LFRIIRrlkaqGVAIIYISHRLDEVFEiADRVTVLRDG 216
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
360-584 |
6.49e-26 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 106.72 E-value: 6.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVS--FGYVenkTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKD--YDINSLRSK 435
Cdd:PRK09493 2 IEFKNVSkhFGPT---QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkVDERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 436 IGVVLQDTYLFAG-TIMDNIRYGRLH---ASDEEVINAAK--------AASAHsfikHLPkqyeteiasegSNLSQGQKQ 503
Cdd:PRK09493 79 AGMVFQQFYLFPHlTALENVMFGPLRvrgASKEEAEKQARellakvglAERAH----HYP-----------SELSGGQQQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 504 LLAIARAILADADILILDEATSNIDT--RTE-LQIQAGLNNlmRGRTSFVIAHRLKTIEK-ADQILVIKDGSILERGNHE 579
Cdd:PRK09493 144 RVAIARALAVKPKLMLFDEPTSALDPelRHEvLKVMQDLAE--EGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQ 221
|
....*
gi 447166293 580 SLMED 584
Cdd:PRK09493 222 VLIKN 226
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
360-582 |
8.23e-26 |
|
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: 106.32 E-value: 8.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYvENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRfyDIQQG---QIHIDGKDIKDYDINSLRSKI 436
Cdd:COG1119 4 LELRNVTVRR-GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITG--DLPPTygnDVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 437 GVV---LQDTYLFAGTIMDNIRYGrLHAS-------DEEVINAAKAASAHSFIKHLPKQ-YETeiasegsnLSQGQKQLL 505
Cdd:COG1119 81 GLVspaLQLRFPRDETVLDVVLSG-FFDSiglyrepTDEQRERARELLELLGLAHLADRpFGT--------LSQGEQRRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 506 AIARAILADADILILDEATSNIDTRTELQIQAGLNNLMR-GRTSFV-IAHRLKTI-EKADQILVIKDGSILERGNHESLM 582
Cdd:COG1119 152 LIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAeGAPTLVlVTHHVEEIpPGITHVLLLKDGRVVAAGPKEEVL 231
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
361-576 |
1.54e-25 |
|
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: 105.21 E-value: 1.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 361 ELENVS--FGYVenkTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINsLRSKIGV 438
Cdd:cd03219 2 EVRGLTkrFGGL---VALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH-EIARLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 439 V--LQDTYLFAG-TIMDNIRYGRLHASDEEVINAAKAAS-------AHSFIK--HLPKqYETEIAsegSNLSQGQKQLLA 506
Cdd:cd03219 78 GrtFQIPRLFPElTVLENVMVAAQARTGSGLLLARARREerearerAEELLErvGLAD-LADRPA---GELSYGQQRRLE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 507 IARAILADADILILDEATsnidtrtelqiqAGLN--------NLMR-----GRTSFVIAHRLKTIEK-ADQILVIKDGSI 572
Cdd:cd03219 154 IARALATDPKLLLLDEPA------------AGLNpeeteelaELIRelrerGITVLLVEHDMDVVMSlADRVTVLDQGRV 221
|
....
gi 447166293 573 LERG 576
Cdd:cd03219 222 IAEG 225
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
376-583 |
2.05e-25 |
|
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: 105.80 E-value: 2.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 376 LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDI---KDYDINSLRSK-IGVVLQDTYLFAG-TI 450
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIaamSRKELRELRRKkISMVFQSFALLPHrTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 451 MDNIRYGRLHASDEEVINAAKAASA------HSFIKHLPKQyeteiasegsnLSQGQKQLLAIARAILADADILILDEAT 524
Cdd:cd03294 120 LENVAFGLEVQGVPRAEREERAAEAlelvglEGWEHKYPDE-----------LSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447166293 525 SNID--TRTELQ-----IQAglnnlMRGRTSFVIAHRL-KTIEKADQILVIKDGSILERGNHESLME 583
Cdd:cd03294 189 SALDplIRREMQdellrLQA-----ELQKTIVFITHDLdEALRLGDRIAIMKDGRLVQVGTPEEILT 250
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
361-584 |
3.61e-25 |
|
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: 103.67 E-value: 3.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 361 ELENVSFGYVENkTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKD---YDINslRSKIG 437
Cdd:cd03224 2 EVENLNAGYGKS-QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGlppHERA--RAGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 438 VVLQDTYLFAG-TIMDNIRYGRLHASDEEVinaaKAASAHSF-----IKHLPKQyeteiasEGSNLSQGQKQLLAIARAI 511
Cdd:cd03224 79 YVPEGRRIFPElTVEENLLLGAYARRRAKR----KARLERVYelfprLKERRKQ-------LAGTLSGGEQQMLAIARAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447166293 512 LADADILILDEATSNIDTRTELQIQAGLNNL-MRGRTSFVIAHRLKTIEK-ADQILVIKDGSILERGNHESLMED 584
Cdd:cd03224 148 MSRPKLLLLDEPSEGLAPKIVEEIFEAIRELrDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLAD 222
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
361-582 |
6.35e-25 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 103.30 E-value: 6.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 361 ELENVSFGYvenKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDInSLRsKIGVVL 440
Cdd:COG3840 3 RLDDLTYRY---GDFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP-AER-PVSMLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 441 QDTYLFAG-TIMDNIRYG-----RLHASD-EEVINAAKAASAHSFIKHLPKQyeteiasegsnLSQGQKQLLAIARAILA 513
Cdd:COG3840 78 QENNLFPHlTVAQNIGLGlrpglKLTAEQrAQVEQALERVGLAGLLDRLPGQ-----------LSGGQRQRVALARCLVR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447166293 514 DADILILDEATSNIDT--RTE-LQIQAGLNNlMRGRTSFVIAHRLKTIEK-ADQILVIKDGSILERGNHESLM 582
Cdd:COG3840 147 KRPILLLDEPFSALDPalRQEmLDLVDELCR-ERGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALL 218
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
360-569 |
9.49e-25 |
|
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: 102.17 E-value: 9.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYvENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDyDINSLRSKIGVV 439
Cdd:COG4133 3 LEAENLSCRR-GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 440 LQDTYLFAG-TIMDNIR-YGRLH--ASDEEVINAAKAA---SAHSfikHLPkqyeteiaseGSNLSQGQKQLLAIARAIL 512
Cdd:COG4133 81 GHADGLKPElTVRENLRfWAALYglRADREAIDEALEAvglAGLA---DLP----------VRQLSAGQKRRVALARLLL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447166293 513 ADADILILDEATSNIDTRTELQIQAGLNNLMRGRTSFVIA-HRLKTIEkADQILVIKD 569
Cdd:COG4133 148 SPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELA-AARVLDLGD 204
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
45-344 |
2.03e-24 |
|
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: 104.07 E-value: 2.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 45 FVIFLVFVTTLLGLLGP---YFMGVIIDQYIVPKD---LNGTARMCMLLIAIYGVTVLLTWLQTYVMINVALKTIQKIRQ 118
Cdd:cd18578 10 LLLLGLIGAIIAGAVFPvfaILFSKLISVFSLPDDdelRSEANFWALMFLVLAIVAGIAYFLQGYLFGIAGERLTRRLRK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 119 DIFEKIqtlsLR----FFD--VRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFI-GVTIAmFSLNWILALVTLITV 191
Cdd:cd18578 90 LAFRAI----LRqdiaWFDdpENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVaGLIIA-FVYGWKLALVGLATV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 192 PIMFFVTKKLVAYSGKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRISATKADTFSAFIFPSM 271
Cdd:cd18578 165 PLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLGFGLS 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447166293 272 NFINNLGMGLVIGTGSVMVLNG-MTTVGVIAAF--INYSRQFsrpLSQFATLMNTIQAAVAGGERVFEIMDEVPEI 344
Cdd:cd18578 245 QSLTFFAYALAFWYGGRLVANGeYTFEQFFIVFmaLIFGAQS---AGQAFSFAPDIAKAKAAAARIFRLLDRKPEI 317
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
46-334 |
2.08e-24 |
|
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: 103.48 E-value: 2.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 46 VIFLVfVTTLLGLLGPYFMGVIIDqyIVPKDLNGT--------ARMCMLLIAIYGVTVLLTWLQTYVMINVALKTIQKIR 117
Cdd:cd18780 2 TIALL-VSSGTNLALPYFFGQVID--AVTNHSGSGgeealralNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 118 QDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFSLNWILALVTLITVPIMFFV 197
Cdd:cd18780 79 KRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 198 TkklVAYSG--KNFAKRQKD-LGELNGFIEEAITGADVTTLYGKEKETVQNFN-KINEQLRISATKADTFSAFiFPSMNF 273
Cdd:cd18780 159 A---VIYGKyvRKLSKKFQDaLAAASTVAEESISNIRTVRSFAKETKEVSRYSeKINESYLLGKKLARASGGF-NGFMGA 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447166293 274 INNLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18780 235 AAQLAIVLVLWYGGRLVIDGELTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAVGASVRV 295
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
360-570 |
3.33e-24 |
|
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: 99.04 E-value: 3.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENV--SFGYVenkTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDIN-SLRSKI 436
Cdd:cd03216 1 LELRGItkRFGGV---KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRdARRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 437 GVVLQdtylfagtimdnirygrlhasdeevinaakaasahsfikhlpkqyeteiasegsnLSQGQKQLLAIARAILADAD 516
Cdd:cd03216 78 AMVYQ-------------------------------------------------------LSVGERQMVEIARALARNAR 102
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 517 ILILDEATSNIDTRtelQIQAgLNNLMR-----GRTSFVIAHRLKTI-EKADQILVIKDG 570
Cdd:cd03216 103 LLILDEPTAALTPA---EVER-LFKVIRrlraqGVAVIFISHRLDEVfEIADRVTVLRDG 158
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
360-584 |
3.70e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 102.57 E-value: 3.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYVENKT-ILKEVSLKARPGETIALVGPTGSGKTTI---INLLTRFYDIQQGQIHIDGKDIKDYDINSLRSK 435
Cdd:PRK13640 6 VEFKHVSFTYPDSKKpALNDISFSIPRGSWTALIGHNGSGKSTIsklINGLLLPDDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 436 IGVVLQ--DTYLFAGTIMDNIRYG---RLHASDEEVINAAKAASAHSFIKHlpkqyeteIASEGSNLSQGQKQLLAIARA 510
Cdd:PRK13640 86 VGIVFQnpDNQFVGATVGDDVAFGlenRAVPRPEMIKIVRDVLADVGMLDY--------IDSEPANLSGGQKQRVAIAGI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447166293 511 ILADADILILDEATSNIDTRTELQIQAGLNNLM--RGRTSFVIAHRLKTIEKADQILVIKDGSILERGNHESLMED 584
Cdd:PRK13640 158 LAVEPKIIILDESTSMLDPAGKEQILKLIRKLKkkNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
40-311 |
4.71e-24 |
|
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: 102.54 E-value: 4.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 40 KAALMFVIFLVFVTTLLGLLGPYFMGVIIDQYIVPKDLNGTARMCMLLIAIYGVTVLLTWLQTYVMINVALKTIQKIRQD 119
Cdd:cd18567 1 KRALLQILLLSLALELFALASPLYLQLVIDEVIVSGDRDLLTVLAIGFGLLLLLQALLSALRSWLVLYLSTSLNLQWTSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 120 IFEKIQTLSLRFFDVRSQGDLMSRVtNDIDNLNQALTQSVVQIISSALTFIGVTIAMFSLNWILALVTLITVPIMFFVtk 199
Cdd:cd18567 81 LFRHLLRLPLSYFEKRHLGDIVSRF-GSLDEIQQTLTTGFVEALLDGLMAILTLVMMFLYSPKLALIVLAAVALYALL-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 200 KLVAYSgknfakRQKDLGEL--------NGFIEEAITGADVTTLYGKEKE---TVQNF--NKINEQLRISatKADTFSAF 266
Cdd:cd18567 158 RLALYP------PLRRATEEqivasakeQSHFLETIRGIQTIKLFGREAEreaRWLNLlvDAINADIRLQ--RLQILFSA 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 447166293 267 IfpsMNFINNLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFS 311
Cdd:cd18567 230 A---NGLLFGLENILVIYLGALLVLDGEFTVGMLFAFLAYKDQFS 271
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
360-584 |
7.46e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 101.69 E-value: 7.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYVENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKdYDINSL---RSKI 436
Cdd:PRK13639 2 LETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK-YDKKSLlevRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 437 GVVLQ--DTYLFAGTIMDNIRYGRLHA--SDEEVIN----AAKAASAHSFIKHLPKqyeteiasegsNLSQGQKQLLAIA 508
Cdd:PRK13639 81 GIVFQnpDDQLFAPTVEEDVAFGPLNLglSKEEVEKrvkeALKAVGMEGFENKPPH-----------HLSGGQKKRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447166293 509 RAILADADILILDEATSNIDTRTELQIQAGLNNLMR-GRTSFVIAHRLKTIEK-ADQILVIKDGSILERGNHESLMED 584
Cdd:PRK13639 150 GILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKeGITIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPKEVFSD 227
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
372-576 |
9.41e-24 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 99.21 E-value: 9.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 372 NKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKdyDINSLRSKIGVVLQDTYLFAG-TI 450
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ--KNIEALRRIGALIEAPGFYPNlTA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 451 MDNIR-----YGRLHASDEEVINAAK-AASAHSFIKhlpkqyeteiasegsNLSQGQKQLLAIARAILADADILILDEAT 524
Cdd:cd03268 90 RENLRllarlLGIRKKRIDEVLDVVGlKDSAKKKVK---------------GFSLGMKQRLGIALALLGNPDLLILDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 447166293 525 SNIDTRTELQIQAGLNNLMR-GRTSFVIAHRLKTIEK-ADQILVIKDGSILERG 576
Cdd:cd03268 155 NGLDPDGIKELRELILSLRDqGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
373-576 |
9.52e-24 |
|
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: 98.78 E-value: 9.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 373 KTILKEVSLKARPGETIALVGPTGSGKTTIINLLT--RFYDIQQGQIHIDGKDIkdyDINSLRSKIGVVLQDTYLFAG-T 449
Cdd:cd03213 22 KQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPL---DKRSFRKIIGYVPQDDILHPTlT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 450 IMDNIRYgrlhasdeevinaakaasahsfikhlpkqyeteiASEGSNLSQGQKQLLAIARAILADADILILDEATSNIDT 529
Cdd:cd03213 99 VRETLMF----------------------------------AAKLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDS 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 447166293 530 RTELQIQAGLNNLMR-GRTSFVIAHRLKT--IEKADQILVIKDGSILERG 576
Cdd:cd03213 145 SSALQVMSLLRRLADtGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
360-572 |
1.01e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 101.28 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYVEN----KTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDIN--SLR 433
Cdd:PRK13637 3 IKIENLTHIYMEGtpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKlsDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 434 SKIGVVLQ--DTYLFAGTIMDNIRYG--RLHASDEEVINAAKAAsahsfIKHLPKQYETEIASEGSNLSQGQKQLLAIAR 509
Cdd:PRK13637 83 KKVGLVFQypEYQLFEETIEKDIAFGpiNLGLSEEEIENRVKRA-----MNIVGLDYEDYKDKSPFELSGGQKRRVAIAG 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447166293 510 AILADADILILDEATSNIDTRTELQIQAGLNNLMR--GRTSFVIAHRLKTIEK-ADQILVIKDGSI 572
Cdd:PRK13637 158 VVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVAKlADRIIVMNKGKC 223
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
360-582 |
1.24e-23 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 100.47 E-value: 1.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYvENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINSLRSKIGVV 439
Cdd:PRK11231 3 LRTENLTVGY-GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 440 LQDTYLFAG-TIMDNIRYGR---------LHASDEEVINAAKAASAhsfIKHLPKQYETEiasegsnLSQGQKQLLAIAR 509
Cdd:PRK11231 82 PQHHLTPEGiTVRELVAYGRspwlslwgrLSAEDNARVNQAMEQTR---INHLADRRLTD-------LSGGQRQRAFLAM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447166293 510 AILADADILILDEATSNIDtrteLQIQAGLNNLMR-----GRTSFVIAHRLKTIEK-ADQILVIKDGSILERGNHESLM 582
Cdd:PRK11231 152 VLAQDTPVVLLDEPTTYLD----INHQVELMRLMRelntqGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEVM 226
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
360-576 |
1.90e-23 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 101.76 E-value: 1.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYvENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIkDYDINSLRSKIGVV 439
Cdd:COG1118 3 IEVRNISKRF-GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL-FTNLPPRERRVGFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 440 LQDTYLFAG-TIMDNIRYG-RLHASDEEVInAAKAAS------AHSFIKHLPKQyeteiasegsnLSQGQKQLLAIARAI 511
Cdd:COG1118 81 FQHYALFPHmTVAENIAFGlRVRPPSKAEI-RARVEEllelvqLEGLADRYPSQ-----------LSGGQRQRVALARAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447166293 512 LADADILILDEATSNIDT--RTELQIQaglnnLMR-----GRTS-FVI-----AHRLktiekADQILVIKDGSILERG 576
Cdd:COG1118 149 AVEPEVLLLDEPFGALDAkvRKELRRW-----LRRlhdelGGTTvFVThdqeeALEL-----ADRVVVMNQGRIEQVG 216
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
40-327 |
2.16e-23 |
|
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: 100.65 E-value: 2.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 40 KAALMFVIFLVFVTTLLGLLGPYFMGVIIDQYIVPKDLNGTARMCMLLIAIYGVTVLLTWLQTYVMINvalkTIQKIrqD 119
Cdd:cd18588 1 KKLLGEVLLASLFLQLFALVTPLFFQVIIDKVLVHRSLSTLDVLAIGLLVVALFEAVLSGLRTYLFSH----TTNRI--D 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 120 ------IFEKIQTLSLRFFDVRSQGDLMSRVtNDIDNLNQALTqsvvqiiSSALT------FIGVTIA-MFSLNWILALV 186
Cdd:cd18588 75 aelgarLFRHLLRLPLSYFESRQVGDTVARV-RELESIRQFLT-------GSALTlvldlvFSVVFLAvMFYYSPTLTLI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 187 TLITVPIMF----FVTKKLvaysgKNFAKRQKDLGELN-GFIEEAITGADVTTLYGKEKETVQNFNKINEQLRISATKAD 261
Cdd:cd18588 147 VLASLPLYAllslLVTPIL-----RRRLEEKFQRGAENqSFLVETVTGIETVKSLAVEPQFQRRWEELLARYVKASFKTA 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447166293 262 TFSAFIFPSMNFINNLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAA 327
Cdd:cd18588 222 NLSNLASQIVQLIQKLTTLAILWFGAYLVMDGELTIGQLIAFNMLAGQVSQPVLRLVQLWQDFQQA 287
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
376-576 |
6.83e-23 |
|
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: 97.05 E-value: 6.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 376 LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGkdikdYDINS----LRSKIGVVLQDTYLFAG-TI 450
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG-----FDVVKepaeARRRLGFVSDSTGLYDRlTA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 451 MDNIRY-GRLHAsdeevinaAKAASAHSFIKHLPKQYETE--IASEGSNLSQGQKQLLAIARAILADADILILDEATSNI 527
Cdd:cd03266 96 RENLEYfAGLYG--------LKGDELTARLEELADRLGMEelLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447166293 528 D---TRTELQIQAGLNNLmrGRTSFVIAHRLKTIEK-ADQILVIKDGSILERG 576
Cdd:cd03266 168 DvmaTRALREFIRQLRAL--GKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
115-581 |
7.48e-23 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 103.90 E-value: 7.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 115 KIRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFSLNWIL-------ALVT 187
Cdd:PLN03232 371 RLRSTLVAAIFHKSLRLTHEARKNFASGKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMVLLYQQLgvaslfgSLIL 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 188 LITVPIMFFVTKKLVAYSGKNFAKRQKDLGELNgfieEAITGADVTTLYGKEKETVQNFNKI-NEQLRI--SATKADTFS 264
Cdd:PLN03232 451 FLLIPLQTLIVRKMRKLTKEGLQWTDKRVGIIN----EILASMDTVKCYAWEKSFESRIQGIrNEELSWfrKAQLLSAFN 526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 265 AFIFPSMNFINNLgmglvIGTGSVMVLNGMTTVGviAAFINYS--RQFSRPLSQFATLMNTIQAAVAGGERVFE------ 336
Cdd:PLN03232 527 SFILNSIPVVVTL-----VSFGVFVLLGGDLTPA--RAFTSLSlfAVLRSPLNMLPNLLSQVVNANVSLQRIEElllsee 599
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 337 -IMDEVPEIQNKKDAFIVQNiqghvelENVSFGYVENKTILKEVSLKARPGETIALVGPTGSGKTTIIN-LLTRFYDIQQ 414
Cdd:PLN03232 600 rILAQNPPLQPGAPAISIKN-------GYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAET 672
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 415 GQIHIdgkdikdydinslRSKIGVVLQDTYLFAGTIMDNIRYGrlhaSDEEVINAAKAASAHSfIKH----LPKQYETEI 490
Cdd:PLN03232 673 SSVVI-------------RGSVAYVPQVSWIFNATVRENILFG----SDFESERYWRAIDVTA-LQHdldlLPGRDLTEI 734
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 491 ASEGSNLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQI-QAGLNNLMRGRTSFVIAHRLKTIEKADQILVIKD 569
Cdd:PLN03232 735 GERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVfDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSE 814
|
490
....*....|..
gi 447166293 570 GSILERGNHESL 581
Cdd:PLN03232 815 GMIKEEGTFAEL 826
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
40-571 |
8.87e-23 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 102.58 E-value: 8.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 40 KAALMF--VIFLVFVTTLLGLLGPYFMGVIIDQyIVPKDLNG----TARMCMLLIAIYGVTVLLTWLQTYVMInvalkti 113
Cdd:COG4178 22 KAWGLLalLLLLTLASVGLNVLLNFWNRDFYDA-LQARDAAAfwqqLGVFALLAAISILLAVYQTYLRQRLQI------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 114 qKIRQDIFEKIQTLSL---RFFDVRSQGDLMS----RVTNDIDNL-NQALT------QSVVQIIS-----------SALT 168
Cdd:COG4178 94 -RWREWLTERLLDRWLsnrAYYRLQLSGGEIDnpdqRIAEDIRLFtETTLSlslgllSSVVTLISfigilwslsgsLTFT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 169 FIGVTIA----MFslnWILALVTLITVPIMFFVTKKLVaysGKNFAKRQK--DL-GEL-----NGfieEAITgadvttLY 236
Cdd:COG4178 173 LGGYSITipgyMV---WAALIYAIIGTLLTHLIGRPLI---RLNFEQQRReaDFrFALvrvreNA---ESIA------LY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 237 GKEKE-----------TVQNFNKINEQLRIsatkadtFSAFIFPSMNFINNLGMGLVigtgSVMVLNGMTTVGVI----A 301
Cdd:COG4178 238 RGEAAerrrlrrrfdaVIANWRRLIRRQRN-------LTFFTTGYGQLAVIFPILVA----APRYFAGEITLGGLmqaaS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 302 AFinysRQFSRPLSQFATLMNTIQAAVAGGERV--FEIMDEVPEIQNKKDAFIVQNIQGHVELENVSFGYVENKTILKEV 379
Cdd:COG4178 307 AF----GQVQGALSWFVDNYQSLAEWRATVDRLagFEEALEAADALPEAASRIETSEDGALALEDLTLRTPDGRPLLEDL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 380 SLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHI-DGKDIkdydinslrskigVVL-QDTYLFAGTIMDNIRY- 456
Cdd:COG4178 383 SLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARV-------------LFLpQRPYLPLGTLREALLYp 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 457 -GRLHASDEEVINAAKAASahsfIKHLPKQYETEiASEGSNLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQI 535
Cdd:COG4178 450 aTAEAFSDAELREALEAVG----LGHLAERLDEE-ADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAAL 524
|
570 580 590
....*....|....*....|....*....|....*.
gi 447166293 536 QAGLNNLMRGRTSFVIAHRLKTIEKADQILVIKDGS 571
Cdd:COG4178 525 YQLLREELPGTTVISVGHRSTLAAFHDRVLELTGDG 560
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
360-572 |
1.55e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 97.88 E-value: 1.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYVENKT--ILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINSLRSKIG 437
Cdd:PRK13650 5 IEVKNLTFKYKEDQEkyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 438 VVLQ--DTYLFAGTIMDNIRYG------RLHASDEEVINAAKAASAHSFIKHLPkqyeteiasegSNLSQGQKQLLAIAR 509
Cdd:PRK13650 85 MVFQnpDNQFVGATVEDDVAFGlenkgiPHEEMKERVNEALELVGMQDFKEREP-----------ARLSGGQKQRVAIAG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447166293 510 AILADADILILDEATSNIDTRTELQIQAGLNNLMR--GRTSFVIAHRLKTIEKADQILVIKDGSI 572
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQV 218
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
361-524 |
1.76e-22 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 96.59 E-value: 1.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 361 ELENVSFGYvENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKD---YDInsLRSKIG 437
Cdd:COG0410 5 EVENLHAGY-GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGlppHRI--ARLGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 438 VVLQDTYLFAG-TIMDNIRYGRLHASDEEVINAAKAASAHSFikhlPKQYEtEIASEGSNLSQGQKQLLAIARAILADAD 516
Cdd:COG0410 82 YVPEGRRIFPSlTVEENLLLGAYARRDRAEVRADLERVYELF----PRLKE-RRRQRAGTLSGGEQQMLAIGRALMSRPK 156
|
....*...
gi 447166293 517 ILILDEAT 524
Cdd:COG0410 157 LLLLDEPS 164
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
360-576 |
1.92e-22 |
|
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: 96.64 E-value: 1.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVS--FGyveNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINslRSKIG 437
Cdd:cd03296 3 IEVRNVSkrFG---DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 438 VVLQDTYLFAG-TIMDNIRYG-RLHASDEEVINAAKAASAHSFIK-----HLPKQYETEiasegsnLSQGQKQLLAIARA 510
Cdd:cd03296 78 FVFQHYALFRHmTVFDNVAFGlRVKPRSERPPEAEIRAKVHELLKlvqldWLADRYPAQ-------LSGGQRQRVALARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447166293 511 ILADADILILDEATSNIDTRTELQIQAGLNNL---MRGRTSFVIAHRLKTIEKADQILVIKDGSILERG 576
Cdd:cd03296 151 LAVEPKVLLLDEPFGALDAKVRKELRRWLRRLhdeLHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVG 219
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
360-572 |
1.99e-22 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 99.25 E-value: 1.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYvENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDY-----DINSlrs 434
Cdd:PRK09452 15 VELRGISKSF-DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVpaenrHVNT--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 435 kigvVLQDTYLFAG-TIMDNIRYG-RLHASDEE-----VINAAKAASAHSFIKHLPKQyeteiasegsnLSQGQKQLLAI 507
Cdd:PRK09452 91 ----VFQSYALFPHmTVFENVAFGlRMQKTPAAeitprVMEALRMVQLEEFAQRKPHQ-----------LSGGQQQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447166293 508 ARAILADADILILDEATSNIDTRTELQIQAGLNNLMR--GRT-SFVIAHRLKTIEKADQILVIKDGSI 572
Cdd:PRK09452 156 ARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRklGITfVFVTHDQEEALTMSDRIVVMRDGRI 223
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
376-584 |
2.61e-22 |
|
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: 100.91 E-value: 2.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 376 LKEVSLKARPGETIALVGPTGSGKTT----IINLLTrfydiQQGQIHIDGKDIKDYD---INSLRSKIGVVLQDTYlfaG 448
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTlglaLLRLIP-----SEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDPF---G 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 449 ------TIMDNIRYG-RLHASD------EEVINAA------KAASAHsfikhlpkQYETEiasegsnLSQGQKQLLAIAR 509
Cdd:COG4172 374 slsprmTVGQIIAEGlRVHGPGlsaaerRARVAEAleevglDPAARH--------RYPHE-------FSGGQRQRIAIAR 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 510 AILADADILILDEATSNIDtRTelqIQAGLNNLMR------GRTSFVIAHRLKTIEK-ADQILVIKDGSILERGNHESLM 582
Cdd:COG4172 439 ALILEPKLLVLDEPTSALD-VS---VQAQILDLLRdlqrehGLAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQVF 514
|
..
gi 447166293 583 ED 584
Cdd:COG4172 515 DA 516
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
360-576 |
3.92e-22 |
|
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: 94.78 E-value: 3.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYVENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYD---INSLRSKI 436
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 437 GVVLQDTYLFAG-TIMDNIRYGR--LHASDEEVINAAKAASAHSFIKHlpkqYETEIASEgsnLSQGQKQLLAIARAILA 513
Cdd:cd03292 81 GVVFQDFRLLPDrNVYENVAFALevTGVPPREIRKRVPAALELVGLSH----KHRALPAE---LSGGEQQRVAIARAIVN 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447166293 514 DADILILDEATSNIDTRTELQIQAGLNNLMRGRTSFVIAHRLKTIEKADQILVIkdgsILERG 576
Cdd:cd03292 154 SPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVI----ALERG 212
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
360-574 |
5.20e-22 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 100.05 E-value: 5.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYVENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINSLRSKIGVV 439
Cdd:PRK10522 323 LELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 440 LQDTYLFagtimdniryGRLHASDEEvinAAKAASAHSFIKHLPKQYETEIASE---GSNLSQGQKQLLAIARAILADAD 516
Cdd:PRK10522 403 FTDFHLF----------DQLLGPEGK---PANPALVEKWLERLKMAHKLELEDGrisNLKLSKGQKKRLALLLALAEERD 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 517 ILILDEATSNIDTRTELQIQAGLNNLMR--GRTSFVIAHRLKTIEKADQILVIKDGSILE 574
Cdd:PRK10522 470 ILLLDEWAADQDPHFRREFYQVLLPLLQemGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
359-577 |
6.37e-22 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 97.07 E-value: 6.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 359 HVELENVSFGYVENK---TILKEVSLKARPGETIALVGPTGSGKTT---IINLLTRFydiQQGQIHIDGKDIKDYDINSL 432
Cdd:COG1135 1 MIELENLSKTFPTKGgpvTALDDVSLTIEKGEIFGIIGYSGAGKSTlirCINLLERP---TSGSVLVDGVDLTALSEREL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 433 ---RSKIGVVLQDTYLFAG-TIMDNIRYG-RLHASDEEVInAAKAAS----------AHSFikhlPKQyeteiasegsnL 497
Cdd:COG1135 78 raaRRKIGMIFQHFNLLSSrTVAENVALPlEIAGVPKAEI-RKRVAEllelvglsdkADAY----PSQ-----------L 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 498 SQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQAGLNNLMR--GRTSFVIAHRLKTIEK-ADQILVIKDGSILE 574
Cdd:COG1135 142 SGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHEMDVVRRiCDRVAVLENGRIVE 221
|
...
gi 447166293 575 RGN 577
Cdd:COG1135 222 QGP 224
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
360-576 |
2.57e-21 |
|
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: 92.56 E-value: 2.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYVENKTILkevSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINslRSKIGVV 439
Cdd:cd03298 1 VRLDKIRFSYGEQPMHF---DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSML 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 440 LQDTYLFAG-TIMDNIRYG-----RLHASDEEVINAAKAASA-HSFIKHLPKQyeteiasegsnLSQGQKQLLAIARAIL 512
Cdd:cd03298 76 FQENNLFAHlTVEQNVGLGlspglKLTAEDRQAIEVALARVGlAGLEKRLPGE-----------LSGGERQRVALARVLV 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447166293 513 ADADILILDEATSNIDTRTELQIQAGLNNL--MRGRTSFVIAHRLKTIEK-ADQILVIKDGSILERG 576
Cdd:cd03298 145 RDKPVLLLDEPFAALDPALRAEMLDLVLDLhaETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
369-577 |
3.18e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 93.30 E-value: 3.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 369 YVENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQ-----QGQIHIDGKDI--KDYDINSLRSKIGVVLQ 441
Cdd:PRK14239 14 YYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIysPRTDTVDLRKEIGMVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 442 DTYLFAGTIMDNIRYG-RL------HASDEEVINAAKAASAHSFIKHlpKQYETEIAsegsnLSQGQKQLLAIARAILAD 514
Cdd:PRK14239 94 QPNPFPMSIYENVVYGlRLkgikdkQVLDEAVEKSLKGASIWDEVKD--RLHDSALG-----LSGGQQQRVCIARVLATS 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447166293 515 ADILILDEATSNIDTRTELQIQAGLNNLMRGRTSFVIAHRLKTIEK-ADQILVIKDGSILERGN 577
Cdd:PRK14239 167 PKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYND 230
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
360-584 |
3.70e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 93.51 E-value: 3.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYVENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYD-INSLRSKIGV 438
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 439 VLQ--DTYLFAGTIMDNIRYG--RLHASDEEVINAAKAASAH----SFIKHLPKqyeteiasegsNLSQGQKQLLAIARA 510
Cdd:PRK13644 82 VFQnpETQFVGRTVEEDLAFGpeNLCLPPIEIRKRVDRALAEigleKYRHRSPK-----------TLSGGQGQCVALAGI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447166293 511 ILADADILILDEATSNIDTRTELQIQAGLNNLMR-GRTSFVIAHRLKTIEKADQILVIKDGSILERGNHESLMED 584
Cdd:PRK13644 151 LTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEkGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSD 225
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
369-581 |
5.40e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 92.80 E-value: 5.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 369 YVENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHID------GKDIKDYDINSLRSKIGVVLQD 442
Cdd:PRK14246 19 YINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDgkvlyfGKDIFQIDAIKLRKEVGMVFQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 443 TYLFAG-TIMDNIRYGRLHASDEEVINAAKAASAHSFIKHLPKQYETEIASEGSNLSQGQKQLLAIARAILADADILILD 521
Cdd:PRK14246 99 PNPFPHlSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447166293 522 EATSNIDTRTELQIQAGLNNLMRGRTSFVIAHRLKTIEK-ADQILVIKDGSILERGNHESL 581
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEI 239
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
360-556 |
5.80e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 92.92 E-value: 5.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFgYVENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDI-----QQGQIHIDGKDIKDYDIN--SL 432
Cdd:PRK14243 11 LRTENLNV-YYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgfrVEGKVTFHGKNLYAPDVDpvEV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 433 RSKIGVVLQDTYLFAGTIMDNIRYG-RLHAS----DEEVINAAKAASAHSFIKHLPKQyeteiasEGSNLSQGQKQLLAI 507
Cdd:PRK14243 90 RRRIGMVFQKPNPFPKSIYDNIAYGaRINGYkgdmDELVERSLRQAALWDEVKDKLKQ-------SGLSLSGGQQQRLCI 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 447166293 508 ARAILADADILILDEATSNIDTRTELQIQAGLNNLMRGRTSFVIAHRLK 556
Cdd:PRK14243 163 ARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQ 211
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
385-576 |
9.32e-21 |
|
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: 90.82 E-value: 9.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 385 PGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKD----YDINSLRSKIGVVLQDTYLFAG-TIMDNIRYGRL 459
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrkkINLPPQQRKIGLVFQQYALFPHlNVRENLAFGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 460 HASDEEVINAAKAASAHSFIKHLPKQYETEiasegsnLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQAGL 539
Cdd:cd03297 102 RKRNREDRISVDELLDLLGLDHLLNRYPAQ-------LSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPEL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 447166293 540 NNLMR--GRTSFVIAHRLKTIEK-ADQILVIKDGSILERG 576
Cdd:cd03297 175 KQIKKnlNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
364-581 |
1.12e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 92.47 E-value: 1.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 364 NVSFGYVeNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDI-----QQGQIHIDGKDIKDY-DINSLRSKIG 437
Cdd:PRK14271 26 NLTLGFA-GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYrDVLEFRRRVG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 438 VVLQDTYLFAGTIMDNIRYG-RLH--ASDEEVINAAKAASAHSfikHLPKQYETEIASEGSNLSQGQKQLLAIARAILAD 514
Cdd:PRK14271 105 MLFQRPNPFPMSIMDNVLAGvRAHklVPRKEFRGVAQARLTEV---GLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVN 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447166293 515 ADILILDEATSNIDTRTELQIQAGLNNLMRGRTSFVIAHRLKTIEK-ADQILVIKDGSILERGNHESL 581
Cdd:PRK14271 182 PEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQL 249
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
375-585 |
1.15e-20 |
|
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: 92.23 E-value: 1.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 375 ILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKdikdydinslrskIGVVLQDTYLFAGTIMDNI 454
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSWIMPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 455 RYGrLHASDEEVINAAKAASAHSFIKHLPKQYETEIASEGSNLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQ 534
Cdd:cd03291 119 IFG-VSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKE 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 447166293 535 I-QAGLNNLMRGRTSFVIAHRLKTIEKADQILVIKDGSILERGNHESLMEDR 585
Cdd:cd03291 198 IfESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLR 249
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
364-576 |
1.44e-20 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 91.37 E-value: 1.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 364 NVSFGyveNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINSLRSKIGVVLQDT 443
Cdd:PRK13548 9 SVRLG---GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 444 YL-FAGTIMDNIRYGRL-----HASDEEVINAAKAASAhsfIKHLPKQYETEiasegsnLSQGQKQLLAIARAI--LADA 515
Cdd:PRK13548 86 SLsFPFTVEEVVAMGRAphglsRAEDDALVAAALAQVD---LAHLAGRDYPQ-------LSGGEQQRVQLARVLaqLWEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447166293 516 D----ILILDEATSNIDTRTELQIQAGLNNLMRGRTSFVIA--HRLK-TIEKADQILVIKDGSILERG 576
Cdd:PRK13548 156 DgpprWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVvlHDLNlAARYADRIVLLHQGRLVADG 223
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
360-572 |
1.55e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 93.22 E-value: 1.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENV--SFGYVEnktILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKdyDINSLRSKIG 437
Cdd:PRK10851 3 IEIANIkkSFGRTQ---VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVS--RLHARDRKVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 438 VVLQDTYLFAG-TIMDNIRYG-----RLHASDEEVINaAKAASAHSFIK--HLPKQYEteiasegSNLSQGQKQLLAIAR 509
Cdd:PRK10851 78 FVFQHYALFRHmTVFDNIAFGltvlpRRERPNAAAIK-AKVTQLLEMVQlaHLADRYP-------AQLSGGQKQRVALAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447166293 510 AILADADILILDEATSNIDTRTELQIQAGLNNL---MRGRTSFVIAHRLKTIEKADQILVIKDGSI 572
Cdd:PRK10851 150 ALAVEPQILLLDEPFGALDAQVRKELRRWLRQLheeLKFTSVFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
360-584 |
1.70e-20 |
|
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: 92.81 E-value: 1.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELEN--VSFgYVENKTI--LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYD---IQQGQIHIDGKDIKDYDINSL 432
Cdd:COG0444 2 LEVRNlkVYF-PTRRGVVkaVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 433 R----SKIGVVLQDTY-----LFagTIMDNIRYG-RLH--ASDEEVINAAKAA-------SAHSFIKHLPKQyeteiase 493
Cdd:COG0444 81 RkirgREIQMIFQDPMtslnpVM--TVGDQIAEPlRIHggLSKAEARERAIELlervglpDPERRLDRYPHE-------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 494 gsnLSQGQKQLLAIARAILADADILILDEATSNID-TrtelqIQAGLNNLMRG-----RTSFV-IAHRLKTIEK-ADQIL 565
Cdd:COG0444 151 ---LSGGMRQRVMIARALALEPKLLIADEPTTALDvT-----IQAQILNLLKDlqrelGLAILfITHDLGVVAEiADRVA 222
|
250
....*....|....*....
gi 447166293 566 VIKDGSILERGNHESLMED 584
Cdd:COG0444 223 VMYAGRIVEEGPVEELFEN 241
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
360-581 |
1.90e-20 |
|
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: 90.12 E-value: 1.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYVENkTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDyDINSLRSKIGVV 439
Cdd:cd03265 1 IEVENLVKKYGDF-EAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 440 LQDTylfagtIMDNIRYGRLHASDEEVINAAKAASAHSFIKHLPKQYE-TEIASE-GSNLSQGQKQLLAIARAILADADI 517
Cdd:cd03265 79 FQDL------SVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGlLEAADRlVKTYSGGMRRRLEIARSLVHRPEV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447166293 518 LILDEATSNIDTRTELQIQAGLNNLMR--GRTSFVIAHRLKTIEK-ADQILVIKDGSILERGNHESL 581
Cdd:cd03265 153 LFLDEPTIGLDPQTRAHVWEYIEKLKEefGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
376-591 |
2.47e-20 |
|
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: 95.78 E-value: 2.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 376 LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKdikdydinslrskIGVVLQDTYLFAGTIMDNIR 455
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-------------VAYVPQQAWIQNDSLRENIL 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 456 YGrlHASDEEVINAAKAASAH-SFIKHLPKQYETEIASEGSNLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQ 534
Cdd:TIGR00957 721 FG--KALNEKYYQQVLEACALlPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKH 798
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 535 I---QAGLNNLMRGRTSFVIAHRLKTIEKADQILVIKDGSILERGNHESLMEDRGFYFEL 591
Cdd:TIGR00957 799 IfehVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEF 858
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
372-584 |
2.56e-20 |
|
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: 90.29 E-value: 2.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 372 NKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINSlRSKIGVVL--QDTYLFAG- 448
Cdd:cd03218 12 KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK-RARLGIGYlpQEASIFRKl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 449 TIMDNIR--YGRLHASDEEVINAAKAASAHSFIKHLPKQYeteiaseGSNLSQGQKQLLAIARAILADADILILDEATSN 526
Cdd:cd03218 91 TVEENILavLEIRGLSKKEREEKLEELLEEFHITHLRKSK-------ASSLSGGERRRVEIARALATNPKFLLLDEPFAG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 527 IDTRTELQIQAGLNNLM-RGRTSFVIAHRLK-TIEKADQILVIKDGSILERGNHESLMED 584
Cdd:cd03218 164 VDPIAVQDIQKIIKILKdRGIGVLITDHNVReTLSITDRAYIIYEGKVLAEGTPEEIAAN 223
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
360-560 |
5.56e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 90.10 E-value: 5.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYvENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQ-----QGQIHIDGKDI--KDYDINSL 432
Cdd:PRK14258 8 IKVNNLSFYY-DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNIyeRRVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 433 RSKIGVVLQDTYLFAGTIMDNIRYG--------RLHAsDEEVINAAKAASAHSFIKHlpkqyetEIASEGSNLSQGQKQL 504
Cdd:PRK14258 87 RRQVSMVHPKPNLFPMSVYDNVAYGvkivgwrpKLEI-DDIVESALKDADLWDEIKH-------KIHKSALDLSGGQQQR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447166293 505 LAIARAILADADILILDEATSNIDTRTELQIQAGLNNL-MRGRTSFVI-AHRLKTIEK 560
Cdd:PRK14258 159 LCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLrLRSELTMVIvSHNLHQVSR 216
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
360-570 |
7.52e-20 |
|
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: 88.11 E-value: 7.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVS--FGyveNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDinslRSKIG 437
Cdd:cd03269 1 LEVENVTkrFG---RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 438 VVLQDTYLFAG-TIMDNIRY-GRLHASDEEVInaakAASAHSFIKHLP-KQYETEIASEgsnLSQGQKQLLAIARAILAD 514
Cdd:cd03269 74 YLPEERGLYPKmKVIDQLVYlAQLKGLKKEEA----RRRIDEWLERLElSEYANKRVEE---LSKGNQQKVQFIAAVIHD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447166293 515 ADILILDEATSNIDTRTELQIQAGLNNLMR-GRTSFVIAHRLKTIEK-ADQILVIKDG 570
Cdd:cd03269 147 PELLILDEPFSGLDPVNVELLKDVIRELARaGKTVILSTHQMELVEElCDRVLLLNKG 204
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
365-576 |
8.62e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 89.20 E-value: 8.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 365 VSFGYVEnktILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQ-----QGQIHIDGKDIKDYDINSLRSKIGVV 439
Cdd:PRK14247 11 VSFGQVE---VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIELRRRVQMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 440 LQDTYLFAG-TIMDNIRYG----RLHASDEEVINAAKAASAHSfikHLPKQYETEIASEGSNLSQGQKQLLAIARAILAD 514
Cdd:PRK14247 88 FQIPNPIPNlSIFENVALGlklnRLVKSKKELQERVRWALEKA---QLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQ 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447166293 515 ADILILDEATSNIDTRTELQIQAGLNNLMRGRTSFVIAHRLKTIEK-ADQILVIKDGSILERG 576
Cdd:PRK14247 165 PEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARiSDYVAFLYKGQIVEWG 227
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
40-334 |
1.47e-19 |
|
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: 89.54 E-value: 1.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 40 KAALMFVIFLVFVTTLLGLLGPYFMGVIIDQYIVPKDLNGTARMCMLLIAIYGVTVLLTWLQTYVMINVALKTIQKIRQD 119
Cdd:cd18568 1 RKLLAEILLASLLLQLLGLALPLFTQIILDRVLVHKNISLLNLILIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 120 IFEKIQTLSLRFFDVRSQGDLMSRVtNDIDNLNQALTQSVVQIISSALTFIGVTIAMFSLNWILALVTLITVP----IMF 195
Cdd:cd18568 81 FYKHLLSLPLSFFASRKVGDIITRF-QENQKIRRFLTRSALTTILDLLMVFIYLGLMFYYNLQLTLIVLAFIPlyvlLTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 196 FVTKKLVAYSGKNFAKRQkdlgELNGFIEEAITGADVTTLYGKEKETVQNF-NKINEQL--RISATKADTFSAFIFpsmN 272
Cdd:cd18568 160 LSSPKLKRNSREIFQANA----EQQSFLVEALTGIATIKALAAERPIRWRWeNKFAKALntRFRGQKLSIVLQLIS---S 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447166293 273 FINNLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18568 233 LINHLGTIAVLWYGAYLVISGQLTIGQLVAFNMLFGSVINPLLALVGLWDELQETRISVERL 294
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
370-581 |
1.65e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 92.08 E-value: 1.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 370 VENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDiQQGQIHIDGKDIKDYDINSL---RSKIGVVLQDTYLF 446
Cdd:PRK15134 296 VDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPNSS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 447 AG---TIMDNIRYG-RLH-------ASDEEVINAAKAASAHSFIKHlpkQYETEiasegsnLSQGQKQLLAIARAILADA 515
Cdd:PRK15134 375 LNprlNVLQIIEEGlRVHqptlsaaQREQQVIAVMEEVGLDPETRH---RYPAE-------FSGGQRQRIAIARALILKP 444
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447166293 516 DILILDEATSNIDTRTELQIQAGLNNLM-RGRTSFV-IAHRLKTIEK-ADQILVIKDGSILERGNHESL 581
Cdd:PRK15134 445 SLIILDEPTSSLDKTVQAQILALLKSLQqKHQLAYLfISHDLHVVRAlCHQVIVLRQGEVVEQGDCERV 513
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
360-576 |
1.97e-19 |
|
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: 86.86 E-value: 1.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYvENKTILKEVSLKARPGeTIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDyDINSLRSKIGVV 439
Cdd:cd03264 1 LQLENLTKRY-GKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 440 LQDTYLFAG-TIMDNIRY-GRLHA-----SDEEVINAAKAASAHSFIKHLPKQyeteiasegsnLSQGQKQLLAIARAIL 512
Cdd:cd03264 78 PQEFGVYPNfTVREFLDYiAWLKGipskeVKARVDEVLELVNLGDRAKKKIGS-----------LSGGMRRRVGIAQALV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447166293 513 ADADILILDEATSNIDTRTELQIQAGLNNLMRGRTSFVIAHRLKTIEK-ADQILVIKDGSILERG 576
Cdd:cd03264 147 GDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
360-597 |
2.07e-19 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 87.76 E-value: 2.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYVENKtILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDG------KDIKDYDINSLR 433
Cdd:PRK11124 3 IQLNGINCFYGAHQ-ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 434 SKIGVVLQDTYLFAG-TIMDNirygrLHASDEEVINAAKAASAHSFIKHLPKQYETEIASEGS-NLSQGQKQLLAIARAI 511
Cdd:PRK11124 82 RNVGMVFQQYNLWPHlTVQQN-----LIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPlHLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 512 LADADILILDEATSNIDTRTELQIQAGLNNLMR-GRTSFVIAHRLKTIEK-ADQILVIKDGSILERGNHESLMEDRgfyf 589
Cdd:PRK11124 157 MMEPQVLLFDEPTAALDPEITAQIVSIIRELAEtGITQVIVTHEVEVARKtASRVVYMENGHIVEQGDASCFTQPQ---- 232
|
....*...
gi 447166293 590 elyTSQFK 597
Cdd:PRK11124 233 ---TEAFK 237
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
370-583 |
2.29e-19 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 92.92 E-value: 2.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 370 VENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDgkdikdydinslRSkIGVVLQDTYLFAGT 449
Cdd:PTZ00243 670 LEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE------------RS-IAYVPQQAWIMNAT 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 450 IMDNIRYgrlhaSDEEviNAAKAASA------HSFIKHLPKQYETEIASEGSNLSQGQKQLLAIARAILADADILILDEA 523
Cdd:PTZ00243 737 VRGNILF-----FDEE--DAARLADAvrvsqlEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDP 809
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447166293 524 TSNIDTRT-ELQIQAGLNNLMRGRTSFVIAHRLKTIEKADQILVIKDGSILERGNHESLME 583
Cdd:PTZ00243 810 LSALDAHVgERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMR 870
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
120-584 |
3.37e-19 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 92.49 E-value: 3.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 120 IFEKiqtlSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFSLNWIL-------ALVTLITVP 192
Cdd:PLN03130 380 VFRK----SLRLTHEGRKKFTSGKITNLMTTDAEALQQICQQLHTLWSAPFRIIIAMVLLYQQLgvasligSLMLVLMFP 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 193 IMFFVTKKLVAYSGKNFAKRQKDLGELNgfieEAITGADVTTLYGKEKE---TVQNFNkiNEQL---RisatKADTFSAF 266
Cdd:PLN03130 456 IQTFIISKMQKLTKEGLQRTDKRIGLMN----EVLAAMDTVKCYAWENSfqsKVQTVR--DDELswfR----KAQLLSAF 525
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 267 ifpsMNFINNlgmglvigtgSVMVLNGMTTVGVIAAF---INYSRQFSRpLSQFATLM-------NTIQAAVAGG----- 331
Cdd:PLN03130 526 ----NSFILN----------SIPVLVTVVSFGVFTLLggdLTPARAFTS-LSLFAVLRfplfmlpNLITQAVNANvslkr 590
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 332 -ERVF----EIMDEVPEIQNKKDAFIVQNiqghvelENVSFGYVENKTILKEVSLKARPGETIALVGPTGSGKTTIIN-L 405
Cdd:PLN03130 591 lEELLlaeeRVLLPNPPLEPGLPAISIKN-------GYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISaM 663
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 406 LTRFYDIQQGQIHIdgkdikdydinslRSKIGVVLQDTYLFAGTIMDNIRYGRLHASD--EEVINAakAASAHSfIKHLP 483
Cdd:PLN03130 664 LGELPPRSDASVVI-------------RGTVAYVPQVSWIFNATVRDNILFGSPFDPEryERAIDV--TALQHD-LDLLP 727
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 484 KQYETEIASEGSNLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQI-QAGLNNLMRGRTSFVIAHRLKTIEKAD 562
Cdd:PLN03130 728 GGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVfDKCIKDELRGKTRVLVTNQLHFLSQVD 807
|
490 500
....*....|....*....|..
gi 447166293 563 QILVIKDGSILERGNHESLMED 584
Cdd:PLN03130 808 RIILVHEGMIKEEGTYEELSNN 829
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
375-571 |
3.72e-19 |
|
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: 92.28 E-value: 3.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 375 ILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKdikdydinslrskIGVVLQDTYLFAGTIMDNI 454
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPGTIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 455 RYGrLHASDEEVINAAKAASAHSFIKHLPKQYETEIASEGSNLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQ 534
Cdd:TIGR01271 508 IFG-LSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKE 586
|
170 180 190
....*....|....*....|....*....|....*...
gi 447166293 535 I-QAGLNNLMRGRTSFVIAHRLKTIEKADQILVIKDGS 571
Cdd:TIGR01271 587 IfESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGV 624
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
373-574 |
5.19e-19 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 87.05 E-value: 5.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 373 KTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYD---INSLRSKIGVVLQDTyLFA-- 447
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqRKAFRRDIQMVFQDS-ISAvn 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 448 --GTIMDNIRYGRLHASD----------EEVINAAKAASAHsfIKHLPKQyeteiasegsnLSQGQKQLLAIARAILADA 515
Cdd:PRK10419 104 prKTVREIIREPLRHLLSldkaerlaraSEMLRAVDLDDSV--LDKRPPQ-----------LSGGQLQRVCLARALAVEP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447166293 516 DILILDEATSNIDTRTELQIQAGLNNLM-RGRTSFV-IAHRLKTIEK-ADQILVIKDGSILE 574
Cdd:PRK10419 171 KLLILDEAVSNLDLVLQAGVIRLLKKLQqQFGTACLfITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
360-585 |
6.41e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 87.19 E-value: 6.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYVENKTI----LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIK----DYDINS 431
Cdd:PRK13641 3 IKFENVDYIYSPGTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 432 LRSKIGVVLQ--DTYLFAGTIMDNIRYGRLH--ASDEEVINAAkaasahsfIKHLPKQYETEIASEGS--NLSQGQKQLL 505
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPKNfgFSEDEAKEKA--------LKWLKKVGLSEDLISKSpfELSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 506 AIARAILADADILILDEATSNIDTRTELQIQAGLNNLMR-GRTSFVIAHRLKTI-EKADQILVIKDGSILERGNHESLME 583
Cdd:PRK13641 155 AIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKaGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKEIFS 234
|
..
gi 447166293 584 DR 585
Cdd:PRK13641 235 DK 236
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
372-546 |
7.02e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 85.31 E-value: 7.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 372 NKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDinslrskigVVLQDTYLfaG--- 448
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPD---------VAEACHYL--Ghrn 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 449 ------TIMDNIRY-GRLHASDEEVINAAKAASAHSFIKHLPKQYeteiasegsnLSQGQKQLLAIARAILADADILILD 521
Cdd:PRK13539 83 amkpalTVAENLEFwAAFLGGEELDIAAALEAVGLAPLAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILD 152
|
170 180
....*....|....*....|....*
gi 447166293 522 EATSNIDTRTelqiQAGLNNLMRGR 546
Cdd:PRK13539 153 EPTAALDAAA----VALFAELIRAH 173
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
361-585 |
1.17e-18 |
|
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: 85.27 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 361 ELENVSFGYVENkTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINSL-RSKIGVV 439
Cdd:TIGR03410 2 EVSNLNVYYGQS-HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaRAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 440 LQDTYLFAG-TIMDNIRYGrlhasdeevinAAKAASAHSFIKhlPKQYE------TEIASEGSNLSQGQKQLLAIARAIL 512
Cdd:TIGR03410 81 PQGREIFPRlTVEENLLTG-----------LAALPRRSRKIP--DEIYElfpvlkEMLGRRGGDLSGGQQQQLAIARALV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447166293 513 ADADILILDEATSNIDTRTELQIQAGLNNL--MRGRTSFVIAHRLK-TIEKADQILVIKDGSILERGNHESLMEDR 585
Cdd:TIGR03410 148 TRPKLLLLDEPTEGIQPSIIKDIGRVIRRLraEGGMAILLVEQYLDfARELADRYYVMERGRVVASGAGDELDEDK 223
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
360-581 |
1.29e-18 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 87.47 E-value: 1.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENV--SFGyveNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINslRSKIG 437
Cdd:PRK11432 7 VVLKNItkRFG---SNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRDIC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 438 VVLQDTYLFAG-TIMDNIRYG--RLHASDEEVINAAKAASAHSFIKHLPKQYETEIasegsnlSQGQKQLLAIARAILAD 514
Cdd:PRK11432 82 MVFQSYALFPHmSLGENVGYGlkMLGVPKEERKQRVKEALELVDLAGFEDRYVDQI-------SGGQQQRVALARALILK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447166293 515 ADILILDEATSNIDT---RT------ELQIQAGLnnlmrgrTSFVIAH-RLKTIEKADQILVIKDGSILERGNHESL 581
Cdd:PRK11432 155 PKVLLFDEPLSNLDAnlrRSmrekirELQQQFNI-------TSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
360-584 |
1.50e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 85.66 E-value: 1.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYVENKTIlKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQ-----GQIHIDGKDIKDYDINSL-- 432
Cdd:PRK14267 5 IETVNLRVYYGSNHVI-KGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNIYSPDVDPIev 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 433 RSKIGVVLQDTYLFAG-TIMDNI----RYGRLHAS----DEEVINAAKAASAHSFIKHLPKQYEteiasegSNLSQGQKQ 503
Cdd:PRK14267 84 RREVGMVFQYPNPFPHlTIYDNVaigvKLNGLVKSkkelDERVEWALKKAALWDEVKDRLNDYP-------SNLSGGQRQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 504 LLAIARAILADADILILDEATSNIDTRTELQIQAGLNNLMRGRTSFVIAHR-LKTIEKADQILVIKDGSILERGNHESLM 582
Cdd:PRK14267 157 RLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTRKVF 236
|
..
gi 447166293 583 ED 584
Cdd:PRK14267 237 EN 238
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
361-575 |
1.80e-18 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 85.52 E-value: 1.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 361 ELENVSFGYvENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDinslrSKIGVVL 440
Cdd:PRK11248 3 QISHLYADY-GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG-----AERGVVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 441 QDTYLFA-GTIMDNIRYG----------RLHASDEEVINAAKAASAHSFIKHlpkqyeteiasegsnLSQGQKQLLAIAR 509
Cdd:PRK11248 77 QNEGLLPwRNVQDNVAFGlqlagvekmqRLEIAHQMLKKVGLEGAEKRYIWQ---------------LSGGQRQRVGIAR 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447166293 510 AILADADILILDEATSNIDTRTELQIQAGLNNLMR--GRTSFVIAHrlkTIEKA-----DQILVIKD-GSILER 575
Cdd:PRK11248 142 ALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQetGKQVLLITH---DIEEAvfmatELVLLSPGpGRVVER 212
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
360-577 |
2.40e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 85.52 E-value: 2.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYVEN-----KTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDY-DINSLR 433
Cdd:PRK13633 5 IKCKNVSYKYESNeesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEeNLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 434 SKIGVVLQ--DTYLFAGTIMDNIRYG--RLHASDEE----VINAAKAASAHSFIKHLPKQyeteiasegsnLSQGQKQLL 505
Cdd:PRK13633 85 NKAGMVFQnpDNQIVATIVEEDVAFGpeNLGIPPEEirerVDESLKKVGMYEYRRHAPHL-----------LSGGQKQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447166293 506 AIARAILADADILILDEATSNIDTRTELQIQAGLNNLMR--GRTSFVIAHRLKTIEKADQILVIKDGSILERGN 577
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKkyGITIILITHYMEEAVEADRIIVMDSGKVVMEGT 227
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
46-256 |
3.10e-18 |
|
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH transporter, and a homolog AarD; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350028 [Multi-domain] Cd Length: 290 Bit Score: 85.54 E-value: 3.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 46 VIFLVFVTTLLGLLGPYFMGVIIDQYIVPK-DLNGTARMCMLLIAIYGVTVLLTWLQTYVMINVALKTIQKIRQDIFEKI 124
Cdd:cd18584 1 AVLLGLLAALLIIAQAWLLARIIAGVFLEGaGLAALLPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLLARL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 125 QTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFSLNWILALVTLITVPI--MFFVtkkLV 202
Cdd:cd18584 81 LALGPALLRRQSSGELATLLTEGVDALDGYFARYLPQLVLAAIVPLLILVAVFPLDWVSALILLVTAPLipLFMI---LI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 447166293 203 AYSGKNFAKRQ-KDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRIS 256
Cdd:cd18584 158 GKAAQAASRRQwAALSRLSGHFLDRLRGLPTLKLFGRARAQAARIARASEDYRRR 212
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
360-584 |
4.26e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 86.04 E-value: 4.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYvENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDyDINSLRSKIGVV 439
Cdd:PRK13536 42 IDLAGVSKSY-GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 440 LQ-DTYLFAGTIMDNI----RYGRLHASD-EEVInaakaASAHSFIKhLPKQYETEIasegSNLSQGQKQLLAIARAILA 513
Cdd:PRK13536 120 PQfDNLDLEFTVRENLlvfgRYFGMSTREiEAVI-----PSLLEFAR-LESKADARV----SDLSGGMKRRLTLARALIN 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447166293 514 DADILILDEATSNIDTRTELQIQAGLNNLM-RGRTSFVIAHRLKTIEK-ADQILVIKDGSILERGNHESLMED 584
Cdd:PRK13536 190 DPQLLILDEPTTGLDPHARHLIWERLRSLLaRGKTILLTTHFMEEAERlCDRLCVLEAGRKIAEGRPHALIDE 262
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
360-577 |
5.15e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 84.78 E-value: 5.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENV--SFGyveNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDydinSLRSKIG 437
Cdd:COG4152 2 LELKGLtkRFG---DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP----EDRRRIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 438 vvlqdtYLFA--G-----TIMDNIRY-GRLHASDEeviNAAKAASAHSFIKH-LPKQYETEIasegSNLSQGQKQLLAIA 508
Cdd:COG4152 75 ------YLPEerGlypkmKVGEQLVYlARLKGLSK---AEAKRRADEWLERLgLGDRANKKV----EELSKGNQQKVQLI 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447166293 509 RAILADADILILDEATS-----NIDT-RTELQIQAGlnnlmRGRTsfVI--AHRLKTIEK-ADQILVIKDGSILERGN 577
Cdd:COG4152 142 AALLHDPELLILDEPFSgldpvNVELlKDVIRELAA-----KGTT--VIfsSHQMELVEElCDRIVIINKGRKVLSGS 212
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
362-528 |
7.07e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 87.04 E-value: 7.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 362 LENVSFGYvENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDgKDIkdydinslrsKIGVVLQ 441
Cdd:COG0488 1 LENLSKSF-GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP-KGL----------RIGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 442 DTYLFAG-TIMDNI------------RYGRL-HASDEEVINAAKAASAHSFIKHL-PKQYETEIAS--EG---------- 494
Cdd:COG0488 69 EPPLDDDlTVLDTVldgdaelraleaELEELeAKLAEPDEDLERLAELQEEFEALgGWEAEARAEEilSGlgfpeedldr 148
|
170 180 190
....*....|....*....|....*....|....*.
gi 447166293 495 --SNLSQGQKQLLAIARAILADADILILDEATSNID 528
Cdd:COG0488 149 pvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
360-584 |
7.63e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 83.65 E-value: 7.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYVENKTI-LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINSLRSKIGV 438
Cdd:PRK13648 8 IVFKNVSFQYQSDASFtLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 439 VLQD-TYLFAGTIMD-NIRYGRLHasdeeviNAAKAASAHSFIKHLPKQYE-TEIA-SEGSNLSQGQKQLLAIARAILAD 514
Cdd:PRK13648 88 VFQNpDNQFVGSIVKyDVAFGLEN-------HAVPYDEMHRRVSEALKQVDmLERAdYEPNALSGGQKQRVAIAGVLALN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447166293 515 ADILILDEATSNIDTrtelQIQAGLNNLMR------GRTSFVIAHRLKTIEKADQILVIKDGSILERGNHESLMED 584
Cdd:PRK13648 161 PSVIILDEATSMLDP----DARQNLLDLVRkvksehNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDH 232
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
360-576 |
9.10e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 83.99 E-value: 9.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYVENKTI--LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINSLRSKIG 437
Cdd:PRK13642 5 LEVENLVFKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 438 VVLQ--DTYLFAGTIMDNIRYGRLHAS---DEEVINAAKAASAHSFIkhlpkQYETEiasEGSNLSQGQKQLLAIARAIL 512
Cdd:PRK13642 85 MVFQnpDNQFVGATVEDDVAFGMENQGiprEEMIKRVDEALLAVNML-----DFKTR---EPARLSGGQKQRVAVAGIIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447166293 513 ADADILILDEATSNIDTRTELQIQAGLNNLMRGR--TSFVIAHRLKTIEKADQILVIKDGSILERG 576
Cdd:PRK13642 157 LRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEA 222
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
360-571 |
9.78e-18 |
|
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: 82.38 E-value: 9.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYVENKTILKEVSLKARPGETIALVGPTGSGKTTIinLLTRFYDIQ--QGQIHIDGKDIKDYDINSLRSK-- 435
Cdd:cd03290 1 VQVTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSL--LLAILGEMQtlEGKVHWSNKNESEPSFEATRSRnr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 436 --IGVVLQDTYLFAGTIMDNIRYGRLHaSDEEVINAAKAASAHSFIKHLPKQYETEIASEGSNLSQGQKQLLAIARAILA 513
Cdd:cd03290 79 ysVAYAAQKPWLLNATVEENITFGSPF-NKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447166293 514 DADILILDEATSNIDTR-TELQIQAGLNNLMRG--RTSFVIAHRLKTIEKADQILVIKDGS 571
Cdd:cd03290 158 NTNIVFLDDPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
47-317 |
1.00e-17 |
|
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: 84.09 E-value: 1.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 47 IFLVFVTTLLGLLGPYFMGVIIDQYIVPkdLNGTARMCMLLIAIYGVT----VLLTWLQTYVMINVALKTIQKIRQDIFE 122
Cdd:cd18582 2 LLLLVLAKLLNVAVPFLLKYAVDALSAP--ASALLAVPLLLLLAYGLArilsSLFNELRDALFARVSQRAVRRLALRVFR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 123 KIQTLSLRFFDVRSQGDL---MSRVTNDIDNLnqaLTQSVVQIISSALTFIGVTIAMFSL-NWILALVTLITVPIMFFVT 198
Cdd:cd18582 80 HLHSLSLRFHLSRKTGALsraIERGTRGIEFL---LRFLLFNILPTILELLLVCGILWYLyGWSYALITLVTVALYVAFT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 199 KKLVAYSGKnFAKRQKDL-GELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRISATKADTFSAFIFPSMNFINNL 277
Cdd:cd18582 157 IKVTEWRTK-FRREMNEAdNEANAKAVDSLLNYETVKYFNNEEYEAERYDKALAKYEKAAVKSQTSLALLNIGQALIISL 235
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 447166293 278 GMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQF 317
Cdd:cd18582 236 GLTAIMLLAAQGVVAGTLTVGDFVLVNTYLLQLYQPLNFL 275
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
355-577 |
1.13e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 83.90 E-value: 1.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 355 NIQGHVELENVSFGYVENKTI----LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQ-------IHIDGKD 423
Cdd:PRK13645 2 DFSKDIILDNVSYTYAKKTPFefkaLNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQtivgdyaIPANLKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 424 IKDydINSLRSKIGVVLQ--DTYLFAGTIMDNIRYGRLHASDEEVINAAKAASAHSFIKhLPKQYETEIASEgsnLSQGQ 501
Cdd:PRK13645 82 IKE--VKRLRKEIGLVFQfpEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQ-LPEDYVKRSPFE---LSGGQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447166293 502 KQLLAIARAILADADILILDEATSNIDTRTE---LQIQAGLNNLMRGRTSFVIAHRLKTIEKADQILVIKDGSILERGN 577
Cdd:PRK13645 156 KRRVALAGIIAMDGNTLVLDEPTGGLDPKGEedfINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
376-590 |
1.32e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 83.98 E-value: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 376 LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKD------------------------YDINS 431
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNkkktkekekvleklviqktrfkkiKKIKE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 432 LRSKIGVVLQ--DTYLFAGTIMDNIRYG--RLHASDEEvinAAKAASAHSFIKHLPKQYeteIASEGSNLSQGQKQLLAI 507
Cdd:PRK13651 103 IRRRVGVVFQfaEYQLFEQTIEKDIIFGpvSMGVSKEE---AKKRAAKYIELVGLDESY---LQRSPFELSGGQKRRVAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 508 ArAILA-DADILILDEATSNIDTRTELQIQAGLNNL-MRGRTSFVIAHRLKTI-EKADQILVIKDGSILERGNHESLMED 584
Cdd:PRK13651 177 A-GILAmEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLDNVlEWTKRTIFFKDGKIIKDGDTYDILSD 255
|
....*.
gi 447166293 585 RGFYFE 590
Cdd:PRK13651 256 NKFLIE 261
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
365-582 |
1.36e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 85.28 E-value: 1.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 365 VSFGYVenkTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINSLRSKIGVVLQDTY 444
Cdd:PRK09536 11 VEFGDT---TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 445 L-FAGTIMDNIRYGRL-H---------ASDEEVINAAKAASAHSFikhlpkqyeteIASEGSNLSQGQKQLLAIARAILA 513
Cdd:PRK09536 88 LsFEFDVRQVVEMGRTpHrsrfdtwteTDRAAVERAMERTGVAQF-----------ADRPVTSLSGGERQRVLLARALAQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447166293 514 DADILILDEATSNIDTRTELQIQAGLNNLMR-GRTSFVIAHRLKTIEK-ADQILVIKDGSILERGNHESLM 582
Cdd:PRK09536 157 ATPVLLLDEPTASLDINHQVRTLELVRRLVDdGKTAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVL 227
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
373-584 |
1.52e-17 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 82.49 E-value: 1.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 373 KTILKEVSLKARPGETIALVGPTGSGKTTI---INLLTRFYD--IQQGQIHIDG-KDIKDYD--INSLRSKIGVVLQDTY 444
Cdd:PRK11264 16 QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLlrcINLLEQPEAgtIRVGDITIDTaRSLSQQKglIRQLRQHVGFVFQNFN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 445 LFAG-TIMDNIRYGRL---HASDEEVINAAKAASAHSFIKHLPKQYEteiasegSNLSQGQKQLLAIARAILADADILIL 520
Cdd:PRK11264 96 LFPHrTVLENIIEGPVivkGEPKEEATARARELLAKVGLAGKETSYP-------RRLSGGQQQRVAIARALAMRPEVILF 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447166293 521 DEATSNIDTRTELQIQAGLNNLMR-GRTSFVIAHRLK-TIEKADQILVIKDGSILERGNHESLMED 584
Cdd:PRK11264 169 DEPTSALDPELVGEVLNTIRQLAQeKRTMVIVTHEMSfARDVADRAIFMDQGRIVEQGPAKALFAD 234
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
355-571 |
2.52e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 85.22 E-value: 2.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 355 NIQGHVELENV--SFGYVenkTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDIN-S 431
Cdd:PRK09700 1 MATPYISMAGIgkSFGPV---HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKlA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 432 LRSKIGVVLQDTYLFAG-TIMDNIRYGRLHASDEEVINAA------KAASAHSFIKHLPKQYETEIAsegsNLSQGQKQL 504
Cdd:PRK09700 78 AQLGIGIIYQELSVIDElTVLENLYIGRHLTKKVCGVNIIdwremrVRAAMMLLRVGLKVDLDEKVA----NLSISHKQM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447166293 505 LAIARAILADADILILDEATSNIDTRTELQIQAGLNNLMRGRTSFV-IAHRLKTIEK-ADQILVIKDGS 571
Cdd:PRK09700 154 LEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVyISHKLAEIRRiCDRYTVMKDGS 222
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
376-584 |
2.80e-17 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 84.31 E-value: 2.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 376 LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKD---IKDYDINSL-RSKIGVVLQDTYLFAG-TI 450
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDiakISDAELREVrRKKIAMVFQSFALMPHmTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 451 MDNIRYGRLHAS------DEEVINAAKAASAHSFIKHLPKQyeteiasegsnLSQGQKQLLAIARAILADADILILDEAT 524
Cdd:PRK10070 124 LDNTAFGMELAGinaeerREKALDALRQVGLENYAHSYPDE-----------LSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447166293 525 SNID--TRTELQIQAGLNNLMRGRTSFVIAHRL-KTIEKADQILVIKDGSILERGNHESLMED 584
Cdd:PRK10070 193 SALDplIRTEMQDELVKLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNN 255
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
361-576 |
2.85e-17 |
|
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: 80.26 E-value: 2.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 361 ELENVSFgYVENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRF--YDIQQGQIHIDGKDIKDYDINSlRSKIGV 438
Cdd:cd03217 2 EIKDLHV-SVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEE-RARLGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 439 VL--QDTYLFAG-TIMDNIRYgrlhasdeevINaakaasahsfikhlpkqyeteiasEGsnLSQGQKQLLAIARAILADA 515
Cdd:cd03217 80 FLafQYPPEIPGvKNADFLRY----------VN------------------------EG--FSGGEKKRNEILQLLLLEP 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447166293 516 DILILDEATSNIDTRTELQIQAGLNNLMRGRTSF-VIAHRLKTIE--KADQILVIKDGSILERG 576
Cdd:cd03217 124 DLAILDEPDSGLDIDALRLVAEVINKLREEGKSVlIITHYQRLLDyiKPDRVHVLYDGRIVKSG 187
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
361-570 |
3.04e-17 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 84.98 E-value: 3.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 361 ELENV--SFGYVenkTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFY--DIQQGQIHIDGKDIKDYDI-NSLRSK 435
Cdd:PRK13549 7 EMKNItkTFGGV---KALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYphGTYEGEIIFEGEELQASNIrDTERAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 436 IGVVLQDTYLFAG-TIMDNI-------RYGRLHasDEEVINAAKAasahsfikhLPKQYETEI--ASEGSNLSQGQKQLL 505
Cdd:PRK13549 84 IAIIHQELALVKElSVLENIflgneitPGGIMD--YDAMYLRAQK---------LLAQLKLDInpATPVGNLGLGQQQLV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447166293 506 AIARAILADADILILDEATSNI---DTRTELQIQAGLNNlmRGRTSFVIAHRLKTIEK-ADQILVIKDG 570
Cdd:PRK13549 153 EIAKALNKQARLLILDEPTASLtesETAVLLDIIRDLKA--HGIACIYISHKLNEVKAiSDTICVIRDG 219
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
360-570 |
3.19e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 84.69 E-value: 3.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVS--FGYVenkTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKdydINS----LR 433
Cdd:COG3845 6 LELRGITkrFGGV---VANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVR---IRSprdaIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 434 SKIGVVLQDTYLFAG-TIMDNIRYGrLHASDEEVINAAKAASAhsfIKHLPKQY------ETEIasegSNLSQGQKQLLA 506
Cdd:COG3845 80 LGIGMVHQHFMLVPNlTVAENIVLG-LEPTKGGRLDRKAARAR---IRELSERYgldvdpDAKV----EDLSVGEQQRVE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 507 IARAILADADILILDEATSNIdtrTELQIQAgLNNLMR-----GRTSFVIAHRLKTI-EKADQILVIKDG 570
Cdd:COG3845 152 ILKALYRGARILILDEPTAVL---TPQEADE-LFEILRrlaaeGKSIIFITHKLREVmAIADRVTVLRRG 217
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
360-576 |
3.89e-17 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 82.93 E-value: 3.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGY-VENKTI--LKEVSLKARPGETIALVGPTGSGKTT---IINLLTRfydIQQGQIHIDGKDI---KDYDIN 430
Cdd:PRK11153 2 IELKNISKVFpQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTlirCINLLER---PTSGRVLVDGQDLtalSEKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 431 SLRSKIGVVLQDTYLFAG-TIMDNIrygrlhASDEEVINAAKAAsahsfIK-------------HLPKQYEteiasegSN 496
Cdd:PRK11153 79 KARRQIGMIFQHFNLLSSrTVFDNV------ALPLELAGTPKAE-----IKarvtellelvglsDKADRYP-------AQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 497 LSQGQKQLLAIARAILADADILILDEATSNID---TRTELQIQAGLNNLMrGRTSFVIAHRLKTI-EKADQILVIKDGSI 572
Cdd:PRK11153 141 LSGGQKQRVAIARALASNPKVLLCDEATSALDpatTRSILELLKDINREL-GLTIVLITHEMDVVkRICDRVAVIDAGRL 219
|
....
gi 447166293 573 LERG 576
Cdd:PRK11153 220 VEQG 223
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
374-574 |
3.95e-17 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 80.98 E-value: 3.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 374 TILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDIN---SLRSK-IGVVLQdTYLFAGT 449
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraKLRAKhVGFVFQ-SFMLIPT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 450 I--MDNIRYGRL------HASDEEVINAAKAASAHSFIKHLPKQyeteiasegsnLSQGQKQLLAIARAILADADILILD 521
Cdd:PRK10584 103 LnaLENVELPALlrgessRQSRNGAKALLEQLGLGKRLDHLPAQ-----------LSGGEQQRVALARAFNGRPDVLFAD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 447166293 522 EATSNIDTRTELQIQAGLNNLMR--GRTSFVIAHRLKTIEKADQILVIKDGSILE 574
Cdd:PRK10584 172 EPTGNLDRQTGDKIADLLFSLNRehGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
378-584 |
4.42e-17 |
|
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: 83.23 E-value: 4.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 378 EVSLKARPGETIALVGPTGSGKTTIINL---LTRFydiQQGQIHIDGKDIKD--YDINsL---RSKIGVVLQDTYLFAG- 448
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAiagLERP---DSGRIRLGGEVLQDsaRGIF-LpphRRRIGYVFQEARLFPHl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 449 TIMDNIRYGRLhasdeeviNAAKAASAHSF--------IKHLPKQYETeiasegsNLSQGQKQLLAIARAILADADILIL 520
Cdd:COG4148 93 SVRGNLLYGRK--------RAPRAERRISFdevvellgIGHLLDRRPA-------TLSGGERQRVAIGRALLSSPRLLLM 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 521 DEATSNIDTRTELQIqagLNNLMRGRTSFVI-----AHRLKTIEK-ADQILVIKDGSILERGNHESLMED 584
Cdd:COG4148 158 DEPLAALDLARKAEI---LPYLERLRDELDIpilyvSHSLDEVARlADHVVLLEQGRVVASGPLAEVLSR 224
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
368-576 |
4.80e-17 |
|
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: 80.27 E-value: 4.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 368 GYVENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDikdydinSLRSKIGVVLQDTYlfa 447
Cdd:cd03220 30 GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRV-------SSLLGLGGGFNPEL--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 448 gTIMDNIR-YGRLH-ASDEEVinAAKAASAHSFiKHLPKQYETEIasegSNLSQGQKQLLAIARAILADADILILDEATS 525
Cdd:cd03220 100 -TGRENIYlNGRLLgLSRKEI--DEKIDEIIEF-SELGDFIDLPV----KTYSSGMKARLAFAIATALEPDILLIDEVLA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447166293 526 NIDTRTELQIQAGLNNLMRGRTSFVIA-HRLKTIEK-ADQILVIKDGSILERG 576
Cdd:cd03220 172 VGDAAFQEKCQRRLRELLKQGKTVILVsHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
360-587 |
4.87e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 81.70 E-value: 4.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYVENKTI----LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDgkDI------KDYDI 429
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFasraLFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVG--DIvvsstsKQKEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 430 NSLRSKIGVVLQ--DTYLFAGTIMDNIRYG--RLHASDEEvinAAKAASAHSFIKHLPKQYETEIASEgsnLSQGQKQLL 505
Cdd:PRK13643 80 KPVRKKVGVVFQfpESQLFEETVLKDVAFGpqNFGIPKEK---AEKIAAEKLEMVGLADEFWEKSPFE---LSGGQMRRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 506 AIARAILADADILILDEATSNIDTRTELQIQAGLNNLMR-GRTSFVIAHRLKTI-EKADQILVIKDGSILERGNHESLME 583
Cdd:PRK13643 154 AIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVaDYADYVYLLEKGHIISCGTPSDVFQ 233
|
....
gi 447166293 584 DRGF 587
Cdd:PRK13643 234 EVDF 237
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
360-569 |
4.99e-17 |
|
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: 78.73 E-value: 4.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYVENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGkdikdydinslRSKIGVV 439
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE-----------GEDLLFL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 440 LQDTYLFAGTIMDNIRYgrlhASDEEvinaakaasahsfikhlpkqyeteiasegsnLSQGQKQLLAIARAILADADILI 519
Cdd:cd03223 70 PQRPYLPLGTLREQLIY----PWDDV-------------------------------LSGGEQQRLAFARLLLHKPKFVF 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 447166293 520 LDEATSNIDTRTELQIQAGLNNLMrgrTSFV-IAHRlKTIEK-ADQILVIKD 569
Cdd:cd03223 115 LDEATSALDEESEDRLYQLLKELG---ITVIsVGHR-PSLWKfHDRVLDLDG 162
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
379-584 |
5.02e-17 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 82.32 E-value: 5.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 379 VSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYD---INSLRSKIGVVLQDTYlfaGTImdNIR 455
Cdd:PRK11308 34 VSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpeaQKLLRQKIQIVFQNPY---GSL--NPR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 456 YgRLHASDEE--VIN-----AAKAASAHSFIKHL---PKQYEteiaSEGSNLSQGQKQLLAIARAILADADILILDEATS 525
Cdd:PRK11308 109 K-KVGQILEEplLINtslsaAERREKALAMMAKVglrPEHYD----RYPHMFSGGQRQRIAIARALMLDPDVVVADEPVS 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447166293 526 NIDtrteLQIQAGLNNLMRG-----RTSFV-IAHRLKTIEK-ADQILVIKDGSILERGNHESLMED 584
Cdd:PRK11308 184 ALD----VSVQAQVLNLMMDlqqelGLSYVfISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFNN 245
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
360-574 |
5.23e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 84.35 E-value: 5.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYvENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIdGKDIkdydinslrsKIGVV 439
Cdd:COG0488 316 LELEGLSKSY-GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV----------KIGYF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 440 LQDTYLFAG--TIMDNIRYGRLHASDEEVINAAKA-----ASAHSFIKhlpkqyeteiasegsNLSQGQKQLLAIARAIL 512
Cdd:COG0488 384 DQHQEELDPdkTVLDELRDGAPGGTEQEVRGYLGRflfsgDDAFKPVG---------------VLSGGEKARLALAKLLL 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447166293 513 ADADILILDEATSN--IDTRTELqiQAGLNNLmRGrTSFVIAH-R--LKTIekADQILVIKDGSILE 574
Cdd:COG0488 449 SPPNVLLLDEPTNHldIETLEAL--EEALDDF-PG-TVLLVSHdRyfLDRV--ATRILEFEDGGVRE 509
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
375-582 |
5.87e-17 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 81.17 E-value: 5.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 375 ILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDI---KDYD----------INSLRSKIGVVLQ 441
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvRDKDgqlkvadknqLRLLRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 442 DTYLFAG-TIMDNIRYGRLhasdeEVINAAKAASAHSFIKHLPKQYETEIASEG--SNLSQGQKQLLAIARAILADADIL 518
Cdd:PRK10619 100 HFNLWSHmTVLENVMEAPI-----QVLGLSKQEARERAVKYLAKVGIDERAQGKypVHLSGGQQQRVSIARALAMEPEVL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447166293 519 ILDEATSNIDTRTELQIQAGLNNLM-RGRTSFVIAHRLKTIEK-ADQILVIKDGSILERGNHESLM 582
Cdd:PRK10619 175 LFDEPTSALDPELVGEVLRIMQQLAeEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLF 240
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
360-587 |
7.35e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 81.33 E-value: 7.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYVENKTI----LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDI----KDYDINS 431
Cdd:PRK13649 3 INLQNVSYTYQAGTPFegraLFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsKNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 432 LRSKIGVVLQ--DTYLFAGTIMDNIRYG--RLHASDEEVINAAKAASAHSFIKhlpkqyETEIASEGSNLSQGQKQLLAI 507
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGpqNFGVSQEEAEALAREKLALVGIS------ESLFEKNPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 508 ArAILA-DADILILDEATSNIDTRTELQIQAGLNNLMR-GRTSFVIAHRLKTI-EKADQILVIKDGSILERGNHESLMED 584
Cdd:PRK13649 157 A-GILAmEPKILVLDEPTAGLDPKGRKELMTLFKKLHQsGMTIVLVTHLMDDVaNYADFVYVLEKGKLVLSGKPKDIFQD 235
|
...
gi 447166293 585 RGF 587
Cdd:PRK13649 236 VDF 238
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
363-576 |
7.49e-17 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 80.80 E-value: 7.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 363 ENVSFGYvENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINSLRSKIGVVLQD 442
Cdd:PRK10253 11 EQLTLGY-GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 443 TYLFAGTIMDNI----RY------GRLHASDEEVINAAKAASAhsfIKHLPKQyeteiasEGSNLSQGQKQLLAIARAIL 512
Cdd:PRK10253 90 ATTPGDITVQELvargRYphqplfTRWRKEDEEAVTKAMQATG---ITHLADQ-------SVDTLSGGQRQRAWIAMVLA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447166293 513 ADADILILDEATSNIDTRTELQIQAGLNNLMR--GRTSFVIAHRL-KTIEKADQILVIKDGSILERG 576
Cdd:PRK10253 160 QETAIMLLDEPTTWLDISHQIDLLELLSELNRekGYTLAAVLHDLnQACRYASHLIALREGKIVAQG 226
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
360-585 |
7.70e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 81.22 E-value: 7.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYVEN----KTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDI----KDYDINS 431
Cdd:PRK13634 3 ITFQKVEHRYQYKtpfeRRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 432 LRSKIGVVLQ--DTYLFAGTIMDNIRYGRLH--ASDEEVINAAKAASAhsfIKHLPKQYETEIASEgsnLSQGQKQLLAI 507
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDICFGPMNfgVSEEDAKQKAREMIE---LVGLPEELLARSPFE---LSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 508 ARAILADADILILDEATSNIDTRTELQIQAGLNNLMR--GRTSFVIAHRLKTIEK-ADQILVIKDGSILERGNHESLMED 584
Cdd:PRK13634 157 AGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKekGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREIFAD 236
|
.
gi 447166293 585 R 585
Cdd:PRK13634 237 P 237
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
361-573 |
8.39e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 84.01 E-value: 8.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 361 ELENVSFGYV---ENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINSL----R 433
Cdd:PRK10535 6 ELKDIRRSYPsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 434 SKIGVVLQDTYLFAG-TIMDNIRYGRLHASDEEvinAAKAASAHSFIKHLpkQYETEIASEGSNLSQGQKQLLAIARAIL 512
Cdd:PRK10535 86 EHFGFIFQRYHLLSHlTAAQNVEVPAVYAGLER---KQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447166293 513 ADADILILDEATSNIDTRTELQIQAGLNNLM-RGRTSFVIAHRLKTIEKADQILVIKDGSIL 573
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMAILHQLRdRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
61-334 |
9.10e-17 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 80.98 E-value: 9.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 61 PYFMGVIIDqYIVPKDLNGTARMCMLLIAIYGVTVLLTWLQTYVMINVALKTIQ-KIRQDIFEKIQTLSLRFFDVRSQGD 139
Cdd:cd18589 16 PYYTGRMTD-WIMNKDAPEAFTAAITVMSLLTIASAVSEFVCDLIYNITMSRIHsRLQGLVFAAVLRQEIAFFDSNQTGD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 140 LMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFSLNWILALVTLITVPIMFFVTKKLVAYSgKNFAKR-QKDLGE 218
Cdd:cd18589 95 IVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQ-QSLAVQvQKSLAR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 219 LNGFIEEAITG-ADVTTLYGKEKETVQNFNKINEQLRISATKADTFSAfifpSMNFINNLGMGLVIGT---GSVMVLNGM 294
Cdd:cd18589 174 ANQVAVETFSAmKTVRSFANEEGEAQRYRQRLQKTYRLNKKEAAAYAV----SMWTSSFSGLALKVGIlyyGGQLVTAGT 249
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 447166293 295 TTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18589 250 VSSGDLVTFVLYELQFTSAVEVLLSYYPSVMKAVGSSEKI 289
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
360-584 |
1.69e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 80.21 E-value: 1.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYVE----NKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDI----KDYDINS 431
Cdd:PRK13646 3 IRFDNVSYTYQKgtpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 432 LRSKIGVVLQ--DTYLFAGTIMDNIRYG--RLHASDEEVinaakAASAHSFIKHLpkQYETEIASEGS-NLSQGQKQLLA 506
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFGpkNFKMNLDEV-----KNYAHRLLMDL--GFSRDVMSQSPfQMSGGQMRKIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 507 IARAILADADILILDEATSNIDTRTELQIQAGLNNLM--RGRTSFVIAHRLKTIEK-ADQILVIKDGSILERGNHESLME 583
Cdd:PRK13646 156 IVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELFK 235
|
.
gi 447166293 584 D 584
Cdd:PRK13646 236 D 236
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
360-585 |
2.22e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 79.89 E-value: 2.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYVENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIkDYD---INSLRSKI 436
Cdd:PRK13636 6 LKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSrkgLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 437 GVVLQ--DTYLFAGTIMDNIRYG--RLHASDEEVINAAKAASAHSFIKHLpKQYETEIasegsnLSQGQKQLLAIARAIL 512
Cdd:PRK13636 85 GMVFQdpDNQLFSASVYQDVSFGavNLKLPEDEVRKRVDNALKRTGIEHL-KDKPTHC------LSFGQKKRVAIAGVLV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447166293 513 ADADILILDEATSNIDTRTELQIQAGLNNLMR--GRTSFVIAHRLKTIE-KADQILVIKDGSILERGNHESLMEDR 585
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAEK 233
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
360-583 |
4.14e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 79.46 E-value: 4.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYVEnKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINSlRSKIGVV 439
Cdd:PRK13537 8 IDFRNVEKRYGD-KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-RQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 440 LQ-DTYLFAGTIMDNIR-YGRLHAsdeevinaakaASAHSFIKHLPK-----QYETEIASEGSNLSQGQKQLLAIARAIL 512
Cdd:PRK13537 86 PQfDNLDPDFTVRENLLvFGRYFG-----------LSAAAARALVPPllefaKLENKADAKVGELSGGMKRRLTLARALV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447166293 513 ADADILILDEATSNIDTRTELQIQAGLNNLM-RGRTSFVIAHRLKTIEK-ADQILVIKDGSILERGNHESLME 583
Cdd:PRK13537 155 NDPDVLVLDEPTTGLDPQARHLMWERLRSLLaRGKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
380-582 |
5.05e-16 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 77.70 E-value: 5.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 380 SLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDikdyDINSLRSK--IGVVLQDTYLFAG-TIMDNIRY 456
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD----HTTTPPSRrpVSMLFQENNLFSHlTVAQNIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 457 G-----RL-HASDEEVINAAKAASAHSFIKHLPKQyeteiasegsnLSQGQKQLLAIARAILADADILILDEATSNIDT- 529
Cdd:PRK10771 95 GlnpglKLnAAQREKLHAIARQMGIEDLLARLPGQ-----------LSGGQRQRVALARCLVREQPILLLDEPFSALDPa 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447166293 530 -RTE-LQIqagLNNLMRGR--TSFVIAHRLktiEKADQI----LVIKDGSILERGNHESLM 582
Cdd:PRK10771 164 lRQEmLTL---VSQVCQERqlTLLMVSHSL---EDAARIaprsLVVADGRIAWDGPTDELL 218
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
376-584 |
5.58e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 81.44 E-value: 5.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 376 LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDI---KDYDINSLRSKIGVVLQDTY-------L 445
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlSPGKLQALRRDIQFIFQDPYasldprqT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 446 FAGTIMDNIRYGRLHASDEEvinAAKAASAHSFIKHLPK---QYETEiasegsnLSQGQKQLLAIARAILADADILILDE 522
Cdd:PRK10261 420 VGDSIMEPLRVHGLLPGKAA---AARVAWLLERVGLLPEhawRYPHE-------FSGGQRQRICIARALALNPKVIIADE 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447166293 523 ATSNIDTRTELQIQAGLNNLMR--GRTSFVIAHRLKTIEK-ADQILVIKDGSILERGNHESLMED 584
Cdd:PRK10261 490 AVSALDVSIRGQIINLLLDLQRdfGIAYLFISHDMAVVERiSHRVAVMYLGQIVEIGPRRAVFEN 554
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
46-329 |
7.43e-16 |
|
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350005 [Multi-domain] Cd Length: 289 Bit Score: 78.48 E-value: 7.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 46 VIFLVFVTTLLGLLGPYFMGVIIDQYIVPKDLNGTARMCMLLIAIYGVTVLLTWLQTYVMINVALKTIQKIRQDIFEKIQ 125
Cdd:cd18561 1 SVLLGLLITALYIAQAWLLARALARIFAGGPWEDIMPPLAGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRLFAKLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 126 TLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFSLNWILALVTLITVPIMFFVTKKLVAYS 205
Cdd:cd18561 81 KLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLIPLSPALWDRLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 206 GKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRISATKADTFSAFIFPSMNFINNLGMGLVIGT 285
Cdd:cd18561 161 KDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSLLSSGIMGLATALGTALALGV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 447166293 286 GSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVA 329
Cdd:cd18561 241 GALRVLGGQLTLSSLLLILFLSREFFRPLRDLGAYWHAGYQGIS 284
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
360-570 |
8.90e-16 |
|
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: 74.41 E-value: 8.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYvENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKdikdydinslrSKIGVV 439
Cdd:cd03221 1 IELENLSKTY-GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST-----------VKIGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 440 LQdtylfagtimdnirygrlhasdeevinaakaasahsfikhlpkqyeteiasegsnLSQGQKQLLAIARAILADADILI 519
Cdd:cd03221 69 EQ-------------------------------------------------------LSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 447166293 520 LDEATSNIDTRTELQIQAGLNNLmrGRTSFVIAH-R--LKTIekADQILVIKDG 570
Cdd:cd03221 94 LDEPTNHLDLESIEALEEALKEY--PGTVILVSHdRyfLDQV--ATKIIELEDG 143
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
360-576 |
1.16e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 78.92 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYVENkTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKdyDINSLRSKIGVV 439
Cdd:PRK11000 4 VTLRNVTKAYGDV-VISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN--DVPPAERGVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 440 LQDTYLFAG-TIMDNIRYGRLHAS------DEEVINAAKAASAHSFIKHLPKQyeteiasegsnLSQGQKQLLAIARAIL 512
Cdd:PRK11000 81 FQSYALYPHlSVAENMSFGLKLAGakkeeiNQRVNQVAEVLQLAHLLDRKPKA-----------LSGGQRQRVAIGRTLV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447166293 513 ADADILILDEATSNIDTRTELQIQAGLNNLMR--GRTSFVIAH-RLKTIEKADQILVIKDGSILERG 576
Cdd:PRK11000 150 AEPSVFLLDEPLSNLDAALRVQMRIEISRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
376-570 |
1.51e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 79.57 E-value: 1.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 376 LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDI-NSLRSKIGVVLQDTYLFAG-TIMDN 453
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTtAALAAGVAIIYQELHLVPEmTVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 454 IRYGRLHASDEEVINAAKAASAHSFIKHL-----PkqyETEIASegsnLSQGQKQLLAIARAILADADILILDEATSNID 528
Cdd:PRK11288 100 LYLGQLPHKGGIVNRRLLNYEAREQLEHLgvdidP---DTPLKY----LSIGQRQMVEIAKALARNARVIAFDEPTSSLS 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 447166293 529 TRtELQIQAGLNNLMR--GRTSFVIAHRLKTI-EKADQILVIKDG 570
Cdd:PRK11288 173 AR-EIEQLFRVIRELRaeGRVILYVSHRMEEIfALCDAITVFKDG 216
|
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
46-334 |
1.55e-15 |
|
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: 77.18 E-value: 1.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 46 VIFLVFVTTLLGLLGPYFMGVIIDQYIvpkdlNGTARMCMLLIAIYGVTVLL------TWLQTYVMINVALKTIQKIRQD 119
Cdd:cd18583 1 CFLCLLAERVLNVLVPRQLGIIVDSLS-----GGSGKSPWKEIGLYVLLRFLqsggglGLLRSWLWIPVEQYSYRALSTA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 120 IFEKIQTLSLRFFDVRSQGDLMSrvtndidNLNQAltQSVVQIISSAL-----TFIGVTIAM----FSLNWILALVTLIT 190
Cdd:cd18583 76 AFNHVMNLSMDFHDSKKSGEVLK-------AIEQG--SSINDLLEQILfqivpMIIDLVIAIvylyYLFDPYMGLIVAVV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 191 VPIMFFVTKKLVAYSgknfAKRQKDLgeLNGFIEEAITGADVTTLYgkekETVQNFNKIN-EQLRISAT-----KADTFS 264
Cdd:cd18583 147 MVLYVWSTIKLTSWR----TKLRRDM--IDADREERSILTESLLNW----ETVKYFNREPyEKERYREAvknyqKAERKY 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447166293 265 AFIFPSMNFINNLGM--GLVIGT--GSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18583 217 LFSLNLLNAVQSLILtlGLLAGCflAAYQVSQGQATVGDFVTLLTYWAQLSGPLNFFATLYRSIQSDLIDAERL 290
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
61-306 |
1.73e-15 |
|
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: 77.35 E-value: 1.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 61 PYFMGVIIDQYIVPKDLNGTARMCMLLIAIYGVTVLLTWLQT-YVMINVALKTIqKIRQDIFEKIQTLSLRFFDVRSQGD 139
Cdd:cd18784 16 PYYTGQVIDGIVIEKSQDKFSRAIIIMGLLAIASSVAAGIRGgLFTLAMARLNI-RIRNLLFRSIVSQEIGFFDTVKTGD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 140 LMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFSLNWILALVTLITVPIMFFVTKKLVAYSGKNFAKRQKDLGEL 219
Cdd:cd18784 95 ITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 220 NGFIEEAITGAdvttlygkekETVQNF-NKINEQLRISATKADTFS-----AFIFPSMNFINNL-GMGLVIGT---GSVM 289
Cdd:cd18784 175 NEVAEETISSI----------RTVRSFaNEDGEANRYSEKLKDTYKlkikeALAYGGYVWSNELtELALTVSTlyyGGHL 244
|
250
....*....|....*..
gi 447166293 290 VLNGMTTVGVIAAFINY 306
Cdd:cd18784 245 VITGQISGGNLISFILY 261
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
357-545 |
1.74e-15 |
|
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: 75.77 E-value: 1.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 357 QGHVELENVSFGYVE-NKT--ILKEVSLKARPGETIALVGPTGSGKTTIINLLT---RFYDIQQGQIHIDGKDIKDYdin 430
Cdd:cd03234 1 QRVLPWWDVGLKAKNwNKYarILNDVSLHVESGQVMAILGSSGSGKTTLLDAISgrvEGGGTTSGQILFNGQPRKPD--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 431 SLRSKIGVVLQDTYLFAG-TIMDNIRYGRLHASDEEVINAAKAASAHSF-IKHLPkqyETEIASEG-SNLSQGQKQLLAI 507
Cdd:cd03234 78 QFQKCVAYVRQDDILLPGlTVRETLTYTAILRLPRKSSDAIRKKRVEDVlLRDLA---LTRIGGNLvKGISGGERRRVSI 154
|
170 180 190
....*....|....*....|....*....|....*...
gi 447166293 508 ARAILADADILILDEATSNIDTRTELQIQAGLNNLMRG 545
Cdd:cd03234 155 AVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARR 192
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
46-325 |
1.95e-15 |
|
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: 77.24 E-value: 1.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 46 VIFLVFVTTLLGLLGPYFMGVIIDQYIVPKDLNGTARMCMLLIAIYGVTVLLTWLQTYVMINVALKTIQKIRQDIFEKIQ 125
Cdd:cd18566 7 VLLASLFINILALATPLFILQVYDRVIPNESIPTLQVLVIGVVIAILLESLLRLLRSYILAWIGARFDHRLSNAAFEHLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 126 TLSLRFFDVRSQGDLMSRVtNDIDNLNQALTQSVVQIISSaLTFIGVTIA-MFSLNWILALVTLITVPIMFFVTkklvAY 204
Cdd:cd18566 87 SLPLSFFEREPSGAHLERL-NSLEQIREFLTGQALLALLD-LPFVLIFLGlIWYLGGKLVLVPLVLLGLFVLVA----IL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 205 SGKNFAKRQKDLGELN----GFIEEAITGADVTTLYGKEKETVQNFNKINEQLRISATKADTFSAFIFPSMNFINNLGMG 280
Cdd:cd18566 161 LGPILRRALKERSRADerrqNFLIETLTGIHTIKAMAMEPQMLRRYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSMV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 447166293 281 LVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQ 325
Cdd:cd18566 241 AVVAFGALLVINGDLTVGALIACTMLSGRVLQPLQRAFGLWTRFQ 285
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
360-570 |
3.15e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 75.30 E-value: 3.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYVENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDI---KDYDINSLRSKI 436
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlKNREVPFLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 437 GVVLQDTYLFAG-TIMDNIRYGRL--HASDEEVINAAKAASAHSFIKHLPKQYETEiasegsnLSQGQKQLLAIARAILA 513
Cdd:PRK10908 82 GMIFQDHHLLMDrTVYDNVAIPLIiaGASGDDIRRRVSAALDKVGLLDKAKNFPIQ-------LSGGEQQRVGIARAVVN 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 447166293 514 DADILILDEATSNIDTRTELQIQAGLNNLMR-GRTSFVIAHRLKTIEKAD-QILVIKDG 570
Cdd:PRK10908 155 KPAVLLADEPTGNLDDALSEGILRLFEEFNRvGVTVLMATHDIGLISRRSyRMLTLSDG 213
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
360-586 |
3.19e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 75.30 E-value: 3.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYVENKTiLKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINS-LRSKIGV 438
Cdd:PRK11614 6 LSFDKVSAHYGKIQA-LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 439 VLQDTYLFAG-TIMDNIRYGRLHASDEEVINAAKAASAhsfikHLPKQYETEIASEGSnLSQGQKQLLAIARAILADADI 517
Cdd:PRK11614 85 VPEGRRVFSRmTVEENLAMGGFFAERDQFQERIKWVYE-----LFPRLHERRIQRAGT-MSGGEQQMLAIGRALMSQPRL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447166293 518 LILDEATSNIDTRTELQIQAGLNNLM-RGRTSFVIAhrlktiEKADQILVIKD-GSILERGNheSLMEDRG 586
Cdd:PRK11614 159 LLLDEPSLGLAPIIIQQIFDTIEQLReQGMTIFLVE------QNANQALKLADrGYVLENGH--VVLEDTG 221
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
373-576 |
3.99e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 78.55 E-value: 3.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 373 KTILKEVSLKARPGETIALVGPTGSGKTTIINLLTrFYDIQ----QGQIHIDGKDIkdyDINSLRSKIGVVLQDTyLFAG 448
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVLLNGMPI---DAKEMRAISAYVQQDD-LFIP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 449 T--------IMDNIRYGRLHASDE------EVINAAKaasahsfikhLPKQYETEIASEG--SNLSQGQKQLLAIARAIL 512
Cdd:TIGR00955 113 TltvrehlmFQAHLRMPRRVTKKEkrervdEVLQALG----------LRKCANTRIGVPGrvKGLSGGERKRLAFASELL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447166293 513 ADADILILDEATSNIDTRTELQIQAGLNNL-MRGRTSFVIAHR--LKTIEKADQILVIKDGSILERG 576
Cdd:TIGR00955 183 TDPPLLFCDEPTSGLDSFMAYSVVQVLKGLaQKGKTIICTIHQpsSELFELFDKIILMAEGRVAYLG 249
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
360-581 |
4.29e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 75.99 E-value: 4.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYVENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINSLRSKIGVV 439
Cdd:PRK13652 4 IETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 440 LQ--DTYLFAGTIMDNIRYGRLHAS-DEEVINAAKAASAHSF-IKHLPKQYEteiasegSNLSQGQKQLLAIARAILADA 515
Cdd:PRK13652 84 FQnpDDQIFSPTVEQDIAFGPINLGlDEETVAHRVSSALHMLgLEELRDRVP-------HHLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447166293 516 DILILDEATSNIDTRTELQIQAGLNNLMR--GRTSFVIAHRLKTI-EKADQILVIKDGSILERGNHESL 581
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| ABC_6TM_NHLM_bacteriocin |
cd18569 |
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ... |
40-334 |
7.90e-15 |
|
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: 75.21 E-value: 7.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 40 KAALMFVIFLVFVTTLLGLLGPYFMGVIIDQYIVpkdlNGTARMCMLLIAIYGVTVL----LTWLQTYVMINVALKTIQK 115
Cdd:cd18569 1 RSALLFVVLAGLLLVIPGLVIPVFSRIFIDDILV----GGLPDWLRPLLLGMALTALlqglLTWLQQYYLLRLETKLALS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 116 IRQDIFEKIQTLSLRFFDVRSQGDLMSRVtndidnlnqALTQSVVQIISSAL--TFIGVT------IAMFSLNWILALVT 187
Cdd:cd18569 77 SSSRFFWHVLRLPVEFFSQRYAGDIASRV---------QSNDRVANLLSGQLatTVLNLVmavfyaLLMLQYDVPLTLIG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 188 LITVPIMFFVTKKLVAYSGKNFAKRQKDLGELNGfieeaitgadvTTLYGKEK-ETVQN-------FNK--------INE 251
Cdd:cd18569 148 IAIALLNLLVLRLVSRKRVDLNRRLLQDSGKLTG-----------TTMSGLQMiETLKAsgaesdfFSRwagyqakvLNA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 252 QLRISATkadtfSAFIFPSMNFINNLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGG 331
Cdd:cd18569 217 QQELGRT-----NQLLGALPTLLSALTNAAILGLGGLLVMDGALTIGMLVAFQSLMASFLAPVNSLVGLGGTLQEMRGDM 291
|
...
gi 447166293 332 ERV 334
Cdd:cd18569 292 ERL 294
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
339-588 |
1.01e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 75.27 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 339 DEVPEIQNKKDAFIVQNIQGHVELENVSFGYVENKTILkevslkarpgetiaLVGPTGSGKTTIIN-----LLTRFYDIQ 413
Cdd:PRK13631 19 DIILRVKNLYCVFDEKQENELVALNNISYTFEKNKIYF--------------IIGNSGSGKSTLVThfnglIKSKYGTIQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 414 QGQIHIDGKDIKDYDINS-----------LRSKIGVVLQ--DTYLFAGTIMDNIRYGRLhASDEEVINAAKAASahsfiK 480
Cdd:PRK13631 85 VGDIYIGDKKNNHELITNpyskkiknfkeLRRRVSMVFQfpEYQLFKDTIEKDIMFGPV-ALGVKKSEAKKLAK-----F 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 481 HLPKQYETEIASEGS--NLSQGQKQLLAIArAILA-DADILILDEATSNIDTRTELQ-IQAGLNNLMRGRTSFVIAHRL- 555
Cdd:PRK13631 159 YLNKMGLDDSYLERSpfGLSGGQKRRVAIA-GILAiQPEILIFDEPTAGLDPKGEHEmMQLILDAKANNKTVFVITHTMe 237
|
250 260 270
....*....|....*....|....*....|...
gi 447166293 556 KTIEKADQILVIKDGSILERGNHESLMEDRGFY 588
Cdd:PRK13631 238 HVLEVADEVIVMDKGKILKTGTPYEIFTDQHII 270
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
364-576 |
1.09e-14 |
|
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: 77.03 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 364 NVSFG-YVENKTILKEVSLKARPGETIALVGPTGSGKT----TIINLLTRFYDIQQGQIHIDGKDI---KDYDINSLR-S 434
Cdd:COG4172 13 SVAFGqGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLlglSERELRRIRgN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 435 KIGVVLQD--TYL---FagTIMDNIRYG-RLH------ASDEEVI---------NAAKAASAHsfikhlPKQyeteiase 493
Cdd:COG4172 93 RIAMIFQEpmTSLnplH--TIGKQIAEVlRLHrglsgaAARARALellervgipDPERRLDAY------PHQ-------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 494 gsnLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQAGLNNLMR--GRTSFVIAHRLKTIEK-ADQILVIKDG 570
Cdd:COG4172 157 ---LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRelGMALLLITHDLGVVRRfADRVAVMRQG 233
|
....*.
gi 447166293 571 SILERG 576
Cdd:COG4172 234 EIVEQG 239
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
369-577 |
1.25e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 73.96 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 369 YVENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKdikdydINSLrskIGVvlqdtylfaG 448
Cdd:COG1134 35 RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR------VSAL---LEL---------G 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 449 TIM-------DNIR-YGRLH-ASDEEVinAAKAASAHSF------IkHLP-KQYeteiasegsnlSQGQKQLLAIARAIL 512
Cdd:COG1134 97 AGFhpeltgrENIYlNGRLLgLSRKEI--DEKFDEIVEFaelgdfI-DQPvKTY-----------SSGMRARLAFAVATA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447166293 513 ADADILILDEATSNIDTRTELQIQAGLNNLM-RGRTSFVIAHRLKTIEK-ADQILVIKDGSILERGN 577
Cdd:COG1134 163 VDPDILLVDEVLAVGDAAFQKKCLARIRELReSGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGD 229
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
366-585 |
2.23e-14 |
|
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: 76.02 E-value: 2.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 366 SFGYVenkTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFY--DIQQGQIHIDGKDIKDYDI-NSLRSKIGVVLQD 442
Cdd:TIGR02633 10 TFGGV---KALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASNIrDTERAGIVIIHQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 443 TYLFAG-TIMDNIRYGRLHASDEEVIN-AAKAASAHSFIKHLpKQYETEIASEGSNLSQGQKQLLAIARAILADADILIL 520
Cdd:TIGR02633 87 LTLVPElSVAENIFLGNEITLPGGRMAyNAMYLRAKNLLREL-QLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLIL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447166293 521 DEATSNIdTRTELQIqagLNNLMR-----GRTSFVIAHRLKTIEK-ADQILVIKDGSILERGNHESLMEDR 585
Cdd:TIGR02633 166 DEPSSSL-TEKETEI---LLDIIRdlkahGVACVYISHKLNEVKAvCDTICVIRDGQHVATKDMSTMSEDD 232
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
376-585 |
3.16e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 75.43 E-value: 3.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 376 LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDI-----KDydinSLRSKIGVVLQDTYLFAG-T 449
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVtfngpKS----SQEAGIGIIHQELNLIPQlT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 450 IMDNIRYGRLHASDEEVINAAKA-ASAHSFIKHLPKQYETEIASegSNLSQGQKQLLAIARAILADADILILDEATSNI- 527
Cdd:PRK10762 96 IAENIFLGREFVNRFGRIDWKKMyAEADKLLARLNLRFSSDKLV--GELSIGEQQMVEIAKVLSFESKVIIMDEPTDALt 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447166293 528 DTRTElqiqaGLNNLMR-----GRTSFVIAHRLKTI-EKADQILVIKDGSILERGNHESLMEDR 585
Cdd:PRK10762 174 DTETE-----SLFRVIRelksqGRGIVYISHRLKEIfEICDDVTVFRDGQFIAEREVADLTEDS 232
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
360-572 |
3.99e-14 |
|
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: 70.92 E-value: 3.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYVenktiLKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDI-NSLRSKIGV 438
Cdd:cd03215 5 LEVRGLSVKGA-----VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPrDAIRAGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 439 VLQD---TYLFAG-TIMDNIRYGRLhasdeevinaakaasahsfikhlpkqyeteiasegsnLSQGQKQLLAIARAILAD 514
Cdd:cd03215 80 VPEDrkrEGLVLDlSVAENIALSSL-------------------------------------LSGGNQQKVVLARWLARD 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 515 ADILILDEATSNIDTRTELQIQAGLNNL-MRGRTSFVIAHRLKTI-EKADQILVIKDGSI 572
Cdd:cd03215 123 PRVLILDEPTRGVDVGAKAEIYRLIRELaDAGKAVLLISSELDELlGLCDRILVMYEGRI 182
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
367-576 |
4.33e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 72.73 E-value: 4.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 367 FGYvENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIkDYD---INSLRSKIGVVLQD- 442
Cdd:PRK13638 9 FRY-QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSkrgLLALRQQVATVFQDp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 443 -TYLFAGTIMDNIRYG--RLHASDEEVI----NAAKAASAHSFiKHLPKQYeteiasegsnLSQGQKQLLAIARAILADA 515
Cdd:PRK13638 87 eQQIFYTDIDSDIAFSlrNLGVPEAEITrrvdEALTLVDAQHF-RHQPIQC----------LSHGQKKRVAIAGALVLQA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447166293 516 DILILDEATSNIDTRTELQIQAGLNNLM-RGRTSFVIAHRLKTI-EKADQILVIKDGSILERG 576
Cdd:PRK13638 156 RYLLLDEPTAGLDPAGRTQMIAIIRRIVaQGNHVIISSHDIDLIyEISDAVYVLRQGQILTHG 218
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
370-587 |
4.86e-14 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 72.37 E-value: 4.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 370 VENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRF--YDIQQGQIHIDGKDIKDYDiNSLRSKIGVVLQDTYLFA 447
Cdd:CHL00131 17 VNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLE-PEERAHLGIFLAFQYPIE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 448 GTIMDNIRYGRLHASDEEVINAAKAASAHSFIKHLPKQYE---------TEIASEGsnLSQGQKQLLAIARAILADADIL 518
Cdd:CHL00131 96 IPGVSNADFLRLAYNSKRKFQGLPELDPLEFLEIINEKLKlvgmdpsflSRNVNEG--FSGGEKKRNEILQMALLDSELA 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447166293 519 ILDEATSNIDTRTELQIQAGLNNLMRGRTSFV-IAH--RLKTIEKADQILVIKDGSILERGNHE--SLMEDRGF 587
Cdd:CHL00131 174 ILDETDSGLDIDALKIIAEGINKLMTSENSIIlITHyqRLLDYIKPDYVHVMQNGKIIKTGDAElaKELEKKGY 247
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
361-584 |
5.68e-14 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 72.18 E-value: 5.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 361 ELENVSFGYVENK--------TILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDInSL 432
Cdd:COG4167 6 EVRNLSKTFKYRTglfrrqqfEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDY-KY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 433 RSK-IGVVLQDtylfAGTIMD-NIRYGRLhaSDEEVINAAK--AASAHSFIKH-------LPKQYETEIasegSNLSQGQ 501
Cdd:COG4167 85 RCKhIRMIFQD----PNTSLNpRLNIGQI--LEEPLRLNTDltAEEREERIFAtlrlvglLPEHANFYP----HMLSSGQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 502 KQLLAIARAILADADILILDEATSNID--TRT-------ELQIQAGLnnlmrgrtSFV-IAHRLKTIEK-ADQILVIKDG 570
Cdd:COG4167 155 KQRVALARALILQPKIIIADEALAALDmsVRSqiinlmlELQEKLGI--------SYIyVSQHLGIVKHiSDKVLVMHQG 226
|
250
....*....|....
gi 447166293 571 SILERGNHESLMED 584
Cdd:COG4167 227 EVVEYGKTAEVFAN 240
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
379-576 |
6.73e-14 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 71.94 E-value: 6.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 379 VSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIK---DYDInslrSKIGVV--LQDTYLFAG-TIMD 452
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEglpGHQI----ARMGVVrtFQHVRLFREmTVIE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 453 N--------IRYGRLHA---------SDEEVINAAkaasAHsfikHLPKQYETEIAS-EGSNLSQGQKQLLAIARAILAD 514
Cdd:PRK11300 100 NllvaqhqqLKTGLFSGllktpafrrAESEALDRA----AT----WLERVGLLEHANrQAGNLAYGQQRRLEIARCMVTQ 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447166293 515 ADILILDEATSNIDTRTELQIQAGLNNLMR--GRTSFVIAHRLKTI-EKADQILVIKDGSILERG 576
Cdd:PRK11300 172 PEILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVmGISDRIYVVNQGTPLANG 236
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
373-554 |
1.04e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 70.76 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 373 KTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIdgkDIKDYDINSLRSkigvvlqdtylfagtIMD 452
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCV---DVPDNQFGREAS---------------LID 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 453 NIryGRLHASDE--EVINAAKAASAHSFIKHLpkqyeteiasegSNLSQGQKQLLAIARAILADADILILDEATSNIDTR 530
Cdd:COG2401 105 AI--GRKGDFKDavELLNAVGLSDAVLWLRRF------------KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
170 180
....*....|....*....|....*.
gi 447166293 531 TELQIQAGLNNLMR--GRTSFVIAHR 554
Cdd:COG2401 171 TAKRVARNLQKLARraGITLVVATHH 196
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
357-580 |
1.17e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 71.45 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 357 QGHVELENVSFGYVENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINSLRSKI 436
Cdd:PRK15056 4 QAGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 437 GVVLQDTYLFAGTIMDNI---RYG------RLHASDEEVINAAKAASAHSFIKHlpkqyeteiaSEGSNLSQGQKQLLAI 507
Cdd:PRK15056 84 PQSEEVDWSFPVLVEDVVmmgRYGhmgwlrRAKKRDRQIVTAALARVDMVEFRH----------RQIGELSGGQKKRVFL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447166293 508 ARAILADADILILDEATSNIDTRTELQIQAGLNNLM-RGRTSFVIAHRLKTI-EKADQILVIKdGSILERGNHES 580
Cdd:PRK15056 154 ARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSVtEFCDYTVMVK-GTVLASGPTET 227
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
378-576 |
1.17e-13 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 71.11 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 378 EVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINSL---------RSKIGVVLQDTylfag 448
Cdd:PRK11701 24 DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaerrrllRTEWGFVHQHP----- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 449 tiMDNIR--------------------YGRLH--ASD--EEV-INAAKaasahsfIKHLPKQYeteiasegsnlSQGQKQ 503
Cdd:PRK11701 99 --RDGLRmqvsaggnigerlmavgarhYGDIRatAGDwlERVeIDAAR-------IDDLPTTF-----------SGGMQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 504 LLAIARAILADADILILDEATSNIDtrteLQIQAGLNNLMRGRTS------FVIAH-----RLktieKADQILVIKDGSI 572
Cdd:PRK11701 159 RLQIARNLVTHPRLVFMDEPTGGLD----VSVQARLLDLLRGLVRelglavVIVTHdlavaRL----LAHRLLVMKQGRV 230
|
....
gi 447166293 573 LERG 576
Cdd:PRK11701 231 VESG 234
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
47-330 |
1.30e-13 |
|
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: 71.49 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 47 IFLVFVTTLLGLLGPYFMGVIIDQyiVPKDLNGTARMCMLLIAIYGVT----VLLTWLQTYVMINVALKTIQKIRQDIFE 122
Cdd:cd18560 2 LLLLILGKACNVLAPLFLGRAVNA--LTLAKVKDLESAVTLILLYALLrfssKLLKELRSLLYRRVQQNAYRELSLKTFA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 123 KIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIA-MFSLNWILALVTLITVPIMFFVTKKL 201
Cdd:cd18560 80 HLHSLSLDWHLSKKTGEVVRIMDRGTESANTLLSYLVFYLVPTLLELIVVSVVfAFHFGAWLALIVFLSVLLYGVFTIKV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 202 VAYSGKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRISATKADTFSAFIFPSMNFINNLGMGL 281
Cdd:cd18560 160 TEWRTKFRRAANKKDNEAHDIAVDSLLNFETVKYFTNEKYEVDRYGEAVKEYQKSSVKVQASLSLLNVGQQLIIQLGLTL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 447166293 282 VIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAG 330
Cdd:cd18560 240 GLLLAGYRVVDGGLSVGDFVAVNTYIFQLFQPLNFLGTIYRMIIQSLTD 288
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
348-576 |
1.35e-13 |
|
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: 70.44 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 348 KDAFIVQNIQGHVELENVSfgyvenKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDY 427
Cdd:cd03267 15 KEPGLIGSLKSLFKRKYRE------VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 428 DINSLRsKIGVVL------------QDTYLFAGTIMDnIRYGRLHASDEEVINAAKaasahsfIKHLPKQyeteiasEGS 495
Cdd:cd03267 89 RKKFLR-RIGVVFgqktqlwwdlpvIDSFYLLAAIYD-LPPARFKKRLDELSELLD-------LEELLDT-------PVR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 496 NLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQAGLNNLMRGRTSFVI--AHRLKTIEK-ADQILVIKDGSI 572
Cdd:cd03267 153 QLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLltSHYMKDIEAlARRVLVIDKGRL 232
|
....
gi 447166293 573 LERG 576
Cdd:cd03267 233 LYDG 236
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
43-199 |
2.66e-13 |
|
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: 70.61 E-value: 2.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 43 LMFVIFLVFVTTLLGLLGPYFMGVIIDQYIVPKDLNGTARMCMLLIAIYGVTVLLTWLQTYVMINVALKTIQKIRQDIFE 122
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSGYYLGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLHDKLLR 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447166293 123 KIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFSLNWILALVTLITVPIMFFVTK 199
Cdd:cd18580 81 SVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLLQR 157
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
363-584 |
2.69e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 69.92 E-value: 2.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 363 ENVSFGYvENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINS-LRSKIGVVLQ 441
Cdd:PRK10895 7 KNLAKAY-KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHArARRGIGYLPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 442 DTYLFAG-TIMDNIRYG---RLHASDEEVINAAKAASAHSFIKHLPKqyeteiaSEGSNLSQGQKQLLAIARAILADADI 517
Cdd:PRK10895 86 EASIFRRlSVYDNLMAVlqiRDDLSAEQREDRANELMEEFHIEHLRD-------SMGQSLSGGERRRVEIARALAANPKF 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447166293 518 LILDEATSNIDTRTELQIQAGLNNLM-RGRTSFVIAHRLK-TIEKADQILVIKDGSILERGNHESLMED 584
Cdd:PRK10895 159 ILLDEPFAGVDPISVIDIKRIIEHLRdSGLGVLITDHNVReTLAVCERAYIVSQGHLIAHGTPTEILQD 227
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
376-588 |
3.61e-13 |
|
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: 69.42 E-value: 3.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 376 LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINSLrskigVVLQDTYLFAG-TIMDNI 454
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPWlTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 455 rygrlhasdeevinaakAASAHSFIKHLPKQYETEIASEG--------------SNLSQGQKQLLAIARAILADADILIL 520
Cdd:TIGR01184 76 -----------------ALAVDRVLPDLSKSERRAIVEEHialvglteaadkrpGQLSGGMKQRVAIARALSIRPKVLLL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 521 DEATSNID--TRTELQIQaglnnLMR-----GRTSFVIAHRL-KTIEKADQILVIKD------GSILE----RGNH-ESL 581
Cdd:TIGR01184 139 DEPFGALDalTRGNLQEE-----LMQiweehRVTVLMVTHDVdEALLLSDRVVMLTNgpaaniGQILEvpfpRPRDrLEV 213
|
....*..
gi 447166293 582 MEDRGFY 588
Cdd:TIGR01184 214 VEDPSYY 220
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
361-582 |
4.91e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 69.19 E-value: 4.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 361 ELENVSFGyvenkTILKEVSLKARPGETIALVGPTGSGKTTiinLLTRFYDI--QQGQIHIDGKDIKDYDINSL-RSKIG 437
Cdd:PRK03695 2 QLNDVAVS-----TRLGPLSAEVRAGEILHLVGPNGAGKST---LLARMAGLlpGSGSIQFAGQPLEAWSAAELaRHRAY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 438 VVLQDTYLFAgtiMDNIRYGRLHASDeeviNAAKAASAH------SFIKHLPKqyeteIASEGSNLSQGQKQ-------L 504
Cdd:PRK03695 74 LSQQQTPPFA---MPVFQYLTLHQPD----KTRTEAVASalnevaEALGLDDK-----LGRSVNQLSGGEWQrvrlaavV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 505 LAIARAILADADILILDEATSNIDTRTelqiQAGLNNLMR-----GRTSFVIAHRL-KTIEKADQILVIKDGSILERGNH 578
Cdd:PRK03695 142 LQVWPDINPAGQLLLLDEPMNSLDVAQ----QAALDRLLSelcqqGIAVVMSSHDLnHTLRHADRVWLLKQGKLLASGRR 217
|
....
gi 447166293 579 ESLM 582
Cdd:PRK03695 218 DEVL 221
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
376-574 |
5.57e-13 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 71.36 E-value: 5.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 376 LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDI--QQGQIHIDG-----KDIKDydinSLRSKIGVVLQD----TY 444
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHgsYEGEILFDGevcrfKDIRD----SEALGIVIIHQElaliPY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 445 LfagTIMDNIRYGRLHASD-----EEVINAAKAASAHSFIKHLPkqyETEIasegSNLSQGQKQLLAIARAILADADILI 519
Cdd:NF040905 93 L---SIAENIFLGNERAKRgvidwNETNRRARELLAKVGLDESP---DTLV----TDIGVGKQQLVEIAKALSKDVKLLI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 447166293 520 LDEATSNI---DTRTELQIQAGLNNlmRGRTSFVIAHRLKTIEK-ADQILVIKDGSILE 574
Cdd:NF040905 163 LDEPTAALneeDSAALLDLLLELKA--QGITSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
362-583 |
7.60e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 69.05 E-value: 7.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 362 LENVSFGyVENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINSLRSKIGVVLQ 441
Cdd:PRK10575 14 LRNVSFR-VPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 442 DTYLFAGTIMDNI----RY------GRLHASDEEVINAAKAAS-----AHSFIkhlpkqyeteiasegSNLSQGQKQLLA 506
Cdd:PRK10575 93 QLPAAEGMTVRELvaigRYpwhgalGRFGAADREKVEEAISLVglkplAHRLV---------------DSLSGGERQRAW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 507 IARAILADADILILDEATSNIDTRTELQIQAGLNNLMRGRTSFVIAhRLKTIEKA----DQILVIKDGSILERGNHESLM 582
Cdd:PRK10575 158 IAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIA-VLHDINMAarycDYLVALRGGEMIAQGTPAELM 236
|
.
gi 447166293 583 E 583
Cdd:PRK10575 237 R 237
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
360-581 |
1.25e-12 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 68.19 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGyvENKTILKEVSLKARPGETIALVGPTGSGKT----TIINLLTRFYDIQQGQIHIDGKDIKDydiNSLRSK 435
Cdd:PRK10418 5 IELRNIALQ--AAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVAP---CALRGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 436 IgvvlqdtylfAGTIMDN-------IRYGRLHA----------SDEEVINAAKAASAHSFIKHLPKQYETEiasegsnLS 498
Cdd:PRK10418 80 K----------IATIMQNprsafnpLHTMHTHAretclalgkpADDATLTAALEAVGLENAARVLKLYPFE-------MS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 499 QGQKQLLAIARAILADADILILDEATSNIDTRTELQIQAGLNNLMRGRTS--FVIAHRLKTIEK-ADQILVIKDGSILER 575
Cdd:PRK10418 143 GGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALgmLLVTHDMGVVARlADDVAVMSHGRIVEQ 222
|
....*.
gi 447166293 576 GNHESL 581
Cdd:PRK10418 223 GDVETL 228
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
385-528 |
1.78e-12 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 69.13 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 385 PGETI-ALVGPTGSGKTTIINL---LTRfydIQQGQIHIDGKDIKDYD--INsL---RSKIGVVLQDTYLFAG-TIMDNI 454
Cdd:PRK11144 22 PAQGItAIFGRSGAGKTSLINAisgLTR---PQKGRIVLNGRVLFDAEkgIC-LppeKRRIGYVFQDARLFPHyKVRGNL 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447166293 455 RYGRLHASDEEVINAAKAASahsfIKHLPKQYEteiasegSNLSQGQKQLLAIARAILADADILILDEATSNID 528
Cdd:PRK11144 98 RYGMAKSMVAQFDKIVALLG----IEPLLDRYP-------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
87-334 |
1.93e-12 |
|
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: 68.34 E-value: 1.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 87 LIAIYGVTVLLTWLQTYVMINVALKTIQKIRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSA 166
Cdd:cd18574 48 LLGLYLLQSLLTFAYISLLSVVGERVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVQEFKSSFKQCVSQGLRSV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 167 LTFIGVTIAMFSLNWILALVTLITVPIMFFV----TKKLVAYSGKnfAKRQkdLGELNGFIEEAITgaDVTTL--YGKEK 240
Cdd:cd18574 128 TQTVGCVVSLYLISPKLTLLLLVIVPVVVLVgtlyGSFLRKLSRR--AQAQ--VAKATGVADEALG--NIRTVraFAMED 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 241 ETVQNFNKINEQLRISATKADT----FSAFifpSMNFINNLGMGlVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQ 316
Cdd:cd18574 202 RELELYEEEVEKAAKLNEKLGLgigiFQGL---SNLALNGIVLG-VLYYGGSLVSRGELTAGDLMSFLVATQTIQRSLAQ 277
|
250
....*....|....*...
gi 447166293 317 FATLMNTIQAAVAGGERV 334
Cdd:cd18574 278 LSVLFGQYVKGKSAGARV 295
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
361-533 |
2.05e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 69.98 E-value: 2.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 361 ELENVSFGyVENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDgkdikdydinslrSKIGVVL 440
Cdd:PRK11147 321 EMENVNYQ-IDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCG-------------TKLEVAY 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 441 QDTYLFA----GTIMDNIRYGRlhasdEEV-INAAKaasAH------SFIKHlPKQYETEIASegsnLSQGQKQLLAIAR 509
Cdd:PRK11147 387 FDQHRAEldpeKTVMDNLAEGK-----QEVmVNGRP---RHvlgylqDFLFH-PKRAMTPVKA----LSGGERNRLLLAR 453
|
170 180
....*....|....*....|....*
gi 447166293 510 AILADADILILDEATSNIDTRT-EL 533
Cdd:PRK11147 454 LFLKPSNLLILDEPTNDLDVETlEL 478
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
364-570 |
2.24e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 67.15 E-value: 2.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 364 NVSFGYVENKT---ILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIkdydiNSLRS------ 434
Cdd:PRK11629 10 NLCKRYQEGSVqtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPM-----SKLSSaakael 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 435 ---KIGVVLQDTYLFAG-TIMDNIRYGRLhasdeevINAAKAASAHSFIKHLPKQYETEIASE--GSNLSQGQKQLLAIA 508
Cdd:PRK11629 85 rnqKLGFIYQFHHLLPDfTALENVAMPLL-------IGKKKPAEINSRALEMLAAVGLEHRANhrPSELSGGERQRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447166293 509 RAILADADILILDEATSNIDTRTELQIQAGLNNL-MRGRTSF-VIAHRLKTIEKADQILVIKDG 570
Cdd:PRK11629 158 RALVNNPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFlVVTHDLQLAKRMSRQLEMRDG 221
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
373-589 |
2.64e-12 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 66.98 E-value: 2.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 373 KTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINsLRSK--IGVVLQDTYLFAG-T 449
Cdd:COG1137 16 RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMH-KRARlgIGYLPQEASIFRKlT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 450 IMDNIR-YGRLHASDEEVINAAKAASAHSF-IKHLPKQYeteiaseGSNLSQGQKQLLAIARAILADADILILDEATSNI 527
Cdd:COG1137 95 VEDNILaVLELRKLSKKEREERLEELLEEFgITHLRKSK-------AYSLSGGERRRVEIARALATNPKFILLDEPFAGV 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447166293 528 DTRTELQIQAGLNNL-MRGrtsfvIA-----HR----LKTIEKAdqiLVIKDGSILERGNHESLMED---RGFYF 589
Cdd:COG1137 168 DPIAVADIQKIIRHLkERG-----IGvlitdHNvretLGICDRA---YIISEGKVLAEGTPEEILNNplvRKVYL 234
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
361-528 |
2.76e-12 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 66.66 E-value: 2.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 361 ELENVSFgYVENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINSLRSKIGVVL 440
Cdd:PRK10247 9 QLQNVGY-LAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 441 QDTYLFAGTIMDNIRYG---RLHASDEEVInaakAASAHSFikHLPkqyETEIASEGSNLSQGQKQLLAIARAILADADI 517
Cdd:PRK10247 88 QTPTLFGDTVYDNLIFPwqiRNQQPDPAIF----LDDLERF--ALP---DTILTKNIAELSGGEKQRISLIRNLQFMPKV 158
|
170
....*....|.
gi 447166293 518 LILDEATSNID 528
Cdd:PRK10247 159 LLLDEITSALD 169
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
42-327 |
3.42e-12 |
|
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: 67.54 E-value: 3.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 42 ALMFVIFLV-FVTTLLGLLGPYFMGVIIDQYIVPKDLNGTARMCMLLIAIYGVTVLLTWLQTYVMINVALKTIQKIRQDI 120
Cdd:cd18783 2 RLFRDVAIAsLILHVLALAPPIFFQIVIDKVLVHQSYSTLYVLTIGVVIALLFEGILGYLRRYLLLVATTRIDARLALRT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 121 FEKIQTLSLRFFDVRSQGDLMSRVtNDIDNLNQALTQSVVQIISSALTFIGVTIAMFSLNWILALVTL-----ITVPIMF 195
Cdd:cd18783 82 FDRLLSLPIDFFERTPAGVLTKHM-QQIERIRQFLTGQLFGTLLDATSLLVFLPVLFFYSPTLALVVLafsalIALIILA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 196 FVtkklvaysgKNFAKRQKDL----GELNGFIEEAITGAD-VTTLyGKEKETVQNFNKINEQLRISATKADTFSAFIFPS 270
Cdd:cd18783 161 FL---------PPFRRRLQALyraeGERQAFLVETVHGIRtVKSL-ALEPRQRREWDERVARAIRARFAVGRLSNWPQTL 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 447166293 271 MNFINNLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAA 327
Cdd:cd18783 231 TGPLEKLMTVGVIWVGAYLVFAGSLTVGALIAFNMLAGRVAGPLVQLAGLVQEYQEA 287
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
374-528 |
4.74e-12 |
|
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: 65.07 E-value: 4.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 374 TILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIkdydinslrSKIGVVLQDTYLFAG----- 448
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPL---------AEQRDEPHENILYLGhlpgl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 449 ----TIMDNIR-YGRLHASDEEVINAAKAASAHSFIKHLPKQYeteiasegsnLSQGQKQLLAIARAILADADILILDEA 523
Cdd:TIGR01189 85 kpelSALENLHfWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQ----------LSAGQQRRLALARLWLSRRPLWILDEP 154
|
....*
gi 447166293 524 TSNID 528
Cdd:TIGR01189 155 TTALD 159
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
378-583 |
5.24e-12 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 67.94 E-value: 5.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 378 EVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKdyDINSLRSKIGVVLQDTYLFAG-TIMDNIRY 456
Cdd:PRK11607 37 DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS--HVPPYQRPINMMFQSYALFPHmTVEQNIAF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 457 G----RLhASDE---EVINAAKAASAHSFIKHLPKQyeteiasegsnLSQGQKQLLAIARAILADADILILDEATSNIDT 529
Cdd:PRK11607 115 GlkqdKL-PKAEiasRVNEMLGLVHMQEFAKRKPHQ-----------LSGGQRQRVALARSLAKRPKLLLLDEPMGALDK 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447166293 530 RTELQIQAGLNNLMR--GRTSFVIAH-RLKTIEKADQILVIKDGSILERGNHESLME 583
Cdd:PRK11607 183 KLRDRMQLEVVDILErvGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEIYE 239
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
360-565 |
8.91e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 65.52 E-value: 8.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELEN--VSFGyveNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKdikdydinsLRskIG 437
Cdd:PRK09544 5 VSLENvsVSFG---QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LR--IG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 438 VVLQDTYLFAGTIMDNIRYGRLH--ASDEEVINAAKAASAHSFIKHlPKQyeteiasegsNLSQGQKQLLAIARAILADA 515
Cdd:PRK09544 71 YVPQKLYLDTTLPLTVNRFLRLRpgTKKEDILPALKRVQAGHLIDA-PMQ----------KLSGGETQRVLLARALLNRP 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447166293 516 DILILDEATSNIDTRTELQIQAGLNNLMR--GRTSFVIAHRLKTI-EKADQIL 565
Cdd:PRK09544 140 QLLVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDLHLVmAKTDEVL 192
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
387-591 |
2.51e-11 |
|
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: 66.96 E-value: 2.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 387 ETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIkDYDINSLRSKIGVVLQDTYLFAG-TIMDNIR-YGRLHA-SD 463
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHlTVAEHILfYAQLKGrSW 1035
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 464 EEVINAAKAASAHSFIKHlpKQYEteiasEGSNLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQAGLNNLM 543
Cdd:TIGR01257 1036 EEAQLEMEAMLEDTGLHH--KRNE-----EAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYR 1108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 447166293 544 RGRTSFVIAHRLKTIE-KADQILVIKDGSILERGNHESLME--DRGFYFEL 591
Cdd:TIGR01257 1109 SGRTIIMSTHHMDEADlLGDRIAIISQGRLYCSGTPLFLKNcfGTGFYLTL 1159
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
370-587 |
2.65e-11 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 64.04 E-value: 2.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 370 VENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLT--RFYDIQQGQIHIDGKDIKDYDINSlRSKIGVVLQDTY--- 444
Cdd:PRK09580 11 VEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPED-RAGEGIFMAFQYpve 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 445 -------LFAGTIMDNIRYGR----LHASDEEVINAAKAAsahsfIKHLPKQYETEIASEGsnLSQGQKQLLAIARAILA 513
Cdd:PRK09580 90 ipgvsnqFFLQTALNAVRSYRgqepLDRFDFQDLMEEKIA-----LLKMPEDLLTRSVNVG--FSGGEKKRNDILQMAVL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447166293 514 DADILILDEATSNIDTRTELQIQAGLNNLMRGRTSFVIA---HRLKTIEKADQILVIKDGSILERGNHESL--MEDRGF 587
Cdd:PRK09580 163 EPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVthyQRILDYIKPDYVHVLYQGRIVKSGDFTLVkqLEEQGY 241
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
356-594 |
2.85e-11 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 64.26 E-value: 2.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 356 IQGHVELENVSFGYVENKTiLKEVSLKARPGETIALVGPTGSGKTTIINLLTRFY---DIQQGQIHIDGKDIK-----DY 427
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQHQA-LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQregrlAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 428 DINSLRSKIGVVLQDTYLFAG-TIMDNIRYGRLHASD--EEVINAAKAASAHSFIKHLPKQYETEIASEG-SNLSQGQKQ 503
Cdd:PRK09984 80 DIRKSRANTGYIFQQFNLVNRlSVLENVLIGALGSTPfwRTCFSWFTREQKQRALQALTRVGMVHFAHQRvSTLSGGQQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 504 LLAIARAILADADILILDEATSNIDTRTELQIQAGLNNLMR--GRTSFVIAHRLK-TIEKADQILVIKDGSILERGNHES 580
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQndGITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQ 239
|
250
....*....|....
gi 447166293 581 LMEDRgfYFELYTS 594
Cdd:PRK09984 240 FDNER--FDHLYRS 251
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
361-583 |
3.38e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 65.81 E-value: 3.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 361 ELENVSFGYVenktiLKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKdydINSLRSKI--GV 438
Cdd:COG1129 258 EVEGLSVGGV-----VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVR---IRSPRDAIraGI 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 439 VL-----QDTYLFAG-TIMDNI------RYGRLHasdeeVINAAK-AASAHSFIKHL---PKQYETEIasegSNLSQGQK 502
Cdd:COG1129 330 AYvpedrKGEGLVLDlSIRENItlasldRLSRGG-----LLDRRReRALAEEYIKRLrikTPSPEQPV----GNLSGGNQ 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 503 QLLAIARAILADADILILDEATSNID--TRTELQiqaglnNLMRGrtsfvIAHRLKTI-----------EKADQILVIKD 569
Cdd:COG1129 401 QKVVLAKWLATDPKVLILDEPTRGIDvgAKAEIY------RLIRE-----LAAEGKAVivisselpellGLSDRILVMRE 469
|
250
....*....|....*....
gi 447166293 570 GSI---LERG--NHESLME 583
Cdd:COG1129 470 GRIvgeLDREeaTEEAIMA 488
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
343-590 |
3.67e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 66.06 E-value: 3.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 343 EIQNKK-DAFIVQNIQGHVELENVSFGYVENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRfyDIQ----QGQI 417
Cdd:PLN03211 50 KFENMKnKGSNIKRILGHKPKISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAG--RIQgnnfTGTI 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 418 HIDGKDIKdydiNSLRSKIGVVLQDTYLFAG-TIMDNIRYGRLHASDEEVINAAKAASAHSFIKH--LPKQYETEIA-SE 493
Cdd:PLN03211 128 LANNRKPT----KQILKRTGFVTQDDILYPHlTVRETLVFCSLLRLPKSLTKQEKILVAESVISElgLTKCENTIIGnSF 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 494 GSNLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQAGLNNLM-RGRTSFVIAHR--LKTIEKADQILVIKDG 570
Cdd:PLN03211 204 IRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAqKGKTIVTSMHQpsSRVYQMFDSVLVLSEG 283
|
250 260
....*....|....*....|
gi 447166293 571 SILERGNHESLMedrgFYFE 590
Cdd:PLN03211 284 RCLFFGKGSDAM----AYFE 299
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
114-334 |
3.86e-11 |
|
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: 64.28 E-value: 3.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 114 QKIRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFSLNWILALVTLITVPI 193
Cdd:cd18590 69 LRLRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 194 MFFVTKKLVAYSGKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRISATKADTFSAFIFPSMNF 273
Cdd:cd18590 149 TAIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRV 228
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447166293 274 INNLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18590 229 LQLGVQVLMLYCGRQLIQSGHLTTGSLVSFILYQKNLGSYVRTLVYIYGDMLSNVGAAAKV 289
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
360-572 |
8.79e-11 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 63.71 E-value: 8.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYvENKT-ILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDI-----KDYDinslr 433
Cdd:PRK11650 4 LKLQAVRKSY-DGKTqVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVnelepADRD----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 434 skIGVVLQDTYLFAG-TIMDNIRYGrL-------HASDEEVINAAKAASAHSFIKHLPKQyeteiasegsnLSQGQKQLL 505
Cdd:PRK11650 78 --IAMVFQNYALYPHmSVRENMAYG-LkirgmpkAEIEERVAEAARILELEPLLDRKPRE-----------LSGGQRQRV 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 506 AIARAILADADILILDEATSNIDTRTELQIQAGLNNLMR--GRTSFVIAH-RLKTIEKADQILVIKDGSI 572
Cdd:PRK11650 144 AMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRrlKTTSLYVTHdQVEAMTLADRVVVMNGGVA 213
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
376-570 |
1.53e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 63.60 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 376 LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIK-DYDINSLRSKIGVVLQDTYLFAG-TIMDN 453
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQELNLVLQrSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 454 IRYGR-----LHASDEEVINAAKAASAHSFIKHLPKQyeteiasEGSNLSQGQKQLLAIARAILADADILILDEATSNID 528
Cdd:PRK10982 94 MWLGRyptkgMFVDQDKMYRDTKAIFDELDIDIDPRA-------KVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLT 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 447166293 529 TRTELQIQAGLNNLM-RGRTSFVIAHRLKTIEK-ADQILVIKDG 570
Cdd:PRK10982 167 EKEVNHLFTIIRKLKeRGCGIVYISHKMEEIFQlCDEITILRDG 210
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
376-577 |
1.61e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 62.11 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 376 LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIK--DYDINSLRskIGVVLQD--TYLFA---- 447
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSYRSQR--IRMIFQDpsTSLNPrqri 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 448 GTIMD-NIRYG-RLHASD-EEVINAAKAASA----H-SFIKHLpkqyeteiasegsnLSQGQKQLLAIARAILADADILI 519
Cdd:PRK15112 107 SQILDfPLRLNtDLEPEQrEKQIIETLRQVGllpdHaSYYPHM--------------LAPGQKQRLGLARALILRPKVII 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447166293 520 LDEATSNIDTRTELQIQaglnNLM------RGRTSFVIAHRLKTIEK-ADQILVIKDGSILERGN 577
Cdd:PRK15112 173 ADEALASLDMSMRSQLI----NLMlelqekQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGS 233
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
384-588 |
1.65e-10 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 62.82 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 384 RPGETIALVGPTGSGKT----TIINLLTRFYDIQqGQIHIDGKDI---KDYDINSLRS-KIGVVLQDT------YLFAGT 449
Cdd:PRK09473 40 RAGETLGIVGESGSGKSqtafALMGLLAANGRIG-GSATFNGREIlnlPEKELNKLRAeQISMIFQDPmtslnpYMRVGE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 450 -----IMDNIRYGRLHASDEEV--INAAKAASAHSFIKHLPKQYeteiasegsnlSQGQKQLLAIARAILADADILILDE 522
Cdd:PRK09473 119 qlmevLMLHKGMSKAEAFEESVrmLDAVKMPEARKRMKMYPHEF-----------SGGMRQRVMIAMALLCRPKLLIADE 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447166293 523 ATSNIDTRTELQIQAGLNNLMR--GRTSFVIAHRLKTIEK-ADQILVIKDGSILERGNHESLmedrgFY 588
Cdd:PRK09473 188 PTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYGNARDV-----FY 251
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
371-570 |
1.70e-10 |
|
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: 60.72 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 371 ENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYD--IQQGQIHIDGKDIKDydinSLRSKIGVVLQ-DTYLFA 447
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTagVITGEILINGRPLDK----NFQRSTGYVEQqDVHSPN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 448 GTIMDNIRYgrlhasdeevinaakaaSAhsfikhlpkqyeteiASEGsnLSQGQKQLLAIARAILADADILILDEATSNI 527
Cdd:cd03232 94 LTVREALRF-----------------SA---------------LLRG--LSVEQRKRLTIGVELAAKPSILFLDEPTSGL 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 447166293 528 DTRTELQIQAGLNNL-MRGRTSFVIAHR--LKTIEKADQILVIKDG 570
Cdd:cd03232 140 DSQAAYNIVRFLKKLaDSGQAILCTIHQpsASIFEKFDRLLLLKRG 185
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
361-581 |
2.49e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 63.19 E-value: 2.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 361 ELENVSFGYV---ENKTILKEVSLKARPGETIALVGPTGSGKT----TIINLL-TRFYDIQQGQIHIDGKDIKDYDINSL 432
Cdd:PRK15134 7 AIENLSVAFRqqqTVRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLpSPPVVYPSGDIRFHGESLLHASEQTL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 433 R----SKIGVVLQDTyLFAGTIMDNI-----------RYGRLHASDEEVINAAKAASAHSFIKHL---PKQyeteiaseg 494
Cdd:PRK15134 87 RgvrgNKIAMIFQEP-MVSLNPLHTLekqlyevlslhRGMRREAARGEILNCLDRVGIRQAAKRLtdyPHQ--------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 495 snLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQAGLNNLMR--GRTSFVIAHRLKTIEK-ADQILVIKDGS 571
Cdd:PRK15134 157 --LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKlADRVAVMQNGR 234
|
250
....*....|
gi 447166293 572 ILERGNHESL 581
Cdd:PRK15134 235 CVEQNRAATL 244
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
46-325 |
2.83e-10 |
|
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: 61.79 E-value: 2.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 46 VIFLVFVTTLLGLLGPYFMGVIIDQYIVPKDLNGTARMC---MLLIAIYGVT-----VLLTWLQTYvmINVALKTiqkir 117
Cdd:cd18779 7 ILLASLLLQLLGLALPLLTGVLVDRVIPRGDRDLLGVLGlglAALVLTQLLAgllrsHLLLRLRTR--LDTQLTL----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 118 qDIFEKIQTLSLRFFDVRSQGDLMSRVtNDIDNLNQALTQSVVQIISSALTFIGVTIAMFSLNWILALVTL----ITVPI 193
Cdd:cd18779 80 -GFLEHLLRLPYRFFQQRSTGDLLMRL-SSNATIRELLTSQTLSALLDGTLVLGYLALLFAQSPLLGLVVLglaaLQVAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 194 MFFVTKKLVAYSGKNFAKRqkdlGELNGFIEEAITGADVTTLYGKEKETVQNF-NKINEQLRISATKAdTFSAFIFPSMN 272
Cdd:cd18779 158 LLATRRRVRELMARELAAQ----AEAQSYLVEALSGIETLKASGAEDRALDRWsNLFVDQLNASLRRG-RLDALVDALLA 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 447166293 273 FINNLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLsqfATLMNTIQ 325
Cdd:cd18779 233 TLRLAAPLVLLWVGAWQVLDGQLSLGTMLALNALAGAFLAPL---ASLVGTAQ 282
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
110-303 |
3.10e-10 |
|
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: 61.34 E-value: 3.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 110 LKTIQKIRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFSLNWILALVTLI 189
Cdd:cd18585 64 FRLLSNLRVWFYRKLEPLAPARLQKYRSGDLLNRIVADIDTLDNLYLRVLSPPVVALLVILATILFLAFFSPALALILLA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 190 TVPIMFFVTKKLVAYSGKNFAKRQKDL-GELNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRISATKADTFSAFIF 268
Cdd:cd18585 144 GLLLAGVVIPLLFYRLGKKIGQQLVQLrAELRTELVDGLQGMAELLIFGALERQRQQLEQLSDALIKEQRRLARLSGLSQ 223
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 447166293 269 PSMNFINNLGMGLVIGTGSVMVLNG--------MTTVGVIAAF 303
Cdd:cd18585 224 ALMILLSGLTVWLVLWLGAPLVQNGaldgallaMLVFAVLASF 266
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
366-584 |
3.11e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 62.76 E-value: 3.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 366 SFGYVEnktILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINsLRSKIGVVL--QDT 443
Cdd:PRK15439 20 QYSGVE---VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA-KAHQLGIYLvpQEP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 444 YLFAG-TIMDNIRYGrlhasdeevinAAKAASAHSFIKHLPKQYETEI--ASEGSNLSQGQKQLLAIARAILADADILIL 520
Cdd:PRK15439 96 LLFPNlSVKENILFG-----------LPKRQASMQKMKQLLAALGCQLdlDSSAGSLEVADRQIVEILRGLMRDSRILIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447166293 521 DEATSN---IDTRTEL-QIQAGLNnlmRGRTSFVIAHRLKTIEK-ADQILVIKDGSILERGNHESLMED 584
Cdd:PRK15439 165 DEPTASltpAETERLFsRIRELLA---QGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADLSTD 230
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
45-214 |
4.02e-10 |
|
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350023 [Multi-domain] Cd Length: 289 Bit Score: 60.96 E-value: 4.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 45 FVIFLVFVTTLLGLLGPYFMGVIIdQYIVPKDLNGTARMCMLLIAIYGVTVLLTWLQTY---------VMINVALKTIqk 115
Cdd:cd18579 1 LAGLLKLLEDLLSLAQPLLLGLLI-SYLSSYPDEPLSEGYLLALALFLVSLLQSLLLHQyfflsfrlgMRVRSALSSL-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 116 irqdIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALtQSVVQIISSALTFIGVTIAMFSL--NWILA--LVTLITV 191
Cdd:cd18579 78 ----IYRKALRLSSSARQETSTGEIVNLMSVDVQRIEDFF-LFLHYLWSAPLQIIVALYLLYRLlgWAALAglGVLLLLI 152
|
170 180
....*....|....*....|...
gi 447166293 192 PIMFFVTKKLVAYSGKNFAKRQK 214
Cdd:cd18579 153 PLQAFLAKLISKLRKKLMKATDE 175
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
360-583 |
4.26e-10 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 62.51 E-value: 4.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYvENKTILKEVSLKARPGETIALVGPTGSGKTTIINLL--TRFYDIQQGQI-----------HID------ 420
Cdd:TIGR03269 1 IEVKNLTKKF-DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIiyhvalcekcgYVErpskvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 421 ------GKDIKDYDIN----------SLRSKIGVVLQDTYLFAG--TIMDNIrygrLHASDEEVINAAKAAS-AHSFIKH 481
Cdd:TIGR03269 80 epcpvcGGTLEPEEVDfwnlsdklrrRIRKRIAIMLQRTFALYGddTVLDNV----LEALEEIGYEGKEAVGrAVDLIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 482 LpkQYETEIASEGSNLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQAGLNNLMR--GRTSFVIAHRLKTIE 559
Cdd:TIGR03269 156 V--QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKasGISMVLTSHWPEVIE 233
|
250 260
....*....|....*....|....*
gi 447166293 560 K-ADQILVIKDGSILERGNHESLME 583
Cdd:TIGR03269 234 DlSDKAIWLENGEIKEEGTPDEVVA 258
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
86-263 |
4.75e-10 |
|
Six-transmembrane helical domain 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: 350002 [Multi-domain] Cd Length: 312 Bit Score: 61.14 E-value: 4.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 86 LLIAIYGVTVLLT-WLQTYVMINVALKTIQKIRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIIS 164
Cdd:cd18558 63 YYYLIIGAIVLITaYIQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQ 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 165 SALTFIGVTIAMFSLNWILALVTLITVPIMFFV----TKKLVAYSGKNfakrQKDLGELNGFIEEAITGA-DVTTLYGKE 239
Cdd:cd18558 143 NIATFGTGFIIGFIRGWKLTLVILAISPVLGLSavvwAKILSGFTDKE----KKAYAKAGAVAEEVLEAFrTVIAFGGQQ 218
|
170 180
....*....|....*....|....
gi 447166293 240 KETVQNFNKINEQLRISATKADTF 263
Cdd:cd18558 219 KEETRYAQNLEIAKRNGIKKAITF 242
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
362-572 |
5.10e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 60.46 E-value: 5.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 362 LENVSFGYVENkTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIhIDGKDikdyDINSLRSKIGVVLQ 441
Cdd:PRK11247 15 LNAVSKRYGER-TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTA----PLAEAREDTRLMFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 442 DTYLFA-GTIMDNIRYGRLHASDEEVINAAKAASAHSFIKHLPkqyeteiasegSNLSQGQKQLLAIARAILADADILIL 520
Cdd:PRK11247 89 DARLLPwKKVIDNVGLGLKGQWRDAALQALAAVGLADRANEWP-----------AALSGGQKQRVALARALIHRPGLLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 447166293 521 DEATSNIDTRTELQIQAGLNNLMR--GRTSFVIAHRL-KTIEKADQILVIKDGSI 572
Cdd:PRK11247 158 DEPLGALDALTRIEMQDLIESLWQqhGFTVLLVTHDVsEAVAMADRVLLIEEGKI 212
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
44-338 |
6.96e-10 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350048 [Multi-domain] Cd Length: 297 Bit Score: 60.56 E-value: 6.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 44 MFVIFLVFVTTLLGLLGPYFMGVIIDQYIVPKDLNGTARMCMLLIAIYG----VTVLLTWLQTYVMINVALKTIQKIRQD 119
Cdd:cd18604 2 ALLLLLFVLSQLLSVGQSWWLGIWASAYETSSALPPSEVSVLYYLGIYAlislLSVLLGTLRYLLFFFGSLRASRKLHER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 120 IFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVTIAMFSLNWILALVTLITVPIMFFVtk 199
Cdd:cd18604 82 LLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLAALYVYI-- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 200 klvaysGKNFAKRQKDLGELN--------GFIEEAITGadVTTL--YGKEKE-TVQNFNKINEQLRisatkadtfSAFIF 268
Cdd:cd18604 160 ------GRLYLRASRELKRLEsvarspilSHFGETLAG--LVTIraFGAEERfIEEMLRRIDRYSR---------AFRYL 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447166293 269 PSMNF-----INNLGMGLVIGTGSVMVLNGMTTVGvIAAF-INYSRQFSRPLSQFATLMNTIQA---AVaggERVFEIM 338
Cdd:cd18604 223 WNLNRwlsvrIDLLGALFSFATAALLVYGPGIDAG-LAGFsLSFALGFSSAILWLVRSYNELELdmnSV---ERIQEYL 297
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
360-586 |
7.73e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 61.45 E-value: 7.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 360 VELENVSFGYvENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTrfydiqqGQIHIDGKDIKdydiNSLRSKIGVV 439
Cdd:PRK15064 320 LEVENLTKGF-DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLV-------GELEPDSGTVK----WSENANIGYY 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 440 LQD-TYLFAG--TIMDNIRYGRLHASDEEVINAAKAASAHSfikhlpkqyETEIASEGSNLSQGQKQLLAIARAILADAD 516
Cdd:PRK15064 388 AQDhAYDFENdlTLFDWMSQWRQEGDDEQAVRGTLGRLLFS---------QDDIKKSVKVLSGGEKGRMLFGKLMMQKPN 458
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447166293 517 ILILDEATSNIDTRTelqIQAgLNN---LMRGRTSFVIAHRLKTIEKADQILVIKDGSILE-RGNHESLMEDRG 586
Cdd:PRK15064 459 VLVMDEPTNHMDMES---IES-LNMaleKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDfSGTYEEYLRSQG 528
|
|
| ABC_6TM_peptidase_like |
cd18571 |
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and ... |
40-189 |
1.42e-09 |
|
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: 59.38 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 40 KAALMFVIFLVFVTTLLGLLGPYFMGVIIDQYIVPKDLN-----GTARMcMLLIAIYGVTVLLTWLQTYV--MINVALKT 112
Cdd:cd18571 1 KKLILQLLLGLLLGSLLQLIFPFLTQSIVDKGINNKDLNfiyliLIAQL-VLFLGSTSIEFIRSWILLHIssRINISIIS 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447166293 113 iqkirqDIFEKIQTLSLRFFDVRSQGDLMSRVtNDIDNLNQALTQSVVQIISSALTFIGVTIAMFSLNWILALVTLI 189
Cdd:cd18571 80 ------DFLIKLMRLPISFFDTKMTGDILQRI-NDHSRIESFLTSSSLSILFSLLNLIVFSIVLAYYNLTIFLIFLI 149
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
354-584 |
4.66e-09 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 57.47 E-value: 4.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 354 QNIQGHVELENVSFGYvENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINSL- 432
Cdd:PRK11831 2 QSVANLVDMRGVSFTR-GNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 433 --RSKIGVVLQDTYLFAG-TIMDNIRYG-RLHASDEE------VINAAKAASAHSFIKHLPkqyeteiasegSNLSQGQK 502
Cdd:PRK11831 81 tvRKRMSMLFQSGALFTDmNVFDNVAYPlREHTQLPApllhstVMMKLEAVGLRGAAKLMP-----------SELSGGMA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 503 QLLAIARAILADADILILDEATSNIDTRTE---LQIQAGLNNLMrGRTSFVIAHRL-KTIEKADQILVIKDGSILERGNH 578
Cdd:PRK11831 150 RRAALARAIALEPDLIMFDEPFVGQDPITMgvlVKLISELNSAL-GVTCVVVSHDVpEVLSIADHAYIVADKKIVAHGSA 228
|
....*.
gi 447166293 579 ESLMED 584
Cdd:PRK11831 229 QALQAN 234
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
373-535 |
7.04e-09 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 55.96 E-value: 7.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 373 KTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINSLRSKIGVVLQDTYLFAGTIMD 452
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 453 NIRYGRLHASDEEVINAAKAASAHSFiKHLPKQYeteiasegsnLSQGQKQLLAIARAILADADILILDEATSNIDTRTE 532
Cdd:cd03231 93 NLRFWHADHSDEQVEEALARVGLNGF-EDRPVAQ----------LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGV 161
|
...
gi 447166293 533 LQI 535
Cdd:cd03231 162 ARF 164
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
378-529 |
8.34e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 55.97 E-value: 8.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 378 EVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKdydinslrsKIGVVLQDTYLFAG--------- 448
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR---------RQRDEYHQDLLYLGhqpgiktel 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 449 TIMDNIR-YGRLH--ASDEEVINAAKAASAHSFiKHLPkqyeteiaseGSNLSQGQKQLLAIARAILADADILILDEATS 525
Cdd:PRK13538 90 TALENLRfYQRLHgpGDDEALWEALAQVGLAGF-EDVP----------VRQLSAGQQRRVALARLWLTRAPLWILDEPFT 158
|
....
gi 447166293 526 NIDT 529
Cdd:PRK13538 159 AIDK 162
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
376-572 |
1.12e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 57.61 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 376 LKE-VSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIkdyDINSLRSKI--GVVL------QDTYLF 446
Cdd:PRK11288 268 LREpISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPI---DIRSPRDAIraGIMLcpedrkAEGIIP 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 447 AGTIMDNIRYG--RLHASDEEVINAAK-AASAHSFIKHL----PKQyETEIAsegsNLSQGQKQLLAIARAILADADILI 519
Cdd:PRK11288 345 VHSVADNINISarRHHLRAGCLINNRWeAENADRFIRSLniktPSR-EQLIM----NLSGGNQQKAILGRWLSEDMKVIL 419
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 447166293 520 LDEATSNIDTRTELQIQAGLNNLM-RGRTSFVIAHRL-KTIEKADQILVIKDGSI 572
Cdd:PRK11288 420 LDEPTRGIDVGAKHEIYNVIYELAaQGVAVLFVSSDLpEVLGVADRIVVMREGRI 474
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
361-572 |
1.76e-08 |
|
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: 57.14 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 361 ELENVSFGYVENKTI--LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQ-QGQIHIDGK--DIKDyDINSLRSK 435
Cdd:TIGR02633 259 EARNLTCWDVINPHRkrVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKpvDIRN-PAQAIRAG 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 436 IGVVLQDTYLfAGTIMD-----NIRYGRLHA-SDEEVINAAKAASAhsfIKHLPKQYETEIASEG---SNLSQGQKQLLA 506
Cdd:TIGR02633 338 IAMVPEDRKR-HGIVPIlgvgkNITLSVLKSfCFKMRIDAAAELQI---IGSAIQRLKVKTASPFlpiGRLSGGNQQKAV 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447166293 507 IARAILADADILILDEATSNIDTRTELQIQAGLNNLM-RGRTSFVIAHRL-KTIEKADQILVIKDGSI 572
Cdd:TIGR02633 414 LAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAqEGVAIIVVSSELaEVLGLSDRVLVIGEGKL 481
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
332-584 |
1.94e-08 |
|
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: 57.12 E-value: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 332 ERVFEIMDEVPEIQNKKDAFIVQNIqghVELENVSFGYVE-NKTILKEV---SLKARPGETIALVGPTGSGKTTIINLLT 407
Cdd:TIGR03269 255 EVVAVFMEGVSEVEKECEVEVGEPI---IKVRNVSKRYISvDRGVVKAVdnvSLEVKEGEIFGIVGTSGAGKTTLSKIIA 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 408 RFYDIQQGQIHID-GKDIKDYD----INSLRSK--IGVVLQDTYLFA-GTIMDNIRYG-RLHASDE----EVINAAKAAS 474
Cdd:TIGR03269 332 GVLEPTSGEVNVRvGDEWVDMTkpgpDGRGRAKryIGILHQEYDLYPhRTVLDNLTEAiGLELPDElarmKAVITLKMVG 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 475 -----AHSFIKHLPKQyeteiasegsnLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQaglNNLMRGR--- 546
Cdd:TIGR03269 412 fdeekAEEILDKYPDE-----------LSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVT---HSILKAReem 477
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 447166293 547 --TSFVIAHRLKTI-EKADQILVIKDGSILERGNHESLMED 584
Cdd:TIGR03269 478 eqTFIIVSHDMDFVlDVCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
382-566 |
2.48e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 56.72 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 382 KARPGETIALVGPTGSGKTTIINLLTrfydiqqGQIHIDGKDIkDYDInslrsKIGVVLQdtYL---FAGTIMDNIRygr 458
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILA-------GVLKPDEGEV-DEDL-----KISYKPQ--YIspdYDGTVEEFLR--- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 459 lhasdeeviNAAKAASAHSFIKH-------LPKQYETEIasegSNLSQGQKQLLAIARAILADADILILDEATSNIDTRT 531
Cdd:COG1245 424 ---------SANTDDFGSSYYKTeiikplgLEKLLDKNV----KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQ 490
|
170 180 190
....*....|....*....|....*....|....*...
gi 447166293 532 ELQIQAGLNNLM--RGRTSFVIAHRLKTIEK-ADQILV 566
Cdd:COG1245 491 RLAVAKAIRRFAenRGKTAMVVDHDIYLIDYiSDRLMV 528
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
361-572 |
2.80e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 56.48 E-value: 2.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 361 ELENVSFGYVEN--KTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQ-QGQIHIDGKDIKdydINS----LR 433
Cdd:PRK13549 261 EVRNLTAWDPVNphIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRwEGEIFIDGKPVK---IRNpqqaIA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 434 SKIGVVLQDTYLFaG--TIMD---NI------RYGRLHASDEevinAAKAASAHSFIKHLPKQYETEIASEGsNLSQGQK 502
Cdd:PRK13549 338 QGIAMVPEDRKRD-GivPVMGvgkNItlaaldRFTGGSRIDD----AAELKTILESIQRLKVKTASPELAIA-RLSGGNQ 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447166293 503 QLLAIARAILADADILILDEATSNIDTRTELQIQAGLNNLM-RGRTSFVIAHRLKTI-EKADQILVIKDGSI 572
Cdd:PRK13549 412 QKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVqQGVAIIVISSELPEVlGLSDRVLVMHEGKL 483
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
364-528 |
2.84e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 56.48 E-value: 2.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 364 NVSFGYVENKTILKEVSLKARPGETIALVGPTGSGKTTIINlltrfydIQQGqihIDgkdiKDYDINSLRS---KIGVVL 440
Cdd:TIGR03719 9 RVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLR-------IMAG---VD----KDFNGEARPQpgiKVGYLP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 441 QDTYLFAG-TIMDNIRYG---RLHASDE-EVINAAKAASAHSFIKHLPKQYE----------------TEIASEG----- 494
Cdd:TIGR03719 75 QEPQLDPTkTVRENVEEGvaeIKDALDRfNEISAKYAEPDADFDKLAAEQAElqeiidaadawdldsqLEIAMDAlrcpp 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 447166293 495 -----SNLSQGQKQLLAIARAILADADILILDEATSNID 528
Cdd:TIGR03719 155 wdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
348-581 |
3.18e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 56.40 E-value: 3.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 348 KDAFIVQNIQGHVELENVSFGYVENktilkeVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIH--------- 418
Cdd:PRK10261 10 RDVLAVENLNIAFMQEQQKIAAVRN------LSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQcdkmllrrr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 419 ----IDGKDIKDYDINSLR-SKIGVVLQD-------TYLFAGTIMDNIrygRLH--ASDEEVINAAK-------AASAHS 477
Cdd:PRK10261 84 srqvIELSEQSAAQMRHVRgADMAMIFQEpmtslnpVFTVGEQIAESI---RLHqgASREEAMVEAKrmldqvrIPEAQT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 478 FIKHLPKQyeteiasegsnLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQAGLNNLMRGRTSFV--IAHRL 555
Cdd:PRK10261 161 ILSRYPHQ-----------LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVifITHDM 229
|
250 260
....*....|....*....|....*..
gi 447166293 556 KTI-EKADQILVIKDGSILERGNHESL 581
Cdd:PRK10261 230 GVVaEIADRVLVMYQGEAVETGSVEQI 256
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
385-572 |
4.20e-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: 52.76 E-value: 4.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 385 PGETIALVGPTGSGKTTIINLLTRFYDIQQGQIH-IDGKDIKDYDINSLRskigvvlqdtylfagtimdnirygrlhasd 463
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIyIDGEDILEEVLDQLL------------------------------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 464 eevinaakaasahsfikhlpkqyETEIASEGSNLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQA------ 537
Cdd:smart00382 51 -----------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelrl 107
|
170 180 190
....*....|....*....|....*....|....*
gi 447166293 538 GLNNLMRGRTSFVIAHRLKTIEKADQILVIKDGSI 572
Cdd:smart00382 108 LLLLKSEKNLTVILTTNDEKDLGPALLRRRFDRRI 142
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
369-566 |
5.26e-08 |
|
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: 54.34 E-value: 5.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 369 YVENKTILKEVSLKARPG-----ETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIK--------DYDINS---L 432
Cdd:cd03237 3 YPTMKKTLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSykpqyikaDYEGTVrdlL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 433 RSKIGVVLQDTYLfagtimdnirygrlhasDEEVINaakaasahsfikhlPKQYETEIASEGSNLSQGQKQLLAIARAIL 512
Cdd:cd03237 83 SSITKDFYTHPYF-----------------KTEIAK--------------PLQIEQILDREVPELSGGELQRVAIAACLS 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447166293 513 ADADILILDEATSNIDTRTELQIQAGLNNLM--RGRTSFVIAHRLKTIEK-ADQILV 566
Cdd:cd03237 132 KDADIYLLDEPSAYLDVEQRLMASKVIRRFAenNEKTAFVVEHDIIMIDYlADRLIV 188
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
383-566 |
1.10e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.81 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 383 ARPGETIALVGPTGSGKTTIINLLTrfydiqqGQIHIDGKDIkDYDInslrsKIGVVLQdtYL---FAGTIMDNIRygrl 459
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLA-------GVLKPDEGEV-DPEL-----KISYKPQ--YIkpdYDGTVEDLLR---- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 460 hasdeevinAAKAASAHSFIKH-------LPKQYETEIasegSNLSQGQKQLLAIARAILADADILILDEATSNIDTRTE 532
Cdd:PRK13409 423 ---------SITDDLGSSYYKSeiikplqLERLLDKNV----KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQR 489
|
170 180 190
....*....|....*....|....*....|....*..
gi 447166293 533 LQIQAGLNNLMRGR--TSFVIAHRLKTIEK-ADQILV 566
Cdd:PRK13409 490 LAVAKAIRRIAEEReaTALVVDHDIYMIDYiSDRLMV 526
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
372-570 |
1.20e-07 |
|
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: 52.26 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 372 NKTILKEVSLKARPGETIALVGPTGSGKTTIINLL---TRFYDIQQGQIHIDGKDIKDYDINSLRSKIGVVLQDTYLFAG 448
Cdd:cd03233 19 KIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHFPTL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 449 TImdnirygrlhasdEEVINAAKAASAHSFIKhlpkqyeteiasegsNLSQGQKQLLAIARAILADADILILDEATSNID 528
Cdd:cd03233 99 TV-------------RETLDFALRCKGNEFVR---------------GISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 447166293 529 TRTELQIQAGLNNLMR--GRTSFVIAHR--LKTIEKADQILVIKDG 570
Cdd:cd03233 151 SSTALEILKCIRTMADvlKTTTFVSLYQasDEIYDLFDKVLVLYEG 196
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
371-570 |
2.54e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.96 E-value: 2.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 371 ENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYD---IQQGQIHIDGKDIKdydiNSLRSKIGVVLQ-DTYLF 446
Cdd:TIGR00956 774 EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTtgvITGGDRLVNGRPLD----SSFQRSIGYVQQqDLHLP 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 447 AGTIMDNIRYGRLHASDEEVINAAKAASAHSFIKHLP-KQY-ETEIASEGSNLSQGQKQLLAIARAILADADILI-LDEA 523
Cdd:TIGR00956 850 TSTVRESLRFSAYLRQPKSVSKSEKMEYVEEVIKLLEmESYaDAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEP 929
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 447166293 524 TSNIDTRTELQIQAGLNNLMR-GRTSFVIAHRLKTI--EKADQILVIKDG 570
Cdd:TIGR00956 930 TSGLDSQTAWSICKLMRKLADhGQAILCTIHQPSAIlfEEFDRLLLLQKG 979
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
335-574 |
3.46e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 53.25 E-value: 3.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 335 FEIMDEVPEIQNKKDAFIVQNIQGHvelenvSFGYVENktilkeVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQ 414
Cdd:PRK09700 250 FNAMKENVSNLAHETVFEVRNVTSR------DRKKVRD------ISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAG 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 415 GQIHIDGKDIK-DYDINSLRSKIGVVLQ---DTYLFAG-TIMDNIR-------------YGRLHASDEEVInaAKAASAH 476
Cdd:PRK09700 318 GEIRLNGKDISpRSPLDAVKKGMAYITEsrrDNGFFPNfSIAQNMAisrslkdggykgaMGLFHEVDEQRT--AENQREL 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 477 SFIK-HLPKQYETEiasegsnLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQaglnNLMR-----GRTSFV 550
Cdd:PRK09700 396 LALKcHSVNQNITE-------LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIY----KVMRqladdGKVILM 464
|
250 260
....*....|....*....|....*
gi 447166293 551 IAHRLKTI-EKADQILVIKDGSILE 574
Cdd:PRK09700 465 VSSELPEIiTVCDRIAVFCEGRLTQ 489
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
385-528 |
3.55e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 51.39 E-value: 3.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 385 PGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDIN---SLRSKIGVVLQDTylfagTIMDNIRY-GRLH 460
Cdd:PRK13543 36 AGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSrfmAYLGHLPGLKADL-----STLENLHFlCGLH 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447166293 461 ASdeeviNAAKAASAHSFIKHLPKQYETEIasegSNLSQGQKQLLAIARAILADADILILDEATSNID 528
Cdd:PRK13543 111 GR-----RAKQMPGSALAIVGLAGYEDTLV----RQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
364-562 |
7.82e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 49.95 E-value: 7.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 364 NVSFGYvENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDyDINSLRSKIGVVLQDT 443
Cdd:PRK13540 6 ELDFDY-HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFVGHRS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 444 ----YLfagTIMDNIRYGrLHASdeevinaakaaSAHSFIKHLPKQYETE--IASEGSNLSQGQKQLLAIARAILADADI 517
Cdd:PRK13540 84 ginpYL---TLRENCLYD-IHFS-----------PGAVGITELCRLFSLEhlIDYPCGLLSSGQKRQVALLRLWMSKAKL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 447166293 518 LILDEATSNIDTRTELQIQAGLN-NLMRGRTSFVIAHRLKTIEKAD 562
Cdd:PRK13540 149 WLLDEPLVALDELSLLTIITKIQeHRAKGGAVLLTSHQDLPLNKAD 194
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
384-567 |
9.91e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 51.73 E-value: 9.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 384 RPGETIALVGPTGSGKTTIINLLTrfydiqqGQI------------------HIDGKDIKDYdINSLRS-KIGVVLQDTY 444
Cdd:PRK13409 97 KEGKVTGILGPNGIGKTTAVKILS-------GELipnlgdyeeepswdevlkRFRGTELQNY-FKKLYNgEIKVVHKPQY 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 445 L------FAGTIMDNIRYGRLHASDEEVINAAKaasahsfIKHLPKQyetEIasegSNLSQGQKQLLAIARAILADADIL 518
Cdd:PRK13409 169 VdlipkvFKGKVRELLKKVDERGKLDEVVERLG-------LENILDR---DI----SELSGGELQRVAIAAALLRDADFY 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 447166293 519 ILDEATSNIDTRTELQIQAGLNNLMRGRTSFVIAHRLKTIEK-ADQILVI 567
Cdd:PRK13409 235 FFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDLAVLDYlADNVHIA 284
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
361-524 |
1.53e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 50.80 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 361 ELENVSFGYVENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINSLR-SKIGVV 439
Cdd:COG3845 259 EVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRrLGVAYI 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 440 LQDTY---LFAG-TIMDNI---RYGRLHASDEEVINAAKaasAHSFIKHLPKQYETEIASEG---SNLSQGQKQLLAIAR 509
Cdd:COG3845 339 PEDRLgrgLVPDmSVAENLilgRYRRPPFSRGGFLDRKA---IRAFAEELIEEFDVRTPGPDtpaRSLSGGNQQKVILAR 415
|
170
....*....|....*
gi 447166293 510 AILADADILILDEAT 524
Cdd:COG3845 416 ELSRDPKLLIAAQPT 430
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
384-567 |
3.02e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 50.17 E-value: 3.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 384 RPGETIALVGPTGSGKTTIINLLTrfydiqqGQI------------------HIDGKDIKDYdINSLRSK-IGVVLQDTY 444
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILS-------GELkpnlgdydeepswdevlkRFRGTELQDY-FKKLANGeIKVAHKPQY 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 445 ------LFAGTIMDnirygRLHASDE-----EVINAAKaasahsfIKHLpkqYETEIasegSNLSQGQKQLLAIARAILA 513
Cdd:COG1245 169 vdlipkVFKGTVRE-----LLEKVDErgkldELAEKLG-------LENI---LDRDI----SELSGGELQRVAIAAALLR 229
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 447166293 514 DADILILDEATSNIDTRTELQIQAGLNNLMR-GRTSFVIAHRLKTIEK-ADQILVI 567
Cdd:COG1245 230 DADFYFFDEPSSYLDIYQRLNVARLIRELAEeGKYVLVVEHDLAILDYlADYVHIL 285
|
|
| ABC_6TM_LapB_like |
cd18587 |
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ... |
46-327 |
3.81e-06 |
|
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: 48.97 E-value: 3.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 46 VIFLVFVTTLLGLLGPYFMGVIIDQyIVPKdlNGTARMCMLLIAI---YGVTVLLTWLQTYvMINVALKTI-QKIRQDIF 121
Cdd:cd18587 7 VLLAALLINLFALASPLFVMNVYDR-VVPN--NAIETLWVLAIGVliaLLFDFILKLLRAY-FIDVAGKRAdVILSSRLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 122 EKIqtLSLRF-FDVRSQGDLMSRVtNDIDNLNQALTQS-VVQIISsaLTFIGVTIA-MFSLNWILALVTLITVPIM---- 194
Cdd:cd18587 83 ERV--LGLRLeARPASVGSFANNL-REFESVRDFFTSAtLTALID--LPFVLLFLAvIALIGGPLALVPLVAIPLVllyg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 195 FFVTKKLVAYSGKNF-AKRQKdlgelNGFIEEAITGADVTTLYGKEKETVQNFNKINEQLRISATKADTFSAFIFPSMNF 273
Cdd:cd18587 158 LLLQKPLRRLVEESMrESAQK-----NALLVESLSGLETIKALGAEGRMQRRWEEAVAALARSSLKSRLLSSSATNFAQF 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 447166293 274 INNLGMGLVIGTGSVMVLNG-MTTVGVIAAFINYSRQFSrPLSQFATLMNTIQAA 327
Cdd:cd18587 233 VQQLVTVAIVIVGVYLISDGeLTMGGLIACVILSGRALA-PLGQIAGLLTRYQQA 286
|
|
| ABC_6TM_PrtD_like |
cd18586 |
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ... |
40-316 |
4.24e-06 |
|
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: 48.75 E-value: 4.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 40 KAALMFVIFLVFVTTLLGLLGPYFMGVIIDQYIVPKDLNGTARMCMLLIAIYGVTVLLTWLQTYVMINVALKTIQKIRQD 119
Cdd:cd18586 1 RRVFVEVGLFSFFINLLALAPPIFMLQVYDRVLPSGSLSTLLGLTLGMVVLLAFDGLLRQVRSRILQRVGLRLDVELGRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 120 IFEKIQTLSLrffDVRSQGDLMSRVtNDIDNLNQALTQSVVQIISSALTFIGVTIAMFSLNWILALVTLITVPIMF---- 195
Cdd:cd18586 81 VFRAVLELPL---ESRPSGYWQQLL-RDLDTLRNFLTGPSLFAFFDLPWAPLFLAVIFLIHPPLGWVALVGAPVLVglaw 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 196 ---FVTKKLVAYSGKNFAKRqkdlgelNGFIEEAITGADVTTLYGKEKETVQNF-----NKINEQLRISaTKADTFSAFI 267
Cdd:cd18586 157 lnhRATRKPLGEANEAQAAR-------DALAAETLRNAETIKALGMLGNLRRRWearhaETLELQIRAS-DLAGAISAIG 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 447166293 268 FPSMNFINNlgmgLVIGTGSVMVLNGMTTVGV-IAAFINYSRQFSrPLSQ 316
Cdd:cd18586 229 KTLRMALQS----LILGVGAYLVIDGELTIGAlIAASILSGRALA-PIDQ 273
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
375-528 |
7.77e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 48.63 E-value: 7.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 375 ILKEVSLKARPGETIALVGPTGSGKTTI-INLLTRFY--DIQqGQIHIDGKDIkdyDINSLRSKI--------------G 437
Cdd:NF040905 275 VVDDVSLNVRRGEIVGIAGLMGAGRTELaMSVFGRSYgrNIS-GTVFKDGKEV---DVSTVSDAIdaglayvtedrkgyG 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 438 VVLQDTylfagtIMDNIRYGRLHA-SDEEVINAAK-AASAHSFIKHLPKQYETeIASEGSNLSQGQKQLLAIARAILADA 515
Cdd:NF040905 351 LNLIDD------IKRNITLANLGKvSRRGVIDENEeIKVAEEYRKKMNIKTPS-VFQKVGNLSGGNQQKVVLSKWLFTDP 423
|
170
....*....|...
gi 447166293 516 DILILDEATSNID 528
Cdd:NF040905 424 DVLILDEPTRGID 436
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
384-555 |
1.11e-05 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 47.36 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 384 RPGETIALVGPTGSGKTTIINLLT--------RFYDIQQGQIHID---GKDIKDYDINSLRSKIGVVLQDTYL------F 446
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAgklkpnlgKFDDPPDWDEILDefrGSELQNYFTKLLEGDVKVIVKPQYVdlipkaV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 447 AGTIMDNirygrLHASDEEvinaakaasahSFIKHLPKQYETE--IASEGSNLSQGQKQLLAIARAILADADILILDEAT 524
Cdd:cd03236 104 KGKVGEL-----LKKKDER-----------GKLDELVDQLELRhvLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPS 167
|
170 180 190
....*....|....*....|....*....|..
gi 447166293 525 SNIDTRTELQIQAGLNNLMR-GRTSFVIAHRL 555
Cdd:cd03236 168 SYLDIKQRLNAARLIRELAEdDNYVLVVEHDL 199
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
141-579 |
2.33e-05 |
|
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: 47.44 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 141 MSRVTNDIDNLNQALTQSVVQI-ISSALTFIGVTIAMfsLNWILALVTLIT------VPIMF---FVTKKLVAYSGKNFA 210
Cdd:TIGR00954 187 VSNLDSRIQNPDQLLTQDVEKFcDSVVELYSNLTKPI--LDVILYSFKLLTalgsvgPAGLFaylFATGVVLTKLRPPIG 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 211 K----RQKDLGELNGFIEEAITGADVTTLYG---KEKETVQN-FNKINEQLRisatKADTFSAfifpSMNFINNL----- 277
Cdd:TIGR00954 265 KltveEQALEGEYRYVHSRLIMNSEEIAFYQgnkVEKETVMSsFYRLVEHLN----LIIKFRF----SYGFLDNIvakyt 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 278 --GMGLVIGTGSVMVLNGMTTVG-----VIAAFINYSR---QFSRPLSQFATLMNTIQAAVAGGERVFEIMD-------- 339
Cdd:TIGR00954 337 wsAVGLVAVSIPIFDKTHPAFLEmseeeLMQEFYNNGRlllKAADALGRLMLAGRDMTRLAGFTARVDTLLQvlddvksg 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 340 -----EVPEIQN----------KKDAFIVQNIQGHVELENVSFGYVENKTILKEVSLKARPGETIALVGPTGSGKTTIIN 404
Cdd:TIGR00954 417 nfkrpRVEEIESgreggrnsnlVPGRGIVEYQDNGIKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFR 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 405 LLTRFYDIQQGQIHIDGKdikdydinslrSKIGVVLQDTYLFAGTIMDNIRYGRlhaSDEEVINaaKAASAHSFIKHLPK 484
Cdd:TIGR00954 497 ILGELWPVYGGRLTKPAK-----------GKLFYVPQRPYMTLGTLRDQIIYPD---SSEDMKR--RGLSDKDLEQILDN 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 485 QYETEIASEGSN----------LSQGQKQLLAIARAILADADILILDEATSNIDTRTElqiQAGLNNLMR-GRTSFVIAH 553
Cdd:TIGR00954 561 VQLTHILEREGGwsavqdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVE---GYMYRLCREfGITLFSVSH 637
|
490 500
....*....|....*....|....*.
gi 447166293 554 RlKTIEKADQILVIKDGsileRGNHE 579
Cdd:TIGR00954 638 R-KSLWKYHEYLLYMDG----RGGYQ 658
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
357-563 |
3.10e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.93 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 357 QGHVELENVSFGYvENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRfyDIQQG---QIHIDGK---------DI 424
Cdd:PRK10938 258 EPRIVLNNGVVSY-NDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG--DHPQGysnDLTLFGRrrgsgetiwDI 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 425 KdydinslrSKIGVV---LQDTYLFAGTIMDNIRYGRLHAsdeevINAAKAASAHSfiKHLPKQYETEIASEGS------ 495
Cdd:PRK10938 335 K--------KHIGYVsssLHLDYRVSTSVRNVILSGFFDS-----IGIYQAVSDRQ--QKLAQQWLDILGIDKRtadapf 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 496 -NLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQAGLNNLMR-GRTS--FV----------IAHRLKTIEKA 561
Cdd:PRK10938 400 hSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISeGETQllFVshhaedapacITHRLEFVPDG 479
|
..
gi 447166293 562 DQ 563
Cdd:PRK10938 480 DI 481
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
376-583 |
5.50e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 45.46 E-value: 5.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 376 LKEVSLKARPGETIALVGPTGSGKTTIINLLTrfydiqqGQIHIDGKDIK--DYDI----NSLRSKIGVV---------- 439
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLT-------GILVPTSGEVRvlGYVPfkrrKEFARRIGVVfgqrsqlwwd 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 440 --LQDTYLFAGTImdnirYGrlhasdeevINAAKAASAhsfIKHLpkqyeTEIASEGS-------NLSQGQKQLLAIARA 510
Cdd:COG4586 111 lpAIDSFRLLKAI-----YR---------IPDAEYKKR---LDEL-----VELLDLGElldtpvrQLSLGQRMRCELAAA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447166293 511 ILADADILILDEATSNIDTRTELQIQAGLN--NLMRGRTSFVIAHRLKTIEK-ADQILVIKDGSILERGNHESLME 583
Cdd:COG4586 169 LLHRPKILFLDEPTIGLDVVSKEAIREFLKeyNRERGTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKE 244
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
384-559 |
6.36e-05 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 46.16 E-value: 6.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 384 RPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDyDINSLRSKIGVVLQ----DTYLfagTIMDNIR-YGR 458
Cdd:TIGR01257 1963 RPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMGYCPQfdaiDDLL---TGREHLYlYAR 2038
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 459 LHASDEEVINAAKAASAHSFIKHLpkqYETEIASegsNLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQAG 538
Cdd:TIGR01257 2039 LRGVPAEEIEKVANWSIQSLGLSL---YADRLAG---TYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNT 2112
|
170 180
....*....|....*....|..
gi 447166293 539 LNNLMR-GRTSFVIAHRLKTIE 559
Cdd:TIGR01257 2113 IVSIIReGRAVVLTSHSMEECE 2134
|
|
| ABC_6TM_ABCB6 |
cd18581 |
Six-transmembrane helical domain of the ATP-binding cassette subfamily B member 6, ... |
47-327 |
6.73e-05 |
|
Six-transmembrane helical domain of the ATP-binding cassette subfamily B member 6, mitochondrial; This group represents the ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, ABCB6 (ABC transporter subfamily B, member 6) is closely related to yeast ATM1 and human ABCB7, which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.
Pssm-ID: 350025 [Multi-domain] Cd Length: 300 Bit Score: 45.31 E-value: 6.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 47 IFLVFVTTLLGLLGPYFMGVIIDQYIVPKDLNGTArMCMLLIAIY-----------GVTVLLTWLQTYVMINVALKTIQK 115
Cdd:cd18581 2 LLLLAAGRVVNVLVPILYKKIVDSLTPDSADSPLA-FPWALILLYvflkflqgggsGSVGLLSNLRSFLWIPVQQFTTRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 116 IRQDIFEKIQTLSLRFFDVRSQGDL---MSRVTNDIDNLNQALTQSVV-QIISSAltfIGVTIAMFSLNWILALVTLITV 191
Cdd:cd18581 81 ISVKLFAHLHSLSLRWHLSRKTGEVlrvMDRGTSSINSLLSYVLFNIGpTIADII---IAIIYFAIAFNPWFGLIVFVTM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 192 PIMFFVTKKLVAYSGK--------NFAKRQKDLGELNGFieeaitgadvttlygkekETVQNFNkiNEQLRI----SAT- 258
Cdd:cd18581 158 ALYLILTIIITEWRTKfrremnklDNEKRAKAVDSLLNF------------------ETVKYYN--AERFEVeryrRAId 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447166293 259 ---KADTFSAFifpSMNFIN---NLGMGLVIGTGSV----MVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAA 327
Cdd:cd18581 218 dyqVAEWKSNA---SLNLLNtaqNLIITIGLLAGSLlcayFVVEGKLTVGDFVLFLTYIIQLYAPLNFFGTYYRMIQQS 293
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
362-425 |
9.87e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.16 E-value: 9.87e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447166293 362 LENVSFGYVEnKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIdGKDIK 425
Cdd:PRK10636 315 MEKVSAGYGD-RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-AKGIK 376
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
88-196 |
1.03e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350050 [Multi-domain] Cd Length: 290 Bit Score: 44.39 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 88 IAIYG----VTVLLTWLQTYVMINVALKTIQKIRQDIFEKIqtlsLR----FFDVRSQGDLMSRVTNDIDNLNQALTQSV 159
Cdd:cd18606 38 IGIYAglgvLQAIFLFLFGLLLAYLGIRASKRLHNKALKRV----LRapmsFFDTTPLGRILNRFSKDTDVLDNELPDSL 113
|
90 100 110
....*....|....*....|....*....|....*...
gi 447166293 160 VQIISSALTFIGVTIAMF-SLNWILALVtlitVPIMFF 196
Cdd:cd18606 114 RMFLYTLSSIIGTFILIIiYLPWFAIAL----PPLLVL 147
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
496-570 |
1.93e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 42.98 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 496 NLSQGQKQL------LAIARAILADADILILDEATSNIDtrtELQIQAGLNNLMRGRTSF------VIAHRLKTIEKADQ 563
Cdd:cd03240 115 RCSGGEKVLasliirLALAETFGSNCGILALDEPTTNLD---EENIEESLAEIIEERKSQknfqliVITHDEELVDAADH 191
|
....*...
gi 447166293 564 IL-VIKDG 570
Cdd:cd03240 192 IYrVEKDG 199
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
360-426 |
1.95e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 44.35 E-value: 1.95e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447166293 360 VELENVSFGYveNKTI-LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKD 426
Cdd:NF033858 2 ARLEGVSHRY--GKTVaLDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD 67
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
364-528 |
2.63e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 43.95 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 364 NVSFGYVENKTILKEVSLKARPGETIALVGPTGSGKTTIINlltrfydIQQGqihIDgkdiKDYDINSLRS---KIGVVL 440
Cdd:PRK11819 11 RVSKVVPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLR-------IMAG---VD----KEFEGEARPApgiKVGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 441 QDTYLFAG-TIMDNIRYG---RLHASDE-EVINAAKAASAHSFIKHLPKQ--YETEIASEG------------------- 494
Cdd:PRK11819 77 QEPQLDPEkTVRENVEEGvaeVKAALDRfNEIYAAYAEPDADFDALAAEQgeLQEIIDAADawdldsqleiamdalrcpp 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 447166293 495 -----SNLSQGQKQLLAIARAILADADILILDEATSNID 528
Cdd:PRK11819 157 wdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
379-528 |
2.73e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 43.96 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 379 VSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKDIKDYDINSlRSKIGVVLQDTYLFAG-TIMDNIRyg 457
Cdd:NF033858 285 VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIAT-RRRVGYMSQAFSLYGElTVRQNLE-- 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 458 rLHAS----DEEVINAAKAASAHSF-----IKHLPkqyeteiasegSNLSQGQKQLLAIARAILADADILILDEATSNID 528
Cdd:NF033858 362 -LHARlfhlPAAEIAARVAEMLERFdladvADALP-----------DSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
88-256 |
3.11e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350047 [Multi-domain] Cd Length: 296 Bit Score: 42.85 E-value: 3.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 88 IAIYG----VTVLLTWLQTYVMINVALKTIQKIRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQII 163
Cdd:cd18603 44 LGVYGalglGQAIFVFLGSLALALGCVRASRNLHNKLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 164 SSALTFIG-VTIAMFSLNWILALVTLITVpIMFFVTKKLVAYSgknfakRQkdLGELNG--------FIEEAITGADVTT 234
Cdd:cd18603 124 NCLFQVIStLVVISISTPIFLVVIIPLAI-LYFFIQRFYVATS------RQ--LKRLESvsrspiysHFSETLQGASTIR 194
|
170 180
....*....|....*....|...
gi 447166293 235 LYGKEKETV-QNFNKINEQLRIS 256
Cdd:cd18603 195 AYGVQERFIrESDRRVDENQRAY 217
|
|
| ABC_6TM_PglK_like |
cd18553 |
Six-transmembrane helical domain of the ABC transporter PglK and similar proteins; This group ... |
87-266 |
3.93e-04 |
|
Six-transmembrane helical domain of the ABC transporter PglK and similar proteins; This group represents the transmembrane (TM) domain of an active lipid-linked oligosaccharides flippase PglK (protein glycosylation K), which is a homodimeric ABC transporter that flips a lipid-linked oligosaccharide that serves as a glycan donor in N-linked protein glycosylation. Pglk mediates the ATP-dependent translocation of the undecaprenylpyrophosphate-linked heptasaccharide intermediate across the cell membrane; this is an essential step during the N-linked protein glycosylation pathway. This TM subunit exhibits 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. Bacterial ABC exporters are typically expressed as half-transporters that contain one transmembrane domain (TMD) fused to a nucleotide-binding domain (NBD), which dimerize to form the full transporter.
Pssm-ID: 349997 Cd Length: 300 Bit Score: 42.92 E-value: 3.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 87 LIAIYGVTVLLTWLQTYVMINVALKTIQKIRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALtQSVVQIISSA 166
Cdd:cd18553 60 LIGFYIFRSLYNIFYTYLLNRFSFGRYHSIAYRLFKNYLKLNYQDFTNKNSSDLSKSIINEASNLSQVI-QSFLFILSEI 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 167 LTFIGVTIAMFSLNWILALV-TLITVPIMFFVTKKLVAYSGKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKETVQN 245
Cdd:cd18553 139 FVILFIYSLLLYVNWKITLVlTLFLGLNVFFITKIVSKKIKKQGKKREESQKKFYKILSETFGNFKIIKLKSNEKEILKN 218
|
170 180
....*....|....*....|.
gi 447166293 246 FNKINEQLRISATKADTFSAF 266
Cdd:cd18553 219 FSQASLKFAKANIINQTLQTV 239
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
88-200 |
4.81e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350045 [Multi-domain] Cd Length: 314 Bit Score: 42.69 E-value: 4.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 88 IAIYGV----TVLLTWLQTYVMINVALKTIQKIRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQII 163
Cdd:cd18601 62 LGIYAGltaaTFVFGFLRSLLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFL 141
|
90 100 110
....*....|....*....|....*....|....*...
gi 447166293 164 SSALTFIGVTIAMFSLN-WIlaLVTLITVPIMFFVTKK 200
Cdd:cd18601 142 QLLLQVVGVVLLAVVVNpWV--LIPVIPLVILFLFLRR 177
|
|
| FlhF |
TIGR03499 |
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility] |
336-401 |
6.04e-04 |
|
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]
Pssm-ID: 274609 [Multi-domain] Cd Length: 282 Bit Score: 41.94 E-value: 6.04e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447166293 336 EIMDEVPEIQNKKDafIVQNIQGHveLENVSFGYVENKTILKEvslkarpGETIALVGPTGSGKTT 401
Cdd:TIGR03499 155 ELLEKLPEDADAED--AWRWLREA--LEGMLPVKPEEDPILEQ-------GGVIALVGPTGVGKTT 209
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
371-597 |
6.87e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 41.73 E-value: 6.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 371 ENKTI--LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGkdikdyDINSLRSKIGVVLQDTYlfag 448
Cdd:PRK13546 33 KNKTFfaLDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG------EVSVIAISAGLSGQLTG---- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 449 tiMDNIRYGRL---------HASDEEVINAAKAAsahSFIKHLPKQYeteiasegsnlSQGQKQLLAIARAILADADILI 519
Cdd:PRK13546 103 --IENIEFKMLcmgfkrkeiKAMTPKIIEFSELG---EFIYQPVKKY-----------SSGMRAKLGFSINITVNPDILV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 520 LDEATSNID-TRTELQIQAGLNNLMRGRTSFVIAHRLKTIEK-ADQILVIKDGSILERGNHESLMEDrgfyFELYTSQFK 597
Cdd:PRK13546 167 IDEALSVGDqTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVLPK----YEAFLNDFK 242
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
496-570 |
1.14e-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: 1.14e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447166293 496 NLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQAGLNNL-MRG-RTSFVIAHRLKTIEKADQILVIKDG 570
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLsEEGkKTALVVEHDLAVLDYLSDRIHVFEG 147
|
|
| SRP54 |
pfam00448 |
SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 ... |
389-572 |
2.65e-03 |
|
SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 family of proteins.
Pssm-ID: 459814 [Multi-domain] Cd Length: 193 Bit Score: 39.45 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 389 IALVGPTGSGKTTIINLLTRFYdIQQGQihidgkdikdydinslrsKIGVVLQDTYlfagtimdnirygRLHASDEEVIN 468
Cdd:pfam00448 3 ILLVGLQGSGKTTTIAKLAAYL-KKKGK------------------KVLLVAADTF-------------RAAAIEQLKQL 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 469 AAKAASAhsFIKHLPKQYETEIASEgsnlsqgqkqllAIARAILADADILIldeatsnIDTRTELQIQAGLNNLMRgrts 548
Cdd:pfam00448 51 AEKLGVP--VFGSKTGADPAAVAFD------------AVEKAKAENYDVVL-------VDTAGRLQNDKNLMDELK---- 105
|
170 180
....*....|....*....|....
gi 447166293 549 fviahRLKTIEKADQILVIKDGSI 572
Cdd:pfam00448 106 -----KIKRVVAPDEVLLVLDATT 124
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
497-582 |
3.37e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 39.79 E-value: 3.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 497 LSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQAGLNNLMR--GRTSFVIAHRLKTIEK-ADQILVIKDGSIL 573
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLSQwADKINVLYCGQTV 238
|
....*....
gi 447166293 574 ERGNHESLM 582
Cdd:PRK15093 239 ETAPSKELV 247
|
|
| ABC_6TM_McjD_like |
cd18556 |
Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter ... |
43-199 |
3.95e-03 |
|
Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter McjD and similar proteins; This group represents the 6-TM subunit of the ABC transporter McjD that exports the antibacterial peptide microcin J25, which is an antimicrobial peptide produced by Enterobacteriaceae against other microorganisms for survival under nutrient starvation. Thus, the ABC exporter McjD provides self-immunity of the producing bacteria through export of the toxic peptide out of the cell. Bacterial ABC exporters are typically expressed as half-transporters that contain one transmembrane domain (TMD) fused to a nucleotide-binding domain (NBD), which dimerize to form the full transporter.
Pssm-ID: 350000 Cd Length: 298 Bit Score: 39.55 E-value: 3.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 43 LMFVIFLVFVTTLLGLLGPYFMGVIIDQyiVPKDLNGTARMCMLLIAIYGVTV----LLTWLQTYVMINVALKTIQKIRQ 118
Cdd:cd18556 4 FFSILFISLLSSILISISPVILAKITDL--LTSSSSDSYNYIVVLAALYVITIsatkLLGFLSLYLQSSLRVELIISISS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 119 DIFEKIQTLSLRFFDVRSQGDLMSRV---TNDI----DNLNQALTQSVVQIISSaltfigVTIAMFSLNWILALVTLITV 191
Cdd:cd18556 82 SYFRYLYEQPKTFFVKENSGDITQRLnqaSNDLytlvRNLSTNILPPLLQLIIA------IVVILSSGDYFVAALFLLYA 155
|
....*...
gi 447166293 192 pIMFFVTK 199
Cdd:cd18556 156 -VLFVINN 162
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
47-212 |
4.28e-03 |
|
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350040 [Multi-domain] Cd Length: 309 Bit Score: 39.40 E-value: 4.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 47 IFLVFVTTLLGLLGPYFMGVIIdQYIVPKDLNGTARMCMLLIAIYGVTVLLTWLQTYVM-----INVALKTIqkIRQDIF 121
Cdd:cd18596 3 ALLAVLSSVLSFAPPFFLNRLL-RYLEDPGEDATVRPWVWVLLLFLGPLLSSLLDQQYLwigrrLSVRLRAI--LTQLIF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166293 122 EKiqtlSLRFFDVR-----------------------SQGDLMSRVTNDIDNLNQALTQsVVQIISSALTFIgvtIAMFS 178
Cdd:cd18596 80 EK----ALRRRDKSgssksseskkkdkeededekssaSVGKINNLMSVDANRISEFAAF-LHLLVSAPLQIV---IAIVF 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 447166293 179 LNWIL-------ALVTLITVPIMFFVTKKLVAYSGKNFAKR 212
Cdd:cd18596 152 LYRLLgwsalvgLAVMVLLLPLNGYLAKRYSRAQKELMKAR 192
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
388-429 |
5.07e-03 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 37.21 E-value: 5.07e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 447166293 388 TIALVGPTGSGKTTIINLLTRFY-----------DIQQGQIHIDGKDIKDYDI 429
Cdd:pfam01926 1 RVALVGRPNVGKSTLINALTGAKaivsdypgttrDPNEGRLELKGKQIILVDT 53
|
|
| |
