|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-610 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 660.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 2 KEFLQLMRR---FVSPYKKYIGWAILLNILSAVFNVFSFTLLIPILDILFktgennkvyeymewgtagfkdvainnfyyy 78
Cdd:COG1132 3 KSPRKLLRRllrYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALL------------------------------ 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 79 vsqmiqDNGPTTALIFLGLFLALMTLFKTSCYFASSAVMIPLRTGVVRDIRIMVYAKVMRLPMGFFSEERKGDIIARMSG 158
Cdd:COG1132 53 ------AGGDLSALLLLLLLLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTN 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 159 DVGEVENSITSSLDMLIKSPIMIILYFITLIATSWKLTLFTVLVLPAMGWLMGKVGRKLKRQSLEAQGKWSDTMSQLEET 238
Cdd:COG1132 127 DVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQES 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 239 LGGLRIIKAFIAEDRMIDRFTRCSNELRDAVNKVAMRQALAHPMSEFLGTILIVSVLWFGGALILghNSSLTAPTFIFYM 318
Cdd:COG1132 207 LSGIRVVKAFGREERELERFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVL--SGSLTVGDLVAFI 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 319 VILYSVINPLKDFAKAGYNIPKGLASMERVDKILKAENNIKEIPNPKPLTGMNDRIEFKDISFSYDGKREVLKHVNLTVP 398
Cdd:COG1132 285 LYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIPDPPGAVPLPPVRGEIEFENVSFSYPGDRPVLKDISLTIP 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 399 KGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRSLIGNVNQEAILFNDTFFNNIAFGVENATME 478
Cdd:COG1132 365 PGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDE 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 479 QVIEAAKIANAHDFIMEKPEGYNTNIGDRGGKLSGGQRQRVSIARAILKNPPILILDEATSALDTESERLVQEALERLMK 558
Cdd:COG1132 445 EVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK 524
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 499421346 559 TRTTIAIAHRLSTIKNADEICVLYEGEIVERGRHEELLELDGYYKRLNDMQA 610
Cdd:COG1132 525 GRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARGGLYARLYRLQF 576
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
4-609 |
4.01e-158 |
|
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: 465.35 E-value: 4.01e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 4 FLQLMRRfVSPYKKYIGWAILLNILSAVFNVFSFTLLIPILDILFKTGENNKvyeymewgtagfkdvainnfyyyvsqmi 83
Cdd:TIGR02203 2 FRRLWSY-VRPYKAGLVLAGVAMILVAATESTLAALLKPLLDDGFGGRDRSV---------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 84 qdngpttaLIFLGLFLALMTLFKTSCYFASSAVMIPLRTGVVRDIRIMVYAKVMRLPMGFFSEERKGDIIARMSGDVGEV 163
Cdd:TIGR02203 53 --------LWWVPLVVIGLAVLRGICSFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQV 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 164 ENSITSSLDMLIKSPIMIILYFITLIATSWKLTLFTVLVLPAMGWLMGKVGRKLKRQSLEAQGKWSDTMSQLEETLGGLR 243
Cdd:TIGR02203 125 ASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYR 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 244 IIKAFIAEDRMIDRFTRCSNELRDAVNKVAMRQALAHPMSEFLGTILIVSVLWFggALILGHNSSLTAPTFIFYMVILYS 323
Cdd:TIGR02203 205 VVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSISSPITQLIASLALAVVLFI--ALFQAQAGSLTAGDFTAFITAMIA 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 324 VINPLKDFAKAGYNIPKGLASMERVDKILKAENNIKEipNPKPLTGMNDRIEFKDISFSYDGK-REVLKHVNLTVPKGKT 402
Cdd:TIGR02203 283 LIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPEKDT--GTRAIERARGDVEFRNVTFRYPGRdRPALDSISLVIEPGET 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 403 VALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRSLIGNVNQEAILFNDTFFNNIAFG-VENATMEQVI 481
Cdd:TIGR02203 361 VALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGrTEQADRAEIE 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 482 EAAKIANAHDFIMEKPEGYNTNIGDRGGKLSGGQRQRVSIARAILKNPPILILDEATSALDTESERLVQEALERLMKTRT 561
Cdd:TIGR02203 441 RALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRT 520
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 499421346 562 TIAIAHRLSTIKNADEICVLYEGEIVERGRHEELLELDGYYKRLNDMQ 609
Cdd:TIGR02203 521 TLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLYAQLHNMQ 568
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
5-610 |
2.33e-157 |
|
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: 468.16 E-value: 2.33e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 5 LQLMRRFVSPYKKYIGWAILLNILSAVFnvfsfTLLIPILdilfktgennkvyeymewgtagfkdvainnfyyyvSQMIQ 84
Cdd:COG2274 144 LRWFLRLLRRYRRLLLQVLLASLLINLL-----ALATPLF-----------------------------------TQVVI 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 85 D----NGPTTALIFLGLFLALMTLFKTSCYFASSAVMIPLRTGVVRDIRIMVYAKVMRLPMGFFSEERKGDIIARMSgDV 160
Cdd:COG2274 184 DrvlpNQDLSTLWVLAIGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DV 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 161 GEVENSITSSLDMLIKSPIMIILYFITLIATSWKLTLFTVLVLPAMGWLMGKVGRKLKRQSLEAQGKWSDTMSQLEETLG 240
Cdd:COG2274 263 ESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLR 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 241 GLRIIKAFIAEDRMIDRFTRCSNELRDAVNKVAMRQALAHPMSEFLGTILIVSVLWFGGALILghNSSLTAPTFI-FYMV 319
Cdd:COG2274 343 GIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVI--DGQLTLGQLIaFNIL 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 320 ILYsVINPLKDFAKAGYNIPKGLASMERVDKILKAENNIKEIPNPKPLTGMNDRIEFKDISFSYDG-KREVLKHVNLTVP 398
Cdd:COG2274 421 SGR-FLAPVAQLIGLLQRFQDAKIALERLDDILDLPPEREEGRSKLSLPRLKGDIELENVSFRYPGdSPPVLDNISLTIK 499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 399 KGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRSLIGNVNQEAILFNDTFFNNIAFGVENATME 478
Cdd:COG2274 500 PGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDE 579
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 479 QVIEAAKIANAHDFIMEKPEGYNTNIGDRGGKLSGGQRQRVSIARAILKNPPILILDEATSALDTESERLVQEALERLMK 558
Cdd:COG2274 580 EIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK 659
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 499421346 559 TRTTIAIAHRLSTIKNADEICVLYEGEIVERGRHEELLELDGYYKRLNDMQA 610
Cdd:COG2274 660 GRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQL 711
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
374-605 |
1.03e-143 |
|
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: 415.86 E-value: 1.03e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYDGK-REVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRSLIGN 452
Cdd:cd03251 1 VEFKNVTFRYPGDgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 453 VNQEAILFNDTFFNNIAFGVENATMEQVIEAAKIANAHDFIMEKPEGYNTNIGDRGGKLSGGQRQRVSIARAILKNPPIL 532
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499421346 533 ILDEATSALDTESERLVQEALERLMKTRTTIAIAHRLSTIKNADEICVLYEGEIVERGRHEELLELDGYYKRL 605
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
5-609 |
3.30e-133 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 402.09 E-value: 3.30e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 5 LQLMRR---FVSPYKKYIGWAILLNILSAVFNVFSFTLLIPILDILFKTGENNkvyeymewgtagfkdvainnfyyyvsq 81
Cdd:PRK11176 10 WQTFRRlwpTIAPFKAGLIVAGVALILNAASDTFMLSLLKPLLDDGFGKADRS--------------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 82 miqdngpttALIFLGLFLALMTLFKTSCYFASSAVMIPLRTGVVRDIRIMVYAKVMRLPMGFFSEERKGDIIARMSGDVG 161
Cdd:PRK11176 63 ---------VLKWMPLVVIGLMILRGITSFISSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 162 EVENSITSSLDMLIKSPIMIILYFITLIATSWKLTLFTVLVLPAMGWLMGKVGRKLKRQSLEAQgkwsDTMSQL----EE 237
Cdd:PRK11176 134 QVASSSSGALITVVREGASIIGLFIMMFYYSWQLSLILIVIAPIVSIAIRVVSKRFRNISKNMQ----NTMGQVttsaEQ 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 238 TLGGLRIIKAFIAEDRMIDRFTRCSNELRDAVNKVAMRQALAHPMSEFLGTILIVSVLWFggALILGHNSSLTAPTFify 317
Cdd:PRK11176 210 MLKGHKEVLIFGGQEVETKRFDKVSNRMRQQGMKMVSASSISDPIIQLIASLALAFVLYA--ASFPSVMDTLTAGTI--- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 318 MVILYSVI---NPLKDFAKAGYNIPKGLASMERVDKILKAE----NNIKEIPNPKpltgmnDRIEFKDISFSYDGKRE-V 389
Cdd:PRK11176 285 TVVFSSMIalmRPLKSLTNVNAQFQRGMAACQTLFAILDLEqekdEGKRVIERAK------GDIEFRNVTFTYPGKEVpA 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 390 LKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRSLIGNVNQEAILFNDTFFNNIA 469
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIA 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 470 FGVENA-TMEQVIEAAKIANAHDFIMEKPEGYNTNIGDRGGKLSGGQRQRVSIARAILKNPPILILDEATSALDTESERL 548
Cdd:PRK11176 439 YARTEQySREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERA 518
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499421346 549 VQEALERLMKTRTTIAIAHRLSTIKNADEICVLYEGEIVERGRHEELLELDGYYKRLNDMQ 609
Cdd:PRK11176 519 IQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQLHKMQ 579
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
179-610 |
7.43e-129 |
|
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: 391.49 E-value: 7.43e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 179 IMIILYFI-TLIATSWKLTLFtvlvlpamgwlmgkvgRKLKRQSLEAQGKWSDtmSQLE-ETlgglriIKAFIAEDRMID 256
Cdd:COG5265 187 VTVVLYIAfTVVVTEWRTKFR----------------REMNEADSEANTRAVD--SLLNyET------VKYFGNEAREAR 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 257 RFTRCSNELRDAvnKVAMRQALAhpmseFLG-------TILIVSVLWFGGALILGHnsSLTAPTFIF---YMVILYSVIN 326
Cdd:COG5265 243 RYDEALARYERA--AVKSQTSLA-----LLNfgqaliiALGLTAMMLMAAQGVVAG--TMTVGDFVLvnaYLIQLYIPLN 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 327 PLkdfakaGY---NIPKGLASMERVDKILKAENNIKEIPNPKPLTGMNDRIEFKDISFSYDGKREVLKHVNLTVPKGKTV 403
Cdd:COG5265 314 FL------GFvyrEIRQALADMERMFDLLDQPPEVADAPDAPPLVVGGGEVRFENVSFGYDPERPILKGVSFEVPAGKTV 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 404 ALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRSLIGNVNQEAILFNDTFFNNIAFGVENATMEQVIEA 483
Cdd:COG5265 388 AIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAA 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 484 AKIANAHDFIMEKPEGYNTNIGDRGGKLSGGQRQRVSIARAILKNPPILILDEATSALDTESERLVQEALERLMKTRTTI 563
Cdd:COG5265 468 ARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTL 547
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 499421346 564 AIAHRLSTIKNADEICVLYEGEIVERGRHEELLELDGYYKRLNDMQA 610
Cdd:COG5265 548 VIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQQ 594
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
374-609 |
2.00e-125 |
|
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: 369.18 E-value: 2.00e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYDGKRE--VLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRSLIG 451
Cdd:cd03249 1 IEFKNVSFRYPSRPDvpILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 452 NVNQEAILFNDTFFNNIAFGVENATMEQVIEAAKIANAHDFIMEKPEGYNTNIGDRGGKLSGGQRQRVSIARAILKNPPI 531
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499421346 532 LILDEATSALDTESERLVQEALERLMKTRTTIAIAHRLSTIKNADEICVLYEGEIVERGRHEELLELDGYYKRLNDMQ 609
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
374-609 |
2.92e-120 |
|
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: 355.77 E-value: 2.92e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYDGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRSLIGNV 453
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 454 NQEAILFNDTFFNNIAFGVENATMEQVIEAAKIANAHDFIMEKPEGYNTNIGDRGGKLSGGQRQRVSIARAILKNPPILI 533
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499421346 534 LDEATSALDTESERLVQEALERLMKTRTTIAIAHRLSTIKNADEICVLYEGEIVERGRHEELLELDGYYKRLNDMQ 609
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1-600 |
1.66e-119 |
|
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: 366.01 E-value: 1.66e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 1 MKEFLQLMRRFVSPYKKYIGWAILLNILSAVFNVFSFTLLIPILDILFktgennkvyeymewgtagfkdvainnfyyyvs 80
Cdd:COG4988 1 QKPLDKRLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLI-------------------------------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 81 qmIQDNGPTTALIFLGLFLALMtLFKTSCYFASSAVMIPLRTGVVRDIRIMVYAKVMRLPMGFFSEERKGDIIARMSGDV 160
Cdd:COG4988 49 --IGGAPLSALLPLLGLLLAVL-LLRALLAWLRERAAFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGV 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 161 GEVENSITSSLDMLIKSPIMIILYFITLIATSWK---LTLFTVLVLPAMGWLMGKVGRKLKRQSLEAQGKWSDtmsQLEE 237
Cdd:COG4988 126 EALDGYFARYLPQLFLAALVPLLILVAVFPLDWLsglILLVTAPLIPLFMILVGKGAAKASRRQWRALARLSG---HFLD 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 238 TLGGLRIIKAFIAEDRMIDRFTRCSNELRDAVNKVAMRQALAHPMSEFLGTILIVSVLWFGGALILGHNSSLTAPTFI-- 315
Cdd:COG4988 203 RLRGLTTLKLFGRAKAEAERIAEASEDFRKRTMKVLRVAFLSSAVLEFFASLSIALVAVYIGFRLLGGSLTLFAALFVll 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 316 ----FYMvilysvinPLKDFAK---AGYNipkGLASMERVDKILKAENNIKEIPNPKPLTGMNDRIEFKDISFSYDGKRE 388
Cdd:COG4988 283 lapeFFL--------PLRDLGSfyhARAN---GIAAAEKIFALLDAPEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGRP 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 389 VLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRSLIGNVNQEAILFNDTFFNNI 468
Cdd:COG4988 352 ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENL 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 469 AFGVENATMEQVIEAAKIANAHDFIMEKPEGYNTNIGDRGGKLSGGQRQRVSIARAILKNPPILILDEATSALDTESERL 548
Cdd:COG4988 432 RLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAE 511
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 499421346 549 VQEALERLMKTRTTIAIAHRLSTIKNADEICVLYEGEIVERGRHEELLELDG 600
Cdd:COG4988 512 ILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
93-605 |
7.98e-118 |
|
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: 361.78 E-value: 7.98e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 93 IFLGLFLALMT------LFKTSCYFASSA--------VMIP---------LRT---------------GVVRDIRIMVYA 134
Cdd:COG4987 17 LLLGVLLGLLTllagigLLALSGWLIAAAalappilnLFVPivgvrafaiGRTvfrylerlvshdatlRLLADLRVRLYR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 135 KVMRLPMGFFSEERKGDIIARMSGDVGEVENSItssLDMLIKSPIMIILYFITLIATSWKLTLFTVLVLPAMG------- 207
Cdd:COG4987 97 RLEPLAPAGLARLRSGDLLNRLVADVDALDNLY---LRVLLPLLVALLVILAAVAFLAFFSPALALVLALGLLlaglllp 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 208 WLMGKVGRKLKRQSLEAQGKWSdtmSQLEETLGGLRIIKAFIAEDRMIDRFTRCSNELRDAVNKVAMRQALAHPMSEFLG 287
Cdd:COG4987 174 LLAARLGRRAGRRLAAARAALR---ARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLSALAQALLQLAA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 288 TILIVSVLWFGGALILGHnsSLTAPTF-IFYMVILYS--VINPLkdfAKAGYNIPKGLASMERVDKILKAENNIKEIPNP 364
Cdd:COG4987 251 GLAVVAVLWLAAPLVAAG--ALSGPLLaLLVLAALALfeALAPL---PAAAQHLGRVRAAARRLNELLDAPPAVTEPAEP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 365 KPLTGMNDrIEFKDISFSYDG-KREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRI 443
Cdd:COG4987 326 APAPGGPS-LELEDVSFRYPGaGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDE 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 444 ADLRSLIGNVNQEAILFNDTFFNNIAFGVENATMEQVIEAAKIANAHDFIMEKPEGYNTNIGDRGGKLSGGQRQRVSIAR 523
Cdd:COG4987 405 DDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALAR 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 524 AILKNPPILILDEATSALDTESERLVQEALERLMKTRTTIAIAHRLSTIKNADEICVLYEGEIVERGRHEELLELDGYYK 603
Cdd:COG4987 485 ALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYR 564
|
..
gi 499421346 604 RL 605
Cdd:COG4987 565 QL 566
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
373-600 |
2.22e-110 |
|
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: 330.34 E-value: 2.22e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 373 RIEFKDISFSYDGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRSLIGN 452
Cdd:cd03254 2 EIEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 453 VNQEAILFNDTFFNNIAFGVENATMEQVIEAAKIANAHDFIMEKPEGYNTNIGDRGGKLSGGQRQRVSIARAILKNPPIL 532
Cdd:cd03254 82 VLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKIL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499421346 533 ILDEATSALDTESERLVQEALERLMKTRTTIAIAHRLSTIKNADEICVLYEGEIVERGRHEELLELDG 600
Cdd:cd03254 162 ILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
103-605 |
4.93e-110 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 345.94 E-value: 4.93e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 103 TLFKTSCYFASSAVMIPLRTG--------VVRDIRIMVYAKVMRLPMGFFSEERKGDIIARMSGDVGEVENSITSSLDML 174
Cdd:TIGR00958 203 AIFFMCLLSIASSVSAGLRGGsfnytmarINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVL 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 175 IKSPIMIILYFITLIATSWKLTLFTVLVLPAMGWL---MGKVGRKLKRQSLEAQGKWSDTMsqlEETLGGLRIIKAFIAE 251
Cdd:TIGR00958 283 LRNLVMLLGLLGFMLWLSPRLTMVTLINLPLVFLAekvFGKRYQLLSEELQEAVAKANQVA---EEALSGMRTVRSFAAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 252 DRMIDRFTRCSNELRDAVNKVAMRQALAHPMSEFLGTILIVSVLWFGGALIL-GHNSSLTAPTFIFYMVILYSVINPLKD 330
Cdd:TIGR00958 360 EGEASRFKEALEETLQLNKRKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLtGKVSSGNLVSFLLYQEQLGEAVRVLSY 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 331 FakagYN-IPKGLASMERVDKILKAENNIkeiPNPKPLT--GMNDRIEFKDISFSYDGK--REVLKHVNLTVPKGKTVAL 405
Cdd:TIGR00958 440 V----YSgMMQAVGASEKVFEYLDRKPNI---PLTGTLAplNLEGLIEFQDVSFSYPNRpdVPVLKGLTFTLHPGEVVAL 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 406 VGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRSLIGNVNQEAILFNDTFFNNIAFGVENATMEQVIEAAK 485
Cdd:TIGR00958 513 VGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAK 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 486 IANAHDFIMEKPEGYNTNIGDRGGKLSGGQRQRVSIARAILKNPPILILDEATSALDTESERLVQEALERlmKTRTTIAI 565
Cdd:TIGR00958 593 AANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSR--ASRTVLLI 670
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 499421346 566 AHRLSTIKNADEICVLYEGEIVERGRHEELLELDGYYKRL 605
Cdd:TIGR00958 671 AHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
182-605 |
3.41e-107 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 335.01 E-value: 3.41e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 182 ILYFITLIATS----WKLTLFTVlVLPAMGWLMGK-VGRKLKRQSLEAQGKWSDTMSQLEETLGGLRIIKAFI---AEDR 253
Cdd:PRK13657 141 LVALVVLLPLAlfmnWRLSLVLV-VLGIVYTLITTlVMRKTKDGQAAVEEHYHDLFAHVSDAIGNVSVVQSYNrieAETQ 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 254 MIDRFTrcsNELRDAVNKVAMRQALAHPMSEFLGTILIVSVLWFGGALIL-GHNSSLTAPTFIFYMVILYSVINPLKDFA 332
Cdd:PRK13657 220 ALRDIA---DNLLAAQMPVLSWWALASVLNRAASTITMLAILVLGAALVQkGQLRVGEVVAFVGFATLLIGRLDQVVAFI 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 333 KagyNIPKGLASMERVDKILKAENNIKEIPNPKPLTGMNDRIEFKDISFSYDGKREVLKHVNLTVPKGKTVALVGQSGSG 412
Cdd:PRK13657 297 N---QVFMAAPKLEEFFEVEDAVPDVRDPPGAIDLGRVKGAVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAG 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 413 KSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRSLIGNVNQEAILFNDTFFNNIAFGVENATMEQVIEAAKIANAHDF 492
Cdd:PRK13657 374 KSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDF 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 493 IMEKPEGYNTNIGDRGGKLSGGQRQRVSIARAILKNPPILILDEATSALDTESERLVQEALERLMKTRTTIAIAHRLSTI 572
Cdd:PRK13657 454 IERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTV 533
|
410 420 430
....*....|....*....|....*....|...
gi 499421346 573 KNADEICVLYEGEIVERGRHEELLELDGYYKRL 605
Cdd:PRK13657 534 RNADRILVFDNGRVVESGSFDELVARGGRFAAL 566
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
132-609 |
2.52e-93 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 301.66 E-value: 2.52e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 132 VYAKVMRLPMGFFSEERKGDIIARMSgDVGEVENSITSSLDMLIKSPIMIILYFITLIATSWKLTLFTVLVLPAMGWLMG 211
Cdd:TIGR01846 218 LYRHLLGLPLGYFESRRVGDTVARVR-ELEQIRNFLTGSALTVVLDLLFVVVFLAVMFFYSPTLTGVVIGSLVCYALLSV 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 212 KVGRKLKRQSLEAQGKWSDTMSQLEETLGGLRIIKAFIAEDRMIDRFTRCSNELRDAVNKVAMRQALAHPMSEFLGTILI 291
Cdd:TIGR01846 297 FVGPILRKRVEDKFERSAAATSFLVESVTGIETIKATATEPQFQNRWDRQLAAYVAASFRVTNLGNIAGQAIELIQKLTF 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 292 VSVLWFGGALILGhnSSLTAPTFIFYMVILYSVINPLKDFAKAGYNIPKGLASMERVDKILkaeNNIKEiPNPKPLTG-- 369
Cdd:TIGR01846 377 AILLWFGAHLVIG--GALSPGQLVAFNMLAGRVTQPVLRLAQLWQDFQQTGIALERLGDIL---NSPTE-PRSAGLAAlp 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 370 -MNDRIEFKDISFSYDGKR-EVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTsikDVRIAD-- 445
Cdd:TIGR01846 451 eLRGAITFENIRFRYAPDSpEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGV---DLAIADpa 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 446 -LRSLIGNVNQEAILFNDTFFNNIAFGVENATMEQVIEAAKIANAHDFIMEKPEGYNTNIGDRGGKLSGGQRQRVSIARA 524
Cdd:TIGR01846 528 wLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARA 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 525 ILKNPPILILDEATSALDTESERLVQEALERLMKTRTTIAIAHRLSTIKNADEICVLYEGEIVERGRHEELLELDGYYKR 604
Cdd:TIGR01846 608 LVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYAR 687
|
....*
gi 499421346 605 LNDMQ 609
Cdd:TIGR01846 688 LWQQQ 692
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
374-609 |
4.69e-89 |
|
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: 275.90 E-value: 4.69e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYDG-KREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRSLIGN 452
Cdd:cd03252 1 ITFEHVRFRYKPdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 453 VNQEAILFNDTFFNNIAFGVENATMEQVIEAAKIANAHDFIMEKPEGYNTNIGDRGGKLSGGQRQRVSIARAILKNPPIL 532
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499421346 533 ILDEATSALDTESERLVQEALERLMKTRTTIAIAHRLSTIKNADEICVLYEGEIVERGRHEELLELDGYYKRLNDMQ 609
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
19-348 |
3.20e-88 |
|
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: 275.46 E-value: 3.20e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 19 IGWAILLNILSAVFNVFSFTLLIPILDILFktgennkvyeymewgtagfkdvainnfyyyvsqmiqDNGPTTALIFLGLF 98
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIF------------------------------------VEKDLEALLLVPLA 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 99 LALMTLFKTSCYFASSAVMIPLRTGVVRDIRIMVYAKVMRLPMGFFSEERKGDIIARMSGDVGEVENSITSSLDMLIKSP 178
Cdd:cd18552 45 IIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDP 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 179 IMIILYFITLIATSWKLTLFTVLVLPAMGWLMGKVGRKLKRQSLEAQGKWSDTMSQLEETLGGLRIIKAFIAEDRMIDRF 258
Cdd:cd18552 125 LTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRF 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 259 TRCSNELRDAVNKVAMRQALAHPMSEFLGTILIVSVLWFGGALILghNSSLTAPTFIFYMVILYSVINPLKDFAKAGYNI 338
Cdd:cd18552 205 RKANERLRRLSMKIARARALSSPLMELLGAIAIALVLWYGGYQVI--SGELTPGEFISFITALLLLYQPIKRLSNVNANL 282
|
330
....*....|
gi 499421346 339 PKGLASMERV 348
Cdd:cd18552 283 QRGLAAAERI 292
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
133-611 |
3.19e-85 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 276.98 E-value: 3.19e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 133 YAKVMRLPMGFFSEERKGDIIARMSGDVGEVENSITSSLDMLIKSPIMIILYFITL-IATSWKLTLFTVLVLPAMGWLMG 211
Cdd:PRK10789 76 YRQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIVMsTQISWQLTLLALLPMPVMAIMIK 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 212 KVGRKLKRQSLEAQGKWSDTMSQLEETLGGLRIIKAFIAEDRMIDRFTRCSNELRDAVNKVAMRQALAHPmseflgTILI 291
Cdd:PRK10789 156 RYGDQLHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDP------TIYI 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 292 V----SVLWFGGALILGHNSSLTAPTFIFYMVILYSVINPLKDFAKAgYNI-PKGLASMERVDKILKAENNIKEIPNPKP 366
Cdd:PRK10789 230 AigmaNLLAIGGGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWM-FNIvERGSAAYSRIRAMLAEAPVVKDGSEPVP 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 367 LTGMNDRIEFKdiSFSYDG-KREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIAD 445
Cdd:PRK10789 309 EGRGELDVNIR--QFTYPQtDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDS 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 446 LRSLIGNVNQEAILFNDTFFNNIAFGVENATMEQVIEAAKIANAHDFIMEKPEGYNTNIGDRGGKLSGGQRQRVSIARAI 525
Cdd:PRK10789 387 WRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARAL 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 526 LKNPPILILDEATSALDTESERLVQEALERLMKTRTTIAIAHRLSTIKNADEICVLYEGEIVERGRHEELLELDGYYKRL 605
Cdd:PRK10789 467 LLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDM 546
|
....*.
gi 499421346 606 NDMQAL 611
Cdd:PRK10789 547 YRYQQL 552
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
136-605 |
1.70e-83 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 276.05 E-value: 1.70e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 136 VMRLPMGFFSEERKGDIIARMSGD--VGEV--ENSITSSLDMlikspIMIILYFITLIATSWKLTLFTVLVLPAMGWLMG 211
Cdd:TIGR03796 237 ILRLPVRFFAQRHAGDIASRVQLNdqVAEFlsGQLATTALDA-----VMLVFYALLMLLYDPVLTLIGIAFAAINVLALQ 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 212 KVGRKLKRQSLEAQ---GKWSDTmsqleeTLGGLRII---KAFIAEDrmiDRFTRCSNELRDAVNkvaMRQALAHP---- 281
Cdd:TIGR03796 312 LVSRRRVDANRRLQqdaGKLTGV------AISGLQSIetlKASGLES---DFFSRWAGYQAKLLN---AQQELGVLtqil 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 282 --MSEFLGTILIVSVLWFGGALILghNSSLTAPTFIFYMVILYSVINPLKDFAKAGYNIPKGLASMERVDKILK------ 353
Cdd:TIGR03796 380 gvLPTLLTSLNSALILVVGGLRVM--EGQLTIGMLVAFQSLMSSFLEPVNNLVGFGGTLQELEGDLNRLDDVLRnpvdpl 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 354 AENNIKEIPNPKPLTGMNDRIEFKDISFSYDG-KREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDIT 432
Cdd:TIGR03796 458 LEEPEGSAATSEPPRRLSGYVELRNITFGYSPlEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEIL 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 433 IDGTSIKDVRIADLRSLIGNVNQEAILFNDTFFNNIAfgVENATM--EQVIEAAKIANAHDFIMEKPEGYNTNIGDRGGK 510
Cdd:TIGR03796 538 FDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLT--LWDPTIpdADLVRACKDAAIHDVITSRPGGYDAELAEGGAN 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 511 LSGGQRQRVSIARAILKNPPILILDEATSALDTESERLVQEALERlmktR--TTIAIAHRLSTIKNADEICVLYEGEIVE 588
Cdd:TIGR03796 616 LSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLRR----RgcTCIIVAHRLSTIRDCDEIIVLERGKVVQ 691
|
490
....*....|....*..
gi 499421346 589 RGRHEELLELDGYYKRL 605
Cdd:TIGR03796 692 RGTHEELWAVGGAYARL 708
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
374-585 |
1.05e-81 |
|
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: 254.23 E-value: 1.05e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYDGK-REVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRSLIGN 452
Cdd:cd03228 1 IEFKNVSFSYPGRpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 453 VNQEAILFNDTFFNNIafgvenatmeqvieaakianahdfimekpegyntnigdrggkLSGGQRQRVSIARAILKNPPIL 532
Cdd:cd03228 81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499421346 533 ILDEATSALDTESERLVQEALERLMKTRTTIAIAHRLSTIKNADEICVLYEGE 585
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
179-605 |
1.37e-80 |
|
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: 265.21 E-value: 1.37e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 179 IMIILYFITLIATSWKLTlFTVLVLPAMGWLMGK-VGRKLKRQSLEAQGKWSDTMSQLEETLGGLRIIKAF---IAEDRM 254
Cdd:TIGR01192 142 VALFLLIPTAFAMDWRLS-IVLMVLGILYILIAKlVMQRTKNGQAAVEHHYHNVFKHVSDSISNVSVVHSYnriEAETSA 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 255 IDRFTrcsNELRDAVNKVAMRQALAHPMSEFLGTILIVSVLWFGGALIL-GHNSSLTAPTFIFYMVILYSVINPLKDFak 333
Cdd:TIGR01192 221 LKQFT---NNLLSAQYPVLDWWALASGLNRMASTISMMCILVIGTVLVIkGELSVGEVIAFIGFANLLIGRLDQMSGF-- 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 334 agynIPKGLASMERVDKILKAENNIKEIPNP---KPLTGMNDRIEFKDISFSYDGKREVLKHVNLTVPKGKTVALVGQSG 410
Cdd:TIGR01192 296 ----ITQIFEARAKLEDFFDLEDSVFQREEPadaPELPNVKGAVEFRHITFEFANSSQGVFDVSFEAKAGQTVAIVGPTG 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 411 SGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRSLIGNVNQEAILFNDTFFNNIAFGVENATMEQVIEAAKIANAH 490
Cdd:TIGR01192 372 AGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAH 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 491 DFIMEKPEGYNTNIGDRGGKLSGGQRQRVSIARAILKNPPILILDEATSALDTESERLVQEALERLMKTRTTIAIAHRLS 570
Cdd:TIGR01192 452 DFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLS 531
|
410 420 430
....*....|....*....|....*....|....*
gi 499421346 571 TIKNADEICVLYEGEIVERGRHEELLELDGYYKRL 605
Cdd:TIGR01192 532 TVRNADLVLFLDQGRLIEKGSFQELIQKDGRFYKL 566
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
77-605 |
2.86e-77 |
|
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: 259.29 E-value: 2.86e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 77 YYVSQMI-----QDNGPTTALIFLGLFLALmtLFKTSCYFASSAVMIPLRTGVVRDIrIMVYAK-VMRLPMGFFSEERKG 150
Cdd:TIGR01193 177 YYLQKIIdtyipHKMMGTLGIISIGLIIAY--IIQQILSYIQIFLLNVLGQRLSIDI-ILSYIKhLFELPMSFFSTRRTG 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 151 DIIARMSgDVGEVENSITSSLDMLIKSPIMIILYFITLIATSWKLTLFTVLVLPAMG---WLMGKVGRKLKRQSLEAQGK 227
Cdd:TIGR01193 254 EIVSRFT-DASSIIDALASTILSLFLDMWILVIVGLFLVRQNMLLFLLSLLSIPVYAviiILFKRTFNKLNHDAMQANAV 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 228 WSdtmSQLEETLGGLRIIKAFIAEDrmiDRFTRCSNELRDAVNK---VAMRQALAHPMSEFLGTILIVSVLWFGGALILG 304
Cdd:TIGR01193 333 LN---SSIIEDLNGIETIKSLTSEA---ERYSKIDSEFGDYLNKsfkYQKADQGQQAIKAVTKLILNVVILWTGAYLVMR 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 305 HNssLTAPTFIFYMVILYSVINPLKDFAKAGYNIPKGLASMERVDKILKAENNIKEIPNPKPLTGMNDRIEFKDISFSYD 384
Cdd:TIGR01193 407 GK--LTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEVYLVDSEFINKKKRTELNNLNGDIVINDVSYSYG 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 385 GKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRSLIGNVNQEAILFNDTF 464
Cdd:TIGR01193 485 YGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSI 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 465 FNNIAFGV-ENATMEQVIEAAKIANAHDFIMEKPEGYNTNIGDRGGKLSGGQRQRVSIARAILKNPPILILDEATSALDT 543
Cdd:TIGR01193 565 LENLLLGAkENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDT 644
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499421346 544 ESERLVQEALERlMKTRTTIAIAHRLSTIKNADEICVLYEGEIVERGRHEELLELDGYYKRL 605
Cdd:TIGR01193 645 ITEKKIVNNLLN-LQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASL 705
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
364-586 |
1.40e-75 |
|
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: 240.45 E-value: 1.40e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 364 PKPLTGmndRIEFKDISFSYDGK--REVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDV 441
Cdd:cd03248 5 PDHLKG---IVKFQNVTFAYPTRpdTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 442 RIADLRSLIGNVNQEAILFNDTFFNNIAFGVENATMEQVIEAAKIANAHDFIMEKPEGYNTNIGDRGGKLSGGQRQRVSI 521
Cdd:cd03248 82 EHKYLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499421346 522 ARAILKNPPILILDEATSALDTESERLVQEALERLMKTRTTIAIAHRLSTIKNADEICVLYEGEI 586
Cdd:cd03248 162 ARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
92-605 |
2.26e-74 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 251.03 E-value: 2.26e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 92 LIFLGLFLALMTLFKTSCYFASSAVMIPLRTGVVRDIRIMVYAKVMRLPMGFFSEERKGDIIARMSGdVGEVENSITSSL 171
Cdd:TIGR03797 175 LVQIALALLAAAVGAAAFQLAQSLAVLRLETRMDASLQAAVWDRLLRLPVSFFRQYSTGDLASRAMG-ISQIRRILSGST 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 172 DMLIKSPIMIILYFITLIATSWKLTLFTVLVLPAMGWLMGKVG---RKLKRQSLEAQGKWSDTMSQLEETLGGLRIIKAf 248
Cdd:TIGR03797 254 LTTLLSGIFALLNLGLMFYYSWKLALVAVALALVAIAVTLVLGllqVRKERRLLELSGKISGLTVQLINGISKLRVAGA- 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 249 iaEDRMIDRFTRCSNELRDAVNKVAMRQALAHPMSEFLGTILIVSVLWFGGALILGhnSSLTAPTFIFYMVILYSVINPL 328
Cdd:TIGR03797 333 --ENRAFARWAKLFSRQRKLELSAQRIENLLTVFNAVLPVLTSAALFAAAISLLGG--AGLSLGSFLAFNTAFGSFSGAV 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 329 KDFAKAGYNIPKGLASMERVDKILKAENNIKEI-PNPKPLTGmndRIEFKDISFSY--DGKReVLKHVNLTVPKGKTVAL 405
Cdd:TIGR03797 409 TQLSNTLISILAVIPLWERAKPILEALPEVDEAkTDPGKLSG---AIEVDRVTFRYrpDGPL-ILDDVSLQIEPGEFVAI 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 406 VGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRSLIGNVNQEAILFNDTFFNNIAfGVENATMEQVIEAAK 485
Cdd:TIGR03797 485 VGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIA-GGAPLTLDEAWEAAR 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 486 IANAHDFIMEKPEGYNTNIGDRGGKLSGGQRQRVSIARAILKNPPILILDEATSALDTESERLVQEALERLMKTRttIAI 565
Cdd:TIGR03797 564 MAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLKVTR--IVI 641
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 499421346 566 AHRLSTIKNADEICVLYEGEIVERGRHEELLELDGYYKRL 605
Cdd:TIGR03797 642 AHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQL 681
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
77-581 |
6.21e-72 |
|
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: 240.65 E-value: 6.21e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 77 YYVSQMIQDNGPTTALIFLGLFLALMTLFKTSCYFASSAVMIPLRTGVVRDIRIMVYAKVMRLPMGFFSEERKGDIIARM 156
Cdd:TIGR02857 28 RVVDGLISAGEPLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLRERLLEAVAALGPRWLQGRPSGELATLA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 157 SGDVGEVENSITSSLDMLIKSpIMIILYFITLIAT-SWKLTLFTVLVLPAMGWLMGKVGRKLKRqslEAQGKWSdTMSQL 235
Cdd:TIGR02857 108 LEGVEALDGYFARYLPQLVLA-VIVPLAILAAVFPqDWISGLILLLTAPLIPIFMILIGWAAQA---AARKQWA-ALSRL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 236 E----ETLGGLRIIKAFIAEDRMIDRFTRCSNELRDA---VNKVAMRQALAhpmSEFLGTILI--VSVlWFGGALILGHn 306
Cdd:TIGR02857 183 SghflDRLRGLPTLKLFGRAKAQAAAIRRSSEEYRERtmrVLRIAFLSSAV---LELFATLSValVAV-YIGFRLLAGD- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 307 ssLTAPTFIFYMVILYSVINPLKDFAKAGYNIPKGLASMERVDKILKAENNIKeiPNPKPLTGMNDR-IEFKDISFSYDG 385
Cdd:TIGR02857 258 --LDLATGLFVLLLAPEFYLPLRQLGAQYHARADGVAAAEALFAVLDAAPRPL--AGKAPVTAAPASsLEFSGVSVAYPG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 386 KREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRSLIGNVNQEAILFNDTFF 465
Cdd:TIGR02857 334 RRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIA 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 466 NNIAFGVENATMEQVIEAAKIANAHDFIMEKPEGYNTNIGDRGGKLSGGQRQRVSIARAILKNPPILILDEATSALDTES 545
Cdd:TIGR02857 414 ENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAET 493
|
490 500 510
....*....|....*....|....*....|....*.
gi 499421346 546 ERLVQEALERLMKTRTTIAIAHRLSTIKNADEICVL 581
Cdd:TIGR02857 494 EAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
92-605 |
1.57e-71 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 240.88 E-value: 1.57e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 92 LIFLGLFLALMTLFKT------SCYF-ASSAV-----------MIP---------LRTG---------------VVRDIR 129
Cdd:PRK11160 17 MLSLGILLAIVTLLASiglltlSGWFlSASAVaglaglysfnyMLPaagvrgaaiGRTAgrygerlvshdatfrVLTHLR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 130 IMVYAKVMRLPMGFFSEERKGDIIARMSGDVGevensitsSLDML---IKSP-------IMIILYFITLIATSWKLTLFT 199
Cdd:PRK11160 97 VFTFSKLLPLSPAGLARYRQGDLLNRLVADVD--------TLDHLylrLISPlvaalvvILVLTIGLSFFDLTLALTLGG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 200 VL--VLPAMGWLMGKVGRKLKRQSLEAQGKWSdtmSQLEETLGGLRIIKAFIAEDRMIDRFTRCSNELRDAVNKVAMRQA 277
Cdd:PRK11160 169 ILllLLLLLPLLFYRLGKKPGQDLTHLRAQYR---VQLTEWLQGQAELTLFGAEDRYRQQLEQTEQQWLAAQRRQANLTG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 278 LAHPMSEFLGTILIVSVLWFGGALILGHNSS--LTApTFIFYMVILYSVINPLkdfAKAGYNIPKGLASMERVDKILKAE 355
Cdd:PRK11160 246 LSQALMILANGLTVVLMLWLAAGGVGGNAQPgaLIA-LFVFAALAAFEALMPV---AGAFQHLGQVIASARRINEITEQK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 356 NNIKEIPNPKPLTGmNDRIEFKDISFSY-DGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITID 434
Cdd:PRK11160 322 PEVTFPTTSTAAAD-QVSLTLNNVSFTYpDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 435 GTSIKDVRIADLRSLIGNVNQEAILFNDTFFNNIAFGVENATMEQVIEAAKIANAHDFImEKPEGYNTNIGDRGGKLSGG 514
Cdd:PRK11160 401 GQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLL-EDDKGLNAWLGEGGRQLSGG 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 515 QRQRVSIARAILKNPPILILDEATSALDTESERLVQEALERLMKTRTTIAIAHRLSTIKNADEICVLYEGEIVERGRHEE 594
Cdd:PRK11160 480 EQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQE 559
|
570
....*....|.
gi 499421346 595 LLELDGYYKRL 605
Cdd:PRK11160 560 LLAQQGRYYQL 570
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1-609 |
5.87e-69 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 234.61 E-value: 5.87e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 1 MKEFLQL---MRRFV---SPYKKYIGWAILLNILSAVFNVFSFTLLIPILDILFKTGEnnkvyeyMEWGTAGfkdvainn 74
Cdd:PRK10790 1 MRSFSQLwptLKRLLaygSPWRKPLGLAVLMLWVAAAAEVSGPLLISYFIDNMVAKGN-------LPLGLVA-------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 75 fyyyvsqmiqdnGPTTALIFLGLFLALMTLFKtSCYFASSAVmiplrtGVVRDIRIMVYAKVMRLPMGFFSEERKGDIIA 154
Cdd:PRK10790 66 ------------GLAAAYVGLQLLAAGLHYAQ-SLLFNRAAV------GVVQQLRTDVMDAALRQPLSAFDTQPVGQLIS 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 155 RMSGDVGEVENSITSSLDMLIKSPIMIILYFITLIATSWKLTLFTVLVLPAMGWLMG-------KVGRKLkRQSLeaqgk 227
Cdd:PRK10790 127 RVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAIMIFPAVLVVMViyqrystPIVRRV-RAYL----- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 228 wSDTMSQLEETLGGLRIIKAFIAEDRMIDRFTRCSNElrdavNKVAMRQALA------HPM-SEFLGTILIVSVLWFG-- 298
Cdd:PRK10790 201 -ADINDGFNEVINGMSVIQQFRQQARFGERMGEASRS-----HYMARMQTLRldgfllRPLlSLFSALILCGLLMLFGfs 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 299 --GALILGhnssltaptfifymvILYSVIN-------PLKDFAKAGYNIPKGLASMERVDKILKAennikeipnPKPLTG 369
Cdd:PRK10790 275 asGTIEVG---------------VLYAFISylgrlnePLIELTTQQSMLQQAVVAGERVFELMDG---------PRQQYG 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 370 MNDR------IEFKDISFSYDGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRI 443
Cdd:PRK10790 331 NDDRplqsgrIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSH 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 444 ADLRSLIGNVNQEAILFNDTFFNNIAFG--VENATMEQVIEAAKIAnahDFIMEKPEGYNTNIGDRGGKLSGGQRQRVSI 521
Cdd:PRK10790 411 SVLRQGVAMVQQDPVVLADTFLANVTLGrdISEEQVWQALETVQLA---ELARSLPDGLYTPLGEQGNNLSVGQKQLLAL 487
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 522 ARAILKNPPILILDEATSALDTESERLVQEALeRLMKTRTT-IAIAHRLSTIKNADEICVLYEGEIVERGRHEELLELDG 600
Cdd:PRK10790 488 ARVLVQTPQILILDEATANIDSGTEQAIQQAL-AAVREHTTlVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQG 566
|
....*....
gi 499421346 601 YYKRLNDMQ 609
Cdd:PRK10790 567 RYWQMYQLQ 575
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
127-569 |
1.13e-65 |
|
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: 224.16 E-value: 1.13e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 127 DIRIMVYAKVMRLPMGFFSEERKGDIIARMSGDVGEVENSITSSLDMLIKSPIMIILyFITLIAT-SWK--------LTL 197
Cdd:TIGR02868 87 ALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAA-AVAAIAVlSVPaalilaagLLL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 198 FTVLVLPAMGWLMGKVGRKLKRQSleaqgkwSDTMSQLEETLGGLRIIKAFIAEDRMIDRFTRCSNELRDAVNKVAMRQA 277
Cdd:TIGR02868 166 AGFVAPLVSLRAARAAEQALARLR-------GELAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAERRAAAATA 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 278 LAHPMSEFLGTILIVSVLWFGGALILGHNsslTAPTFIFYMVIL-YSVINPLKDFAKAGYNIPKGLASMERVDKILKAEN 356
Cdd:TIGR02868 239 LGAALTLLAAGLAVLGALWAGGPAVADGR---LAPVTLAVLVLLpLAAFEAFAALPAAAQQLTRVRAAAERIVEVLDAAG 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 357 NIKEIPNPKPLTGMND--RIEFKDISFSYDGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITID 434
Cdd:TIGR02868 316 PVAEGSAPAAGAVGLGkpTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLD 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 435 GTSIKDVRIADLRSLIGNVNQEAILFNDTFFNNIAFGVENATMEQVIEAAKIANAHDFIMEKPEGYNTNIGDRGGKLSGG 514
Cdd:TIGR02868 396 GVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGG 475
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 499421346 515 QRQRVSIARAILKNPPILILDEATSALDTESERLVQEALERLMKTRTTIAIAHRL 569
Cdd:TIGR02868 476 ERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
372-590 |
3.92e-65 |
|
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: 212.83 E-value: 3.92e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 372 DRIEFKDISFSYDG-KREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRSLI 450
Cdd:cd03245 1 GRIEFRNVSFSYPNqEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 451 GNVNQEAILFNDTFFNNIAFGVENATMEQVIEAAKIANAHDFIMEKPEGYNTNIGDRGGKLSGGQRQRVSIARAILKNPP 530
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 531 ILILDEATSALDTESERLVQEALERLMKTRTTIAIAHRLSTIKNADEICVLYEGEIVERG 590
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
373-590 |
6.92e-63 |
|
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: 206.96 E-value: 6.92e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 373 RIEFKDISFSY-DGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRSLIG 451
Cdd:cd03244 2 DIEFKNVSLRYrPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 452 NVNQEAILFNDTFFNNIA-FGVenATMEQVIEAAKIANAHDFIMEKPEGYNTNIGDRGGKLSGGQRQRVSIARAILKNPP 530
Cdd:cd03244 82 IIPQDPVLFSGTIRSNLDpFGE--YSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 531 ILILDEATSALDTESERLVQEALERLMKTRTTIAIAHRLSTIKNADEICVLYEGEIVERG 590
Cdd:cd03244 160 ILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFD 219
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
91-585 |
5.04e-59 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 214.12 E-value: 5.04e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 91 ALIFLGLFLALMTlfktscyFASSAVMIPLRTGVVRDIRIMvYAKVMRLPMGFFSEERKGdiiARMSGDVG----EVENS 166
Cdd:PTZ00265 102 SLVLIGIFQFILS-------FISSFCMDVVTTKILKTLKLE-FLKSVFYQDGQFHDNNPG---SKLTSDLDfyleQVNAG 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 167 I-TSSLDMLIKSPIMIILYFITLIATSwKLTLFTVLVLPAM---GWLMGKVGRKLKRQSLEAQgkwSDTMSQLEETLGGL 242
Cdd:PTZ00265 171 IgTKFITIFTYASAFLGLYIWSLFKNA-RLTLCITCVFPLIyicGVICNKKVKINKKTSLLYN---NNTMSIIEEALVGI 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 243 RIIKAFIAEDRMIDRFTRCSNELRDAVNKVAMRQALAHPMSEflGTILIVSVL--WFGGALILgHNSSLTAPTFIFYMVi 320
Cdd:PTZ00265 247 RTVVSYCGEKTILKKFNLSEKLYSKYILKANFMESLHIGMIN--GFILASYAFgfWYGTRIII-SDLSNQQPNNDFHGG- 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 321 lySVINPLKDFAKAGYNIPKGLASMERVDKILKAENNIKEIPNPKPLTGMND---------RIEFKDISFSYDGKR--EV 389
Cdd:PTZ00265 323 --SVISILLGVLISMFMLTIILPNITEYMKSLEATNSLYEIINRKPLVENNDdgkklkdikKIQFKNVRFHYDTRKdvEI 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 390 LKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITI-DGTSIKDVRIADLRSLIGNVNQEAILFNDTFFNNI 468
Cdd:PTZ00265 401 YKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNI 480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 469 AFGV----------------ENATME-----------------------------------QVIEAAKIANA------HD 491
Cdd:PTZ00265 481 KYSLyslkdlealsnyynedGNDSQEnknkrnscrakcagdlndmsnttdsneliemrknyQTIKDSEVVDVskkvliHD 560
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 492 FIMEKPEGYNTNIGDRGGKLSGGQRQRVSIARAILKNPPILILDEATSALDTESERLVQEALERLM--KTRTTIAIAHRL 569
Cdd:PTZ00265 561 FVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRL 640
|
570
....*....|....*.
gi 499421346 570 STIKNADEICVLYEGE 585
Cdd:PTZ00265 641 STIRYANTIFVLSNRE 656
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
195-597 |
8.11e-58 |
|
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: 203.44 E-value: 8.11e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 195 LTLFTVLVLPAMGWLMGKVGRKLKRQSLEAQGKwsdTMSQLEETLGGLRIIKAFIAEDRMIDRFTRCSNELRDAVNKVAM 274
Cdd:COG4618 160 LALVGALVLVALALLNERLTRKPLKEANEAAIR---ANAFAEAALRNAEVIEAMGMLPALRRRWQRANARALALQARASD 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 275 RQALAHPMSEFLGTILIVSVLWFGGALILghNSSLTAPTFIFYMVILYSVINPL-------KDFAKAgynipkgLASMER 347
Cdd:COG4618 237 RAGGFSALSKFLRLLLQSAVLGLGAYLVI--QGEITPGAMIAASILMGRALAPIeqaiggwKQFVSA-------RQAYRR 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 348 VDKILKA-ENNIKEIPNPKPlTGmndRIEFKDISFSYDG-KREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLL----P 421
Cdd:COG4618 308 LNELLAAvPAEPERMPLPRP-KG---RLSVENLTVVPPGsKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLvgvwP 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 422 ryhdVQGGDITIDGTSIKDVRIADLRSLIGNVNQEAILFNDTFFNNIA-FGveNATMEQVIEAAKIANAHDFIMEKPEGY 500
Cdd:COG4618 384 ----PTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIArFG--DADPEKVVAAAKLAGVHEMILRLPDGY 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 501 NTNIGDRGGKLSGGQRQRVSIARAILKNPPILILDEATSALDTESERLVQEALERLmKTR--TTIAIAHRLSTIKNADEI 578
Cdd:COG4618 458 DTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAL-KARgaTVVVITHRPSLLAAVDKL 536
|
410
....*....|....*....
gi 499421346 579 CVLYEGEIVERGRHEELLE 597
Cdd:COG4618 537 LVLRDGRVQAFGPRDEVLA 555
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
297-605 |
1.24e-57 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 203.54 E-value: 1.24e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 297 FGGALILghnssLTAPTFifYMvilysvinPLKDF-----AKAgynipKGLASMERVDKILKAE-----NNIKEIPNPKP 366
Cdd:PRK11174 288 FAGFFVL-----ILAPEF--YQ--------PLRDLgtfyhAKA-----QAVGAAESLVTFLETPlahpqQGEKELASNDP 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 367 LTgmndrIEFKDIS-FSYDGKReVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGgDITIDGTSIKDVRIAD 445
Cdd:PRK11174 348 VT-----IEAEDLEiLSPDGKT-LAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQG-SLKINGIELRELDPES 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 446 LRSLIGNVNQEAILFNDTFFNNIAFGVENATMEQVIEAAKIANAHDFIMEKPEGYNTNIGDRGGKLSGGQRQRVSIARAI 525
Cdd:PRK11174 421 WRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARAL 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 526 LKNPPILILDEATSALDTESERLVQEALERLMKTRTTIAIAHRLSTIKNADEICVLYEGEIVERGRHEELLELDGYYKRL 605
Cdd:PRK11174 501 LQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
86-348 |
2.48e-57 |
|
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: 194.69 E-value: 2.48e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 86 NGPTTALIFLGLFLALMTLFKTSCYFASSAVMIPLRTGVVRDIRIMVYAKVMRLPMGFFSEERKGDIIARMSGDVGEVEN 165
Cdd:cd07346 32 AGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 166 SITSSLDMLIKSPIMIILYFITLIATSWKLTLFTVLVLPAMGWLMGKVGRKLKRQSLEAQGKWSDTMSQLEETLGGLRII 245
Cdd:cd07346 112 LVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVV 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 246 KAFIAEDRMIDRFTRCSNELRDAVNKVAMRQALAHPMSEFLGTILIVSVLWFGGALILghNSSLTAPTFIFYMVILYSVI 325
Cdd:cd07346 192 KAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVLLYGGYLVL--QGSLTIGELVAFLAYLGMLF 269
|
250 260
....*....|....*....|...
gi 499421346 326 NPLKDFAKAGYNIPKGLASMERV 348
Cdd:cd07346 270 GPIQRLANLYNQLQQALASLERI 292
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
95-602 |
1.32e-52 |
|
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: 195.16 E-value: 1.32e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 95 LGLFLALMTLFKTSCYFASSAVMIplrTGVV--RDIRIMVYAKVMRLPMGFFSEERKGDIIARMSGDVGEVENSITSSLD 172
Cdd:TIGR00957 1008 LSVYGALGILQGFAVFGYSMAVSI---GGIQasRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIK 1084
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 173 MLIKSPIMIILYFITLIATSwklTLFTVLVLPaMGWLMGKV-------GRKLKRqsLEAQGKwSDTMSQLEETLGGLRII 245
Cdd:TIGR00957 1085 MFMGSLFNVIGALIVILLAT---PIAAVIIPP-LGLLYFFVqrfyvasSRQLKR--LESVSR-SPVYSHFNETLLGVSVI 1157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 246 KAFIAEDRMIDRF-TRCSNELRDAVNKVAMRQALAHPMsEFLGTILIVSVLWFG---------GALILGHNSSLTAPTFI 315
Cdd:TIGR00957 1158 RAFEEQERFIHQSdLKVDENQKAYYPSIVANRWLAVRL-ECVGNCIVLFAALFAvisrhslsaGLVGLSVSYSLQVTFYL 1236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 316 FYMVILYSvinplkdfakagyNIPKGLASMERVDKILKAENN----IKEIPNPK--PLTGmndRIEFKDISFSY-DGKRE 388
Cdd:TIGR00957 1237 NWLVRMSS-------------EMETNIVAVERLKEYSETEKEapwqIQETAPPSgwPPRG---RVEFRNYCLRYrEDLDL 1300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 389 VLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRSLIGNVNQEAILFNDTFFNNI 468
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL 1380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 469 -AFGveNATMEQVIEAAKIANAHDFIMEKPEGYNTNIGDRGGKLSGGQRQRVSIARAILKNPPILILDEATSALDTESER 547
Cdd:TIGR00957 1381 dPFS--QYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDN 1458
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 499421346 548 LVQEALERLMKTRTTIAIAHRLSTIKNADEICVLYEGEIVERGRHEELLELDGYY 602
Cdd:TIGR00957 1459 LIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIF 1513
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
86-596 |
1.40e-51 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 186.01 E-value: 1.40e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 86 NGPT---TALIFLGLFLALMTLfktscYFASSAVMIplRTGVVRDIRI--MVYAKVMRLPMgffseeRKGDIIARMS-GD 159
Cdd:TIGR01842 41 SVPTllmLTVLALGLYLFLGLL-----DALRSFVLV--RIGEKLDGALnqPIFAASFSATL------RRGSGDGLQAlRD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 160 VGEVENSITSS-LDMLIKSPIMIILYFITLIATSW--KLTLFTVLVLPAMGWLMGKVGRKLKRQSLEAQGKwsdTMSQLE 236
Cdd:TIGR01842 108 LDQLRQFLTGPgLFAFFDAPWMPIYLLVCFLLHPWigILALGGAVVLVGLALLNNRATKKPLKEATEASIR---ANNLAD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 237 ETLGGLRIIKAFIAEDRMIDRFTRCSNELRDAVNKVAMRQALAHPMSEFLGTILIVSVLWFGGALILGHNssLTAPTFIF 316
Cdd:TIGR01842 185 SALRNAEVIEAMGMMGNLTKRWGRFHSKYLSAQSAASDRAGMLSNLSKYFRIVLQSLVLGLGAYLAIDGE--ITPGMMIA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 317 YMVILYSVINPLkDFAKAGY-NIPKGLASMERVDKILkaeNNIKEIPNPKPLTGMNDRIEFKDISFSY-DGKREVLKHVN 394
Cdd:TIGR01842 263 GSILVGRALAPI-DGAIGGWkQFSGARQAYKRLNELL---ANYPSRDPAMPLPEPEGHLSVENVTIVPpGGKKPTLRGIS 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 395 LTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRSLIGNVNQEAILFNDTFFNNIAFGVEN 474
Cdd:TIGR01842 339 FSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIARFGEN 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 475 ATMEQVIEAAKIANAHDFIMEKPEGYNTNIGDRGGKLSGGQRQRVSIARAILKNPPILILDEATSALDTESERLVQEALE 554
Cdd:TIGR01842 419 ADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIK 498
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 499421346 555 RLMKTR-TTIAIAHRLSTIKNADEICVLYEGEIVERGRHEELL 596
Cdd:TIGR01842 499 ALKARGiTVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVL 541
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
296-604 |
2.26e-51 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 191.40 E-value: 2.26e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 296 WFGGALI-----LGHNSSLTAPTFIFYMVILYSVINPLKDFAKAGYNIPKGLASMERVDKILKAENNIKEIPNPKPLTGm 370
Cdd:PTZ00265 1086 WFGSFLIrrgtiLVDDFMKSLFTFLFTGSYAGKLMSLKGDSENAKLSFEKYYPLIIRKSNIDVRDNGGIRIKNKNDIKG- 1164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 371 ndRIEFKDISFSYDGKREV--LKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQ--------------------- 427
Cdd:PTZ00265 1165 --KIEIMDVNFRYISRPNVpiYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKndhhivfknehtndmtneqdy 1242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 428 ---------------------------------GGDITIDGTSIKDVRIADLRSLIGNVNQEAILFNDTFFNNIAFGVEN 474
Cdd:PTZ00265 1243 qgdeeqnvgmknvnefsltkeggsgedstvfknSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKED 1322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 475 ATMEQVIEAAKIANAHDFIMEKPEGYNTNIGDRGGKLSGGQRQRVSIARAILKNPPILILDEATSALDTESERLVQEALE 554
Cdd:PTZ00265 1323 ATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIV 1402
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 499421346 555 RLMKT--RTTIAIAHRLSTIKNADEICVL----YEGEIVE-RGRHEELLEL-DGYYKR 604
Cdd:PTZ00265 1403 DIKDKadKTIITIAHRIASIKRSDKIVVFnnpdRTGSFVQaHGTHEELLSVqDGVYKK 1460
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
374-597 |
1.17e-49 |
|
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: 172.13 E-value: 1.17e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYDGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLL-----PryhdvQGGDITIDGTSIKDVRIADLRS 448
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLngllkP-----TSGEVLVDGKDITKKNLRELRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 449 LIGNV--NQEAILFNDTFFNNIAFGVEN-----ATMEQ-VIEAAKIANahdfiMEKPEGYNTNigdrggKLSGGQRQRVS 520
Cdd:COG1122 76 KVGLVfqNPDDQLFAPTVEEDVAFGPENlglprEEIRErVEEALELVG-----LEHLADRPPH------ELSGGQKQRVA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499421346 521 IARAILKNPPILILDEATSALDTESERLVQEALERLMKTRTTIAIA-HRLSTI-KNADEICVLYEGEIVERGRHEELLE 597
Cdd:COG1122 145 IAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLDLVaELADRVIVLDDGRIVADGTPREVFS 223
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
100-600 |
1.71e-48 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 182.87 E-value: 1.71e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 100 ALMTLFKTSCYFASSAVMIPLRTGVVRDIRIMVYAKVMRLPMGFFSEERKGDIIARMSGDVGEVENSITSSLDMLIKSPI 179
Cdd:PLN03232 957 ALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLW 1036
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 180 MIILYFItLIATSWKLTLFTV---LVLPAMGWLMGK-VGRKLKRqsLEAQGKwSDTMSQLEETLGGLRIIKAFIAEDRM- 254
Cdd:PLN03232 1037 QLLSTFA-LIGTVSTISLWAImplLILFYAAYLYYQsTSREVRR--LDSVTR-SPIYAQFGEALNGLSSIRAYKAYDRMa 1112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 255 IDRFTRCSNELRDAVNKVAMRQALAhPMSEFLGTILIvsvlWFGGAL-ILGHNSSLTAPTFIFYMVILYS----VINPLK 329
Cdd:PLN03232 1113 KINGKSMDNNIRFTLANTSSNRWLT-IRLETLGGVMI----WLTATFaVLRNGNAENQAGFASTMGLLLSytlnITTLLS 1187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 330 DFAKAGYNIPKGLASMERVDKILKAENNIKEI-PNPKPLTGMNDR--IEFKDISFSY-DGKREVLKHVNLTVPKGKTVAL 405
Cdd:PLN03232 1188 GVLRQASKAENSLNSVERVGNYIDLPSEATAIiENNRPVSGWPSRgsIKFEDVHLRYrPGLPPVLHGLSFFVSPSEKVGV 1267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 406 VGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRSLIGNVNQEAILFNDTF-FNNIAFGVEN-ATMEQVIEA 483
Cdd:PLN03232 1268 VGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVrFNIDPFSEHNdADLWEALER 1347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 484 AKIanaHDFIMEKPEGYNTNIGDRGGKLSGGQRQRVSIARAILKNPPILILDEATSALDTESERLVQEALERLMKTRTTI 563
Cdd:PLN03232 1348 AHI---KDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTML 1424
|
490 500 510
....*....|....*....|....*....|....*..
gi 499421346 564 AIAHRLSTIKNADEICVLYEGEIVERGRHEELLELDG 600
Cdd:PLN03232 1425 VIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDT 1461
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
375-585 |
3.26e-47 |
|
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: 164.95 E-value: 3.26e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 375 EFKDISFSY-DGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRSLIGNV 453
Cdd:cd03225 1 ELKNLSFSYpDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 454 --NQEAILFNDTFFNNIAFGVENATMEQVIEAAKIANA-HDFIMEKPEGYNTNigdrggKLSGGQRQRVSIARAILKNPP 530
Cdd:cd03225 81 fqNPDDQFFGPTVEEEVAFGLENLGLPEEEIEERVEEAlELVGLEGLRDRSPF------TLSGGQKQRVAIAGVLAMDPD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499421346 531 ILILDEATSALDTESERLVQEALERLMKTRTTIAIA-HRLSTIKN-ADEICVLYEGE 585
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVtHDLDLLLElADRVIVLEDGK 211
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
136-600 |
9.71e-46 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 174.54 E-value: 9.71e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 136 VMRLPMGFFSEERKGDIIARMSGDVGEVENSITSSLDMLIKSPIMIILYFItLIATSWKLTLFTVLVLpamgwLMGKVGR 215
Cdd:PLN03130 996 ILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFLGQIFQLLSTFV-LIGIVSTISLWAIMPL-----LVLFYGA 1069
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 216 KLKRQSLEAQGKWSDTMS------QLEETLGGLRIIKAFIAEDRMIDRFTRC-SNELRDAVNKVAMRQALAHPMsEFLGT 288
Cdd:PLN03130 1070 YLYYQSTAREVKRLDSITrspvyaQFGEALNGLSTIRAYKAYDRMAEINGRSmDNNIRFTLVNMSSNRWLAIRL-ETLGG 1148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 289 ILIvsvlWFGGALILGHNSSLTAP-TFIFYMVILYS----VINPLKDFAKAGYNIPKGLASMERVdkilkaeNNIKEIPN 363
Cdd:PLN03130 1149 LMI----WLTASFAVMQNGRAENQaAFASTMGLLLSyalnITSLLTAVLRLASLAENSLNAVERV-------GTYIDLPS 1217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 364 PKPLTGMNDR----------IEFKDISFSYDGK-REVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDIT 432
Cdd:PLN03130 1218 EAPLVIENNRpppgwpssgsIKFEDVVLRYRPElPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRIL 1297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 433 IDGTSIKDVRIADLRSLIGNVNQEAILFNDTF-FNNIAFGVENATmeQVIEAAKIANAHDFIMEKPEGYNTNIGDRGGKL 511
Cdd:PLN03130 1298 IDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVrFNLDPFNEHNDA--DLWESLERAHLKDVIRRNSLGLDAEVSEAGENF 1375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 512 SGGQRQRVSIARAILKNPPILILDEATSALDTESERLVQEALERLMKTRTTIAIAHRLSTIKNADEICVLYEGEIVERGR 591
Cdd:PLN03130 1376 SVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDT 1455
|
....*....
gi 499421346 592 HEELLELDG 600
Cdd:PLN03130 1456 PENLLSNEG 1464
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
374-590 |
1.82e-45 |
|
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: 159.02 E-value: 1.82e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYDGKRE-VLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRiADLRSLIGN 452
Cdd:cd03247 1 LSINNVSFSYPEQEQqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 453 VNQEAILFNDTFFNNIafgvenatmeqvieaakianahdfimekpegyntnigdrGGKLSGGQRQRVSIARAILKNPPIL 532
Cdd:cd03247 80 LNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499421346 533 ILDEATSALDTESERLVQEALERLMKTRTTIAIAHRLSTIKNADEICVLYEGEIVERG 590
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
374-595 |
1.98e-45 |
|
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: 160.42 E-value: 1.98e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYdGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQG-----GDITIDGTSI--KDVRIADL 446
Cdd:cd03260 1 IELRDLNVYY-GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPgapdeGEVLLDGKDIydLDVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 447 RSLIGNVNQEAILFNDTFFNNIAFGV------ENATMEQVIEAA-KIANAHDfimekpegyntNIGDR--GGKLSGGQRQ 517
Cdd:cd03260 80 RRRVGMVFQKPNPFPGSIYDNVAYGLrlhgikLKEELDERVEEAlRKAALWD-----------EVKDRlhALGLSGGQQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499421346 518 RVSIARAILKNPPILILDEATSALDTESERLVQEALERLMKTRTTIAIAHRLSTIKN-ADEICVLYEGEIVERGRHEEL 595
Cdd:cd03260 149 RLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
374-586 |
2.72e-45 |
|
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: 158.15 E-value: 2.72e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYDG-KREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRSLIGN 452
Cdd:cd03246 1 LEVENVSFRYPGaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 453 VNQEAILFNDTFFNNIafgvenatmeqvieaakianahdfimekpegyntnigdrggkLSGGQRQRVSIARAILKNPPIL 532
Cdd:cd03246 81 LPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499421346 533 ILDEATSALDTESERLVQEALERL-MKTRTTIAIAHRLSTIKNADEICVLYEGEI 586
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
370-597 |
1.96e-43 |
|
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: 162.77 E-value: 1.96e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 370 MNDRIEFKDISFSY-DGKREVLKHVNLTVPKGKTVALVGQSGSGKSTL----VDLLPRYHDVqGGDITIDGTSIKDVRIA 444
Cdd:COG1123 1 MTPLLEVRDLSVRYpGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLalalMGLLPHGGRI-SGEVLLDGRDLLELSEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 445 DLRSLIGNVNQEAI--LFNDTFFNNIAFGVENATM------EQVIEAAKIANAHDFIMEKPegyntnigdrgGKLSGGQR 516
Cdd:COG1123 80 LRGRRIGMVFQDPMtqLNPVTVGDQIAEALENLGLsraearARVLELLEAVGLERRLDRYP-----------HQLSGGQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 517 QRVSIARAILKNPPILILDEATSALDTESERLVQEALERLMKTR--TTIAIAHRLSTIKN-ADEICVLYEGEIVERGRHE 593
Cdd:COG1123 149 QRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPE 228
|
....
gi 499421346 594 ELLE 597
Cdd:COG1123 229 EILA 232
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
339-597 |
3.34e-43 |
|
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: 162.38 E-value: 3.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 339 PKGLASMERVDKilKAENNIKEIPNPKPLtgmndrIEFKDISFSYDGKR----EVLKHVNLTVPKGKTVALVGQSGSGKS 414
Cdd:COG1123 234 PQALAAVPRLGA--ARGRAAPAAAAAEPL------LEVRNLSKRYPVRGkggvRAVDDVSLTLRRGETLGLVGESGSGKS 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 415 TLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRSLIGNVnqeAILFNDTF--FN-------NIAFGVENATMEQVIEAAK 485
Cdd:COG1123 306 TLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRELRRRV---QMVFQDPYssLNprmtvgdIIAEPLRLHGLLSRAERRE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 486 IANAhdfIMEK---PEGYntniGDR-GGKLSGGQRQRVSIARAILKNPPILILDEATSALDteseRLVQEALERLMKT-- 559
Cdd:COG1123 383 RVAE---LLERvglPPDL----ADRyPHELSGGQRQRVAIARALALEPKLLILDEPTSALD----VSVQAQILNLLRDlq 451
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 499421346 560 ----RTTIAIAHRLSTIKN-ADEICVLYEGEIVERGRHEELLE 597
Cdd:COG1123 452 relgLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEVFA 494
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
19-348 |
1.36e-42 |
|
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: 154.90 E-value: 1.36e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 19 IGWAILLNILSAVFnvfsfTLLIPILdilfktgennkvyeymewgtagfkdvaINNFyyyVSQMIQDNGPTTALIFLGLF 98
Cdd:cd18551 1 LILALLLSLLGTAA-----SLAQPLL---------------------------VKNL---IDALSAGGSSGGLLALLVAL 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 99 LALMTLFKTSCYFASSavmiplRTG--VVRDIRIMVYAKVMRLPMGFFSEERKGDIIARMSGDVGEVENSITSSLDMLIK 176
Cdd:cd18551 46 FLLQAVLSALSSYLLG------RTGerVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVT 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 177 SPIMIILYFITLIATSWKLTLFTVLVLPAMGWLMGKVGRKLKRQSLEAQGKWSDTMSQLEETLGGLRIIKAFIAEDRMID 256
Cdd:cd18551 120 GVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETK 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 257 RFTRCSNELRDAVNKVAMRQALAHPMSEFLGTILIVSVLWFGGALILghNSSLTAPTFIFYMVILYSVINPLKDFAKAGY 336
Cdd:cd18551 200 RGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLALLVVLGVGGARVA--SGALTVGTLVAFLLYLFQLITPLSQLSSFFT 277
|
330
....*....|..
gi 499421346 337 NIPKGLASMERV 348
Cdd:cd18551 278 QLQKALGALERI 289
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
374-596 |
3.52e-42 |
|
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: 151.96 E-value: 3.52e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYDGKR---EVLKHVNLTVPKGKTVALVGQSGSGKSTLV---DLLPRYhdvQGGDITIDGTSIKDVRIADLR 447
Cdd:cd03258 2 IELKNVSKVFGDTGgkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIrciNGLERP---TSGSVLVDGTDLTLLSGKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 448 SL---IGNVNQEAILFND-TFFNNIAFGVENATMEQVIEAAKIANAHDFI--MEKPEGYNTNigdrggkLSGGQRQRVSI 521
Cdd:cd03258 79 KArrrIGMIFQHFNLLSSrTVFENVALPLEIAGVPKAEIEERVLELLELVglEDKADAYPAQ-------LSGGQKQRVGI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499421346 522 ARAILKNPPILILDEATSALDTESERLVQEALERLMKTR--TTIAIAHRLSTIKN-ADEICVLYEGEIVERGRHEELL 596
Cdd:cd03258 152 ARALANNPKVLLCDEATSALDPETTQSILALLRDINRELglTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVF 229
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
89-321 |
1.64e-41 |
|
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: 151.87 E-value: 1.64e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 89 TTALIFLGLFL--ALMTLFKTScYFAssavmiplRTG--VVRDIRIMVYAKVMRLPMGFFSEERKGDIIARMSGDVGEVE 164
Cdd:cd18576 37 QIALLLLGLFLlqAVFSFFRIY-LFA--------RVGerVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 165 NSITSSLDMLIKSPIMIILYFITLIATSWKLTLFTVLVLPAMGWLMGKVGRKLKRQSLEAQGKWSDTMSQLEETLGGLRI 244
Cdd:cd18576 108 DTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRIRKLSKKVQDELAEANTIVEETLQGIRV 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 245 IKAFIAEDRMIDRFTRCSNELRDAVNKVAMRQALAHPMSEFLGTILIVSVLWFGGALILghNSSLTAP---TFIFYMVIL 321
Cdd:cd18576 188 VKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWYGGRLVL--AGELTAGdlvAFLLYTLFI 265
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
374-586 |
3.08e-41 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 148.43 E-value: 3.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYDGKReVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRSLIGNV 453
Cdd:COG4619 1 LELEGLSFRVGGKP-ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 454 NQEAILFNDTFFNNIAFGV----ENATMEQVIEAAKIANAHDFIMEKPEGyntnigdrggKLSGGQRQRVSIARAILKNP 529
Cdd:COG4619 80 PQEPALWGGTVRDNLPFPFqlreRKFDRERALELLERLGLPPDILDKPVE----------RLSGGERQRLALIRALLLQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 530 PILILDEATSALDTESERLVQEALERLMKT--RTTIAIAHRLSTIKN-ADEICVLYEGEI 586
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRVEELLREYLAEegRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
70-348 |
4.68e-41 |
|
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: 150.66 E-value: 4.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 70 VAINNFYYYVSQMIQDN----GPTTALIFLGLFLALMTLFKTSCYFASSAVMIPLRTGVVRDIRIMVYAKVMRLPMGFFS 145
Cdd:cd18542 12 TALNLLIPLLIRRIIDSviggGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSFSFHD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 146 EERKGDIIARMSGDVGEVENSITSSLDMLIKSPIMIILYFITLIATSWKLTLFTVLVLPAMGWLMGKVGRKLKRQSLEAQ 225
Cdd:cd18542 92 KARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFFKKVRPAFEEIR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 226 GKWSDTMSQLEETLGGLRIIKAFIAEDRMIDRFTRCSNELRDAVNKVAMRQALAHPMSEFLGTILIVSVLWFGGALILgh 305
Cdd:cd18542 172 EQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLVLWVGGYLVI-- 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 499421346 306 NSSLTAPT---FIFYMVILysvINPLK-------DFAKAgynipkgLASMERV 348
Cdd:cd18542 250 NGEITLGElvaFISYLWML---IWPVRqlgrlinDMSRA-------SASAERI 292
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
374-596 |
8.77e-41 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 149.12 E-value: 8.77e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSY-DGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLL-----PryhdvQGGDITIDGTSIKDV-RIADL 446
Cdd:TIGR04520 1 IEVENVSFSYpESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLnglllP-----TSGKVTVDGLDTLDEeNLWEI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 447 RSLIGNV-----NQ--EAILFNDtffnnIAFGVEN-----ATMEQVI-EAAKIANAHDFIMEKPEgyntnigdrggKLSG 513
Cdd:TIGR04520 76 RKKVGMVfqnpdNQfvGATVEDD-----VAFGLENlgvprEEMRKRVdEALKLVGMEDFRDREPH-----------LLSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 514 GQRQRVSIARAILKNPPILILDEATSALDTESERLVQEALERLMKTR--TTIAIAHRLSTIKNADEICVLYEGEIVERGR 591
Cdd:TIGR04520 140 GQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEgiTVISITHDMEEAVLADRVIVMNKGKIVAEGT 219
|
....*
gi 499421346 592 HEELL 596
Cdd:TIGR04520 220 PREIF 224
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
374-597 |
2.07e-40 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 147.13 E-value: 2.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYdGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIAdLRSLIGNV 453
Cdd:COG1131 1 IEVRGLTKRY-GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAE-VRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 454 NQEAILFND-TFFNNIAF-----GVENAT----MEQVIEAAKIANAHDfimekpegyntnigDRGGKLSGGQRQRVSIAR 523
Cdd:COG1131 79 PQEPALYPDlTVRENLRFfarlyGLPRKEarerIDELLELFGLTDAAD--------------RKVGTLSGGMKQRLGLAL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499421346 524 AILKNPPILILDEATSALDTESERLVQEALERLMKTRTTIAIA-HRLSTI-KNADEICVLYEGEIVERGRHEELLE 597
Cdd:COG1131 145 ALLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAeRLCDRVAIIDKGRIVADGTPDELKA 220
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
374-590 |
3.18e-40 |
|
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: 146.50 E-value: 3.18e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSY---DGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRSLI 450
Cdd:cd03257 2 LEVKNLSVSFptgGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 451 GNVnqeAILFNDtffnniAFGVENATM---EQVIEAAKIANAHD-------FIMEKPEGyntnIGDRGG-------KLSG 513
Cdd:cd03257 82 KEI---QMVFQD------PMSSLNPRMtigEQIAEPLRIHGKLSkkearkeAVLLLLVG----VGLPEEvlnryphELSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 514 GQRQRVSIARAILKNPPILILDEATSALDTESERLVQEALERLMKTR--TTIAIAHRLSTIKN-ADEICVLYEGEIVERG 590
Cdd:cd03257 149 GQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELglTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
373-591 |
5.89e-40 |
|
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: 144.86 E-value: 5.89e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 373 RIEFKDISFSYDGK-REVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRSLIG 451
Cdd:cd03369 6 EIEVENLSVRYAPDlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 452 NVNQEAILFNDTFFNNIafGVENA-TMEQVIEAAKIAnahdfimekpEGyntnigdrGGKLSGGQRQRVSIARAILKNPP 530
Cdd:cd03369 86 IIPQDPTLFSGTIRSNL--DPFDEySDEEIYGALRVS----------EG--------GLNLSQGQRQLLCLARALLKRPR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499421346 531 ILILDEATSALDTESERLVQEALERLMKTRTTIAIAHRLSTIKNADEICVLYEGEIVERGR 591
Cdd:cd03369 146 VLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
374-585 |
7.97e-40 |
|
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: 144.53 E-value: 7.97e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYDGKRE----VLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTsikdvriadlrsl 449
Cdd:cd03250 1 ISVEDASFTWDSGEQetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 450 IGNVNQEAILFNDTFFNNIAFGVE-NATM-EQVIEAAKIANahDF-IMekPEGYNTNIGDRGGKLSGGQRQRVSIARAIL 526
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKPfDEERyEKVIKACALEP--DLeIL--PDGDLTEIGEKGINLSGGQKQRISLARAVY 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499421346 527 KNPPILILDEATSALDTE-SERLVQEAL-ERLMKTRTTIAIAHRLSTIKNADEICVLYEGE 585
Cdd:cd03250 144 SDADIYLLDDPLSAVDAHvGRHIFENCIlGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
373-596 |
1.26e-39 |
|
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: 145.57 E-value: 1.26e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 373 RIEFKDISFSYdGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRSLIGN 452
Cdd:COG1120 1 MLEAENLSVGY-GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 453 VNQEAIL-FNDTFFNNIA---------FGVENATMEQVIEAAkianahdfiMEKpegynTNIG---DRG-GKLSGGQRQR 518
Cdd:COG1120 80 VPQEPPApFGLTVRELVAlgryphlglFGRPSAEDREAVEEA---------LER-----TGLEhlaDRPvDELSGGERQR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 519 VSIARAILKNPPILILDEATSALDTESERLVQEALERLMKT--RTTIAIAHRLS-TIKNADEICVLYEGEIVERGRHEEL 595
Cdd:COG1120 146 VLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErgRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEV 225
|
.
gi 499421346 596 L 596
Cdd:COG1120 226 L 226
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
374-597 |
2.39e-39 |
|
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: 144.56 E-value: 2.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYDGK---REVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRSLI 450
Cdd:COG1124 2 LEVRNLSVSYGQGgrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 451 GnvnqeaILFNDtffnniAFGVENA--TMEQVI-EAAKIANaHDFIMEKPE------GYNTNIGDR-GGKLSGGQRQRVS 520
Cdd:COG1124 82 Q------MVFQD------PYASLHPrhTVDRILaEPLRIHG-LPDREERIAelleqvGLPPSFLDRyPHQLSGGQRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 521 IARAILKNPPILILDEATSALDTESERLVQEALERLMKTR--TTIAIAHRLSTIKN-ADEICVLYEGEIVERGRHEELLE 597
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERglTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLA 228
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
374-595 |
3.28e-39 |
|
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: 143.80 E-value: 3.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYDGKReVLKHVNLTVPKGKTVALVGQSGSGKSTL----VDLLPRyhdvQGGDITIDGTSIKDVRIADLRSL 449
Cdd:cd03261 1 IELRGLTKSFGGRT-VLKGVDLDVRRGEILAIIGPSGSGKSTLlrliVGLLRP----DSGEVLIDGEDISGLSEAELYRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 450 ---IGNVNQEAILFND-TFFNNIAFGV-ENATM-EQVIEaakianahDFIMEKPEgyntNIGDRG------GKLSGGQRQ 517
Cdd:cd03261 76 rrrMGMLFQSGALFDSlTVFENVAFPLrEHTRLsEEEIR--------EIVLEKLE----AVGLRGaedlypAELSGGMKK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 518 RVSIARAILKNPPILILDEATSALDTESERLVQEALERLMKTR--TTIAIAHRLSTI-KNADEICVLYEGEIVERGRHEE 594
Cdd:cd03261 144 RVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELglTSIMVTHDLDTAfAIADRIAVLYDGKIVAEGTPEE 223
|
.
gi 499421346 595 L 595
Cdd:cd03261 224 L 224
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
374-588 |
3.85e-39 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 143.27 E-value: 3.85e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYDGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDG---TSIKDVRIADLRSLI 450
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGqdlSRLKRREIPYLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 451 GNVNQEAILFND-TFFNNIAF-----GVENATMEQVIEAAkianahdfiMEKpegynTNIGDRGGK----LSGGQRQRVS 520
Cdd:COG2884 82 GVVFQDFRLLPDrTVYENVALplrvtGKSRKEIRRRVREV---------LDL-----VGLSDKAKAlpheLSGGEQQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499421346 521 IARAILKNPPILILDEATSALDTE-SERLVqEALERLMKTRTTIAIA-HRLSTIKNADE-ICVLYEGEIVE 588
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLDPEtSWEIM-ELLEEINRRGTTVLIAtHDLELVDRMPKrVLELEDGRLVR 217
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
375-585 |
5.72e-39 |
|
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: 140.46 E-value: 5.72e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 375 EFKDISFSYdGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRSLIGNVN 454
Cdd:cd00267 1 EIENLSFRY-GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 455 QeailfndtffnniafgvenatmeqvieaakianahdfimekpegyntnigdrggkLSGGQRQRVSIARAILKNPPILIL 534
Cdd:cd00267 80 Q-------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499421346 535 DEATSALDTESERLVQEALERLMKT-RTTIAIAHRLSTIKNA-DEICVLYEGE 585
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
374-597 |
6.00e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 144.36 E-value: 6.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYDG-KREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRSLIGn 452
Cdd:PRK13632 8 IKVENVSFSYPNsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 453 vnqeaILFND--------TFFNNIAFGVEN-----ATMEQVI-EAAKIANAHDFIMEKPEgyntnigdrggKLSGGQRQR 518
Cdd:PRK13632 87 -----IIFQNpdnqfigaTVEDDIAFGLENkkvppKKMKDIIdDLAKKVGMEDYLDKEPQ-----------NLSGGQKQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 519 VSIARAILKNPPILILDEATSALDTESERLVQEALERLMKTR--TTIAIAHRLSTIKNADEICVLYEGEIVERGRHEELL 596
Cdd:PRK13632 151 VAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEIL 230
|
.
gi 499421346 597 E 597
Cdd:PRK13632 231 N 231
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
90-348 |
7.36e-39 |
|
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: 144.48 E-value: 7.36e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 90 TALIFLGLFLALMTLFKTSCYFAssavmiplrtgvvRDIRIMVYAKVMRLPMGFFSEERKGDIIARMSGDVGEVENSITS 169
Cdd:cd18541 50 ALLIGIFRFLWRYLIFGASRRIE-------------YDLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGP 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 170 SLDMLIKSPIMIILYFITLIATSWKLTLFTVLVLPAMGWLMGKVGRKLKRQSLEAQGKWSDTMSQLEETLGGLRIIKAFI 249
Cdd:cd18541 117 GILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFV 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 250 AEDRMIDRFTRCSNELRDAVNKVAMRQALAHPMSEFLGTILIVSVLWFGGALILGHNSS---LTAptFIFYMVILysvIN 326
Cdd:cd18541 197 QEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLIVLWYGGRLVIRGTITlgdLVA--FNSYLGML---IW 271
|
250 260
....*....|....*....|....*
gi 499421346 327 PLkdFAkAGY---NIPKGLASMERV 348
Cdd:cd18541 272 PM--MA-LGWvinLIQRGAASLKRI 293
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
370-605 |
7.46e-39 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 144.39 E-value: 7.46e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 370 MNDRIEFKDISFSY-DGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRS 448
Cdd:PRK13635 2 KEEIIRVEHISFRYpDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 449 LIGNV-----NQeaiLFNDTFFNNIAFGVENATM------EQVIEAAKIANAHDFIMEKPEgyntnigdrggKLSGGQRQ 517
Cdd:PRK13635 82 QVGMVfqnpdNQ---FVGATVQDDVAFGLENIGVpreemvERVDQALRQVGMEDFLNREPH-----------RLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 518 RVSIARAILKNPPILILDEATSALDTESERLVQEALERLMKTR--TTIAIAHRLSTIKNADEICVLYEGEIVERGRHEEL 595
Cdd:PRK13635 148 RVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKgiTVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEI 227
|
250
....*....|
gi 499421346 596 LELDGYYKRL 605
Cdd:PRK13635 228 FKSGHMLQEI 237
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
370-591 |
8.16e-39 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 142.49 E-value: 8.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 370 MNDRIEFKDISFSY---DGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLL-----PryhdvQGGDITIDGTSI--- 438
Cdd:COG1136 1 MSPLLELRNLTKSYgtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILggldrP-----TSGEVLIDGQDIssl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 439 KDVRIADLR-SLIGNVNQeailfndtFFNNIAF--GVENATMEQVIEAAKIANAHDFIMEKPEgyNTNIGDRGGK----L 511
Cdd:COG1136 76 SERELARLRrRHIGFVFQ--------FFNLLPEltALENVALPLLLAGVSRKERRERARELLE--RVGLGDRLDHrpsqL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 512 SGGQRQRVSIARAILKNPPILILDEATSALDTESERLVQEALERLMKTR-TTIAIA-HRLSTIKNADEICVLYEGEIVER 589
Cdd:COG1136 146 SGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELgTTIVMVtHDPELAARADRVIRLRDGRIVSD 225
|
..
gi 499421346 590 GR 591
Cdd:COG1136 226 ER 227
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
78-348 |
9.70e-39 |
|
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: 144.57 E-value: 9.70e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 78 YVSQMIQDN--------GPTTALIFLGLFLALMTLFKTSCYFASSAVMIPLRTGVVRDIRIMVYAKVMRLPMGFFSEERK 149
Cdd:cd18563 20 YLTKILIDDvliqlgpgGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLRRDLYEHLQRLSLSFFDKRQT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 150 GDIIARMSGDVGEVENSITSSLDMLIKSPIMIILYFITLIATSWKLTLFTVLVLPAMGWLMGKVGRKLKRQSLEAQGKWS 229
Cdd:cd18563 100 GSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGSYFFWKKIRRLFHRQWRRWS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 230 DTMSQLEETLGGLRIIKAFIAEDRMIDRFTRCSNELRDAVNKVAMRQALAHPMSEFLGTILIVSVLWFGGALILGHNSSL 309
Cdd:cd18563 180 RLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFLTSLGTLIVWYFGGRQVLSGTMTL 259
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 499421346 310 -TAPTFIFYMVILYsviNPLKDFAKAGYNIPKGLASMERV 348
Cdd:cd18563 260 gTLVAFLSYLGMFY---GPLQWLSRLNNWITRALTSAERI 296
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
374-596 |
1.29e-38 |
|
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: 142.44 E-value: 1.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYDGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRSLIGNV 453
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 454 NQEAILF-NDTFFNNIAFgveNATMEQVIEAAKIANAHDFI----MEkPEGYntniGDR-GGKLSGGQRQRVSIARAILK 527
Cdd:cd03295 81 IQQIGLFpHMTVEENIAL---VPKLLKWPKEKIRERADELLalvgLD-PAEF----ADRyPHELSGGQQQRVGVARALAA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499421346 528 NPPILILDEATSALDTESERLVQEALERLMKT--RTTIAIAHRL-STIKNADEICVLYEGEIVERGRHEELL 596
Cdd:cd03295 153 DPPLLLMDEPFGALDPITRDQLQEEFKRLQQElgKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
374-590 |
1.67e-38 |
|
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: 141.12 E-value: 1.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYDGKReVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRslIGNV 453
Cdd:cd03259 1 LELKGLSKTYGSVR-ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRN--IGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 454 NQEAILF-NDTFFNNIAFGVENATM------EQVIEAAKIANAHDFIMEKPEgyntnigdrggKLSGGQRQRVSIARAIL 526
Cdd:cd03259 78 FQDYALFpHLTVAENIAFGLKLRGVpkaeirARVRELLELVGLEGLLNRYPH-----------ELSGGQQQRVALARALA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499421346 527 KNPPILILDEATSALDTES-ERLVQEALERLMKTR-TTIAIAHRLS-TIKNADEICVLYEGEIVERG 590
Cdd:cd03259 147 REPSLLLLDEPLSALDAKLrEELREELKELQRELGiTTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
374-597 |
2.14e-38 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 141.67 E-value: 2.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYdGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSI--KDVRIADLRSLIG 451
Cdd:COG1126 2 IEIENLHKSF-GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 452 NVNQEAILFND-TFFNNIAFG---VENATMEqviEAAKIANAhdfIMEKpegynTNIGDRGGK----LSGGQRQRVSIAR 523
Cdd:COG1126 81 MVFQQFNLFPHlTVLENVTLApikVKKMSKA---EAEERAME---LLER-----VGLADKADAypaqLSGGQQQRVAIAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499421346 524 AILKNPPILILDEATSALDTEserLVQEALE---RLMKTRTTIAIA-HRLSTIKN-ADEICVLYEGEIVERGRHEELLE 597
Cdd:COG1126 150 ALAMEPKVMLFDEPTSALDPE---LVGEVLDvmrDLAKEGMTMVVVtHEMGFAREvADRVVFMDGGRIVEEGPPEEFFE 225
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
374-599 |
2.68e-38 |
|
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: 141.27 E-value: 2.68e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYdGKREVLKHVNLTVPKGKTVALVGQSGSGKSTL----VDLLPryhdVQGGDITIDGTSIKDVRIADLRSL 449
Cdd:COG1127 6 IEVRNLTKSF-GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLlkliIGLLR----PDSGEILVDGQDITGLSEKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 450 ---IGNVNQEAILFND-TFFNNIAFG-VENATM-EQVIEaaKIAnahdfiMEKPEgyNTNIGDRGGK----LSGGQRQRV 519
Cdd:COG1127 81 rrrIGMLFQGGALFDSlTVFENVAFPlREHTDLsEAEIR--ELV------LEKLE--LVGLPGAADKmpseLSGGMRKRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 520 SIARAILKNPPILILDEATSALDTESERLVQEALERLMKTR--TTIAIAHRLSTIKN-ADEICVLYEGEIVERGRHEELL 596
Cdd:COG1127 151 ALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELglTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELL 230
|
...
gi 499421346 597 ELD 599
Cdd:COG1127 231 ASD 233
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
365-595 |
2.18e-37 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 139.40 E-value: 2.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 365 KPLTGMNDRIEFKDISFSYdGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQG-----GDITIDGTSI- 438
Cdd:COG1117 3 APASTLEPKIEVRNLNVYY-GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPgarveGEILLDGEDIy 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 439 -KDVRIADLRSLIGNVNQEAILFNDTFFNNIAFGVE------NATMEQVIEAA-KIANAHDfimekpegyntNIGDR--- 507
Cdd:COG1117 82 dPDVDVVELRRRVGMVFQKPNPFPKSIYDNVAYGLRlhgiksKSELDEIVEESlRKAALWD-----------EVKDRlkk 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 508 -GGKLSGGQRQRVSIARAILKNPPILILDEATSALDTESERLVQEALERLmKTRTTIAI-------AHRLStiknaDEIC 579
Cdd:COG1117 151 sALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILEL-KKDYTIVIvthnmqqAARVS-----DYTA 224
|
250
....*....|....*.
gi 499421346 580 VLYEGEIVERGRHEEL 595
Cdd:COG1117 225 FFYLGELVEFGPTEQI 240
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
90-602 |
2.76e-37 |
|
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: 148.94 E-value: 2.76e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 90 TALIFLGLFLALMTLFKTSCYFASSAVMIplRTGVVRdiriMVYAKVMRLPMGFFSEERKGDIIARMSGDVGEVENsITS 169
Cdd:TIGR00957 361 TGLLFVCACLQTLILHQYFHICFVSGMRI--KTAVMG----AVYRKALVITNSARKSSTVGEIVNLMSVDAQRFMD-LAT 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 170 SLDMLIKSPIMIIL--YFITLIATSWKLTLFTVLVLpaMGWLMGKVGRKLKRQSLeAQGKWSDTMSQL-EETLGGLRIIK 246
Cdd:TIGR00957 434 YINMIWSAPLQVILalYFLWLNLGPSVLAGVAVMVL--MVPLNAVMAMKTKTYQV-AHMKSKDNRIKLmNEILNGIKVLK 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 247 AFIAEDRMIDRFTrcsnELRDAVNKVAMRQALAHPMSEF--LGTILIVSVLWFGGALILGHNSSLTAPTfIFYMVILYSV 324
Cdd:TIGR00957 511 LYAWELAFLDKVE----GIRQEELKVLKKSAYLHAVGTFtwVCTPFLVALITFAVYVTVDENNILDAEK-AFVSLALFNI 585
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 325 IN-PLKDFAKAGYNIPKGLASMERVDKILKAENNIKEIPNPKPLT-GMNDRIEFKDISFSY-DGKREVLKHVNLTVPKGK 401
Cdd:TIGR00957 586 LRfPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDSIERRTIKpGEGNSITVHNATFTWaRDLPPTLNGITFSIPEGA 665
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 402 TVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTsikdvriadlrslIGNVNQEAILFNDTFFNNIAFG--VENATMEQ 479
Cdd:TIGR00957 666 LVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-------------VAYVPQQAWIQNDSLRENILFGkaLNEKYYQQ 732
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 480 VIEAAKIANAHDFImekPEGYNTNIGDRGGKLSGGQRQRVSIARAILKNPPILILDEATSALDTESERLVQEAL---ERL 556
Cdd:TIGR00957 733 VLEACALLPDLEIL---PSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpEGV 809
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 499421346 557 MKTRTTIAIAHRLSTIKNADEICVLYEGEIVERGRHEELLELDGYY 602
Cdd:TIGR00957 810 LKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAF 855
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
79-348 |
3.14e-37 |
|
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: 139.98 E-value: 3.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 79 VSQMIQDNGPTTALIFLGLFLALMTLFKTSCYFASSAVMIPLRTGVVRDIRIMVYAKVMRLPMGFFSEERKGDIIARMSG 158
Cdd:cd18778 26 VDLVTIGSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDLYDKLQRLSLRYFDDRQTGDLMSRVIN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 159 DVGEVENSITSSLDMLIKSPIMIILYFITLIATSWKLTLFTVLVLPAMGWLMGKVGRKLKRQSLEAQGKWSDTMSQLEET 238
Cdd:cd18778 106 DVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLYSKKVRPRYRKVREALGELNALLQDN 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 239 LGGLRIIKAFIAEDRMIDRFTRCSNELRDAVNKVAMRQALAHPMSEFLGTILIVSVLWFGGALILGHN---SSLTAptFI 315
Cdd:cd18778 186 LSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPLMEFLTSLGTVLVLGFGGRLVLAGEltiGDLVA--FL 263
|
250 260 270
....*....|....*....|....*....|...
gi 499421346 316 FYMVILYsviNPLKDFAKAGYNIPKGLASMERV 348
Cdd:cd18778 264 LYLGLFY---EPITSLHGLNEMLQRALAGAERV 293
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
390-539 |
5.09e-37 |
|
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: 134.70 E-value: 5.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 390 LKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRSLIGNVNQEAILFND-TFFNNI 468
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499421346 469 AFGVENATMEQVIEAAKIANAHDFiMEKPEGYNTNIGDRGGKLSGGQRQRVSIARAILKNPPILILDEATS 539
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEK-LGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
375-590 |
6.50e-37 |
|
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: 135.64 E-value: 6.50e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 375 EFKDISFSYdGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRSLIgnvn 454
Cdd:cd03214 1 EVENLSVGY-GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKI---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 455 qeailfndtffnniafgvenATMEQVIEAAKIAN-AHDFIMEkpegyntnigdrggkLSGGQRQRVSIARAILKNPPILI 533
Cdd:cd03214 76 --------------------AYVPQALELLGLAHlADRPFNE---------------LSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 534 LDEATSALDTESERLVQEALERLMKTR--TTIAIAHRLS-TIKNADEICVLYEGEIVERG 590
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRRLARERgkTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
374-586 |
1.39e-36 |
|
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: 136.08 E-value: 1.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYDG---KREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRSL- 449
Cdd:cd03255 1 IELKNLSKTYGGggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 450 ---IGNVNQEAILFND-TFFNNIAF-----GVENATMEQVIEAA----KIANAHDfimEKPegyntnigdrgGKLSGGQR 516
Cdd:cd03255 81 rrhIGFVFQSFNLLPDlTALENVELplllaGVPKKERRERAEELlervGLGDRLN---HYP-----------SELSGGQQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499421346 517 QRVSIARAILKNPPILILDEATSALDTESERLVQEALERLMKTR-TTIAIA-HRLSTIKNADEICVLYEGEI 586
Cdd:cd03255 147 QRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAgTTIVVVtHDPELAEYADRIIELRDGKI 218
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
91-605 |
1.52e-36 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 146.81 E-value: 1.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 91 ALIFLGLFLALMTlfkTSCYFASsaVMiplRTGVvrDIRIMVYAKVMRLPMGFFSEERK----GDIIARMSGDvGEVENS 166
Cdd:PLN03130 345 FSIFVGVVLGVLC---EAQYFQN--VM---RVGF--RLRSTLVAAVFRKSLRLTHEGRKkftsGKITNLMTTD-AEALQQ 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 167 ITSSLDMLIKSPIMII----LYFITLIATSWKLTLFTVLVLPAMGWLMGKVgRKLKRQSLEAQGKWSDTMSqleETLGGL 242
Cdd:PLN03130 414 ICQQLHTLWSAPFRIIiamvLLYQQLGVASLIGSLMLVLMFPIQTFIISKM-QKLTKEGLQRTDKRIGLMN---EVLAAM 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 243 RIIKAFIAEDRMIDRFTRCSNE----LRDAvnkvamrQALAHPMSEFLGTI-LIVSVLWFGGALILGHNssLTaPTFIFY 317
Cdd:PLN03130 490 DTVKCYAWENSFQSKVQTVRDDelswFRKA-------QLLSAFNSFILNSIpVLVTVVSFGVFTLLGGD--LT-PARAFT 559
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 318 MVILYSVIN-PLKDFAKAGYNIPKGLASMERVDKILKAENNIKeIPNPkPLTGMNDRIEFKDISFSYDGK--REVLKHVN 394
Cdd:PLN03130 560 SLSLFAVLRfPLFMLPNLITQAVNANVSLKRLEELLLAEERVL-LPNP-PLEPGLPAISIKNGYFSWDSKaeRPTLSNIN 637
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 395 LTVPKGKTVALVGQSGSGKSTLVD-LLPRYHDVQGGDITIDGTsikdvriadlrslIGNVNQEAILFNDTFFNNIAFGV- 472
Cdd:PLN03130 638 LDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGT-------------VAYVPQVSWIFNATVRDNILFGSp 704
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 473 -ENATMEQVIEAAKIANAHDFImekPEGYNTNIGDRGGKLSGGQRQRVSIARAILKNPPILILDEATSALDTESERLV-Q 550
Cdd:PLN03130 705 fDPERYERAIDVTALQHDLDLL---PGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVfD 781
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 499421346 551 EALERLMKTRTTIAIAHRLSTIKNADEICVLYEGEIVERGRHEELLELDGYYKRL 605
Cdd:PLN03130 782 KCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKL 836
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
123-348 |
1.96e-36 |
|
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: 138.00 E-value: 1.96e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 123 GVVRDIRIMVYAKVMRLPMGFFSEERKGDIIARMSGDVGEVENSITSSLDMLIKSPIMIILYFITLIATSWKLTLFTVLV 202
Cdd:cd18550 69 GVMYDLRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 203 LPAMGWLMGKVGRKLKRQSLEAQGKWSDTMSQLEETL--GGLRIIKAFIAEDRMIDRFTRCSNELRDavnkVAMRQALAH 280
Cdd:cd18550 149 LPLFVLPTRRVGRRRRKLTREQQEKLAELNSIMQETLsvSGALLVKLFGREDDEAARFARRSRELRD----LGVRQALAG 224
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499421346 281 PMS----EFLGTILIVSVLWFGGALILGHNSSL-TAPTFIFYMVILYsviNPLKDFAKAGYNIPKGLASMERV 348
Cdd:cd18550 225 RWFfaalGLFTAIGPALVYWVGGLLVIGGGLTIgTLVAFTALLGRLY---GPLTQLLNIQVDLMTSLALFERI 294
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
374-597 |
6.27e-36 |
|
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: 137.11 E-value: 6.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYDGKREVLK---HVNLTVPKGKTVALVGQSGSGKSTL----VDLLPRYHDVqGGDITIDGTSIKDVRIADL 446
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVKavdGVSFDVRRGETLGLVGESGSGKSTLaraiLGLLPPPGIT-SGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 447 RSLIGNvnQEAILFNDtffnniAFGVENATM---EQVIEAAKIanaHDfIMEKPEGYN-----------TNIGDRGGK-- 510
Cdd:COG0444 81 RKIRGR--EIQMIFQD------PMTSLNPVMtvgDQIAEPLRI---HG-GLSKAEAREraiellervglPDPERRLDRyp 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 511 --LSGGQRQRVSIARAILKNPPILILDEATSALDTESERLVQEALERLMKTR--TTIAIAHRLSTIKN-ADEICVLYEGE 585
Cdd:COG0444 149 heLSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELglAILFITHDLGVVAEiADRVAVMYAGR 228
|
250
....*....|..
gi 499421346 586 IVERGRHEELLE 597
Cdd:COG0444 229 IVEEGPVEELFE 240
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
374-586 |
6.51e-36 |
|
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: 133.81 E-value: 6.51e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYdGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSI--KDVRIADLRSLIG 451
Cdd:cd03262 1 IEIKNLHKSF-GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 452 NVNQEAILF-NDTFFNNIAFGVENATMEQVIEAAKIANAH-------DFIMEKPegyntnigdrgGKLSGGQRQRVSIAR 523
Cdd:cd03262 80 MVFQQFNLFpHLTVLENITLAPIKVKGMSKAEAEERALELlekvglaDKADAYP-----------AQLSGGQQQRVAIAR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499421346 524 AILKNPPILILDEATSALDTEserLVQEALE---RLMKTRTTIAIA-HRLSTIKN-ADEICVLYEGEI 586
Cdd:cd03262 149 ALAMNPKVMLFDEPTSALDPE---LVGEVLDvmkDLAEEGMTMVVVtHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
86-328 |
1.10e-35 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 135.46 E-value: 1.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 86 NGPTTALIFLGLFLALMTLFKTSCYFASSAVMIPLRTGVVRDIRIMVYAKVMRLPMGFFSEERKGDIIARMSGDVGEVEN 165
Cdd:pfam00664 34 DPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRD 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 166 SITSSLDMLIKSPIMIILYFITLIATSWKLTLFTVLVLPAMGWLMGKVGRKLKRQSLEAQGKWSDTMSQLEETLGGLRII 245
Cdd:pfam00664 114 GLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTV 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 246 KAFIAEDRMIDRFTRCSNELRDAVNKVAMRQALAHPMSEFLGTILIVSVLWFGGALIlgHNSSLTAPTFIFYMVILYSVI 325
Cdd:pfam00664 194 KAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALALWFGAYLV--ISGELSVGDLVAFLSLFAQLF 271
|
...
gi 499421346 326 NPL 328
Cdd:pfam00664 272 GPL 274
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
374-586 |
1.19e-35 |
|
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: 131.75 E-value: 1.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYdGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDvRIADLRSLIGNV 453
Cdd:cd03230 1 IEVRNLSKRY-GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 454 NQEAILFndtffnniafgvENATMEQVIeaakianahdfimekpegyntnigdrggKLSGGQRQRVSIARAILKNPPILI 533
Cdd:cd03230 79 PEEPSLY------------ENLTVRENL----------------------------KLSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499421346 534 LDEATSALDTESERLVQEALERLMKTRTTIAIA-HRLSTIKN-ADEICVLYEGEI 586
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELKKEGKTILLSsHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
87-348 |
1.43e-35 |
|
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: 135.72 E-value: 1.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 87 GPTTALIFLGLFLALMTLFKTSCYFASSAVMIplRTG--VVRDIRIMVYAKVMRLPMGFFSEERKGDIIARMSGDVGEVE 164
Cdd:cd18564 48 DPLALLLLAAAALVGIALLRGLASYAGTYLTA--LVGqrVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 165 NSITSSLDMLIKSPIMIILYFITLIATSWKLTLFTVLVLPAMGWLMGKVGRKLKRQSLEAQGKWSDTMSQLEETLGGLRI 244
Cdd:cd18564 126 DLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRV 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 245 IKAFIAEDRMIDRFTRCSNELRDAVNKVAMRQALAHPMSEFLGTILIVSVLWFGGALILGHnsSLTAPT---FIFYMVIL 321
Cdd:cd18564 206 VQAFGREEHEERRFARENRKSLRAGLRAARLQALLSPVVDVLVAVGTALVLWFGAWLVLAG--RLTPGDllvFLAYLKNL 283
|
250 260
....*....|....*....|....*..
gi 499421346 322 YSvinPLKDFAKAGYNIPKGLASMERV 348
Cdd:cd18564 284 YK---PVRDLAKLTGRIAKASASAERV 307
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
86-348 |
4.42e-35 |
|
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: 133.84 E-value: 4.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 86 NGPTTALIFLGLFLALMTLFKtSCYFASSAVMIplrtgvVRDIRIMVYAKVMRLPMGFFSEERKGDIIARMSGDVGEVEN 165
Cdd:cd18557 36 NELALILLAIYLLQSVFTFVR-YYLFNIAGERI------VARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 166 SITSSLDMLIKSPIMIILYFITLIATSWKLTLFTVLVLPAMGWLMGKVGRKLKRQSLEAQGKWSDTMSQLEETLGGLRII 245
Cdd:cd18557 109 AVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTV 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 246 KAFIAEDRMIDRFTRCSNELRDAVNKVAMRQALAHPMSEFLGTILIVSVLWFGGALIL-GHNSSLTAPTFIFYMVILYSV 324
Cdd:cd18557 189 RSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYGGYLVLsGQLTVGELTSFILYTIMVASS 268
|
250 260
....*....|....*....|....*
gi 499421346 325 INPLKDFakagYN-IPKGLASMERV 348
Cdd:cd18557 269 VGGLSSL----LAdIMKALGASERV 289
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
374-585 |
4.93e-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: 4.93e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYdGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVR--IADLRSLIG 451
Cdd:cd03229 1 LELKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 452 NVNQEAILF-NDTFFNNIAFGvenatmeqvieaakianahdfimekpegyntnigdrggkLSGGQRQRVSIARAILKNPP 530
Cdd:cd03229 80 MVFQDFALFpHLTVLENIALG---------------------------------------LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499421346 531 ILILDEATSALDTESERLVQEALERLMKT--RTTIAIAHRLS-TIKNADEICVLYEGE 585
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDeAARLADRVVVLRDGK 178
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
364-596 |
6.69e-35 |
|
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: 132.73 E-value: 6.69e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 364 PKPLTGMNDRIEFKDISFSYDGK-REVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVR 442
Cdd:cd03288 10 NSGLVGLGGEIKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 443 IADLRSLIGNVNQEAILFNDTffnnIAFGVE---NATMEQVIEAAKIANAHDFIMEKPEGYNTNIGDRGGKLSGGQRQRV 519
Cdd:cd03288 90 LHTLRSRLSIILQDPILFSGS----IRFNLDpecKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLF 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499421346 520 SIARAILKNPPILILDEATSALDTESERLVQEALERLMKTRTTIAIAHRLSTIKNADEICVLYEGEIVERGRHEELL 596
Cdd:cd03288 166 CLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLL 242
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
374-596 |
8.06e-35 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 134.43 E-value: 8.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYDGKR---EVLKHVNLTVPKGKTVALVGQSGSGKSTLV---DLLPRYhdvQGGDITIDGTSIKDVRIADLR 447
Cdd:COG1135 2 IELENLSKTFPTKGgpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIrciNLLERP---TSGSVLVDGVDLTALSERELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 448 SL---IGNVNQEAILFND-TFFNNIAFGVENATMEQVIEAAKIANAHDFImekpegyntNIGDRGGK----LSGGQRQRV 519
Cdd:COG1135 79 AArrkIGMIFQHFNLLSSrTVAENVALPLEIAGVPKAEIRKRVAELLELV---------GLSDKADAypsqLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 520 SIARAILKNPPILILDEATSALDTESerlVQEALERLMKTR-----TTIAIAHRLSTIKN-ADEICVLYEGEIVERGRHE 593
Cdd:COG1135 150 GIARALANNPKVLLCDEATSALDPET---TRSILDLLKDINrelglTIVLITHEMDVVRRiCDRVAVLENGRIVEQGPVL 226
|
...
gi 499421346 594 ELL 596
Cdd:COG1135 227 DVF 229
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
22-348 |
1.29e-34 |
|
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: 132.91 E-value: 1.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 22 AILLNILSAVFNVfsftlLIPILdilfkTGEnnkvyeymewgtagfkdvAINNFYYYVSQMIQDNgpTTALIFLGLFLAL 101
Cdd:cd18547 4 VIILAIISTLLSV-----LGPYL-----LGK------------------AIDLIIEGLGGGGGVD--FSGLLRILLLLLG 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 102 MTLFKTSCYFASSAVMIPLRTGVVRDIRIMVYAKVMRLPMGFFSEERKGDIIARMSGDVGEVENSITSSLDMLIKSPIMI 181
Cdd:cd18547 54 LYLLSALFSYLQNRLMARVSQRTVYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTI 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 182 ILYFITLIATSWKLTLFTVLVLPAMGWLMGKVGRK----LKRQSlEAQGKWSdtmSQLEETLGGLRIIKAFIAEDRMIDR 257
Cdd:cd18547 134 VGTLIMMLYISPLLTLIVLVTVPLSLLVTKFIAKRsqkyFRKQQ-KALGELN---GYIEEMISGQKVVKAFNREEEAIEE 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 258 FTRCSNELRDAVNKVAMRQALAHPMSEFLGTILIVSVLWFGGALILGHNSSL-TAPTFIFYMvilYSVINPLKDFAkAGY 336
Cdd:cd18547 210 FDEINEELYKASFKAQFYSGLLMPIMNFINNLGYVLVAVVGGLLVINGALTVgVIQAFLQYS---RQFSQPINQIS-QQI 285
|
330
....*....|...
gi 499421346 337 N-IPKGLASMERV 348
Cdd:cd18547 286 NsLQSALAGAERV 298
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
70-348 |
2.17e-34 |
|
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: 132.13 E-value: 2.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 70 VAINNFyyyvsqMIQDNGPTTALIFLGLFLALMTLFKTSCYFASSAVMipLRTG--VVRDIRIMVYAKVMRLPMGFFSEE 147
Cdd:cd18544 24 RAIDDY------IVPGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLL--QKLGqrIIYDLRRDLFSHIQRLPLSFFDRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 148 RKGDIIARMSGDVGEVENSITSSLDMLIKSPIMIILYFITLIATSWKLTLFTVLVLPAMGWLMGKVGRKLKRQSLEAQGK 227
Cdd:cd18544 96 PVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYLFRKKSRKAYREVREK 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 228 WSDTMSQLEETLGGLRIIKAFIAEDRMIDRFTRCSNELRDAVNKVAMRQALAHPMSEFLGTILIVSVLWFGGALILGHNS 307
Cdd:cd18544 176 LSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALALVLWYGGGQVLSGAV 255
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 499421346 308 S---LTAptFIFYMVILYsviNPLKDFA-KagYNI-PKGLASMERV 348
Cdd:cd18544 256 TlgvLYA--FIQYIQRFF---RPIRDLAeK--FNIlQSAMASAERI 294
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
374-597 |
2.54e-34 |
|
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: 130.36 E-value: 2.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYdGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIAdLRSLIGNV 453
Cdd:COG4555 2 IEVENLSKKY-GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-ARRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 454 NQEAILF-NDTFFNNIAF-----GVENATMEQVIEAAkianAHDFIMEkpegyntNIGDRG-GKLSGGQRQRVSIARAIL 526
Cdd:COG4555 80 PDERGLYdRLTVRENIRYfaelyGLFDEELKKRIEEL----IELLGLE-------EFLDRRvGELSTGMKKKVALARALV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499421346 527 KNPPILILDEATSALDTESERLVQEALERLMKTRTTIAIA-HRLSTIKN-ADEICVLYEGEIVERGRHEELLE 597
Cdd:COG4555 149 HDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSsHIMQEVEAlCDRVVILHKGKVVAQGSLDELRE 221
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
370-596 |
3.41e-34 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 130.21 E-value: 3.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 370 MNDRIEFKDISFSYDGkREVLKHVNLTVPKGKTVALVGQSGSGKSTLV----DLLPRYHdvqgGDITIDGTSIKDVRiad 445
Cdd:COG1121 3 MMPAIELENLTVSYGG-RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLkailGLLPPTS----GTVRLFGKPPRRAR--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 446 lrSLIGNVNQEAiLFNDTFfnniafgveNATMEQVI-----------------EAAKIANAhdfiMEKpegynTNIGDRG 508
Cdd:COG1121 75 --RRIGYVPQRA-EVDWDF---------PITVRDVVlmgrygrrglfrrpsraDREAVDEA----LER-----VGLEDLA 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 509 ----GKLSGGQRQRVSIARAILKNPPILILDEATSALDTESERLVQEALERLMKTRTTI-AIAHRLSTI-KNADEICVLy 582
Cdd:COG1121 134 drpiGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTIlVVTHDLGAVrEYFDRVLLL- 212
|
250
....*....|....
gi 499421346 583 EGEIVERGRHEELL 596
Cdd:COG1121 213 NRGLVAHGPPEEVL 226
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
375-587 |
5.66e-34 |
|
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: 128.42 E-value: 5.66e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 375 EFKDISFSYDGkREVLKHVNLTVPKGKTVALVGQSGSGKSTLV----DLLPRYHdvqgGDITIDGtsikdVRIADLRSLI 450
Cdd:cd03235 1 EVEDLTVSYGG-HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLkailGLLKPTS----GSIRVFG-----KPLEKERKRI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 451 GNVNQEAiLFNDTFfnniafgveNATMEQVI-----------------EAAKIANAHDFI-MekpegynTNIGDRG-GKL 511
Cdd:cd03235 71 GYVPQRR-SIDRDF---------PISVRDVVlmglyghkglfrrlskaDKAKVDEALERVgL-------SELADRQiGEL 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499421346 512 SGGQRQRVSIARAILKNPPILILDEATSALDTESERLVQEALERL-MKTRTTIAIAHRLSTIKNADEICVLYEGEIV 587
Cdd:cd03235 134 SGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
91-320 |
6.12e-34 |
|
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: 130.68 E-value: 6.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 91 ALIFLGLFLALMTLFKTscYFASsavmiplRTG--VVRDIRIMVYAKVMRLPMGFFSEERKGDIIARMSGDVGEVENSIT 168
Cdd:cd18575 41 LLLAVALVLALASALRF--YLVS-------WLGerVVADLRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 169 SSLDMLIKSPIMIILYFITLIATSWKLTLFTVLVLPAMGWLMGKVGRKLKRQSLEAQGKWSDTMSQLEETLGGLRIIKAF 248
Cdd:cd18575 112 SSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAF 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499421346 249 IAEDRMIDRFTRCSNELRDAVNKVAMRQALAHPMSEFLGTILIVSVLWFGG-ALILGHNSS--LTAptFIFYMVI 320
Cdd:cd18575 192 TREDAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIVFVLWLGAhDVLAGRMSAgeLSQ--FVFYAVL 264
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
92-605 |
8.23e-34 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 138.19 E-value: 8.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 92 LIFLGLFLALMTlfkTSCYFASSavmipLRTGVvrDIRIMVYAKVMRLPMGFFSEERK----GDIIARMSGDVGEVEnSI 167
Cdd:PLN03232 346 LIFFGVTFGVLC---ESQYFQNV-----GRVGF--RLRSTLVAAIFHKSLRLTHEARKnfasGKVTNMITTDANALQ-QI 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 168 TSSLDMLIKSPIMIILYFITLIATSWKLTLFTVLVL----PAMGWLMGKVgRKLKRQSLEaqgkWSDT-MSQLEETLGGL 242
Cdd:PLN03232 415 AEQLHGLWSAPFRIIVSMVLLYQQLGVASLFGSLILflliPLQTLIVRKM-RKLTKEGLQ----WTDKrVGIINEILASM 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 243 RIIKAFIAEDRMIDRFTRCSNELRDAVNKVamrQALAHPMSEFLGTI-LIVSVLWFGGALILGhnSSLTaPTFIFYMVIL 321
Cdd:PLN03232 490 DTVKCYAWEKSFESRIQGIRNEELSWFRKA---QLLSAFNSFILNSIpVVVTLVSFGVFVLLG--GDLT-PARAFTSLSL 563
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 322 YSVIN-PLKDFAKAGYNIPKGLASMERVDKILKAENNIKEiPNPkPLTGMNDRIEFKDISFSYDGKRE--VLKHVNLTVP 398
Cdd:PLN03232 564 FAVLRsPLNMLPNLLSQVVNANVSLQRIEELLLSEERILA-QNP-PLQPGAPAISIKNGYFSWDSKTSkpTLSDINLEIP 641
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 399 KGKTVALVGQSGSGKSTLVDLLPryhdvqgGDITIDGTSIkdvriADLRSLIGNVNQEAILFNDTFFNNIAFG--VENAT 476
Cdd:PLN03232 642 VGSLVAIVGGTGEGKTSLISAML-------GELSHAETSS-----VVIRGSVAYVPQVSWIFNATVRENILFGsdFESER 709
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 477 MEQVIEAAKIANAHDFImekPEGYNTNIGDRGGKLSGGQRQRVSIARAILKNPPILILDEATSALDTESERLV-QEALER 555
Cdd:PLN03232 710 YWRAIDVTALQHDLDLL---PGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVfDSCMKD 786
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 499421346 556 LMKTRTTIAIAHRLSTIKNADEICVLYEGEIVERGRHEELLELDGYYKRL 605
Cdd:PLN03232 787 ELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKL 836
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
374-581 |
1.07e-33 |
|
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: 127.97 E-value: 1.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYDGKR---EVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIAdlrslI 450
Cdd:cd03293 1 LEVRNVSKTYGGGGgavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 451 GNVNQEAILFN-DTFFNNIAFGVENATM------EQVIEAAKIANAHDFIMEKPegyntnigdrgGKLSGGQRQRVSIAR 523
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLELQGVpkaearERAEELLELVGLSGFENAYP-----------HQLSGGMRQRVALAR 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499421346 524 AILKNPPILILDEATSALDTESERLVQEALERLMKTR--TTIAIAHRLS-TIKNADEICVL 581
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETgkTVLLVTHDIDeAVFLADRVVVL 205
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
374-596 |
2.96e-33 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 127.18 E-value: 2.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYDGKRevlKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADlRSLignv 453
Cdd:COG3840 2 LRLDDLTYRYGDFP---LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE-RPV---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 454 nqeAILFND-------TFFNNIAFGVE-----NAT-MEQVIEAAKIANAHDFIMEKPegyntnigdrgGKLSGGQRQRVS 520
Cdd:COG3840 74 ---SMLFQEnnlfphlTVAQNIGLGLRpglklTAEqRAQVEQALERVGLAGLLDRLP-----------GQLSGGQRQRVA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 521 IARAILKNPPILILDEATSALD----TESERLVQE-ALERLMktrTTIAIAHRLSTIKN-ADEICVLYEGEIVERGRHEE 594
Cdd:COG3840 140 LARCLVRKRPILLLDEPFSALDpalrQEMLDLVDElCRERGL---TVLMVTHDPEDAARiADRVLLVADGRIAADGPTAA 216
|
..
gi 499421346 595 LL 596
Cdd:COG3840 217 LL 218
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
390-597 |
4.28e-33 |
|
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: 127.76 E-value: 4.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 390 LKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRSL----IGNVNQEAILF-NDTF 464
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrrkkISMVFQSFALLpHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 465 FNNIAFGVENATM------EQVIEAAKIANAHDFIMEKPegyntnigdrgGKLSGGQRQRVSIARAILKNPPILILDEAT 538
Cdd:cd03294 120 LENVAFGLEVQGVpraereERAAEALELVGLEGWEHKYP-----------DELSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499421346 539 SALDTESERLVQEALERLMKT--RTTIAIAHRLS-TIKNADEICVLYEGEIVERGRHEELLE 597
Cdd:cd03294 189 SALDPLIRREMQDELLRLQAElqKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILT 250
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
368-603 |
5.37e-33 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 127.13 E-value: 5.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 368 TGMNDRIEFKDISFSY---DGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTsikdvRIA 444
Cdd:COG1116 2 SAAAPALELRGVSKRFptgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGK-----PVT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 445 DLRSLIGNVNQEAILFN-DTFFNNIAFGVENATMEQViEAAKIANAH-------DFIMEKPegyntnigdrgGKLSGGQR 516
Cdd:COG1116 77 GPGPDRGVVFQEPALLPwLTVLDNVALGLELRGVPKA-ERRERARELlelvglaGFEDAYP-----------HQLSGGMR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 517 QRVSIARAILKNPPILILDEATSALDTESERLVQEALERL-MKTRTTI---------AIahRLstiknADEICVLYE--G 584
Cdd:COG1116 145 QRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLwQETGKTVlfvthdvdeAV--FL-----ADRVVVLSArpG 217
|
250 260
....*....|....*....|....*.
gi 499421346 585 EIVE-------RGRHEELLELDGYYK 603
Cdd:COG1116 218 RIVEeidvdlpRPRDRELRTSPEFAA 243
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
374-595 |
6.59e-33 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 126.64 E-value: 6.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYDGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRSL---I 450
Cdd:TIGR02315 2 LEVENLSKVYPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLrrrI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 451 GNVNQEailfndtfFNNIafgvENAT-MEQVIEAAkiANAHDFIM---------EKPEGYNT----NIGD----RGGKLS 512
Cdd:TIGR02315 82 GMIFQH--------YNLI----ERLTvLENVLHGR--LGYKPTWRsllgrfseeDKERALSAlervGLADkayqRADQLS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 513 GGQRQRVSIARAILKNPPILILDEATSALDTESERLVQEALERLMKTR--TTIAIAHRLSTIKN-ADEICVLYEGEIVER 589
Cdd:TIGR02315 148 GGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDgiTVIINLHQVDLAKKyADRIVGLKAGEIVFD 227
|
....*.
gi 499421346 590 GRHEEL 595
Cdd:TIGR02315 228 GAPSEL 233
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
373-590 |
9.84e-33 |
|
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: 124.59 E-value: 9.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 373 RIEFKDISFSYDGK-----REVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQG--GDITIDGTSIKDVRIad 445
Cdd:cd03213 3 TLSFRNLTVTVKSSpsksgKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRPLDKRSF-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 446 lRSLIGNVNQEAILF-NDTFFNNIAFgvenatmeqvieAAKIanahdfimekpegyntnigdRGgkLSGGQRQRVSIARA 524
Cdd:cd03213 81 -RKIIGYVPQDDILHpTLTVRETLMF------------AAKL--------------------RG--LSGGERKRVSIALE 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499421346 525 ILKNPPILILDEATSALDTESERLVQEALERLMKT-RTTIAIAHRLST--IKNADEICVLYEGEIVERG 590
Cdd:cd03213 126 LVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTgRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
77-348 |
1.17e-32 |
|
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: 127.13 E-value: 1.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 77 YYVSQMIQD---NGPTTALIFLGLFLALMTLFKTSC-----YFASSAVMiplrtGVVRDIRIMVYAKVMRLPMGFFSEER 148
Cdd:cd18548 20 TLMADIIDEgiaNGDLSYILRTGLLMLLLALLGLIAgilagYFAAKASQ-----GFGRDLRKDLFEKIQSFSFAEIDKFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 149 KGDIIARMSGDVGEVENSITSSLDMLIKSPIMIILYFITLIATSWKLTLFTVLVLPAMGWLMGKVGRKLKRQSLEAQgKW 228
Cdd:cd18548 95 TSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIMKKAIPLFKKVQ-KK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 229 SDTMSQ-LEETLGGLRIIKAFIAEDRMIDRFTRCSNELRDAVNKVAMRQALAHPMSEFLGTILIVSVLWFGGALILGHN- 306
Cdd:cd18548 174 LDRLNRvVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAILWFGGHLINAGSl 253
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 499421346 307 --SSLTAptFIFYMV-ILYSVINplkdFAKAGYNIPKGLASMERV 348
Cdd:cd18548 254 qvGDLVA--FINYLMqILMSLMM----LSMVFVMLPRASASAKRI 292
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
374-587 |
1.45e-32 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 125.55 E-value: 1.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYDGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRSL---I 450
Cdd:COG3638 3 LELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLrrrI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 451 GNVNQEailfndtfFNNiafgVENATmeqVIE---------------------AAKIANAHDfIMEKpegynTNIGD--- 506
Cdd:COG3638 83 GMIFQQ--------FNL----VPRLS---VLTnvlagrlgrtstwrsllglfpPEDRERALE-ALER-----VGLADkay 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 507 -RGGKLSGGQRQRVSIARAILKNPPILILDEATSALDTESERLVQEALERLMKTR--TTIAIAHRLSTIKN-ADEICVLY 582
Cdd:COG3638 142 qRADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDgiTVVVNLHQVDLARRyADRIIGLR 221
|
....*
gi 499421346 583 EGEIV 587
Cdd:COG3638 222 DGRVV 226
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
373-595 |
2.84e-32 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 127.88 E-value: 2.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 373 RIEFKDISFSYdGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADlRSlIGN 452
Cdd:COG3839 3 SLELENVSKSY-GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD-RN-IAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 453 VNQEAILF-NDTFFNNIAFGVENATM------EQVIEAAKIANAHDFIMEKPegyntnigdrgGKLSGGQRQRVSIARAI 525
Cdd:COG3839 80 VFQSYALYpHMTVYENIAFPLKLRKVpkaeidRRVREAAELLGLEDLLDRKP-----------KQLSGGQRQRVALGRAL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 526 LKNPPILILDEATSALD------TESE--RLVQEalerlMKTrTTIAIAHRLS---TIknADEICVLYEGEIVERGRHEE 594
Cdd:COG3839 149 VREPKVFLLDEPLSNLDaklrveMRAEikRLHRR-----LGT-TTIYVTHDQVeamTL--ADRIAVMNDGRIQQVGTPEE 220
|
.
gi 499421346 595 L 595
Cdd:COG3839 221 L 221
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
374-601 |
3.41e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 125.66 E-value: 3.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYDG----KREVLKHVNLTVPKGKTVALVGQSGSGKSTLVD-----LLPRYHDVQGGDITIDGTSiKDVRIA 444
Cdd:PRK13646 3 IRFDNVSYTYQKgtpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQninalLKPTTGTVTVDDITITHKT-KDKYIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 445 DLRSLIGNVNQ--EAILFNDTFFNNIAFGVENATMEqvIEAAKiANAHDFIMEKpeGYNTNIGDRGG-KLSGGQRQRVSI 521
Cdd:PRK13646 82 PVRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMN--LDEVK-NYAHRLLMDL--GFSRDVMSQSPfQMSGGQMRKIAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 522 ARAILKNPPILILDEATSALDTESERLVQEALERLM--KTRTTIAIAHRLSTI-KNADEICVLYEGEIVERGRHEELLEL 598
Cdd:PRK13646 157 VSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFKD 236
|
...
gi 499421346 599 DGY 601
Cdd:PRK13646 237 KKK 239
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
374-597 |
4.11e-32 |
|
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: 123.89 E-value: 4.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYDGKReVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIAdlRSLIGNV 453
Cdd:cd03300 1 IELENVSKFYGGFV-ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 454 NQEAILFND-TFFNNIAFGVENATMEQVIEAAKIANAHDFI-MEKPEGYNTNigdrggKLSGGQRQRVSIARAILKNPPI 531
Cdd:cd03300 78 FQNYALFPHlTVFENIAFGLRLKKLPKAEIKERVAEALDLVqLEGYANRKPS------QLSGGQQQRVAIARALVNEPKV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499421346 532 LILDEATSALDTESERLVQEALERLMKTR--TTIAIAHRLS-TIKNADEICVLYEGEIVERGRHEELLE 597
Cdd:cd03300 152 LLLDEPLGALDLKLRKDMQLELKRLQKELgiTFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEIYE 220
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
87-348 |
8.15e-32 |
|
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: 124.90 E-value: 8.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 87 GPTTALIFLGLFLALMTLFKTSCYFASSAVMIPLRTGVVRDIRIMVYAKVMRLPMGFFSEERKGDIIARMSGDVGEVENS 166
Cdd:cd18543 33 GDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 167 ITSSLdMLIKSPIMIILYFITLIATSWKLTLFTVLVLPAMGWLMGKVGRKLKRQSLEAQGKWSDTMSQLEETLGGLRIIK 246
Cdd:cd18543 113 LAFGP-FLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFRRRYFPASRRAQDQAGDLATVVEESVTGIRVVK 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 247 AFIAEDRMIDRFTRCSNELRDAVNKVAMRQALAHPMSEFLGTILIVSVLWFGGALILghNSSLTAPTFIFYMVILYSVIN 326
Cdd:cd18543 192 AFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEALPELGLAAVLALGGWLVA--NGSLTLGTLVAFSAYLTMLVW 269
|
250 260
....*....|....*....|..
gi 499421346 327 PLKDFAKAGYNIPKGLASMERV 348
Cdd:cd18543 270 PVRMLGWLLAMAQRARAAAERV 291
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
374-597 |
2.97e-31 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 121.74 E-value: 2.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYdGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKD--VRIADLRSLIG 451
Cdd:PRK09493 2 IEFKNVSKHF-GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 452 NVNQEAILFND-TFFNNIAFGVenatmEQVIEAAKiANAHDFIME--KPEGYNTNIGDRGGKLSGGQRQRVSIARAILKN 528
Cdd:PRK09493 81 MVFQQFYLFPHlTALENVMFGP-----LRVRGASK-EEAEKQAREllAKVGLAERAHHYPSELSGGQQQRVAIARALAVK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499421346 529 PPILILDEATSALDTEserLVQEALeRLMKT-----RTTIAIAHRLS-TIKNADEICVLYEGEIVERGRHEELLE 597
Cdd:PRK09493 155 PKLMLFDEPTSALDPE---LRHEVL-KVMQDlaeegMTMVIVTHEIGfAEKVASRLIFIDKGRIAEDGDPQVLIK 225
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
371-597 |
3.08e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 122.99 E-value: 3.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 371 NDRIEFKDISFSY-DGKREVLKHVNLTVPKGKTVALVGQSGSGKST---LVD--LLPryHDVQGGDITIDGTSIKDVRIA 444
Cdd:PRK13640 3 DNIVEFKHVSFTYpDSKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINglLLP--DDNPNSKITVDGITLTAKTVW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 445 DLRSLIGNV--NQEAILFNDTFFNNIAFGVEN---------ATMEQVIEAAKIAnahDFIMEKPEgyntnigdrggKLSG 513
Cdd:PRK13640 81 DIREKVGIVfqNPDNQFVGATVGDDVAFGLENravprpemiKIVRDVLADVGML---DYIDSEPA-----------NLSG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 514 GQRQRVSIARAILKNPPILILDEATSALDTESERLVQEALERLMKTR--TTIAIAHRLSTIKNADEICVLYEGEIVERGR 591
Cdd:PRK13640 147 GQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGS 226
|
....*.
gi 499421346 592 HEELLE 597
Cdd:PRK13640 227 PVEIFS 232
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
97-311 |
3.72e-31 |
|
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: 123.01 E-value: 3.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 97 LFLALMTLFKTSCyFASSAVMIPLRT---GVVRDIRIMVYAKVMRLPMGFFSEERKGDIIARMSGDVGEVENSITSSLDM 173
Cdd:cd18573 43 FALALLGVFVVGA-AANFGRVYLLRIageRIVARLRKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSD 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 174 LIKSPIMIILYFITLIATSWKLTLFTVLVLPAMGWLMGKVGRKLKRQSLEAQGKWSDTMSQLEETLGGLRIIKAFIAEDR 253
Cdd:cd18573 122 GLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERK 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499421346 254 MIDRFTRCSNELRDAVNKVAMRQALAHPMSEFLGTILIVSVLWFGGALILghNSSLTA 311
Cdd:cd18573 202 EVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLYYGGSLVA--SGELTV 257
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
374-595 |
6.82e-31 |
|
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: 120.75 E-value: 6.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYDGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRSL---I 450
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLrrqI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 451 GNVNQ-----------EAILF----NDTFFNNIAFGVENATMEQVIEAAKIANAHDFIMEkpegyntnigdRGGKLSGGQ 515
Cdd:cd03256 81 GMIFQqfnlierlsvlENVLSgrlgRRSTWRSLFGLFPKEEKQRALAALERVGLLDKAYQ-----------RADQLSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 516 RQRVSIARAILKNPPILILDEATSALDTESERLVQEALERLMKTR--TTIAIAHRLSTIK-NADEICVLYEGEIVERGRH 592
Cdd:cd03256 150 QQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEgiTVIVSLHQVDLAReYADRIVGLKDGRIVFDGPP 229
|
...
gi 499421346 593 EEL 595
Cdd:cd03256 230 AEL 232
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
371-597 |
7.70e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 121.40 E-value: 7.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 371 NDRIEFKDISFSYDGKRE-VLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRSL 449
Cdd:PRK13648 5 NSIIVFKNVSFQYQSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 450 IGNV--NQEAILFNDTFFNNIAFGVENATM------EQVIEAAKIANAHDFIMEKPEGyntnigdrggkLSGGQRQRVSI 521
Cdd:PRK13648 85 IGIVfqNPDNQFVGSIVKYDVAFGLENHAVpydemhRRVSEALKQVDMLERADYEPNA-----------LSGGQKQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 522 ARAILKNPPILILDEATSALDTESE----RLVQEALERlmKTRTTIAIAHRLSTIKNADEICVLYEGEIVERGRHEELLE 597
Cdd:PRK13648 154 AGVLALNPSVIILDEATSMLDPDARqnllDLVRKVKSE--HNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
374-597 |
8.57e-31 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 123.67 E-value: 8.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYDGKReVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADlRSlIGNV 453
Cdd:COG3842 6 LELENVSKRYGDVT-ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEK-RN-VGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 454 NQEAILF-NDTFFNNIAFGVENATM------EQVIEAAKIanahdfimekpegynTNIGDRGGK----LSGGQRQRVSIA 522
Cdd:COG3842 83 FQDYALFpHLTVAENVAFGLRMRGVpkaeirARVAELLEL---------------VGLEGLADRyphqLSGGQQQRVALA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 523 RAILKNPPILILDEATSALDTES-ERLVQEaLERLMKTR--TTIAIAHRLS---TIknADEICVLYEGEIVERGRHEELL 596
Cdd:COG3842 148 RALAPEPRVLLLDEPLSALDAKLrEEMREE-LRRLQRELgiTFIYVTHDQEealAL--ADRIAVMNDGRIEQVGTPEEIY 224
|
.
gi 499421346 597 E 597
Cdd:COG3842 225 E 225
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
374-595 |
9.64e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 121.67 E-value: 9.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYDGK----REVLKHVNLTVPKGKTVALVGQSGSGKSTLVD-----LLPRYHDVQGGDITID-GTSIKDVRi 443
Cdd:PRK13634 3 ITFQKVEHRYQYKtpfeRRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQhlnglLQPTSGTVTIGERVITaGKKNKKLK- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 444 aDLRSLIGNVNQ--EAILFNDTFFNNIAFGVENATMEQViEAAKIANAhdfiMEKPEGYNTNIGDRGG-KLSGGQRQRVS 520
Cdd:PRK13634 82 -PLRKKVGIVFQfpEHQLFEETVEKDICFGPMNFGVSEE-DAKQKARE----MIELVGLPEELLARSPfELSGGQMRRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499421346 521 IARAILKNPPILILDEATSALDTESERLVQEALERLMKTR--TTIAIAHRLSTIKN-ADEICVLYEGEIVERGRHEEL 595
Cdd:PRK13634 156 IAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKglTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREI 233
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
84-328 |
1.19e-30 |
|
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: 121.44 E-value: 1.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 84 QDNGPTTALIFLGLFLALMTLFKTSCYFASSAvmiplRTG--VVRDIRIMVYAKVMRLPMGFFSEERKGDIIARMSGDVG 161
Cdd:cd18546 33 GDLGVLLLAAAAYLAVVLAGWVAQRAQTRLTG-----RTGerLLYDLRLRVFAHLQRLSLDFHERETSGRIMTRMTSDID 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 162 EVENSITSSLDMLIKSPIMIILYFITLIATSWKLTLFTVLVLPAMGWLMGKVGRKLKRQSLEAQGKWSDTMSQLEETLGG 241
Cdd:cd18546 108 ALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALATRWFRRRSSRAYRRARERIAAVNADLQETLAG 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 242 LRIIKAFIAEDRMIDRFTRCSNELRDAvNKVAMR-QALAHPMSEFLGTILIVSVLWFGGALILGHNSS---LTAptFIFY 317
Cdd:cd18546 188 IRVVQAFRRERRNAERFAELSDDYRDA-RLRAQRlVAIYFPGVELLGNLATAAVLLVGAWRVAAGTLTvgvLVA--FLLY 264
|
250
....*....|.
gi 499421346 318 MVILYSVINPL 328
Cdd:cd18546 265 LRRFFAPIQQL 275
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
370-599 |
1.37e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 120.99 E-value: 1.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 370 MNDRIEFKDISFSYDGKRE--VLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLR 447
Cdd:PRK13650 1 MSNIIEVKNLTFKYKEDQEkyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 448 SLIGNV--NQEAILFNDTFFNNIAFGVENATM------EQVIEAAKIANAHDFIMEKPegyntnigdrgGKLSGGQRQRV 519
Cdd:PRK13650 81 HKIGMVfqNPDNQFVGATVEDDVAFGLENKGIpheemkERVNEALELVGMQDFKEREP-----------ARLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 520 SIARAILKNPPILILDEATSALDTESeRLvqEALERLMKTR-----TTIAIAHRLSTIKNADEICVLYEGEiVER----- 589
Cdd:PRK13650 150 AIAGAVAMRPKIIILDEATSMLDPEG-RL--ELIKTIKGIRddyqmTVISITHDLDEVALSDRVLVMKNGQ-VEStstpr 225
|
250
....*....|...
gi 499421346 590 ---GRHEELLELD 599
Cdd:PRK13650 226 elfSRGNDLLQLG 238
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
91-348 |
2.16e-30 |
|
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: 121.04 E-value: 2.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 91 ALIFLGLFLALMTLFKTSCYFASSavmipLRTGVVRDIRIMVYAKVMRLPMGFFSEERKGDIIARMSGDVGEVENSITSS 170
Cdd:cd18545 43 ALLFLALNLVNWVASRLRIYLMAK-----VGQRILYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 171 LDMLIKSPIMIILYFITLIATSWKLTLFTVLVLPAMGWLMGKVGRKLKRQSLEAQGKWSDTMSQLEETLGGLRIIKAFIA 250
Cdd:cd18545 118 LINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAR 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 251 EDRMIDRFTRCSNELRDAVNKVAMRQALAHPMSEFLGTILIVSVLWFGGALILGHNSSL-TAPTFIFYMVILYSVINPLK 329
Cdd:cd18545 198 EDENEEIFDELNRENRKANMRAVRLNALFWPLVELISALGTALVYWYGGKLVLGGAITVgVLVAFIGYVGRFWQPIRNLS 277
|
250 260
....*....|....*....|
gi 499421346 330 DFakagYN-IPKGLASMERV 348
Cdd:cd18545 278 NF----YNqLQSAMASAERI 293
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
374-596 |
2.58e-30 |
|
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: 119.42 E-value: 2.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYDGKReVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRY-HDVQGGDITIDGTSIKDVRIADLRSLIGN 452
Cdd:COG1119 4 LELRNVTVRRGGKT-ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDlPPTYGNDVRLFGERRGGEDVWELRKRIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 453 VN---QEAILFNDT--------FFNNIafGV-ENATMEQVIEAAKIAnaHDFIMEKpegyntnIGDRG-GKLSGGQRQRV 519
Cdd:COG1119 83 VSpalQLRFPRDETvldvvlsgFFDSI--GLyREPTDEQRERARELL--ELLGLAH-------LADRPfGTLSQGEQRRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 520 SIARAILKNPPILILDEATSALDTESERLVQEALERLMKT--RTTIAIAHRLstiknaDEI--CV-----LYEGEIVERG 590
Cdd:COG1119 152 LIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEgaPTLVLVTHHV------EEIppGIthvllLKDGRVVAAG 225
|
....*.
gi 499421346 591 RHEELL 596
Cdd:COG1119 226 PKEEVL 231
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
374-586 |
7.39e-30 |
|
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: 117.12 E-value: 7.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYDGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVR---IADLRSLI 450
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 451 GNVNQEA-ILFNDTFFNNIAFGVENATMEQVIEAAKIANAHDFImekpeGYNTNIGDRGGKLSGGQRQRVSIARAILKNP 529
Cdd:cd03292 81 GVVFQDFrLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELV-----GLSHKHRALPAELSGGEQQRVAIARAIVNSP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499421346 530 PILILDEATSALDTESERLVQEALERLMKTRTTIAIAHRLSTIKNA--DEICVLYEGEI 586
Cdd:cd03292 156 TILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTtrHRVIALERGKL 214
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
374-591 |
8.67e-30 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 120.29 E-value: 8.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYD-GKREV--LKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRSL- 449
Cdd:PRK11153 2 IELKNISKVFPqGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 450 --IGNVNQEailFN----DTFFNNIAFGVE---------NATMEQVIEAAKIANAHDFimekpegYNTNigdrggkLSGG 514
Cdd:PRK11153 82 rqIGMIFQH---FNllssRTVFDNVALPLElagtpkaeiKARVTELLELVGLSDKADR-------YPAQ-------LSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 515 QRQRVSIARAILKNPPILILDEATSALDTESERLVQEALERLMKTR--TTIAIAHRLSTIKN-ADEICVLYEGEIVERGR 591
Cdd:PRK11153 145 QKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELglTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGT 224
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
77-348 |
1.45e-29 |
|
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: 118.41 E-value: 1.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 77 YYVSQMI----QDNGPTT---ALIFLGLFLALMTLFKTSCYFASSAVMiplrTGVVRDIRIMVYAKVMRLPMGFFSEERK 149
Cdd:cd18572 17 HYTGAVIdavvADGSREAfyrAVLLLLLLSVLSGLFSGLRGGCFSYAG----TRLVRRLRRDLFRSLLRQDIAFFDATKT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 150 GDIIARMSGDVGEVENSITSSLDMLIKSPIMIILYFITLIATSWKLTLFTVLVLPAMGWLMGKVGRKLKRQSLEAQGKWS 229
Cdd:cd18572 93 GELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYYRKLSKEIQDALA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 230 DTMSQLEETLGGLRIIKAFIAEDRMIDRFTRCSNELRdavnKVAMRQALA----HPMSEFLGTILIVSVLWFGGALILgh 305
Cdd:cd18572 173 EANQVAEEALSNIRTVRSFATEEREARRYERALDKAL----KLSVRQALAyagyVAVNTLLQNGTQVLVLFYGGHLVL-- 246
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 499421346 306 NSSLTAPTFIFYMVILYSVINPLKDFAKAGYNIPKGLASMERV 348
Cdd:cd18572 247 SGRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGAAEKV 289
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
385-595 |
2.37e-29 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 118.68 E-value: 2.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 385 GKREVLK---HVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRSLIGNVnQeaILFN 461
Cdd:COG4608 26 RTVGVVKavdGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLRRRM-Q--MVFQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 462 DTF--FNN-------IAFGVENATMEQVIEAAKIANAhdfIMEK----PEGYNtnigdR-GGKLSGGQRQRVSIARAILK 527
Cdd:COG4608 103 DPYasLNPrmtvgdiIAEPLRIHGLASKAERRERVAE---LLELvglrPEHAD-----RyPHEFSGGQRQRIGIARALAL 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499421346 528 NPPILILDEATSALDTeSerlVQeA-----LERLMKTR--TTIAIAHRLSTIKN-ADEICVLYEGEIVERGRHEEL 595
Cdd:COG4608 175 NPKLIVCDEPVSALDV-S---IQ-AqvlnlLEDLQDELglTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDEL 245
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
75-347 |
1.05e-28 |
|
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: 116.01 E-value: 1.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 75 FYYYVSQMIQD---NGPTTALIFLGLFLALMTLFKTSCYFASSA---VMiplrtGV--VRDIRIMVYAKVMRLPMGFFSE 146
Cdd:cd18549 21 FPLIVRYIIDDllpSKNLRLILIIGAILLALYILRTLLNYFVTYwghVM-----GAriETDMRRDLFEHLQKLSFSFFDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 147 ERKGDIIARMSGDVGEVensitSSL------DMLIkSPIMIILYFITLIATSWKLTLFTVLVLPAMGWLMGKVGRKLKRQ 220
Cdd:cd18549 96 NKTGQLMSRITNDLFDI-----SELahhgpeDLFI-SIITIIGSFIILLTINVPLTLIVFALLPLMIIFTIYFNKKMKKA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 221 SLEAQGKWSDTMSQLEETLGGLRIIKAFIAEDRMIDRFTRCSNELRDAVNKVAMRQALAHPMSEFLGTILIVSVLWFGGA 300
Cdd:cd18549 170 FRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDRFLESKKKAYKAMAYFFSGMNFFTNLLNLVVLVAGGY 249
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 499421346 301 LILghNSSLTAPTFIFYMVILYSVINPLKDFAKAGYNIPKGLASMER 347
Cdd:cd18549 250 FII--KGEITLGDLVAFLLYVNVFIKPIRRLVNFTEQYQKGMAGFER 294
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
13-597 |
2.01e-28 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 121.42 E-value: 2.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 13 SPYKKYIGWAILLNILSAVFNVFSFTLLIPIldilfktgeNNKVYEYMeWGTAGFKDVAINNFYYYVsqmiqdngpttAL 92
Cdd:PTZ00243 949 STYVAYLRFCGGLHAAGFVLATFAVTELVTV---------SSGVWLSM-WSTRSFKLSAATYLYVYL-----------GI 1007
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 93 IFLGLFLALMTLFktSCYFAssavmipLRTGVVRDIRIMVYAkVMRLPMGFFSEERKGDIIARMSGDVGEVENSITSSLD 172
Cdd:PTZ00243 1008 VLLGTFSVPLRFF--LSYEA-------MRRGSRNMHRDLLRS-VSRGTMSFFDTTPLGRILNRFSRDIDILDNTLPMSYL 1077
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 173 MLIKSPIMIILYFITLIATSwkltLFTVLVLPAMGWLMGKV-------GRKLKRQSLEAQgkwSDTMSQLEETLGGLRII 245
Cdd:PTZ00243 1078 YLLQCLFSICSSILVTSASQ----PFVLVALVPCGYLYYRLmqfynsaNREIRRIKSVAK---SPVFTLLEEALQGSATI 1150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 246 KAF------IAED-RMIDRFTRCSNeLRDAVNK-VAMRqalahpmSEFLGTILIVSVLWFG-GALILGHNS--------S 308
Cdd:PTZ00243 1151 TAYgkahlvMQEAlRRLDVVYSCSY-LENVANRwLGVR-------VEFLSNIVVTVIALIGvIGTMLRATSqeiglvslS 1222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 309 LTAPT-------FIFYMV-ILYSVINPLKDFAKAGYNIPK-GLASM-ERVDKILKAENNIKEI-----------PNPKPL 367
Cdd:PTZ00243 1223 LTMAMqttatlnWLVRQVaTVEADMNSVERLLYYTDEVPHeDMPELdEEVDALERRTGMAADVtgtvviepaspTSAAPH 1302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 368 TGMNDRIEFKDISFSY-DGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADL 446
Cdd:PTZ00243 1303 PVQAGSLVFEGVQMRYrEGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLREL 1382
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 447 RSLIGNVNQEAILFNDTFFNNIAFGVEnATMEQVIEAAKIANAHDFIMEKPEGYNTNIGDRGGKLSGGQRQRVSIARAIL 526
Cdd:PTZ00243 1383 RRQFSMIPQDPVLFDGTVRQNVDPFLE-ASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALL 1461
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499421346 527 KNPPILIL-DEATSALDTESERLVQEALERLMKTRTTIAIAHRLSTIKNADEICVLYEGEIVERGRHEELLE 597
Cdd:PTZ00243 1462 KKGSGFILmDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVM 1533
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
390-597 |
2.44e-28 |
|
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: 119.40 E-value: 2.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 390 LKHVNLTVPKGKTVALVGQSGSGKSTL----VDLLPryhdvQGGDITIDGTSIKDVRIADLRSLIGNVnQeaILFNDTF- 464
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLglalLRLIP-----SEGEIRFDGQDLDGLSRRALRPLRRRM-Q--VVFQDPFg 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 465 -FN---NIA------FGV------ENATMEQVIEA-------AKIAN--AHDFimekpegyntnigdrggklSGGQRQRV 519
Cdd:COG4172 374 sLSprmTVGqiiaegLRVhgpglsAAERRARVAEAleevgldPAARHryPHEF-------------------SGGQRQRI 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 520 SIARAILKNPPILILDEATSALDteseRLVQ----EALERLMKTR--TTIAIAHRLSTIKN-ADEICVLYEGEIVERGRH 592
Cdd:COG4172 435 AIARALILEPKLLVLDEPTSALD----VSVQaqilDLLRDLQREHglAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPT 510
|
....*
gi 499421346 593 EELLE 597
Cdd:COG4172 511 EQVFD 515
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
374-590 |
4.22e-28 |
|
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: 111.96 E-value: 4.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYdGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADlRSlIGNV 453
Cdd:cd03301 1 VELENVTKRF-GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD-RD-IAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 454 NQEAILF-NDTFFNNIAFGVENATM------EQVIEAAKIANAHDFIMEKPEgyntnigdrggKLSGGQRQRVSIARAIL 526
Cdd:cd03301 78 FQNYALYpHMTVYDNIAFGLKLRKVpkdeidERVREVAELLQIEHLLDRKPK-----------QLSGGQRQRVALGRAIV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499421346 527 KNPPILILDEATSALDTESERLVQEALERLMKT--RTTIAIAH-RLSTIKNADEICVLYEGEIVERG 590
Cdd:cd03301 147 REPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRlgTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
380-597 |
5.24e-28 |
|
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: 112.43 E-value: 5.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 380 SFSYDGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRiADLRSlIGNVNQEAIL 459
Cdd:cd03299 5 NLSKDWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLP-PEKRD-ISYVPQNYAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 460 F-NDTFFNNIAFGVENATM------EQVIEAAKIANAHDFIMEKPEgyntnigdrggKLSGGQRQRVSIARAILKNPPIL 532
Cdd:cd03299 83 FpHMTVYKNIAYGLKKRKVdkkeieRKVLEIAEMLGIDHLLNRKPE-----------TLSGGEQQRVAIARALVVNPKIL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499421346 533 ILDEATSALDTESERLVQEALERLMKTR--TTIAIAHRLSTIKN-ADEICVLYEGEIVERGRHEELLE 597
Cdd:cd03299 152 LLDEPFSALDVRTKEKLREELKKIRKEFgvTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFK 219
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
379-597 |
5.48e-28 |
|
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: 118.25 E-value: 5.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 379 ISF-SYDGKREVLKHVNLTVPKGKTVALVGQSGSGKS----TLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRSLIGN- 452
Cdd:COG4172 14 VAFgQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRIRGNr 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 453 ---VNQEAI--LfndtffnNIAFGVEnatmEQVIEAAKI------ANAHDFIME--------KPEgynTNIGDRGGKLSG 513
Cdd:COG4172 94 iamIFQEPMtsL-------NPLHTIG----KQIAEVLRLhrglsgAAARARALEllervgipDPE---RRLDAYPHQLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 514 GQRQRVSIARAILKNPPILILDEATSALDTESERLVQEALERLmKTRTTIA---IAHRLSTIKN-ADEICVLYEGEIVER 589
Cdd:COG4172 160 GQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDL-QRELGMAlllITHDLGVVRRfADRVAVMRQGEIVEQ 238
|
....*...
gi 499421346 590 GRHEELLE 597
Cdd:COG4172 239 GPTAELFA 246
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
377-587 |
9.28e-28 |
|
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: 110.81 E-value: 9.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 377 KDISFSYDGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGtsiKDVRIADLRSLIGNVNQE 456
Cdd:cd03226 3 ENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKERRKSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 457 A--ILFNDTFFNNIAFGVENA--TMEQVIEAAKIANAHDFIMEKPEgyntnigdrggKLSGGQRQRVSIARAILKNPPIL 532
Cdd:cd03226 80 VdyQLFTDSVREELLLGLKELdaGNEQAETVLKDLDLYALKERHPL-----------SLSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499421346 533 ILDEATSALDTESERLVQEALERLMK-TRTTIAIAHRLSTIKN-ADEICVLYEGEIV 587
Cdd:cd03226 149 IFDEPTSGLDYKNMERVGELIRELAAqGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
374-597 |
1.15e-27 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 115.04 E-value: 1.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYDGKrEVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRiADLRSlIGNV 453
Cdd:PRK09452 15 VELRGISKSFDGK-EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP-AENRH-VNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 454 NQEAILF-NDTFFNNIAFG-----VENATME-QVIEAAKIANAHDFIMEKPEgyntnigdrggKLSGGQRQRVSIARAIL 526
Cdd:PRK09452 92 FQSYALFpHMTVFENVAFGlrmqkTPAAEITpRVMEALRMVQLEEFAQRKPH-----------QLSGGQQQRVAIARAVV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499421346 527 KNPPILILDEATSALDTESERLVQEALERLMKTR--TTIAIAH-RLSTIKNADEICVLYEGEIVERGRHEELLE 597
Cdd:PRK09452 161 NKPKVLLLDESLSALDYKLRKQMQNELKALQRKLgiTFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPREIYE 234
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
370-599 |
1.32e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 112.52 E-value: 1.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 370 MNDRIEFKDISFSYDGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRSL 449
Cdd:PRK13647 1 MDNIIEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 450 IGNVNQEA--ILFNDTFFNNIAFGVENATM------EQVIEAAKIANAHDFiMEKPEGYntnigdrggkLSGGQRQRVSI 521
Cdd:PRK13647 81 VGLVFQDPddQVFSSTVWDDVAFGPVNMGLdkdeveRRVEEALKAVRMWDF-RDKPPYH----------LSYGQKKRVAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 522 ARAILKNPPILILDEATSALDTESERLVQEALERLMKTRTTIAIA-HRLS-TIKNADEICVLYEGEIVERGRHEELLELD 599
Cdd:PRK13647 150 AGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDlAAEWADQVIVLKEGRVLAEGDKSLLTDED 229
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
374-590 |
1.48e-27 |
|
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: 110.38 E-value: 1.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYdGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGtsIKDVRIADLRSLIGnv 453
Cdd:cd03268 1 LKTNDLTKTY-GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDG--KSYQKNIEALRRIG-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 454 nqeAILFNDTFFNNI-----------AFGVENATMEQVIEAAKIANAHDfimekpegyntnigDRGGKLSGGQRQRVSIA 522
Cdd:cd03268 76 ---ALIEAPGFYPNLtarenlrllarLLGIRKKRIDEVLDVVGLKDSAK--------------KKVKGFSLGMKQRLGIA 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 523 RAILKNPPILILDEATSALDTESERLVQEALERLMKTRTTIAIA-HRLSTI-KNADEICVLYEGEIVERG 590
Cdd:cd03268 139 LALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISsHLLSEIqKVADRIGIINKGKLIEEG 208
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
364-599 |
1.63e-27 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 111.80 E-value: 1.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 364 PKPLTGMNDRIEFKDISFSYdGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHD-VQG----GDITIDGTSI 438
Cdd:PRK14243 1 TSTLNGTETVLRTENLNVYY-GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlIPGfrveGKVTFHGKNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 439 --KDVRIADLRSLIGNVNQEAILFNDTFFNNIAFGVE----NATMEQVIEAA-KIANAHDFIMEKpegyntnIGDRGGKL 511
Cdd:PRK14243 80 yaPDVDPVEVRRRIGMVFQKPNPFPKSIYDNIAYGARingyKGDMDELVERSlRQAALWDEVKDK-------LKQSGLSL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 512 SGGQRQRVSIARAILKNPPILILDEATSALDTESERLVQEALERLMKTRTTIAIAHRLSTIKNADEICVLYEGEIVERG- 590
Cdd:PRK14243 153 SGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTEGGg 232
|
....*....
gi 499421346 591 RHEELLELD 599
Cdd:PRK14243 233 RYGYLVEFD 241
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
19-348 |
2.05e-27 |
|
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: 112.66 E-value: 2.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 19 IGWAILLNILSAVFNVFSFTLLIPILDILFKtgennkvyeymewGTAGFKDVainnfyyyVSQMIQDNGPTTALIFLGLF 98
Cdd:cd18565 1 LVLGLLASILNRLFDLAPPLLIGVAIDAVFN-------------GEASFLPL--------VPASLGPADPRGQLWLLGGL 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 99 LALMTLFKTSCYFASSAVMIPLRTGVVRDIRIMVYAKVMRLPMGFFSEERKGDIIARMSGDVGEVENSITSSLDMLIKSP 178
Cdd:cd18565 60 TVAAFLLESLFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 179 IMIILYFITLIATSWKLTLFTVLVLPAMGWLMGKVGRKLKRQSLEAQGKWSDTMSQLEETLGGLRIIKAFIAEDRMIDRF 258
Cdd:cd18565 140 VTVLGIGAILFYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERERV 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 259 TRCSNELRDAvNKVAMRQALAH-PMSEFLGTILIVSVLWFGGALIL----GHNSSLTAPTFIFYMVILYSVINPLKDFAK 333
Cdd:cd18565 220 ADASEEYRDA-NWRAIRLRAAFfPVIRLVAGAGFVATFVVGGYWVLdgppLFTGTLTVGTLVTFLFYTQRLLWPLTRLGD 298
|
330
....*....|....*
gi 499421346 334 AGYNIPKGLASMERV 348
Cdd:cd18565 299 LIDQYQRAMASAKRV 313
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
374-597 |
2.17e-27 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 113.70 E-value: 2.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYdGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLL-----PryhdvQGGDITIDGtsiKDVRIA---- 444
Cdd:COG1118 3 IEVRNISKRF-GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIagletP-----DSGRIVLNG---RDLFTNlppr 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 445 DLRslIGNVNQEAILF-NDTFFNNIAFGvenATMEQVIEAAKIANAHDFI----MEkpegyntNIGDR-GGKLSGGQRQR 518
Cdd:COG1118 74 ERR--VGFVFQHYALFpHMTVAENIAFG---LRVRPPSKAEIRARVEELLelvqLE-------GLADRyPSQLSGGQRQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 519 VSIARAILKNPPILILDEATSALDTEserlVQEALER-LMKT-----RTTIAIAH------RLstiknADEICVLYEGEI 586
Cdd:COG1118 142 VALARALAVEPEVLLLDEPFGALDAK----VRKELRRwLRRLhdelgGTTVFVTHdqeealEL-----ADRVVVMNQGRI 212
|
250
....*....|.
gi 499421346 587 VERGRHEELLE 597
Cdd:COG1118 213 EQVGTPDEVYD 223
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
1-536 |
2.96e-27 |
|
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: 116.05 E-value: 2.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 1 MKEFLQLMRrfvsPYKKYIGWAILLNILSAVFNVfsftLLIPIldilfktgennkvyeymewgtagfkdvaINNfyyyVS 80
Cdd:COG4615 1 MNLLRLLLR----ESRWLLLLALLLGLLSGLANA----GLIAL----------------------------INQ----AL 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 81 QMIQDNGPTTALIFLGLFLALMTlfktsCYFASSAVMIPLRTGVVRDIRIMVYAKVMRLPMGFFSEERKGDIIARMSGDV 160
Cdd:COG4615 41 NATGAALARLLLLFAGLLVLLLL-----SRLASQLLLTRLGQHAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDV 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 161 GEVENSiTSSLDMLIKSPIMIILYFITLIATSWKLTLFTVLVLP---AMGWLMGKVGRKLKRQSLEAQGKWSDtmsQLEE 237
Cdd:COG4615 116 RTISQA-FVRLPELLQSVALVLGCLAYLAWLSPPLFLLTLVLLGlgvAGYRLLVRRARRHLRRAREAEDRLFK---HFRA 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 238 TLGGLRIIK-------AFIAEDrmidrFTRCSNELRDAVNKVAMRQALAHPMSEFLGTILIVSVLWFggALILGHNSSLT 310
Cdd:COG4615 192 LLEGFKELKlnrrrrrAFFDED-----LQPTAERYRDLRIRADTIFALANNWGNLLFFALIGLILFL--LPALGWADPAV 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 311 APTFIfyMVILYsVINPLKDFAKAgynIP---KGLASMERVDKILKAENNIKEIPNPKPLTGMN---DRIEFKDISFSYD 384
Cdd:COG4615 265 LSGFV--LVLLF-LRGPLSQLVGA---LPtlsRANVALRKIEELELALAAAEPAAADAAAPPAPadfQTLELRGVTYRYP 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 385 GKRE----VLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPR-YHDvQGGDITIDGTSIKDVRIADLRSLIGNVNQEAIL 459
Cdd:COG4615 339 GEDGdegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGlYRP-ESGEILLDGQPVTADNREAYRQLFSAVFSDFHL 417
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499421346 460 FNDTFfnNIAFGVENATMEQVIEAAKIAnahdfimEKPEGYNTNIGDRggKLSGGQRQRVSIARAILKNPPILILDE 536
Cdd:COG4615 418 FDRLL--GLDGEADPARARELLERLELD-------HKVSVEDGRFSTT--DLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
374-590 |
7.39e-27 |
|
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: 108.43 E-value: 7.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYDGKReVLKHVNLTVPKGKTvALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIAdLRSLIGNV 453
Cdd:cd03264 1 LQLENLTKRYGKKR-ALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK-LRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 454 NQEailFN-------DTFFNNIAF--GVENATM-EQVIEAAKIANAHDFIMEKPegyntnigdrgGKLSGGQRQRVSIAR 523
Cdd:cd03264 78 PQE---FGvypnftvREFLDYIAWlkGIPSKEVkARVDEVLELVNLGDRAKKKI-----------GSLSGGMRRRVGIAQ 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499421346 524 AILKNPPILILDEATSALDTEsERL-VQEALERLMKTRTTIAIAHRLSTIKN-ADEICVLYEGEIVERG 590
Cdd:cd03264 144 ALVGDPSILIVDEPTAGLDPE-ERIrFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
374-587 |
9.20e-27 |
|
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: 106.36 E-value: 9.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYDGKReVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGtsiKDVRIADLRslignv 453
Cdd:cd03216 1 LELRGITKRFGGVK-ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG---KEVSFASPR------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 454 nqEAIlfndtffnniafgvenatmeqvieAAKIANAHdfimekpegyntnigdrggKLSGGQRQRVSIARAILKNPPILI 533
Cdd:cd03216 71 --DAR------------------------RAGIAMVY-------------------QLSVGERQMVEIARALARNARLLI 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499421346 534 LDEATSAL-DTESERLVqEALERLMKT-RTTIAIAHRLSTIKN-ADEICVLYEGEIV 587
Cdd:cd03216 106 LDEPTAALtPAEVERLF-KVIRRLRAQgVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
374-597 |
1.14e-26 |
|
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: 108.58 E-value: 1.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYDGKReVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADlRSlIGNV 453
Cdd:cd03296 3 IEVRNVSKRFGDFV-ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE-RN-VGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 454 NQEAILFND-TFFNNIAFGVENATMEQVIEAAKI-ANAHDFI-MEKPEGYntniGDR-GGKLSGGQRQRVSIARAILKNP 529
Cdd:cd03296 80 FQHYALFRHmTVFDNVAFGLRVKPRSERPPEAEIrAKVHELLkLVQLDWL----ADRyPAQLSGGQRQRVALARALAVEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499421346 530 PILILDEATSALDTESERLVQEALERLMKTR--TTIAIAHRLS-TIKNADEICVLYEGEIVERGRHEELLE 597
Cdd:cd03296 156 KVLLLDEPFGALDAKVRKELRRWLRRLHDELhvTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEVYD 226
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
373-580 |
3.89e-26 |
|
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: 106.02 E-value: 3.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 373 RIEFKDISFSYDGkREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLL-----PryhdvQGGDITIDGTSIKDVRiADLR 447
Cdd:COG4133 2 MLEAENLSCRRGE-RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILagllpP-----SAGEVLWNGEPIRDAR-EDYR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 448 SLIGNVNQEAILFND-TFFNNIAF-------GVENATMEQVIEAAKIANAhdfiMEKPegyntnigdrGGKLSGGQRQRV 519
Cdd:COG4133 75 RRLAYLGHADGLKPElTVRENLRFwaalyglRADREAIDEALEAVGLAGL----ADLP----------VRQLSAGQKRRV 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499421346 520 SIARAILKNPPILILDEATSALDTESERLVQEALERLMKTRTTIAIA-HRLSTIKNADEICV 580
Cdd:COG4133 141 ALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVLDL 202
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
405-597 |
5.44e-26 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 109.12 E-value: 5.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 405 LVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRiADLRSlIGNVNQEAILF-NDTFFNNIAFG-----VENATM- 477
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVP-PHLRH-INMVFQSYALFpHMTVEENVAFGlkmrkVPRAEIk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 478 EQVIEAAKIANAHDFIMEKPEgyntnigdrggKLSGGQRQRVSIARAILKNPPILILDEATSALDTESERLVQEALERLM 557
Cdd:TIGR01187 79 PRVLEALRLVQLEEFADRKPH-----------QLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQ 147
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499421346 558 KTR--TTIAIAHRLS-TIKNADEICVLYEGEIVERGRHEELLE 597
Cdd:TIGR01187 148 EQLgiTFVFVTHDQEeAMTMSDRIAIMRKGKIAQIGTPEEIYE 190
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
381-584 |
5.91e-26 |
|
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: 106.26 E-value: 5.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 381 FSYDGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLV-DLLPRYHDVQG----GDITIDGTSIKDVRIADlRSLIGNVNQ 455
Cdd:cd03290 8 FSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTLEGkvhwSNKNESEPSFEATRSRN-RYSVAYAAQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 456 EAILFNDTFFNNIAFG--VENATMEQVIEAAKIANAHDFImekPEGYNTNIGDRGGKLSGGQRQRVSIARAILKNPPILI 533
Cdd:cd03290 87 KPWLLNATVEENITFGspFNKQRYKAVTDACSLQPDIDLL---PFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499421346 534 LDEATSALDTE-SERLVQEALERLMK--TRTTIAIAHRLSTIKNADEICVLYEG 584
Cdd:cd03290 164 LDDPFSALDIHlSDHLMQEGILKFLQddKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
370-590 |
6.03e-26 |
|
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: 105.84 E-value: 6.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 370 MNDRIEFKDISFSYDgkrevlkhVNLTVPkGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIA-DL-- 446
Cdd:cd03297 2 LCVDIEKRLPDFTLK--------IDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKiNLpp 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 447 -RSLIGNVNQEAILF-NDTFFNNIAFGVE-NATMEQVIEAAKIANAHDFimekpegynTNIGDRG-GKLSGGQRQRVSIA 522
Cdd:cd03297 73 qQRKIGLVFQQYALFpHLNVRENLAFGLKrKRNREDRISVDELLDLLGL---------DHLLNRYpAQLSGGEKQRVALA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499421346 523 RAILKNPPILILDEATSALDTESERLVQEALERLMKT--RTTIAIAHRLSTI-KNADEICVLYEGEIVERG 590
Cdd:cd03297 144 RALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKNlnIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
374-594 |
9.64e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 107.44 E-value: 9.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYDGK----REVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSI--KDVRIADLR 447
Cdd:PRK13637 3 IKIENLTHIYMEGtpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 448 SLIGNVNQ--EAILFNDTFFNNIAFGVENATMEQVIEAAKIANAHDFIMEKPEGYNtnigDRGG-KLSGGQRQRVSIARA 524
Cdd:PRK13637 83 KKVGLVFQypEYQLFEETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYEDYK----DKSPfELSGGQKRRVAIAGV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499421346 525 ILKNPPILILDEATSALDTESERLVQEALERLMKTR--TTIAIAHRLSTI-KNADEICVLYEGEIVERGRHEE 594
Cdd:PRK13637 159 VAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYnmTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPRE 231
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
370-596 |
1.16e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 107.10 E-value: 1.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 370 MNDRIEFKDISFSYDGKREV--LKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLR 447
Cdd:PRK13642 1 MNKILEVENLVFKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 448 SLIGNV--NQEAILFNDTFFNNIAFGVENA------TMEQVIEAAKIANAHDFIMEKPegyntnigdrgGKLSGGQRQRV 519
Cdd:PRK13642 81 RKIGMVfqNPDNQFVGATVEDDVAFGMENQgipreeMIKRVDEALLAVNMLDFKTREP-----------ARLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 520 SIARAILKNPPILILDEATSALD----TESERLVQEALERLMktRTTIAIAHRLSTIKNADEICVLYEGEIVERGRHEEL 595
Cdd:PRK13642 150 AVAGIIALRPEIIILDESTSMLDptgrQEIMRVIHEIKEKYQ--LTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
.
gi 499421346 596 L 596
Cdd:PRK13642 228 F 228
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
375-601 |
1.20e-25 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 105.92 E-value: 1.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 375 EFKDISFSYDGKrEVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLL---PRYHdVQGGDITIDGTSIKDVRIaDLRSLIG 451
Cdd:COG0396 2 EIKNLHVSVEGK-EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmghPKYE-VTSGSILLDGEDILELSP-DERARAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 452 nvnqeaiLFndtffnnIAF-------GVEN------ATMEQVIEAAKIANAHDFIMEKPE--GYNTNIGDRG--GKLSGG 514
Cdd:COG0396 79 -------IF-------LAFqypveipGVSVsnflrtALNARRGEELSAREFLKLLKEKMKelGLDEDFLDRYvnEGFSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 515 QRQRVSIARAILKNPPILILDEATSALDTESERLVQEALERLM-KTRTTIAIAH--RLSTIKNADEICVLYEGEIVERGR 591
Cdd:COG0396 145 EKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRsPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGG 224
|
250
....*....|..
gi 499421346 592 HEELLELD--GY 601
Cdd:COG0396 225 KELALELEeeGY 236
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
372-596 |
1.37e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 106.15 E-value: 1.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 372 DRIEFKDISFSYdGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPR----YHDVQ-GGDITIDGTSIKDVRIADL 446
Cdd:PRK14247 2 NKIEIRDLKVSF-GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRlielYPEARvSGEVYLDGQDIFKMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 447 RSLIGNVNQ-EAILFNDTFFNNIAFGVE--------NATMEQVIEAAKIANAHDFIMEKpegyntnIGDRGGKLSGGQRQ 517
Cdd:PRK14247 81 RRRVQMVFQiPNPIPNLSIFENVALGLKlnrlvkskKELQERVRWALEKAQLWDEVKDR-------LDAPAGKLSGGQQQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 518 RVSIARAILKNPPILILDEATSALDTESERLVQEALERLMKTRTTIAIAH------RLStiknaDEICVLYEGEIVERGR 591
Cdd:PRK14247 154 RLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRIS-----DYVAFLYKGQIVEWGP 228
|
....*
gi 499421346 592 HEELL 596
Cdd:PRK14247 229 TREVF 233
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
374-590 |
1.47e-25 |
|
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: 104.88 E-value: 1.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYdgkREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTsikDVRIADL-RSLIGN 452
Cdd:cd03298 1 VRLDKIRFSY---GEQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGV---DVTAAPPaDRPVSM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 453 VNQEAILFND-TFFNNIAFGVE-----NATMEQVIEAA----KIANahdFIMEKPegyntnigdrgGKLSGGQRQRVSIA 522
Cdd:cd03298 75 LFQENNLFAHlTVEQNVGLGLSpglklTAEDRQAIEVAlarvGLAG---LEKRLP-----------GELSGGERQRVALA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499421346 523 RAILKNPPILILDEATSALDTEserLVQEALERLMKTR-----TTIAIAHRLSTIKN-ADEICVLYEGEIVERG 590
Cdd:cd03298 141 RVLVRDKPVLLLDEPFAALDPA---LRAEMLDLVLDLHaetkmTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
374-595 |
1.78e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 105.63 E-value: 1.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYdGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQ-----GGDITIDGTSIKDVRI--ADL 446
Cdd:PRK14239 6 LQVSDLSVYY-NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIYSPRTdtVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 447 RSLIGNVNQEAILFNDTFFNNIAFGV------ENATMEQVIEAA-KIANAHDFImeKPEGYNTNIGdrggkLSGGQRQRV 519
Cdd:PRK14239 85 RKEIGMVFQQPNPFPMSIYENVVYGLrlkgikDKQVLDEAVEKSlKGASIWDEV--KDRLHDSALG-----LSGGQQQRV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499421346 520 SIARAILKNPPILILDEATSALDTESERLVQEALERLMKTRTTIAIAHRL---STIknADEICVLYEGEIVERGRHEEL 595
Cdd:PRK14239 158 CIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMqqaSRI--SDRTGFFLDGDLIEYNDTKQM 234
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
374-596 |
1.91e-25 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 105.60 E-value: 1.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYDGKReVLKHVNLTVPKGKTVALVGQSGSGKSTL---VDLL--PRYHDVQGGDITIDGT---SIKDVRIAD 445
Cdd:PRK11264 4 IEVKNLVKKFHGQT-VLHGIDLEVKPGEVVAIIGPSGSGKTTLlrcINLLeqPEAGTIRVGDITIDTArslSQQKGLIRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 446 LRSLIGNVNQEAILF-NDTFFNNIAFG---VENATMEQVIEAAKIANAHDFIMEKPEGYNTnigdrggKLSGGQRQRVSI 521
Cdd:PRK11264 83 LRQHVGFVFQNFNLFpHRTVLENIIEGpviVKGEPKEEATARARELLAKVGLAGKETSYPR-------RLSGGQQQRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 522 ARAILKNPPILILDEATSALDTEserLVQEALERLM----KTRTTIAIAHRLSTIKN-ADEICVLYEGEIVERGRHEELL 596
Cdd:PRK11264 156 ARALAMRPEVILFDEPTSALDPE---LVGEVLNTIRqlaqEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALF 232
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
370-595 |
1.94e-25 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 110.11 E-value: 1.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 370 MNDRIEFKDISFSYDGKReVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGtsiKDVRIAD---- 445
Cdd:COG1129 1 AEPLLEMRGISKSFGGVK-ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDG---EPVRFRSprda 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 446 LRSLIGNVNQEAILFND-TFFNNIAFGVENATM------EQVIEAAKIANAHDFimekpegyNTNIGDRGGKLSGGQRQR 518
Cdd:COG1129 77 QAAGIAIIHQELNLVPNlSVAENIFLGREPRRGglidwrAMRRRARELLARLGL--------DIDPDTPVGDLSVAQQQL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 519 VSIARAILKNPPILILDEATSAL-DTESERLVqEALERLMKTRTTIA-IAHRLSTIKN-ADEICVLYEGEIVERGRHEEL 595
Cdd:COG1129 149 VEIARALSRDARVLILDEPTASLtEREVERLF-RIIRRLKAQGVAIIyISHRLDEVFEiADRVTVLRDGRLVGTGPVAEL 227
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
361-597 |
3.10e-25 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 108.00 E-value: 3.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 361 IPNPKPLTG--MNDRIEFKDISFSYDGKREVlKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSI 438
Cdd:PRK11607 5 IPRPQAKTRkaLTPLLEIRNLTKSFDGQHAV-DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 439 KDVriADLRSLIGNVNQEAILF-NDTFFNNIAFGVENATM------EQVIEAAKIANAHDFIMEKPEgyntnigdrggKL 511
Cdd:PRK11607 84 SHV--PPYQRPINMMFQSYALFpHMTVEQNIAFGLKQDKLpkaeiaSRVNEMLGLVHMQEFAKRKPH-----------QL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 512 SGGQRQRVSIARAILKNPPILILDEATSALDTE-SERL---VQEALERLmkTRTTIAIAH-RLSTIKNADEICVLYEGEI 586
Cdd:PRK11607 151 SGGQRQRVALARSLAKRPKLLLLDEPMGALDKKlRDRMqleVVDILERV--GVTCVMVTHdQEEAMTMAGRIAIMNRGKF 228
|
250
....*....|.
gi 499421346 587 VERGRHEELLE 597
Cdd:PRK11607 229 VQIGEPEEIYE 239
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
89-317 |
5.08e-25 |
|
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: 105.41 E-value: 5.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 89 TTALIFLGLFL--ALMTLFKTSCYFASSavmiplrTGVVRDIRIMVYAKVMRLPMGFFSEERKGDIIARMSGDVGEVENS 166
Cdd:cd18780 43 QAVLILLGVVLigSIATFLRSWLFTLAG-------ERVVARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 167 ITSSLDMLIKSPIMIILYFITLIATSWKLTLFTVLVLPA---MGWLMGKVGRKLKRQSLEAQGKWSDTMsqlEETLGGLR 243
Cdd:cd18780 116 VTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPlsiGAVIYGKYVRKLSKKFQDALAAASTVA---EESISNIR 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 244 IIKAFIAEDRMIDRFtrcsNELRDAVNKVAMRQALAHP-----MSeFLGTILIVSVLWFGGALIL-GHNS--SLTAptFI 315
Cdd:cd18780 193 TVRSFAKETKEVSRY----SEKINESYLLGKKLARASGgfngfMG-AAAQLAIVLVLWYGGRLVIdGELTtgLLTS--FL 265
|
..
gi 499421346 316 FY 317
Cdd:cd18780 266 LY 267
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
374-596 |
8.06e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 104.30 E-value: 8.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYDGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDV-RIADLRSLIGN 452
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFsKLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 453 V--NQEAILFNDTFFNNIAFGVENATMEQVIEAAKIANAHDFImeKPEGYNtnigDRGGK-LSGGQRQRVSIARAILKNP 529
Cdd:PRK13644 82 VfqNPETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEI--GLEKYR----HRSPKtLSGGQGQCVALAGILTMEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499421346 530 PILILDEATSALDTESERLVQEALERLM-KTRTTIAIAHRLSTIKNADEICVLYEGEIVERGRHEELL 596
Cdd:PRK13644 156 ECLIFDEVTSMLDPDSGIAVLERIKKLHeKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
89-334 |
9.77e-25 |
|
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: 104.86 E-value: 9.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 89 TTALIFLGLFLALMTLfktsCYFASSAVMIplrTG--VVRDIRIMVYAKVMRLPMGFFSEERKGDIIARMSGDVGEVENS 166
Cdd:cd18577 48 KYALYFVYLGIGSFVL----SYIQTACWTI---TGerQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDG 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 167 ITSSLDMLIKSpimiILYFITLIA----TSWKLTLFTVLVLPAM---GWLMGKVGRKLKRQSLEAQGKwsdTMSQLEETL 239
Cdd:cd18577 121 IGEKLGLLIQS----LSTFIAGFIiafiYSWKLTLVLLATLPLIaivGGIMGKLLSKYTKKEQEAYAK---AGSIAEEAL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 240 GGLRIIKAFIAEDRMIDRFTRCSNELRDAVNKVAMRQALAHPMSEFLGTILIVSVLWFGGALILGHNSSLTAPTFIFYMV 319
Cdd:cd18577 194 SSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLFFIIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAV 273
|
250 260
....*....|....*....|
gi 499421346 320 I-----LYSVINPLKDFAKA 334
Cdd:cd18577 274 LigafsLGQIAPNLQAFAKA 293
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
374-586 |
1.37e-24 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 105.70 E-value: 1.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYDGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADlRSlIGNV 453
Cdd:PRK11650 4 LKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD-RD-IAMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 454 NQEAILF-NDTFFNNIAFGVENATM------EQVIEAAKIANAHDFIMEKPEgyntnigdrggKLSGGQRQRVSIARAIL 526
Cdd:PRK11650 82 FQNYALYpHMSVRENMAYGLKIRGMpkaeieERVAEAARILELEPLLDRKPR-----------ELSGGQRQRVAMGRAIV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499421346 527 KNPPILILDEATSALDTeseRL-VQEALE-----RLMKTrTTIAIAH-RLSTIKNADEICVLYEGEI 586
Cdd:PRK11650 151 REPAVFLFDEPLSNLDA---KLrVQMRLEiqrlhRRLKT-TSLYVTHdQVEAMTLADRVVVMNGGVA 213
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
359-590 |
1.40e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 104.93 E-value: 1.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 359 KEIPNPKPLTGmNDRIEFKDISFSYDGKRE----VLKHVNLTVPKGKTVALVGQSGSGKSTLVD-----LLPRYHDVQGG 429
Cdd:PRK13631 8 KKLKVPNPLSD-DIILRVKNLYCVFDEKQEnelvALNNISYTFEKNKIYFIIGNSGSGKSTLVThfnglIKSKYGTIQVG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 430 DI-----------TIDGTSIKDVRIADLRSLIGNVNQ--EAILFNDTFFNNIAFGVENATMEQvIEAAKIANAHDFIMek 496
Cdd:PRK13631 87 DIyigdkknnhelITNPYSKKIKNFKELRRRVSMVFQfpEYQLFKDTIEKDIMFGPVALGVKK-SEAKKLAKFYLNKM-- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 497 peGYNTNIGDRGG-KLSGGQRQRVSIARAILKNPPILILDEATSALDTESER-LVQEALERLMKTRTTIAIAHRLSTI-K 573
Cdd:PRK13631 164 --GLDDSYLERSPfGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVlE 241
|
250
....*....|....*..
gi 499421346 574 NADEICVLYEGEIVERG 590
Cdd:PRK13631 242 VADEVIVMDKGKILKTG 258
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
374-601 |
1.61e-24 |
|
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: 101.45 E-value: 1.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYDGKrEVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLL---PRYhDVQGGDITIDGTSIKDVRIaDLRSLI 450
Cdd:cd03217 1 LEIKDLHVSVGGK-EILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImghPKY-EVTEGEILFKGEDITDLPP-EERARL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 451 GnvnqeaiLFndtffnnIAF-------GVENAtmeqvieaakianahDFIMEKPEGyntnigdrggkLSGGQRQRVSIAR 523
Cdd:cd03217 78 G-------IF-------LAFqyppeipGVKNA---------------DFLRYVNEG-----------FSGGEKKRNEILQ 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 524 AILKNPPILILDEATSALDTESERLVQEALERLM-KTRTTIAIAH--RLSTIKNADEICVLYEGEIVERGRHEELLELD- 599
Cdd:cd03217 118 LLLLEPDLAILDEPDSGLDIDALRLVAEVINKLReEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGDKELALEIEk 197
|
...
gi 499421346 600 -GY 601
Cdd:cd03217 198 kGY 200
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
374-587 |
3.97e-24 |
|
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: 100.66 E-value: 3.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSY-DGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDvRIADLRSLIGN 452
Cdd:cd03263 1 LQIRNLTKTYkKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 453 VNQEAILFND-TFFNNIAF-----GVENATMEQVIEAAKIAnahdfimekpegynTNIGD----RGGKLSGGQRQRVSIA 522
Cdd:cd03263 80 CPQFDALFDElTVREHLRFyarlkGLPKSEIKEEVELLLRV--------------LGLTDkankRARTLSGGMKRKLSLA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499421346 523 RAILKNPPILILDEATSALDTESERLVQEALERLMKTRTTIAIAHRLSTIKN-ADEICVLYEGEIV 587
Cdd:cd03263 146 IALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLR 211
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
374-591 |
1.17e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 100.97 E-value: 1.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYDG----KREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSI----KDVRIAD 445
Cdd:PRK13649 3 INLQNVSYTYQAgtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsKNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 446 LRSLIGNVNQ--EAILFNDTFFNNIAFGVENATMEQvIEAAKIANahdfimEKPE--GYNTNIGDRGG-KLSGGQRQRVS 520
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQNFGVSQ-EEAEALAR------EKLAlvGISESLFEKNPfELSGGQMRRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499421346 521 IARAILKNPPILILDEATSALDTESERLVQEALERLMKTRTTIA-IAHRLSTIKN-ADEICVLYEGEIVERGR 591
Cdd:PRK13649 156 IAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVlVTHLMDDVANyADFVYVLEKGKLVLSGK 228
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
374-593 |
1.42e-23 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 100.09 E-value: 1.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYdGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDG------TSIKDVRIADLR 447
Cdd:COG4161 3 IQLKNINCFY-GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIRLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 448 SLIGNVNQEAILFNDTffnniafgvenATMEQVIEA----AKIANAHdfIMEKPEGYNTN--IGDRGGK----LSGGQRQ 517
Cdd:COG4161 82 QKVGMVFQQYNLWPHL-----------TVMENLIEApckvLGLSKEQ--AREKAMKLLARlrLTDKADRfplhLSGGQQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499421346 518 RVSIARAILKNPPILILDEATSALDTESERLVQEALERLMKTR-TTIAIAHRLSTI-KNADEICVLYEGEIVERGRHE 593
Cdd:COG4161 149 RVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGiTQVIVTHEVEFArKVASQVVYMEKGRIIEQGDAS 226
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
370-597 |
1.43e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 100.30 E-value: 1.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 370 MNDRIEFKDISFSYdGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQG-----GDITIDGTSI--KDVR 442
Cdd:PRK14267 1 MKFAIETVNLRVYY-GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNIysPDVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 443 IADLRSLIGNVNQEAILF-NDTFFNNIAFGVE-------NATMEQVIE-AAKIANAHDFIMEKpegyntnIGDRGGKLSG 513
Cdd:PRK14267 80 PIEVRREVGMVFQYPNPFpHLTIYDNVAIGVKlnglvksKKELDERVEwALKKAALWDEVKDR-------LNDYPSNLSG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 514 GQRQRVSIARAILKNPPILILDEATSALDTESERLVQEALERLMKTRTTIAIAHR-LSTIKNADEICVLYEGEIVERGRH 592
Cdd:PRK14267 153 GQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPT 232
|
....*
gi 499421346 593 EELLE 597
Cdd:PRK14267 233 RKVFE 237
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
382-597 |
3.81e-23 |
|
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: 97.89 E-value: 3.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 382 SYDGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDV---RIAdlRSLIGNVNQEAI 458
Cdd:cd03224 8 AGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLpphERA--RAGIGYVPEGRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 459 LFND-TFFNNIAFGVEN-------ATMEQVIEAakianahdF--IMEKpegyntnIGDRGGKLSGGQRQRVSIARAILKN 528
Cdd:cd03224 86 IFPElTVEENLLLGAYArrrakrkARLERVYEL--------FprLKER-------RKQLAGTLSGGEQQMLAIARALMSR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499421346 529 PPILILDEATSALdteSERLVQE---ALERLMKTRTTIAI----AHRLSTIknADEICVLYEGEIVERGRHEELLE 597
Cdd:cd03224 151 PKLLLLDEPSEGL---APKIVEEifeAIRELRDEGVTILLveqnARFALEI--ADRAYVLERGRVVLEGTAAELLA 221
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
394-586 |
4.11e-23 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 97.62 E-value: 4.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 394 NLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIkdVRIADLRSLIGNVNQEAILFND-TFFNNIAFGV 472
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSH--TGLAPYQRPVSMLFQENNLFAHlTVRQNIGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 473 E-----NAT-MEQVIEAAKIANAHDFIMEKPegyntnigdrgGKLSGGQRQRVSIARAILKNPPILILDEATSALDtesE 546
Cdd:TIGR01277 96 HpglklNAEqQEKVVDAAQQVGIADYLDRLP-----------EQLSGGQRQRVALARCLVRPNPILLLDEPFSALD---P 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499421346 547 RLVQEALERLMKT-----RTTIAIAHRLS-TIKNADEICVLYEGEI 586
Cdd:TIGR01277 162 LLREEMLALVKQLcserqRTLLMVTHHLSdARAIASQIAVVSQGKI 207
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
374-596 |
4.74e-23 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 98.69 E-value: 4.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYdGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRSLIGNV 453
Cdd:PRK13548 3 LEARNLSVRL-GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 454 NQEAILfndTFfnniAFGVE-------------NATMEQVIEAAkianahdfiMEKpegynTNIGDRGGK----LSGGQR 516
Cdd:PRK13548 82 PQHSSL---SF----PFTVEevvamgraphglsRAEDDALVAAA---------LAQ-----VDLAHLAGRdypqLSGGEQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 517 QRVSIARAIL------KNPPILILDEATSALDTeserLVQEALERLMKTRTT------IAIAHRLstikN-----ADEIC 579
Cdd:PRK13548 141 QRVQLARVLAqlwepdGPPRWLLLDEPTSALDL----AHQHHVLRLARQLAHerglavIVVLHDL----NlaaryADRIV 212
|
250
....*....|....*..
gi 499421346 580 VLYEGEIVERGRHEELL 596
Cdd:PRK13548 213 LLHQGRLVADGTPAEVL 229
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
390-596 |
6.88e-23 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 101.26 E-value: 6.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 390 LKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRSL----IGNVNQE-AILFNDTF 464
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVrrkkIAMVFQSfALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 465 FNNIAFGVENATM------EQVIEAAKIANAHDFIMEKPEgyntnigdrggKLSGGQRQRVSIARAILKNPPILILDEAT 538
Cdd:PRK10070 124 LDNTAFGMELAGInaeerrEKALDALRQVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499421346 539 SALDTESERLVQEALERLM--KTRTTIAIAHRL-STIKNADEICVLYEGEIVERGRHEELL 596
Cdd:PRK10070 193 SALDPLIRTEMQDELVKLQakHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
387-597 |
9.51e-23 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 103.71 E-value: 9.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 387 REVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGditidgtsikdvRIADLRSlIGNVNQEAILFNDTFFN 466
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEG------------RVWAERS-IAYVPQQAWIMNATVRG 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 467 NIAFGVENATmEQVIEAAKIANAHDFIMEKPEGYNTNIGDRGGKLSGGQRQRVSIARAILKNPPILILDEATSALDTE-S 545
Cdd:PTZ00243 740 NILFFDEEDA-ARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHvG 818
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499421346 546 ERLVQEALERLMKTRTTIAIAHRLSTIKNADEICVLYEGEIVERGRHEELLE 597
Cdd:PTZ00243 819 ERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMR 870
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
374-597 |
1.10e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 98.65 E-value: 1.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYDGKR----EVLKHVNLTVPKGKTVALVGQSGSGKSTLVD-----LLPRYHDVQGGDITIDGTSiKDVRIA 444
Cdd:PRK13643 2 IKFEKVNYTYQPNSpfasRALFDIDLEVKKGSYTALIGHTGSGKSTLLQhlnglLQPTEGKVTVGDIVVSSTS-KQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 445 DLRSLIGNVNQ--EAILFNDTFFNNIAFGVENATMEQViEAAKIAnahdfiMEKPE--GYNTNIGDRGG-KLSGGQRQRV 519
Cdd:PRK13643 81 PVRKKVGVVFQfpESQLFEETVLKDVAFGPQNFGIPKE-KAEKIA------AEKLEmvGLADEFWEKSPfELSGGQMRRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 520 SIARAILKNPPILILDEATSALDTESERLVQEALERLMKT-RTTIAIAHRLSTIKN-ADEICVLYEGEIVERGRHEELLE 597
Cdd:PRK13643 154 AIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSgQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
370-595 |
1.27e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 98.24 E-value: 1.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 370 MNDRIEFKDISFSYDGKRE-----VLKHVNLTVPKGKTVALVGQSGSGKSTLVD-----LLPryhdvQGGDITIDGTSIK 439
Cdd:PRK13633 1 MNEMIKCKNVSYKYESNEEsteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKhmnalLIP-----SEGKVYVDGLDTS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 440 DVR-IADLRSLIGNVNQE-------AILFNDtffnnIAFGVENATMEQ------VIEAAKIANAHDFIMEKPEgyntnig 505
Cdd:PRK13633 76 DEEnLWDIRNKAGMVFQNpdnqivaTIVEED-----VAFGPENLGIPPeeirerVDESLKKVGMYEYRRHAPH------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 506 drggKLSGGQRQRVSIARAILKNPPILILDEATSALDTESERLVQEALERLMKTR--TTIAIAHRLSTIKNADEICVLYE 583
Cdd:PRK13633 144 ----LLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVEADRIIVMDS 219
|
250
....*....|..
gi 499421346 584 GEIVERGRHEEL 595
Cdd:PRK13633 220 GKVVMEGTPKEI 231
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
82-348 |
1.45e-22 |
|
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: 98.40 E-value: 1.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 82 MIQDNGPTTALIFLGLFLALMtlfktsCYFASSAV--MIPLRTGVVRDIRIMV--YAKVMRLPMGFFSEERKGDIIARms 157
Cdd:cd18568 33 LVHKNISLLNLILIGLLIVGI------FQILLSAVrqYLLDYFANRIDLSLLSdfYKHLLSLPLSFFASRKVGDIITR-- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 158 gdVGE--------VENSITSSLDMLikspiMIILYFITLIATSWKLTLFTVLVLPAMGWLMGKVGRKLKRQSLEAQGKWS 229
Cdd:cd18568 105 --FQEnqkirrflTRSALTTILDLL-----MVFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLKRNSREIFQANA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 230 DTMSQLEETLGGLRIIKAFIAEDRMIDRFtrcSNELRDAVNKVAMRQALAH---PMSEFLGTILIVSVLWFGGALILghN 306
Cdd:cd18568 178 EQQSFLVEALTGIATIKALAAERPIRWRW---ENKFAKALNTRFRGQKLSIvlqLISSLINHLGTIAVLWYGAYLVI--S 252
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 499421346 307 SSLTAPTFIFYMVILYSVINPLKDFAKAGYNIPKGLASMERV 348
Cdd:cd18568 253 GQLTIGQLVAFNMLFGSVINPLLALVGLWDELQETRISVERL 294
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
374-595 |
1.68e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 97.46 E-value: 1.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYDGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIK--DVRIADLRSLIG 451
Cdd:PRK13639 2 LETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydKKSLLEVRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 452 NV--NQEAILFNDTFFNNIAFGVENATM------EQVIEAAKIANAHDFiMEKPEGYntnigdrggkLSGGQRQRVSIAR 523
Cdd:PRK13639 82 IVfqNPDDQLFAPTVEEDVAFGPLNLGLskeeveKRVKEALKAVGMEGF-ENKPPHH----------LSGGQKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499421346 524 AILKNPPILILDEATSALDTESERLVQEALERLMKTRTTIAIA-HRLSTI-KNADEICVLYEGEIVERGRHEEL 595
Cdd:PRK13639 151 ILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIIStHDVDLVpVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
381-596 |
4.99e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 95.88 E-value: 4.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 381 FSYDGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSI---KDVRIAD---LRSLIGNVN 454
Cdd:PRK14246 17 YLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgKDIFQIDaikLRKEVGMVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 455 QEAILF-NDTFFNNIAFGVENATMEQVIEAAKIANAhdfiMEKPEGYNTNIGDR----GGKLSGGQRQRVSIARAILKNP 529
Cdd:PRK14246 97 QQPNPFpHLSIYDNIAYPLKSHGIKEKREIKKIVEE----CLRKVGLWKEVYDRlnspASQLSGGQQQRLTIARALALKP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499421346 530 PILILDEATSALDTESERLVQEALERLMKTRTTIAIAHRLSTI-KNADEICVLYEGEIVERGRHEELL 596
Cdd:PRK14246 173 KVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEIF 240
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
374-595 |
7.65e-22 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 97.46 E-value: 7.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYdGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRslIGNV 453
Cdd:PRK10851 3 IEIANIKKSF-GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRK--VGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 454 NQEAILFND-TFFNNIAFGVENATMEQVIEAAKIANAHDFIMEKPEgyNTNIGDR-GGKLSGGQRQRVSIARAILKNPPI 531
Cdd:PRK10851 80 FQHYALFRHmTVFDNIAFGLTVLPRRERPNAAAIKAKVTQLLEMVQ--LAHLADRyPAQLSGGQKQRVALARALAVEPQI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499421346 532 LILDEATSALDTEserlVQEALERLMKTR------TTIAIAH-RLSTIKNADEICVLYEGEIVERGRHEEL 595
Cdd:PRK10851 158 LLLDEPFGALDAQ----VRKELRRWLRQLheelkfTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
374-590 |
7.67e-22 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 94.70 E-value: 7.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYdGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDG------TSIKDVRIADLR 447
Cdd:PRK11124 3 IQLNGINCFY-GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 448 SLIGNVNQEAILFNDTffnniafgvenATMEQVIEA-AKIANahdfiMEKPEGYN-----------TNIGDRGG-KLSGG 514
Cdd:PRK11124 82 RNVGMVFQQYNLWPHL-----------TVQQNLIEApCRVLG-----LSKDQALAraekllerlrlKPYADRFPlHLSGG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499421346 515 QRQRVSIARAILKNPPILILDEATSALDTESERLVQEALERLMKTR-TTIAIAHRLSTI-KNADEICVLYEGEIVERG 590
Cdd:PRK11124 146 QQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGiTQVIVTHEVEVArKTASRVVYMENGHIVEQG 223
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
124-589 |
8.78e-22 |
|
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: 100.76 E-value: 8.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 124 VVRDIRIMVYAKVMRLPMGFFSEERKGDIIARMSGDVGEVENSITSSLDMLIKSPIMI--------ILYFITLIATSWKL 195
Cdd:TIGR01271 956 VSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVlgaifvvsVLQPYIFIAAIPVA 1035
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 196 TLFTVLvlpAMGWLmgKVGRKLKRqsLEAQGKwSDTMSQLEETLGGLRIIKAFIAEDRMIDRFTRCSNelrdavNKVAMR 275
Cdd:TIGR01271 1036 VIFIML---RAYFL--RTSQQLKQ--LESEAR-SPIFSHLITSLKGLWTIRAFGRQSYFETLFHKALN------LHTANW 1101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 276 QALAHPMSEFLGTILIVSVLWFGGALILGHNSSLTAPTFIFYMVILYSVINPLKDFAKAGYNIPKGLasMERVDKILKAE 355
Cdd:TIGR01271 1102 FLYLSTLRWFQMRIDIIFVFFFIAVTFIAIGTNQDGEGEVGIILTLAMNILSTLQWAVNSSIDVDGL--MRSVSRVFKFI 1179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 356 NNIKEIPNPKPLTGMND--------------------RIEFKDISFSY-DGKREVLKHVNLTVPKGKTVALVGQSGSGKS 414
Cdd:TIGR01271 1180 DLPQEEPRPSGGGGKYQlstvlvienphaqkcwpsggQMDVQGLTAKYtEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKS 1259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 415 TLVDLLPRYHDVQGgDITIDGTSIKDVRIADLRSLIGNVNQEAILFNDTFFNNIAfGVENATMEQVIEAAKIANAHDFIM 494
Cdd:TIGR01271 1260 TLLSALLRLLSTEG-EIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLD-PYEQWSDEEIWKVAEEVGLKSVIE 1337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 495 EKPEGYNTNIGDRGGKLSGGQRQRVSIARAILKNPPILILDEATSALDTESERLVQEALERLMKTRTTIAIAHRLSTIKN 574
Cdd:TIGR01271 1338 QFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLE 1417
|
490
....*....|....*
gi 499421346 575 ADEICVLyEGEIVER 589
Cdd:TIGR01271 1418 CQQFLVI-EGSSVKQ 1431
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
370-567 |
8.90e-22 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 94.42 E-value: 8.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 370 MNDRIEFKDISFSY-----DGKR-EVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDI-------TIDGT 436
Cdd:COG4778 1 MTTLLEVENLSKTFtlhlqGGKRlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIlvrhdggWVDLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 437 SIKDVRIADLR-SLIGNVNQ---------------EAILfndtffnniAFGVENATMEqviEAAKIANAHdfiMEKPEgy 500
Cdd:COG4778 81 QASPREILALRrRTIGYVSQflrviprvsaldvvaEPLL---------ERGVDREEAR---ARARELLAR---LNLPE-- 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499421346 501 ntnigdrggKL--------SGGQRQRVSIARAILKNPPILILDEATSALDTESERLVQEALERLMKTRTT-IAIAH 567
Cdd:COG4778 144 ---------RLwdlppatfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAiIGIFH 210
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
374-599 |
9.23e-22 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 97.99 E-value: 9.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYdGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRSLIGNV 453
Cdd:PRK09536 4 IDVSDLSVEF-GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 454 NQEAilfndtffnNIAFgveNATMEQVIEAAKIANAHDF-------------IMEKPEGynTNIGDRG-GKLSGGQRQRV 519
Cdd:PRK09536 83 PQDT---------SLSF---EFDVRQVVEMGRTPHRSRFdtwtetdraaverAMERTGV--AQFADRPvTSLSGGERQRV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 520 SIARAILKNPPILILDEATSALDTESERLVQEALERLMKT-RTTIAIAHRLS-TIKNADEICVLYEGEIVERGRHEELLE 597
Cdd:PRK09536 149 LLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDgKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVLT 228
|
..
gi 499421346 598 LD 599
Cdd:PRK09536 229 AD 230
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
378-596 |
9.51e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 95.55 E-value: 9.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 378 DISFSYDGKrEVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHD-VQG----GDITIDGTSIKDVR-IADLRSLIG 451
Cdd:PRK14271 26 NLTLGFAGK-TVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDkVSGyrysGDVLLGGRSIFNYRdVLEFRRRVG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 452 NVNQEAILFNDTFFNNIAFGVENATMEQVIEAAKIANAHDFIMEKPEGYNTNIGDRGGKLSGGQRQRVSIARAILKNPPI 531
Cdd:PRK14271 105 MLFQRPNPFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEV 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499421346 532 LILDEATSALDTESERLVQEALERLMKTRTTIAIAHRLS-TIKNADEICVLYEGEIVERGRHEELL 596
Cdd:PRK14271 185 LLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQLF 250
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
374-584 |
1.14e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 95.10 E-value: 1.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYDGKReVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQG-----GDITIDGTSI--KDVRIADL 446
Cdd:PRK14258 8 IKVNNLSFYYDTQK-ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyeRRVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 447 RSLIGNVNQEAILFNDTFFNNIAFGVE------NATMEQVIEAA-KIANAHDFIMEKpegyntnIGDRGGKLSGGQRQRV 519
Cdd:PRK14258 87 RRQVSMVHPKPNLFPMSVYDNVAYGVKivgwrpKLEIDDIVESAlKDADLWDEIKHK-------IHKSALDLSGGQQQRL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499421346 520 SIARAILKNPPILILDEATSALDTESERLVQEALE--RLMKTRTTIAIAHRLSTIKNADEICVLYEG 584
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQVSRLSDFTAFFKG 226
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
376-595 |
1.20e-21 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 97.02 E-value: 1.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 376 FKDISFSYdGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADlRSlIGNVNQ 455
Cdd:PRK11000 6 LRNVTKAY-GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE-RG-VGMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 456 EAILF-NDTFFNNIAFG-----VENATMEQ-VIEAAKIANAHDFIMEKPEGyntnigdrggkLSGGQRQRVSIARAILKN 528
Cdd:PRK11000 83 SYALYpHLSVAENMSFGlklagAKKEEINQrVNQVAEVLQLAHLLDRKPKA-----------LSGGQRQRVAIGRTLVAE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499421346 529 PPILILDEATSALDTESErlVQEALE--RLMKT--RTTIAIAH-RLSTIKNADEICVLYEGEIVERGRHEEL 595
Cdd:PRK11000 152 PSVFLLDEPLSNLDAALR--VQMRIEisRLHKRlgRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
385-588 |
1.30e-21 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 94.75 E-value: 1.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 385 GKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRSLIGNVNqeaILFNDtf 464
Cdd:PRK10419 23 QHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRRDIQ---MVFQD-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 465 fnniAFGVENA--TMEQVI-----------EAAKIANAHDfiMEKPEGYNTNIGDR-GGKLSGGQRQRVSIARAILKNPP 530
Cdd:PRK10419 98 ----SISAVNPrkTVREIIreplrhllsldKAERLARASE--MLRAVDLDDSVLDKrPPQLSGGQLQRVCLARALAVEPK 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499421346 531 ILILDEATSALDteseRLVQEALERLMKT---RTTIA---IAHRLSTIKN-ADEICVLYEGEIVE 588
Cdd:PRK10419 172 LLILDEAVSNLD----LVLQAGVIRLLKKlqqQFGTAclfITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
374-595 |
1.32e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 95.25 E-value: 1.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYDGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRSLIGNV 453
Cdd:PRK13652 4 IETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 454 --NQEAILFNDTFFNNIAFGVENATMEQVIEAAKIANAhdFIMEKPEGYNTNIGDRggkLSGGQRQRVSIARAILKNPPI 531
Cdd:PRK13652 84 fqNPDDQIFSPTVEQDIAFGPINLGLDEETVAHRVSSA--LHMLGLEELRDRVPHH---LSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499421346 532 LILDEATSALDTESERLVQEALERLMKT--RTTIAIAHRLSTIKN-ADEICVLYEGEIVERGRHEEL 595
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEI 225
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
86-348 |
1.37e-21 |
|
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: 95.21 E-value: 1.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 86 NGPTTALIFLGLFLALMTLFKTSC-YFASSAVmipLRTGVVRDIRIM--VYAKVMRLPMGFFSEERKGDIIARMSgDVGE 162
Cdd:cd18570 35 SGDINLLNIISIGLILLYLFQSLLsYIRSYLL---LKLSQKLDIRLIlgYFKHLLKLPLSFFETRKTGEIISRFN-DANK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 163 VENSITSSLDMLIKSPIMIILYFITLIATSWKLTLFTVLVLPAMG---WLMGKVGRKLKRQSLEAQgkwSDTMSQLEETL 239
Cdd:cd18570 111 IREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLYIliiLLFNKPFKKKNREVMESN---AELNSYLIESL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 240 GGLRIIKAFIAEDRMIDRFTRCSNELRDAVNKVAMRQALAHPMSEFLGTILIVSVLWFGGALILghNSSLTAPTFIFYMV 319
Cdd:cd18570 188 KGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLIGSLLILWIGSYLVI--KGQLSLGQLIAFNA 265
|
250 260
....*....|....*....|....*....
gi 499421346 320 ILYSVINPLKDFAKAGYNIPKGLASMERV 348
Cdd:cd18570 266 LLGYFLGPIENLINLQPKIQEAKVAADRL 294
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
374-590 |
1.44e-21 |
|
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: 93.59 E-value: 1.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYDGKRE---VLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSI-KDVRIADLRsl 449
Cdd:cd03266 2 ITADALTKRFRDVKKtvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVvKEPAEARRR-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 450 IGNVNQEAILFND-TFFNNIAF-----GVENATMEQVIEaaKIANAHDF--IMEKpegyntnigdRGGKLSGGQRQRVSI 521
Cdd:cd03266 80 LGFVSDSTGLYDRlTARENLEYfaglyGLKGDELTARLE--ELADRLGMeeLLDR----------RVGGFSTGMRQKVAI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499421346 522 ARAILKNPPILILDEATSALDTESERLVQEALERLMKTRTTIAIA-HRLSTIKN-ADEICVLYEGEIVERG 590
Cdd:cd03266 148 ARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFStHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
377-586 |
1.56e-21 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 94.36 E-value: 1.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 377 KDISFSYdGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRiADLRSLIgnvnQE 456
Cdd:PRK11247 16 NAVSKRY-GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAR-EDTRLMF----QD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 457 AILFN-DTFFNNIAFGVE---NATMEQVIEAAKIAN-AHDFimekPegyntnigdrgGKLSGGQRQRVSIARAILKNPPI 531
Cdd:PRK11247 90 ARLLPwKKVIDNVGLGLKgqwRDAALQALAAVGLADrANEW----P-----------AALSGGQKQRVALARALIHRPGL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499421346 532 LILDEATSALDTESERLVQEALERLMKTR--TTIAIAHRLS-TIKNADEICVLYEGEI 586
Cdd:PRK11247 155 LLLDEPLGALDALTRIEMQDLIESLWQQHgfTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
375-597 |
1.71e-21 |
|
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: 93.51 E-value: 1.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 375 EFKDISFSYdGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRSL-IGNV 453
Cdd:COG0410 5 EVENLHAGY-GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLgIGYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 454 NQEAILFND-TFFNNIAFGVENATMEQVIEAAKianahDFIMEK-PegyntNIGDR----GGKLSGGQRQRVSIARAILK 527
Cdd:COG0410 84 PEGRRIFPSlTVEENLLLGAYARRDRAEVRADL-----ERVYELfP-----RLKERrrqrAGTLSGGEQQMLAIGRALMS 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499421346 528 NPPILILDEATSALdteSERLVQE---ALERLMKTRTTIAI----AHRLSTIknADEICVLYEGEIVERGRHEELLE 597
Cdd:COG0410 154 RPKLLLLDEPSLGL---APLIVEEifeIIRRLNREGVTILLveqnARFALEI--ADRAYVLERGRIVLEGTAAELLA 225
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
385-596 |
1.78e-21 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 94.27 E-value: 1.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 385 GKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRSLIGNVNQEAIL---FN 461
Cdd:PRK10619 16 GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLKVADKNQLRLLrtrLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 462 DTF--FNNIAF--GVENaTMEQVIEAAKIANAHdfIMEKPEGYNTNIG--DRG-GK----LSGGQRQRVSIARAILKNPP 530
Cdd:PRK10619 96 MVFqhFNLWSHmtVLEN-VMEAPIQVLGLSKQE--ARERAVKYLAKVGidERAqGKypvhLSGGQQQRVSIARALAMEPE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499421346 531 ILILDEATSALDTEserLVQEALeRLMKT-----RTTIAIAHRLSTIKN-ADEICVLYEGEIVERGRHEELL 596
Cdd:PRK10619 173 VLLFDEPTSALDPE---LVGEVL-RIMQQlaeegKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLF 240
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
374-596 |
1.84e-21 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 93.99 E-value: 1.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYDGKReVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADL-RSLign 452
Cdd:COG4604 2 IEIKNVSKRYGGKV-VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELaKRL--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 453 vnqeAILFNDTFFNN-------IAFG----------VE-NATMEQVIEAAKIAN-AHDFIMEkpegyntnigdrggkLSG 513
Cdd:COG4604 78 ----AILRQENHINSrltvrelVAFGrfpyskgrltAEdREIIDEAIAYLDLEDlADRYLDE---------------LSG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 514 GQRQRVSIARAILKNPPILILDEATSALDTESERLVQEALERLMKT--RTTIAIAHRLstikN-----ADEICVLYEGEI 586
Cdd:COG4604 139 GQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADElgKTVVIVLHDI----NfascyADHIVAMKDGRV 214
|
250
....*....|
gi 499421346 587 VERGRHEELL 596
Cdd:COG4604 215 VAQGTPEEII 224
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
393-596 |
1.89e-21 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 96.33 E-value: 1.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 393 VNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIA-DL---RSLIGNVNQEAILFND-TFFNN 467
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGiFLppeKRRIGYVFQEARLFPHlSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 468 IAFGVENATMEQ-VIEAAKIANAhdfimekpegynTNIG---DRG-GKLSGGQRQRVSIARAILKNPPILILDEATSALD 542
Cdd:TIGR02142 96 LRYGMKRARPSErRISFERVIEL------------LGIGhllGRLpGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499421346 543 TESERLVQEALERLmkTRTT----IAIAHRLSTIKN-ADEICVLYEGEIVERGRHEELL 596
Cdd:TIGR02142 164 DPRKYEILPYLERL--HAEFgipiLYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVW 220
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
374-596 |
2.18e-21 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 94.03 E-value: 2.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYdGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRSLIGNV 453
Cdd:COG4559 2 LEAENLSVRL-GGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 454 NQEAILfndTFfnniAFGVE-------------NATMEQVIEAAkianahdfiMEKpegynTNIGDRGGK----LSGGQR 516
Cdd:COG4559 81 PQHSSL---AF----PFTVEevvalgraphgssAAQDRQIVREA---------LAL-----VGLAHLAGRsyqtLSGGEQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 517 QRVSIARAI--LKNPP-----ILILDEATSALDteserLV-QEALERLMKTRTT-----IAIAHRLstikN-----ADEI 578
Cdd:COG4559 140 QRVQLARVLaqLWEPVdggprWLFLDEPTSALD-----LAhQHAVLRLARQLARrgggvVAVLHDL----NlaaqyADRI 210
|
250
....*....|....*...
gi 499421346 579 CVLYEGEIVERGRHEELL 596
Cdd:COG4559 211 LLLHQGRLVAQGTPEEVL 228
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
374-591 |
2.89e-21 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 92.88 E-value: 2.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSY---DGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSI----KDVRiADL 446
Cdd:COG4181 9 IELRGLTKTVgtgAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLfaldEDAR-ARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 447 RS-LIGNVNQEAILF-NDTFFNNIAFGVENATMEqviEAAKIANAhdfIMEKpegynTNIGDRG----GKLSGGQRQRVS 520
Cdd:COG4181 88 RArHVGFVFQSFQLLpTLTALENVMLPLELAGRR---DARARARA---LLER-----VGLGHRLdhypAQLSGGEQQRVA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499421346 521 IARAILKNPPILILDEATSALDTESERLVQEALERLMKTR-TT-IAIAHRLSTIKNADEICVLYEGEIVERGR 591
Cdd:COG4181 157 LARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERgTTlVLVTHDPALAARCDRVLRLRAGRLVEDTA 229
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
374-595 |
4.24e-21 |
|
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: 92.05 E-value: 4.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYDGKREVlKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSI-KDVRiaDLRSLIGN 452
Cdd:cd03265 1 IEVENLVKKYGDFEAV-RGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVvREPR--EVRRRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 453 VNQEAILFND-TFFNNIA-----FGVENATMEQvieaaKIANAHDFImekpegyntNIGDRGGKL----SGGQRQRVSIA 522
Cdd:cd03265 78 VFQDLSVDDElTGWENLYiharlYGVPGAERRE-----RIDELLDFV---------GLLEAADRLvktySGGMRRRLEIA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 523 RAILKNPPILILDEATSALDTESERLVQEALERLMKTR-TTIAI-------AHRLstiknADEICVLYEGEIVERGRHEE 594
Cdd:cd03265 144 RSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFgMTILLtthymeeAEQL-----CDRVAIIDHGRIIAEGTPEE 218
|
.
gi 499421346 595 L 595
Cdd:cd03265 219 L 219
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
374-596 |
4.45e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 93.92 E-value: 4.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYDGKR----EVLKHVNLTVPKGKTVALVGQSGSGKSTLVDL-----LPRYHDVQGGDITIDGTSIKDVRIA 444
Cdd:PRK13645 7 IILDNVSYTYAKKTpfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLtngliISETGQTIVGDYAIPANLKKIKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 445 DLRSLIGNVNQ--EAILFNDTFFNNIAFGVENATMEQVIEAAKIANAHDFImEKPEGYntnIGDRGGKLSGGQRQRVSIA 522
Cdd:PRK13645 87 RLRKEIGLVFQfpEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLV-QLPEDY---VKRSPFELSGGQKRRVALA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499421346 523 RAILKNPPILILDEATSALDTESERLVQEALERLMKT--RTTIAIAHRLSTI-KNADEICVLYEGEIVERGRHEELL 596
Cdd:PRK13645 163 GIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEykKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGSPFEIF 239
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
370-605 |
6.36e-21 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 92.59 E-value: 6.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 370 MNDRIEFKDISFSYD--------GKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSI--- 438
Cdd:COG4167 1 MSALLEVRNLSKTFKyrtglfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLeyg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 439 ------KDVRIA--------DLRSLIGNVNQEAILFNdTFFNniafgvENATMEQVIEAAKIANAHdfimekPEGYNTNI 504
Cdd:COG4167 81 dykyrcKHIRMIfqdpntslNPRLNIGQILEEPLRLN-TDLT------AEEREERIFATLRLVGLL------PEHANFYP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 505 GDrggkLSGGQRQRVSIARAILKNPPILILDEATSALDTeSER-----LVQEALERLmkTRTTIAIAHRLSTIKN-ADEI 578
Cdd:COG4167 148 HM----LSSGQKQRVALARALILQPKIIIADEALAALDM-SVRsqiinLMLELQEKL--GISYIYVSQHLGIVKHiSDKV 220
|
250 260
....*....|....*....|....*....
gi 499421346 579 CVLYEGEIVERGRHEELLE--LDGYYKRL 605
Cdd:COG4167 221 LVMHQGEVVEYGKTAEVFAnpQHEVTKRL 249
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
379-556 |
6.90e-21 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 92.46 E-value: 6.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 379 ISFSYDGKReVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGtsikdVRIADLRSLIGNVNQ-EA 457
Cdd:PRK11248 7 LYADYGGKP-ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDG-----KPVEGPGAERGVVFQnEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 458 ILFNDTFFNNIAFGVENATMEQvieAAKIANAHDfiMEKPEGYNTNIGDRGGKLSGGQRQRVSIARAILKNPPILILDEA 537
Cdd:PRK11248 81 LLPWRNVQDNVAFGLQLAGVEK---MQRLEIAHQ--MLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEP 155
|
170
....*....|....*....
gi 499421346 538 TSALDTESERLVQEALERL 556
Cdd:PRK11248 156 FGALDAFTREQMQTLLLKL 174
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
373-586 |
9.75e-21 |
|
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: 92.61 E-value: 9.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 373 RIEFKDISFSY-DGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGgDITIDGTSIKDVRIADLRSLIG 451
Cdd:cd03289 2 QMTVKDLTAKYtEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEG-DIQIDGVSWNSVPLQKWRKAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 452 NVNQEAILFNDTFFNNI-AFGVENAtmEQVIEAAKIANAHDFIMEKPEGYNTNIGDRGGKLSGGQRQRVSIARAILKNPP 530
Cdd:cd03289 81 VIPQKVFIFSGTFRKNLdPYGKWSD--EEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAK 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499421346 531 ILILDEATSALDTESERLVQEALERLMKTRTTIAIAHRLSTIKNADEICVLYEGEI 586
Cdd:cd03289 159 ILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKV 214
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
86-319 |
1.12e-20 |
|
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: 92.61 E-value: 1.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 86 NGPTTALIFLGLFLALMTlfktSCYFASSAVMiplRTGVVRDIRIMVYAKVMRLPMGFFSEERKGDIIARMSGDVGEVEn 165
Cdd:cd18574 42 KKPALKLLGLYLLQSLLT----FAYISLLSVV---GERVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVQEFK- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 166 sitSSLDMLI----KSPIMIILYFITLIATSWKLTLFTVLVLPAMGWLMGKVGRKLKRQSLEAQGKWSDTMSQLEETLGG 241
Cdd:cd18574 114 ---SSFKQCVsqglRSVTQTVGCVVSLYLISPKLTLLLLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGN 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 242 LRIIKAFIAEDRMIDRFTRCSNELRDAVNKVAMR----QALAhpmSEFLGTIlIVSVLWFGGALILghNSSLTAPTFIFY 317
Cdd:cd18574 191 IRTVRAFAMEDRELELYEEEVEKAAKLNEKLGLGigifQGLS---NLALNGI-VLGVLYYGGSLVS--RGELTAGDLMSF 264
|
..
gi 499421346 318 MV 319
Cdd:cd18574 265 LV 266
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
91-348 |
1.15e-20 |
|
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: 92.66 E-value: 1.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 91 ALIFLGLFLALMTLFKT------SCYFASSAVMIPLRTGVvrdiriMVYAKVMRLPMGFFSEERKGDIIARmsgdVGEVE 164
Cdd:cd18782 40 TLYVIGVVMLVAALLEAvltalrTYLFTDTANRIDLELGG------TIIDHLLRLPLGFFDKRPVGELSTR----ISELD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 165 N--------SITSSLDMlikspIMIILYFITLIATSWKLTLFTVLVLPAMGWLMGKVGRKLKRQSLEAQGKWSDTMSQLE 236
Cdd:cd18782 110 TirgfltgtALTTLLDV-----LFSVIYIAVLFSYSPLLTLVVLATVPLQLLLTFLFGPILRRQIRRRAEASAKTQSYLV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 237 ETLGGLRIIKAFIAEDRMIDRFTRCSNELRDAVNKVAMRQALAHPMSEFLGTILIVSVLWFGGALILGHNSSLTAptFIF 316
Cdd:cd18782 185 ESLTGIQTVKAQNAELKARWRWQNRYARSLGEGFKLTVLGTTSGSLSQFLNKLSSLLVLWVGAYLVLRGELTLGQ--LIA 262
|
250 260 270
....*....|....*....|....*....|..
gi 499421346 317 YMVILYSVINPLKDFAKAGYNIPKGLASMERV 348
Cdd:cd18782 263 FRILSGYVTGPILRLSTLWQQFQELRVSLERL 294
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
343-581 |
1.31e-20 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 95.64 E-value: 1.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 343 ASMERVDKILKAENNIKEIPNpkpltgmnDRIEFKDISFSYDGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLV----D 418
Cdd:COG4178 340 EALEAADALPEAASRIETSED--------GALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLraiaG 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 419 LLPRYHdvqgGDIT----------------IDGTsikdvriadLRslignvnqEAILFNDTffnniafgVENATMEQVIE 482
Cdd:COG4178 412 LWPYGS----GRIArpagarvlflpqrpylPLGT---------LR--------EALLYPAT--------AEAFSDAELRE 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 483 AAKIANAHDFImekpEGYNTNiGDRGGKLSGGQRQRVSIARAILKNPPILILDEATSALDTESERLVQEALERLMKTRTT 562
Cdd:COG4178 463 ALEAVGLGHLA----ERLDEE-ADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTV 537
|
250
....*....|....*....
gi 499421346 563 IAIAHRLSTIKNADEICVL 581
Cdd:COG4178 538 ISVGHRSTLAAFHDRVLEL 556
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
393-595 |
1.41e-20 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 93.11 E-value: 1.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 393 VNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGtsiKDVRIAD------LRSLIGNVnqeailfndtfFN 466
Cdd:PRK11308 34 VSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQG---QDLLKADpeaqklLRQKIQIV-----------FQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 467 NiAFGVENA--TMEQVIE-----------AAKIANAHDfIMEK----PEGYntnigDRGGKL-SGGQRQRVSIARAILKN 528
Cdd:PRK11308 100 N-PYGSLNPrkKVGQILEepllintslsaAERREKALA-MMAKvglrPEHY-----DRYPHMfSGGQRQRIAIARALMLD 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499421346 529 PPILILDEATSALDTEserlVQEA-------LERLMKTrTTIAIAHRLSTIKN-ADEICVLYEGEIVERGRHEEL 595
Cdd:PRK11308 173 PDVVVADEPVSALDVS----VQAQvlnlmmdLQQELGL-SYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQI 242
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
393-596 |
1.49e-20 |
|
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: 93.63 E-value: 1.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 393 VNLTVPKGKTVALVGQSGSGKSTLVDLL-----PryhdvQGGDITIDGT----SIKDVRIADLRSLIGNVNQEAILFND- 462
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIaglerP-----DSGRIRLGGEvlqdSARGIFLPPHRRRIGYVFQEARLFPHl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 463 TFFNNIAFGVENA-------TMEQVIEAakianahdfimekpegynTNIG---DRG-GKLSGGQRQRVSIARAILKNPPI 531
Cdd:COG4148 93 SVRGNLLYGRKRApraerriSFDEVVEL------------------LGIGhllDRRpATLSGGERQRVAIGRALLSSPRL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499421346 532 LILDEATSALDTESERLVQEALERLmktRTTIAI-----AH------RLstiknADEICVLYEGEIVERGRHEELL 596
Cdd:COG4148 155 LLMDEPLAALDLARKAEILPYLERL---RDELDIpilyvSHsldevaRL-----ADHVVLLEQGRVVASGPLAEVL 222
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
370-581 |
1.66e-20 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 90.54 E-value: 1.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 370 MNDR---IEFKDISFSYDGKReVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADL 446
Cdd:PRK10247 1 MQENsplLQLQNVGYLAGDAK-ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 447 RSLIGNVNQEAILFNDTFFNNIAF--GVENATMEQVIEAAKIA--NAHDFIMEKpegyntNIGDrggkLSGGQRQRVSIA 522
Cdd:PRK10247 80 RQQVSYCAQTPTLFGDTVYDNLIFpwQIRNQQPDPAIFLDDLErfALPDTILTK------NIAE----LSGGEKQRISLI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499421346 523 RAILKNPPILILDEATSALDTESERLVQEALERLMKTRtTIAI---AHRLSTIKNADEICVL 581
Cdd:PRK10247 150 RNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQ-NIAVlwvTHDKDEINHADKVITL 210
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
373-556 |
2.01e-20 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 91.08 E-value: 2.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 373 RIEFKDISFSYDGKRE---VLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKdvriadlrsl 449
Cdd:COG4525 3 MLTVRHVSVRYPGGGQpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVT---------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 450 iGNVNQEAILF-NDTFF------NNIAF-----GVENATMEQVIEA----AKIANAHD-FIMEkpegyntnigdrggkLS 512
Cdd:COG4525 73 -GPGADRGVVFqKDALLpwlnvlDNVAFglrlrGVPKAERRARAEEllalVGLADFARrRIWQ---------------LS 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499421346 513 GGQRQRVSIARAILKNPPILILDEATSALDTESERLVQEALERL 556
Cdd:COG4525 137 GGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDV 180
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
385-588 |
2.14e-20 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 91.41 E-value: 2.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 385 GKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRSLIGNVNqeaILFNDtf 464
Cdd:TIGR02769 22 QRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAFRRDVQ---LVFQD-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 465 fnniAFGVENA--TMEQVI-----------EAAKIANAHDfiMEKPEGYNTNIGDR-GGKLSGGQRQRVSIARAILKNPP 530
Cdd:TIGR02769 97 ----SPSAVNPrmTVRQIIgeplrhltsldESEQKARIAE--LLDMVGLRSEDADKlPRQLSGGQLQRINIARALAVKPK 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499421346 531 ILILDEATSALDTESERLVQEALERLmKTRTTIA---IAHRLSTIKN-ADEICVLYEGEIVE 588
Cdd:TIGR02769 171 LIVLDEAVSNLDMVLQAVILELLRKL-QQAFGTAylfITHDLRLVQSfCQRVAVMDKGQIVE 231
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
369-598 |
3.25e-20 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 94.32 E-value: 3.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 369 GMNDRIEFKDISFSYDGKReVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGtsiKDVRIAD--- 445
Cdd:COG3845 1 MMPPALELRGITKRFGGVV-ANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG---KPVRIRSprd 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 446 -LRSLIGNVNQEAILFnDTF--FNNIAFGVENaTMEQVIEAAKIANAhdfIMEKPEGYNTNI--GDRGGKLSGGQRQRVS 520
Cdd:COG3845 77 aIALGIGMVHQHFMLV-PNLtvAENIVLGLEP-TKGGRLDRKAARAR---IRELSERYGLDVdpDAKVEDLSVGEQQRVE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 521 IARAILKNPPILILDEATSAL-DTESERLVqEALERLMKTRTTIA-IAHRLSTIK-NADEICVLYEGEIVERGR-----H 592
Cdd:COG3845 152 ILKALYRGARILILDEPTAVLtPQEADELF-EILRRLAAEGKSIIfITHKLREVMaIADRVTVLRRGKVVGTVDtaetsE 230
|
....*.
gi 499421346 593 EELLEL 598
Cdd:COG3845 231 EELAEL 236
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
363-595 |
4.27e-20 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 93.96 E-value: 4.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 363 NPKPLtgmndrIEFKDISFSYDGKrEVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVR 442
Cdd:PRK15439 7 TAPPL------LCARSISKQYSGV-EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 443 IADLRSL-IGNVNQEAILF-NDTFFNNIAFGV--ENATMEQVieAAKIANAhdfimekpeGYNTNIGDRGGKLSGGQRQR 518
Cdd:PRK15439 80 PAKAHQLgIYLVPQEPLLFpNLSVKENILFGLpkRQASMQKM--KQLLAAL---------GCQLDLDSSAGSLEVADRQI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499421346 519 VSIARAILKNPPILILDEATSALD-TESERLVQEALERLMKTRTTIAIAHRLSTIKN-ADEICVLYEGEIVERGRHEEL 595
Cdd:PRK15439 149 VEILRGLMRDSRILILDEPTASLTpAETERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADL 227
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
388-570 |
4.63e-20 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 89.49 E-value: 4.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 388 EVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRI---ADLRSL-IGNVNQEAILFNDt 463
Cdd:PRK11629 23 DVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaakAELRNQkLGFIYQFHHLLPD- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 464 fFNniafGVENATMEQVIEAAKIANAHD--FIMEKPEGYNTNIGDRGGKLSGGQRQRVSIARAILKNPPILILDEATSAL 541
Cdd:PRK11629 102 -FT----ALENVAMPLLIGKKKPAEINSraLEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNL 176
|
170 180 190
....*....|....*....|....*....|....*..
gi 499421346 542 DTESERLVQEALERLMKTRTT--------IAIAHRLS 570
Cdd:PRK11629 177 DARNADSIFQLLGELNRLQGTaflvvthdLQLAKRMS 213
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
93-595 |
6.92e-20 |
|
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: 94.59 E-value: 6.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 93 IFLGLFLALM----TLFKTSCYFASSAVMIPLRTGVVRdiriMVYAKVMRLPMGFFSEERKGDIIARMSGDVGEVENSIT 168
Cdd:TIGR01271 122 YYLALGLCLLfivrTLLLHPAIFGLHHLGMQMRIALFS----LIYKKTLKLSSRVLDKISTGQLVSLLSNNLNKFDEGLA 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 169 SSLDMLIkSPIMIILyfitLIATSWKLtlFTVLVLPAMGWLM------GKVGRKLKRQSLEAQGKWSDTMSQLEETLGGL 242
Cdd:TIGR01271 198 LAHFVWI-APLQVIL----LMGLIWEL--LEVNGFCGLGFLIllalfqACLGQKMMPYRDKRAGKISERLAITSEIIENI 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 243 RIIKAFIAED---RMIDRFTRCSNELRDAVNKVAMRQALAHPMSEFLgtILIVSVLWFggALILGHNSSLTAPTFIFYMV 319
Cdd:TIGR01271 271 QSVKAYCWEEameKIIKNIRQDELKLTRKIAYLRYFYSSAFFFSGFF--VVFLSVVPY--ALIKGIILRRIFTTISYCIV 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 320 ILYSV-----------------INPLKDFAKAG------YNIPKGLASMERV------------DKIlKAENNIKEIPNP 364
Cdd:TIGR01271 347 LRMTVtrqfpgaiqtwydslgaITKIQDFLCKEeyktleYNLTTTEVEMVNVtaswdegigelfEKI-KQNNKARKQPNG 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 365 kpltgmNDRIEFKDISFSYDgkrEVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTsikdvria 444
Cdd:TIGR01271 426 ------DDGLFFSNFSLYVT---PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------- 488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 445 dlrslIGNVNQEAILFNDTFFNNIAFGV--ENATMEQVIEAAKIanaHDFIMEKPEGYNTNIGDRGGKLSGGQRQRVSIA 522
Cdd:TIGR01271 489 -----ISFSPQTSWIMPGTIKDNIIFGLsyDEYRYTSVIKACQL---EEDIALFPEKDKTVLGEGGITLSGGQRARISLA 560
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499421346 523 RAILKNPPILILDEATSALDTESERLVQEA-LERLMKTRTTIAIAHRLSTIKNADEICVLYEGEIVERGRHEEL 595
Cdd:TIGR01271 561 RAVYKDADLYLLDSPFTHLDVVTEKEIFEScLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSEL 634
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
389-595 |
8.22e-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: 89.92 E-value: 8.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 389 VLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTsikdvriadlrslIGNVNQEAILFNDTFFNNI 468
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSWIMPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 469 AFGV--ENATMEQVIEAAKIanaHDFIMEKPEGYNTNIGDRGGKLSGGQRQRVSIARAILKNPPILILDEATSALDTESE 546
Cdd:cd03291 119 IFGVsyDEYRYKSVVKACQL---EEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTE 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499421346 547 RLVQEA-LERLMKTRTTIAIAHRLSTIKNADEICVLYEGEIVERGRHEEL 595
Cdd:cd03291 196 KEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
71-358 |
1.44e-19 |
|
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: 89.82 E-value: 1.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 71 AINNFYYYVSQMIQDNGPTTALIFLGL-FLALMTLFKTSCYFASSAVMiplrtgVVRDIRIMVYAKVMRLPMGFFSEERK 149
Cdd:cd18578 35 LISVFSLPDDDELRSEANFWALMFLVLaIVAGIAYFLQGYLFGIAGER------LTRRLRKLAFRAILRQDIAWFDDPEN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 150 --GDIIARMSGDVGEVENSITSSLDMLIKSPIMIILYFITLIATSWKLTLFTVLVLPAM---GWLMGKVGRKLKRQSLEA 224
Cdd:cd18578 109 stGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALVGLATVPLLllaGYLRMRLLSGFEEKNKKA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 225 QgkwSDTMSQLEETLGGLRIIKAFIAEDRMIDRFTRCSNELRDAVNKVAMRQALAHPMSEFLGTILIVSVLWFGGALILG 304
Cdd:cd18578 189 Y---EESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLGFGLSQSLTFFAYALAFWYGGRLVAN 265
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 499421346 305 HNSSLTApTFIFYMVILYSVINPLKDFAKAGyNIPKGLASMERVDKILKAENNI 358
Cdd:cd18578 266 GEYTFEQ-FFIVFMALIFGAQSAGQAFSFAP-DIAKAKAAAARIFRLLDRKPEI 317
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
374-597 |
1.81e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 89.12 E-value: 1.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYDG----KREVLKHVNLTVPKGKTVALVGQSGSGKSTLVD-----LLPryhdvQGGDITIDGTSIK----D 440
Cdd:PRK13641 3 IKFENVDYIYSPgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQhfnalLKP-----SSGTITIAGYHITpetgN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 441 VRIADLRSLIGNVNQ--EAILFNDTFFNNIAFGVEN--ATMEQVIEAA-----KIANAHDFIMEKPegyntnigdrgGKL 511
Cdd:PRK13641 78 KNLKKLRKKVSLVFQfpEAQLFENTVLKDVEFGPKNfgFSEDEAKEKAlkwlkKVGLSEDLISKSP-----------FEL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 512 SGGQRQRVSIARAILKNPPILILDEATSALDTESERLVQEALERLMKT-RTTIAIAHRLSTI-KNADEICVLYEGEIVER 589
Cdd:PRK13641 147 SGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAgHTVILVTHNMDDVaEYADDVLVLEHGKLIKH 226
|
....*...
gi 499421346 590 GRHEELLE 597
Cdd:PRK13641 227 ASPKEIFS 234
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
374-585 |
2.01e-19 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 91.53 E-value: 2.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYDGKReVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLL----PryHDVQGGDITIDGTSIKDVRIADL-RS 448
Cdd:PRK13549 6 LEMKNITKTFGGVK-ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLsgvyP--HGTYEGEIIFEGEELQASNIRDTeRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 449 LIGNVNQEAILFND-TFFNNIAFGVEnATMEQVIEAAKIANAHDFIMEKPeGYNTNIGDRGGKLSGGQRQRVSIARAILK 527
Cdd:PRK13549 83 GIAIIHQELALVKElSVLENIFLGNE-ITPGGIMDYDAMYLRAQKLLAQL-KLDINPATPVGNLGLGQQQLVEIAKALNK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499421346 528 NPPILILDEATSALdTESERLVQEALERLMKTR--TTIAIAHRLSTIKN-ADEICVLYEGE 585
Cdd:PRK13549 161 QARLLILDEPTASL-TESETAVLLDIIRDLKAHgiACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
16-348 |
2.17e-19 |
|
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: 89.08 E-value: 2.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 16 KKYIGWAILLNILSAVFNVfsftlLIPILdilfktgenNKvyeYmewgtagfkdvAINNFyyyvsqmIQDNGPTTALIFL 95
Cdd:cd18540 1 KKLLILLIILMLLVALLDA-----VFPLL---------TK---Y-----------AIDHF-------ITPGTLDGLTGFI 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 96 GLFLALMTLFKTSCYFASSAVMIpLRTGVVRDIRIMVYAKVMRLPMGFFSEERKGDIIARMSGDVGEVENSITSSLDMLI 175
Cdd:cd18540 46 LLYLGLILIQALSVFLFIRLAGK-IEMGVSYDLRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLV 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 176 KSPIMIILYFITLIATSWKLTLFTVLVLPAMGWLMGKVGRKLKRQSLEAQGKWSDTMSQLEETLGGLRIIKAFIAEDRMI 255
Cdd:cd18540 125 WGITYMIGILIVMLILNWKLALIVLAVVPVLAVVSIYFQKKILKAYRKVRKINSRITGAFNEGITGAKTTKTLVREEKNL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 256 DRFTRCSNELRDAVNKVAMRQALAHPMSEFLGTILIVSVLWFGGALILghNSSLTAPTFIFYMVILYSVINPLKDFAKAG 335
Cdd:cd18540 205 REFKELTEEMRRASVRAARLSALFLPIVLFLGSIATALVLWYGGILVL--AGAITIGTLVAFISYATQFFEPIQQLARVL 282
|
330
....*....|...
gi 499421346 336 YNIPKGLASMERV 348
Cdd:cd18540 283 AELQSAQASAERV 295
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
370-587 |
2.87e-19 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 91.71 E-value: 2.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 370 MNDRIEFKDISFSY---DGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADL 446
Cdd:PRK10535 1 MTALLELKDIRRSYpsgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 447 ----RSLIGNVNQEAILFND-TFFNNIAFGVENATMEQvieAAKIANAHDFIMEKpeGYNTNIGDRGGKLSGGQRQRVSI 521
Cdd:PRK10535 81 aqlrREHFGFIFQRYHLLSHlTAAQNVEVPAVYAGLER---KQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499421346 522 ARAILKNPPILILDEATSALDTESERLVQEALERLM-KTRTTIAIAHRLSTIKNADEICVLYEGEIV 587
Cdd:PRK10535 156 ARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRdRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
371-608 |
2.89e-19 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 89.78 E-value: 2.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 371 NDRIEFKDISFSYdGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADlRSlI 450
Cdd:PRK11432 4 KNFVVLKNITKRF-GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ-RD-I 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 451 GNVNQEAILF-NDTFFNNIAFG-----VENATMEQ-VIEAAKIANAHDFimekpegyntniGDRG-GKLSGGQRQRVSIA 522
Cdd:PRK11432 81 CMVFQSYALFpHMSLGENVGYGlkmlgVPKEERKQrVKEALELVDLAGF------------EDRYvDQISGGQQQRVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 523 RAILKNPPILILDEATSALDTESERLVQEALERLMKTR--TTIAIAHRLS-TIKNADEICVLYEGEIVERGRHEELleld 599
Cdd:PRK11432 149 RALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFniTSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQEL---- 224
|
....*....
gi 499421346 600 gyYKRLNDM 608
Cdd:PRK11432 225 --YRQPASR 231
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
382-581 |
3.03e-19 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 85.75 E-value: 3.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 382 SYDGkREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDG----------TSIKD---VRIADL-- 446
Cdd:NF040873 1 GYGG-RPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgarvayvpqrSEVPDslpLTVRDLva 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 447 ------RSLIGNVNQEAilfndtffnniafgveNATMEQVIEAAKIAnahDFImekpegyntniGDRGGKLSGGQRQRVS 520
Cdd:NF040873 80 mgrwarRGLWRRLTRDD----------------RAAVDDALERVGLA---DLA-----------GRQLGELSGGQRQRAL 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499421346 521 IARAILKNPPILILDEATSALDTESERLVQEALERLMKT-RTTIAIAHRLSTIKNADEICVL 581
Cdd:NF040873 130 LAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHARgATVVVVTHDLELVRRADPCVLL 191
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
384-587 |
3.03e-19 |
|
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: 86.94 E-value: 3.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 384 DGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLP---RYHDVQGGDITIDGtsiKDVRIADLRSLIGNVNQ-EAIL 459
Cdd:cd03234 17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISgrvEGGGTTSGQILFNG---QPRKPDQFQKCVAYVRQdDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 460 FNDTFFNNIAFGVENATMEQVIEAAKIANAHDFIMEkpEGYNTNIGD-RGGKLSGGQRQRVSIARAILKNPPILILDEAT 538
Cdd:cd03234 94 PGLTVRETLTYTAILRLPRKSSDAIRKKRVEDVLLR--DLALTRIGGnLVKGISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499421346 539 SALDTESERLVQEALERLMKT-RTTIAIAH--RLSTIKNADEICVLYEGEIV 587
Cdd:cd03234 172 SGLDSFTALNLVSTLSQLARRnRIVILTIHqpRSDLFRLFDRILLLSSGEIV 223
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
358-597 |
3.74e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 89.12 E-value: 3.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 358 IKEIPNPKPLTGMNDRIEFKDISFSYDGKrEVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTS 437
Cdd:PRK13536 26 ISEAKASIPGSMSTVAIDLAGVSKSYGDK-AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 438 IKD-VRIAdlRSLIGNVNQ-----------EAILFNDTFFNNIAFGVEnATMEQVIEAAKIANAHDFimekpegyntnig 505
Cdd:PRK13536 105 VPArARLA--RARIGVVPQfdnldleftvrENLLVFGRYFGMSTREIE-AVIPSLLEFARLESKADA------------- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 506 dRGGKLSGGQRQRVSIARAILKNPPILILDEATSALDTESERLVQEALERLMKTRTTIAI-------AHRLstiknADEI 578
Cdd:PRK13536 169 -RVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLtthfmeeAERL-----CDRL 242
|
250
....*....|....*....
gi 499421346 579 CVLYEGEIVERGRHEELLE 597
Cdd:PRK13536 243 CVLEAGRKIAEGRPHALID 261
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
374-594 |
4.54e-19 |
|
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: 86.72 E-value: 4.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYDGKReVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRSL-IGN 452
Cdd:cd03219 1 LEVRGLTKRFGGLV-ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLgIGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 453 VNQEAILFND-TFFNNIAFGVENATMEQVI-------EAAKIANAHDfIMEKpegynTNIGDRG----GKLSGGQRQRVS 520
Cdd:cd03219 80 TFQIPRLFPElTVLENVMVAAQARTGSGLLlararreEREARERAEE-LLER-----VGLADLAdrpaGELSYGQQRRLE 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499421346 521 IARAILKNPPILILDEATSAL-DTESERLVqEALERL-MKTRTTIAIAHRLSTIKN-ADEICVLYEGEIVERGRHEE 594
Cdd:cd03219 154 IARALATDPKLLLLDEPAAGLnPEETEELA-ELIRELrERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDE 229
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
376-567 |
4.73e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 90.51 E-value: 4.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 376 FKDISFSYdGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDgtsiKDVRIADLRslignvnQ 455
Cdd:COG0488 1 LENLSKSF-GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP----KGLRIGYLP-------Q 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 456 EAILFND-TFFNNIAFG-------------VENATMEQVIEAAKIANAHDfIMEKPEGYN---------------TNIGD 506
Cdd:COG0488 69 EPPLDDDlTVLDTVLDGdaelraleaeleeLEAKLAEPDEDLERLAELQE-EFEALGGWEaearaeeilsglgfpEEDLD 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499421346 507 RG-GKLSGGQRQRVSIARAILKNPPILILDEATSALDTESerlvQEALERLMKTR--TTIAIAH 567
Cdd:COG0488 148 RPvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES----IEWLEEFLKNYpgTVLVVSH 207
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
340-554 |
4.73e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 90.51 E-value: 4.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 340 KGLASMERVDkILKAENNIK-EIPNPKPLTgmNDRIEFKDISFSYDGKrEVLKHVNLTVPKGKTVALVGQSGSGKSTLVD 418
Cdd:COG0488 284 KALEKLEREE-PPRRDKTVEiRFPPPERLG--KKVLELEGLSKSYGDK-TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLK 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 419 LL-----PryhdvQGGDITIdGTSIKdvriadlrslIGNVNQEAILFNdtffnniafgvENATMEQVIEAAkianahdfi 493
Cdd:COG0488 360 LLageleP-----DSGTVKL-GETVK----------IGYFDQHQEELD-----------PDKTVLDELRDG--------- 403
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499421346 494 meKPEGYNTNI----------GDRG----GKLSGGQRQRVSIARAILKNPPILILDEATSALDTESERLVQEALE 554
Cdd:COG0488 404 --APGGTEQEVrgylgrflfsGDDAfkpvGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALD 476
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
370-595 |
4.94e-19 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 87.06 E-value: 4.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 370 MNDRIEFKDISFSYDgkREVLKHVNLTVPKGKTVALVGQSGSGKS----TLVDLLPRYHDVQGGDITIDGtsiKDVRIAD 445
Cdd:PRK10418 1 MPQQIELRNIALQAA--QPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDG---KPVAPCA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 446 LRS-LIGNVNQEAilfnDTFFNNI----AFGVE----------NATMEQVIEAAKIANAHDFIMEKPegyntnigdrgGK 510
Cdd:PRK10418 76 LRGrKIATIMQNP----RSAFNPLhtmhTHAREtclalgkpadDATLTAALEAVGLENAARVLKLYP-----------FE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 511 LSGGQRQRVSIARAILKNPPILILDEATSALDTESERLVQEALERLMKTRT--TIAIAHRLSTI-KNADEICVLYEGEIV 587
Cdd:PRK10418 141 MSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVaRLADDVAVMSHGRIV 220
|
....*...
gi 499421346 588 ERGRHEEL 595
Cdd:PRK10418 221 EQGDVETL 228
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
375-595 |
5.86e-19 |
|
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: 86.04 E-value: 5.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 375 EFKDISFSYdGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADL-RSLIGNV 453
Cdd:TIGR03410 2 EVSNLNVYY-GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaRAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 454 NQEAILFND-TFFNNIafgvenatmEQVIEAAKIANAH--DFIMEKPEGYNTNIGDRGGKLSGGQRQRVSIARAILKNPP 530
Cdd:TIGR03410 81 PQGREIFPRlTVEENL---------LTGLAALPRRSRKipDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPK 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499421346 531 ILILDEATSALDTESERLVQEALERLmKTRTTIAI---------AHRLstiknADEICVLYEGEIVERGRHEEL 595
Cdd:TIGR03410 152 LLLLDEPTEGIQPSIIKDIGRVIRRL-RAEGGMAIllveqyldfAREL-----ADRYYVMERGRVVASGAGDEL 219
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
377-599 |
7.39e-19 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 86.77 E-value: 7.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 377 KDISFSYDGkREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDvriadlrslignvnqe 456
Cdd:PRK10575 15 RNVSFRVPG-RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLES---------------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 457 ailfndtfFNNIAFGVENATMEQVIEAAKIANAHD---------------FIMEKPEGYNTNIGDRGGK---------LS 512
Cdd:PRK10575 78 --------WSSKAFARKVAYLPQQLPAAEGMTVRElvaigrypwhgalgrFGAADREKVEEAISLVGLKplahrlvdsLS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 513 GGQRQRVSIARAILKNPPILILDEATSALDTESERLVQEALERLMKTR--TTIAIAHRLS-TIKNADEICVLYEGEIVER 589
Cdd:PRK10575 150 GGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERglTVIAVLHDINmAARYCDYLVALRGGEMIAQ 229
|
250
....*....|
gi 499421346 590 GRHEELLELD 599
Cdd:PRK10575 230 GTPAELMRGE 239
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
385-544 |
1.00e-18 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 84.84 E-value: 1.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 385 GKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQ---GGDITIDGTSIKDVRIADLRslIGNVNQEAILF- 460
Cdd:COG4136 12 GGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAEQRR--IGILFQDDLLFp 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 461 NDTFFNNIAFGVENAT-----MEQVIEAAKIANAHDFimekpegyntniGDRG-GKLSGGQRQRVSIARAILKNPPILIL 534
Cdd:COG4136 90 HLSVGENLAFALPPTIgraqrRARVEQALEEAGLAGF------------ADRDpATLSGGQRARVALLRALLAEPRALLL 157
|
170
....*....|
gi 499421346 535 DEATSALDTE 544
Cdd:COG4136 158 DEPFSKLDAA 167
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
387-587 |
1.15e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 86.29 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 387 REVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDG---TSIKDVRIAdlrSLIGNVNQE------- 456
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGkdvTKLPEYKRA---KYIGRVFQDpmmgtap 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 457 --------AILFNDTFFNNIAFGVENATMEQVIEAAKIANAhdfimekpeGYNTNIGDRGGKLSGGQRQRVSIARAILKN 528
Cdd:COG1101 96 smtieenlALAYRRGKRRGLRRGLTKKRRELFRELLATLGL---------GLENRLDTKVGLLSGGQRQALSLLMATLTK 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499421346 529 PPILILDEATSALDTESERLVQEALERLMKTR--TTIAIAHRLS-TIKNADEICVLYEGEIV 587
Cdd:COG1101 167 PKLLLLDEHTAALDPKTAALVLELTEKIVEENnlTTLMVTHNMEqALDYGNRLIMMHEGRII 228
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
379-596 |
1.30e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 89.38 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 379 ISFSYDGK-REVLKHVNLTVPKGKTVALVGQSGSGKS----TLVDLLPRYHDV-QGGDITIDGTSIKDVRIADLRSLIGN 452
Cdd:PRK15134 13 VAFRQQQTvRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSPPVVyPSGDIRFHGESLLHASEQTLRGVRGN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 453 vnQEAILFNDTFFN-NIAFGVENATMEQVI-------EAAK-----------IANAHDFIMEKPEgyntnigdrggKLSG 513
Cdd:PRK15134 93 --KIAMIFQEPMVSlNPLHTLEKQLYEVLSlhrgmrrEAARgeilncldrvgIRQAAKRLTDYPH-----------QLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 514 GQRQRVSIARAILKNPPILILDEATSALDTEserlVQEALERLMK------TRTTIAIAHRLSTIKN-ADEICVLYEGEI 586
Cdd:PRK15134 160 GERQRVMIAMALLTRPELLIADEPTTALDVS----VQAQILQLLRelqqelNMGLLFITHNLSIVRKlADRVAVMQNGRC 235
|
250
....*....|
gi 499421346 587 VERGRHEELL 596
Cdd:PRK15134 236 VEQNRAATLF 245
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
112-321 |
1.31e-18 |
|
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: 86.60 E-value: 1.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 112 ASSAVMIPLRTGVVR------DIRI--MVYAKVMRLPMGFFSEERKGDIIARMSGDVGEVENSITSSLDMLIKSPIMIIL 183
Cdd:cd18784 47 IASSVAAGIRGGLFTlamarlNIRIrnLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 184 YFITLIATSWKLTLFTVLVLPAMGWLMGKVGRKLKRQSLEAQGKWSDTMSQLEETLGGLRIIKAFIAEDRMIDRFtrcSN 263
Cdd:cd18784 127 VIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRY---SE 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499421346 264 ELRDaVNKVAMRQALAHPM----SEFLGTILIVSVLWFGGALIL-GHNSSLTAPTFIFYMVIL 321
Cdd:cd18784 204 KLKD-TYKLKIKEALAYGGyvwsNELTELALTVSTLYYGGHLVItGQISGGNLISFILYQLEL 265
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
349-588 |
1.83e-18 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 88.88 E-value: 1.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 349 DKI--LKAENNIKEIPNPKPLTGMNdRIEFKDISFSYDGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDV 426
Cdd:PRK10522 297 NKLnkLALAPYKAEFPRPQAFPDWQ-TLELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQP 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 427 QGGDITIDGTSIKDVRIADLRSLIGNVNQEAILFnDTFFNNIAFGVENATMEQVIEAAKIANAhdfiMEKPEGYNTNIgd 506
Cdd:PRK10522 376 QSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLF-DQLLGPEGKPANPALVEKWLERLKMAHK----LELEDGRISNL-- 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 507 rggKLSGGQRQRVSIARAILKNPPILILDEATSALDTESERLVQEALERLMKT--RTTIAIAHRLSTIKNADEICVLYEG 584
Cdd:PRK10522 449 ---KLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEmgKTIFAISHDDHYFIHADRLLEMRNG 525
|
....
gi 499421346 585 EIVE 588
Cdd:PRK10522 526 QLSE 529
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
400-598 |
2.01e-18 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 88.95 E-value: 2.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 400 GKTVALVGQSGSGKSTLVDLLPRYH--DVQG-GDITIDGTSIKD---------VRIADLrsLIGNVN-QEAILFNDTFF- 465
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAFRSpkGVKGsGSVLLNGMPIDAkemraisayVQQDDL--FIPTLTvREHLMFQAHLRm 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 466 -NNIAFGVENATMEQVIEAAKIANAHdfimekpegyNTNIGDRGGK--LSGGQRQRVSIARAILKNPPILILDEATSALD 542
Cdd:TIGR00955 129 pRRVTKKEKRERVDEVLQALGLRKCA----------NTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499421346 543 TESERLVQEALERL-MKTRTTIAIAHRLST--IKNADEICVLYEGEIVERGRHEELLEL 598
Cdd:TIGR00955 199 SFMAYSVVQVLKGLaQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAVPF 257
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
374-595 |
4.14e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 85.16 E-value: 4.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYDGKReVLKHVNLTVPKGKTVALVGQSGSGKSTLV----DLLprYHDvqGGDITIDGTSIKdvriADLRSL 449
Cdd:COG4152 2 LELKGLTKRFGDKT-AVDDVSFTVPKGEIFGLLGPNGAGKTTTIriilGIL--APD--SGEVLWDGEPLD----PEDRRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 450 IG------------NVnqeailfndtffnniafgvenatMEQVI--------EAAKIANAHDFIMEKpegynTNIGDRGG 509
Cdd:COG4152 73 IGylpeerglypkmKV-----------------------GEQLVylarlkglSKAEAKRRADEWLER-----LGLGDRAN 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 510 K----LSGGQRQRVSIARAILKNPPILILDEATSALDTESERLVQEALERLMKTRTTIaI--AHRLSTI-KNADEICVLY 582
Cdd:COG4152 125 KkveeLSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTV-IfsSHQMELVeELCDRIVIIN 203
|
250
....*....|...
gi 499421346 583 EGEIVERGRHEEL 595
Cdd:COG4152 204 KGRKVLSGSVDEI 216
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
374-597 |
6.53e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 84.86 E-value: 6.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYdGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDvRIADLRSLIGNV 453
Cdd:PRK13537 8 IDFRNVEKRY-GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 454 NQEAILFND-TFFNNIA-----FGVENATMEQVI----EAAKIANAHDfimekpegyntnigDRGGKLSGGQRQRVSIAR 523
Cdd:PRK13537 86 PQFDNLDPDfTVRENLLvfgryFGLSAAAARALVppllEFAKLENKAD--------------AKVGELSGGMKRRLTLAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 524 AILKNPPILILDEATSALDTESERLVQEALERLMKTRTTIAI-------AHRLstiknADEICVLYEGEIVERGRHEELL 596
Cdd:PRK13537 152 ALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLtthfmeeAERL-----CDRLCVIEEGRKIAEGAPHALI 226
|
.
gi 499421346 597 E 597
Cdd:PRK13537 227 E 227
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
374-596 |
7.11e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 84.13 E-value: 7.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYDGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVR--IADLRSLIG 451
Cdd:PRK13636 6 LKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRkgLMKLRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 452 NVNQEA--ILFNDTFFNNIAFGVENATMEQvieaAKIANAHDFIMEKpegynTNIGDRGGK----LSGGQRQRVSIARAI 525
Cdd:PRK13636 86 MVFQDPdnQLFSASVYQDVSFGAVNLKLPE----DEVRKRVDNALKR-----TGIEHLKDKpthcLSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499421346 526 LKNPPILILDEATSALD----TESERLVQEALERLmktRTTIAIA-HRLSTIK-NADEICVLYEGEIVERGRHEELL 596
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKEL---GLTIIIAtHDIDIVPlYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
373-609 |
1.00e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 84.37 E-value: 1.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 373 RIEFKDISFSYDGKR----EVLKHVNLTVPKGKTVALVGQSGSGKSTLVD-----LLP------------------RYHD 425
Cdd:PRK13651 2 QIKVKNIVKIFNKKLptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEhlnalLLPdtgtiewifkdeknkkktKEKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 426 VQGGDITIDGTSIKDVR-IADLRSLIGNVNQ--EAILFNDTFFNNIAFGVENATMEQViEAAKIANAHDFIMEKPEGYnt 502
Cdd:PRK13651 82 KVLEKLVIQKTRFKKIKkIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKE-EAKKRAAKYIELVGLDESY-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 503 nIGDRGGKLSGGQRQRVSIARAILKNPPILILDEATSALDTESERLVQEALERLMKTRTTIAIA-HRL-STIKNADEICV 580
Cdd:PRK13651 159 -LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVtHDLdNVLEWTKRTIF 237
|
250 260
....*....|....*....|....*....
gi 499421346 581 LYEGEIVERGRHEELLElDGYYKRLNDMQ 609
Cdd:PRK13651 238 FKDGKIIKDGDTYDILS-DNKFLIENNME 265
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
374-596 |
1.23e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 82.75 E-value: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYdGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADL-RSLI-- 450
Cdd:PRK11231 3 LRTENLTVGY-GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLaRRLAll 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 451 --------GNVNQEAILFNDTFFNNIaFGVENATMEQVIEAAkianahdfiMEKPEgyNTNIGDRG-GKLSGGQRQRVSI 521
Cdd:PRK11231 82 pqhhltpeGITVRELVAYGRSPWLSL-WGRLSAEDNARVNQA---------MEQTR--INHLADRRlTDLSGGQRQRAFL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 522 ARAILKNPPILILDEATSALDTESerlvQEALERLM-----KTRTTIAIAHRLS-TIKNADEICVLYEGEIVERGRHEEL 595
Cdd:PRK11231 150 AMVLAQDTPVVLLDEPTTYLDINH----QVELMRLMrelntQGKTVVTVLHDLNqASRYCDHLVVLANGHVMAQGTPEEV 225
|
.
gi 499421346 596 L 596
Cdd:PRK11231 226 M 226
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
392-596 |
1.47e-17 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 82.32 E-value: 1.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 392 HVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGtsIKDVRIADLRSLIGNVNQEAILFND-TFFNNIAF 470
Cdd:PRK10771 17 RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNG--QDHTTTPPSRRPVSMLFQENNLFSHlTVAQNIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 471 GVENA---TMEQVIEAAKIANA---HDFIMEKPegyntnigdrgGKLSGGQRQRVSIARAILKNPPILILDEATSALD-- 542
Cdd:PRK10771 95 GLNPGlklNAAQREKLHAIARQmgiEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALDpa 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499421346 543 --TESERLVQEALERlmKTRTTIAIAHRLS-TIKNADEICVLYEGEIVERGRHEELL 596
Cdd:PRK10771 164 lrQEMLTLVSQVCQE--RQLTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELL 218
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
374-568 |
1.69e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 81.84 E-value: 1.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYDGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSI---KDVRIADLRSLI 450
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlKNREVPFLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 451 GNVNQEA-ILFNDTFFNNIAFG--VENATMEQVIEAAKIANAHDFIMEKPEGYNTnigdrggKLSGGQRQRVSIARAILK 527
Cdd:PRK10908 82 GMIFQDHhLLMDRTVYDNVAIPliIAGASGDDIRRRVSAALDKVGLLDKAKNFPI-------QLSGGEQQRVGIARAVVN 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499421346 528 NPPILILDEATSALDTE-SE---RLVQE----ALERLMKTRTTIAIAHR 568
Cdd:PRK10908 155 KPAVLLADEPTGNLDDAlSEgilRLFEEfnrvGVTVLMATHDIGLISRR 203
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
374-597 |
1.72e-17 |
|
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: 85.62 E-value: 1.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYDGKrEVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLL-------PR-----YH----------------- 424
Cdd:TIGR03269 1 IEVKNLTKKFDGK-EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgmdqyePTsgriiYHvalcekcgyverpskvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 425 ---DVQGGDIT---IDGTSIKDVRIADLRSLIgnvnqeAILFNDTFfnniAFGVENATMEQVIEA---------AKIANA 489
Cdd:TIGR03269 80 epcPVCGGTLEpeeVDFWNLSDKLRRRIRKRI------AIMLQRTF----ALYGDDTVLDNVLEAleeigyegkEAVGRA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 490 HDFI-MEKPEGYNTNIGDrggKLSGGQRQRVSIARAILKNPPILILDEATSALDTESERLVQEALERLMKTR--TTIAIA 566
Cdd:TIGR03269 150 VDLIeMVQLSHRITHIAR---DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTS 226
|
250 260 270
....*....|....*....|....*....|..
gi 499421346 567 HRLSTIKNADEICVLYE-GEIVERGRHEELLE 597
Cdd:TIGR03269 227 HWPEVIEDLSDKAIWLEnGEIKEEGTPDEVVA 258
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
389-594 |
2.07e-17 |
|
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: 82.39 E-value: 2.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 389 VLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSI---KDVRIADL---RSLignvnQEAILFND 462
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDItglPPHRIARLgiaRTF-----QNPRLFPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 463 -TFFNNIAFGVENATMEQVI------------EAAKIANAHDfIMEKpegynTNIGDRG----GKLSGGQRQRVSIARAI 525
Cdd:COG0411 94 lTVLENVLVAAHARLGRGLLaallrlprarreEREARERAEE-LLER-----VGLADRAdepaGNLSYGQQRRLEIARAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499421346 526 LKNPPILILDEATSAL-DTESERLVqEALERLMKTR--TTIAIAHRLSTIKN-ADEICVLYEGEIVERGRHEE 594
Cdd:COG0411 168 ATEPKLLLLDEPAAGLnPEETEELA-ELIRRLRDERgiTILLIEHDMDLVMGlADRIVVLDFGRVIAEGTPAE 239
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
378-597 |
2.09e-17 |
|
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: 81.82 E-value: 2.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 378 DISFSYdGKREVLKHVNLTVPKGKTVALVGQSGSGKSTL----VDLLPryhdVQGGDITIDGTSIKDVRIADLRSL-IGN 452
Cdd:cd03218 5 NLSKRY-GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTfymiVGLVK----PDSGKILLDGQDITKLPMHKRARLgIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 453 VNQEAILFND-TFFNNIAFGVENATMEQVIEAAKIANA-HDFIMEKpegyntNIGDRGGKLSGGQRQRVSIARAILKNPP 530
Cdd:cd03218 80 LPQEASIFRKlTVEENILAVLEIRGLSKKEREEKLEELlEEFHITH------LRKSKASSLSGGERRRVEIARALATNPK 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499421346 531 ILILDEATSALDTESERLVQEALERLMK-----------TRTTIAIAHRlstiknadeICVLYEGEIVERGRHEELLE 597
Cdd:cd03218 154 FLLLDEPFAGVDPIAVQDIQKIIKILKDrgigvlitdhnVRETLSITDR---------AYIIYEGKVLAEGTPEEIAA 222
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
374-567 |
2.22e-17 |
|
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: 79.03 E-value: 2.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYDGKrEVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLpryhdvqGGDITIDGTSIKdvriadlrslignv 453
Cdd:cd03221 1 IELENLSKTYGGK-LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLI-------AGELEPDEGIVT-------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 454 nqeailfndtffnnIAFGVENATMEQvieaakianahdfimekpegyntnigdrggkLSGGQRQRVSIARAILKNPPILI 533
Cdd:cd03221 59 --------------WGSTVKIGYFEQ-------------------------------LSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190
....*....|....*....|....*....|....*.
gi 499421346 534 LDEATSALDTESerlvQEALERLMKT--RTTIAIAH 567
Cdd:cd03221 94 LDEPTNHLDLES----IEALEEALKEypGTVILVSH 125
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
374-536 |
3.55e-17 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 81.74 E-value: 3.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSyDGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDV---RIADLRSLI 450
Cdd:PRK11831 8 VDMRGVSFT-RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMsrsRLYTVRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 451 GNVNQEAILFND-TFFNNIAFGVENATM--EQVIeaakianaHDFIMEKPEGyntnIGDRGG------KLSGGQRQRVSI 521
Cdd:PRK11831 87 SMLFQSGALFTDmNVFDNVAYPLREHTQlpAPLL--------HSTVMMKLEA----VGLRGAaklmpsELSGGMARRAAL 154
|
170
....*....|....*
gi 499421346 522 ARAILKNPPILILDE 536
Cdd:PRK11831 155 ARAIALEPDLIMFDE 169
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
371-584 |
3.96e-17 |
|
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: 79.98 E-value: 3.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 371 NDRIEFKDISFSYD---GKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLP-RYHD-VQGGDITIDGTSIKDvriaD 445
Cdd:cd03232 1 GSVLTWKNLNYTVPvkgGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAgRKTAgVITGEILINGRPLDK----N 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 446 LRSLIGNVNQEAILFndtffnniafgvENATMEQVIE-AAKIanahdfimekpegyntnigdRGgkLSGGQRQRVSIARA 524
Cdd:cd03232 77 FQRSTGYVEQQDVHS------------PNLTVREALRfSALL--------------------RG--LSVEQRKRLTIGVE 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499421346 525 ILKNPPILILDEATSALDTESERLVQEALERLMKT-RTTIAIAHRLS--TIKNADEICVLYEG 584
Cdd:cd03232 123 LAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSgQAILCTIHQPSasIFEKFDRLLLLKRG 185
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
370-609 |
4.59e-17 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 81.60 E-value: 4.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 370 MNDRIEFKDISFSYDgKREVLKHVNLTVPKGKTVALVGQSGSGKSTLV---------DLLPRYH-DVQGGDITIDGTSIK 439
Cdd:PRK09984 1 MQTIIRVEKLAKTFN-QHQALHAVDLNIHHGEMVALLGPSGSGKSTLLrhlsglitgDKSAGSHiELLGRTVQREGRLAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 440 DVRIAdlRSLIGNVNQEAILFND-TFFNNIAFGVENAT--------------MEQVIEA-AKIANAHdFIMEkpegyntn 503
Cdd:PRK09984 80 DIRKS--RANTGYIFQQFNLVNRlSVLENVLIGALGSTpfwrtcfswftreqKQRALQAlTRVGMVH-FAHQ-------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 504 igdRGGKLSGGQRQRVSIARAILKNPPILILDEATSALDTESERLVQEALERLMKTR--TTIAIAHRLS-TIKNADEICV 580
Cdd:PRK09984 149 ---RVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDyALRYCERIVA 225
|
250 260 270
....*....|....*....|....*....|.
gi 499421346 581 LYEGEIVERG--RHEELLELDGYYKRLNDMQ 609
Cdd:PRK09984 226 LRQGHVFYDGssQQFDNERFDHLYRSINRVE 256
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
385-597 |
4.60e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 84.37 E-value: 4.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 385 GKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGgDITIDGTSIKDVriaDLRSLIGNVNQEAILFND-- 462
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQG-EIWFDGQPLHNL---NRRQLLPVRHRIQVVFQDpn 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 463 -------TFFNNIAFGVE------NATM--EQVIEAakianahdfiMEKPeGYNTNIGDR-GGKLSGGQRQRVSIARAIL 526
Cdd:PRK15134 373 sslnprlNVLQIIEEGLRvhqptlSAAQreQQVIAV----------MEEV-GLDPETRHRyPAEFSGGQRQRIAIARALI 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499421346 527 KNPPILILDEATSALDteseRLVQEALERLMKTRTT------IAIAHRLSTIKN-ADEICVLYEGEIVERGRHEELLE 597
Cdd:PRK15134 442 LKPSLIILDEPTSSLD----KTVQAQILALLKSLQQkhqlayLFISHDLHVVRAlCHQVIVLRQGEVVEQGDCERVFA 515
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
95-309 |
6.04e-17 |
|
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: 81.82 E-value: 6.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 95 LGLFLALMTLFKTSCYFASSAVMIPLRTGVvrDIRIM--VYAKVMRLPMGFFSEERKGDIIARMSGdVGEVENSITSS-L 171
Cdd:cd18779 44 LGLGLAALVLTQLLAGLLRSHLLLRLRTRL--DTQLTlgFLEHLLRLPYRFFQQRSTGDLLMRLSS-NATIRELLTSQtL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 172 DMLIKSPiMIILYFITLIATSWKLTLfTVLVLPAMG----WLMGKVGRKLKRQSLEAQGKwsdTMSQLEETLGGLRIIKA 247
Cdd:cd18779 121 SALLDGT-LVLGYLALLFAQSPLLGL-VVLGLAALQvallLATRRRVRELMARELAAQAE---AQSYLVEALSGIETLKA 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499421346 248 FIAEDRMIDRFtrcSNELRDAVNKVAMRQALAHPMSEFLGTILIVS---VLWFGGALILGHNSSL 309
Cdd:cd18779 196 SGAEDRALDRW---SNLFVDQLNASLRRGRLDALVDALLATLRLAAplvLLWVGAWQVLDGQLSL 257
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
374-590 |
7.01e-17 |
|
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: 79.63 E-value: 7.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYdGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGtsiKDVRIADlRSLIGNV 453
Cdd:cd03269 1 LEVENVTKRF-GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG---KPLDIAA-RNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 454 NQEAILFNDTffnniafgvenATMEQVIEAAK--------IANAHDFIMEKPEgyntnIGDRGGK----LSGGQRQRVSI 521
Cdd:cd03269 76 PEERGLYPKM-----------KVIDQLVYLAQlkglkkeeARRRIDEWLERLE-----LSEYANKrveeLSKGNQQKVQF 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499421346 522 ARAILKNPPILILDEATSALDTESERLVQEALERLMKTRTTIAI-AHRLSTIKN-ADEICVLYEGEIVERG 590
Cdd:cd03269 140 IAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILsTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
373-599 |
1.31e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 80.03 E-value: 1.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 373 RIEFKDISFSYdGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRSLIGN 452
Cdd:PRK10253 7 RLRGEQLTLGY-GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 453 VNQEAILFNDTffnniafgvenaTMEQVIEAAKIANAHDFIMEKPEGYN--------TNIGDRGGK----LSGGQRQRVS 520
Cdd:PRK10253 86 LAQNATTPGDI------------TVQELVARGRYPHQPLFTRWRKEDEEavtkamqaTGITHLADQsvdtLSGGQRQRAW 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 521 IARAILKNPPILILDEATSALDTESERLVQEALERLMKTR--TTIAIAHRLS-TIKNADEICVLYEGEIVERGRHEELLE 597
Cdd:PRK10253 154 IAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKgyTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIVT 233
|
..
gi 499421346 598 LD 599
Cdd:PRK10253 234 AE 235
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
385-601 |
1.63e-16 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 79.69 E-value: 1.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 385 GKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLL---PRYhDVQGGDITIDGTSIKDVRiADLRSLIGnvnqeaiLFn 461
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIaghPAY-KILEGDILFKGESILDLE-PEERAHLG-------IF- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 462 dtffnnIAF-------GVENATM-------EQVIEAAKIANAHDF---IMEKPE---------GYNTNIGdrggkLSGGQ 515
Cdd:CHL00131 88 ------LAFqypieipGVSNADFlrlaynsKRKFQGLPELDPLEFleiINEKLKlvgmdpsflSRNVNEG-----FSGGE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 516 RQRVSIARAILKNPPILILDEATSALDTESERLVQEALERLM-KTRTTIAIAH--RLSTIKNADEICVLYEGEIVERGRH 592
Cdd:CHL00131 157 KKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMtSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGDA 236
|
250
....*....|.
gi 499421346 593 E--ELLELDGY 601
Cdd:CHL00131 237 ElaKELEKKGY 247
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
378-595 |
2.91e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 82.21 E-value: 2.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 378 DISFSYDGKR-EVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDG------------------TSI 438
Cdd:PRK10261 19 NIAFMQEQQKiAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvielseqsaAQM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 439 KDVRIADlrslIGNVNQEAILFNDTFF---NNIA--------FGVENATME--QVIEAAKIANAHDFIMEKPEgyntnig 505
Cdd:PRK10261 99 RHVRGAD----MAMIFQEPMTSLNPVFtvgEQIAesirlhqgASREEAMVEakRMLDQVRIPEAQTILSRYPH------- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 506 drggKLSGGQRQRVSIARAILKNPPILILDEATSALDTESERLVQEALERLMKTRT--TIAIAHRLSTIKN-ADEICVLY 582
Cdd:PRK10261 168 ----QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEiADRVLVMY 243
|
250
....*....|...
gi 499421346 583 EGEIVERGRHEEL 595
Cdd:PRK10261 244 QGEAVETGSVEQI 256
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
393-596 |
6.73e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 77.57 E-value: 6.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 393 VNLTVPKGKTVALVGQSGSGKSTLV----DLLPryhdvQGGDITIDGTSIKDVRIADL---RSLIGNvnQEAILFNDTFF 465
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLarmaGLLP-----GQGEILLNGRPLSDWSAAELarhRAYLSQ--QQSPPFAMPVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 466 NNIAFGVENATMEQVIEAAKIANAHDF-IMEKpegYNTNIGdrggKLSGGQRQRVSIARAILK-----NPP--ILILDEA 537
Cdd:COG4138 88 QYLALHQPAGASSEAVEQLLAQLAEALgLEDK---LSRPLT----QLSGGEWQRVRLAAVLLQvwptiNPEgqLLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499421346 538 TSALDteserLVQE-ALERLMKT-----RTTIAIAHRLS-TIKNADEICVLYEGEIVERGRHEELL 596
Cdd:COG4138 161 MNSLD-----VAQQaALDRLLRElcqqgITVVMSSHDLNhTLRHADRVWLLKQGKLVASGETAEVM 221
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
390-608 |
7.53e-16 |
|
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: 77.12 E-value: 7.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 390 LKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDV---RIAdlrslignVNQEAILFN-DTFF 465
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPgpdRMV--------VFQNYSLLPwLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 466 NNIAFGVeNATMEQV--IEAAKIANAHDFIMekpeGYNTNIGDRGGKLSGGQRQRVSIARAILKNPPILILDEATSALDT 543
Cdd:TIGR01184 73 ENIALAV-DRVLPDLskSERRAIVEEHIALV----GLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499421346 544 ESERLVQEALERLMKTR--TTIAIAHRL-STIKNADEICVL------YEGEIVE----RGRH-EELLELDGYYKRLNDM 608
Cdd:TIGR01184 148 LTRGNLQEELMQIWEEHrvTVLMVTHDVdEALLLSDRVVMLtngpaaNIGQILEvpfpRPRDrLEVVEDPSYYDLRNEA 226
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
389-586 |
7.81e-16 |
|
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: 75.93 E-value: 7.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 389 VLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGtsiKDVRIADLRslignvnqEAIlfndtffnni 468
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDG---KPVTRRSPR--------DAI---------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 469 afgvenatmeqvieAAKIA------NAHDFIMEKPEGYNTNIGDRggkLSGGQRQRVSIARAILKNPPILILDEATSALD 542
Cdd:cd03215 74 --------------RAGIAyvpedrKREGLVLDLSVAENIALSSL---LSGGNQQKVVLARWLARDPRVLILDEPTRGVD 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499421346 543 TESERLVQEALERLMKTRTTIAIahrLST-----IKNADEICVLYEGEI 586
Cdd:cd03215 137 VGAKAEIYRLIRELADAGKAVLL---ISSeldelLGLCDRILVMYEGRI 182
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
374-587 |
8.97e-16 |
|
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: 80.25 E-value: 8.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYDGKReVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRY--HDVQGGDITIDGTSIKDVRIADL-RSLI 450
Cdd:TIGR02633 2 LEMKGIVKTFGGVK-ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKASNIRDTeRAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 451 GNVNQEAILFND-TFFNNIAFGVEnATMEQVI--EAAKIANAHDfIMEKPEGYNTNIGDRGGKLSGGQRQRVSIARAILK 527
Cdd:TIGR02633 81 VIIHQELTLVPElSVAENIFLGNE-ITLPGGRmaYNAMYLRAKN-LLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNK 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499421346 528 NPPILILDEATSALdTESERLVQEALERLMKTR--TTIAIAHRLSTIKN-ADEICVLYEGEIV 587
Cdd:TIGR02633 159 QARLLILDEPSSSL-TEKETEILLDIIRDLKAHgvACVYISHKLNEVKAvCDTICVIRDGQHV 220
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
132-303 |
9.23e-16 |
|
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: 78.31 E-value: 9.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 132 VYAKVMRLPMGFFSEERKGDIIARmsgdVGEVENS---ITSSLDMLIKSPIMIILYFITLIATSWKLTLFTVLVLPAMGW 208
Cdd:cd18588 81 LFRHLLRLPLSYFESRQVGDTVAR----VRELESIrqfLTGSALTLVLDLVFSVVFLAVMFYYSPTLTLIVLASLPLYAL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 209 LMGKVGRKLKRQSLEAQGKWSDTMSQLEETLGGLRIIKAFIAEDRMIDRFtrcSNELRDAVN---KVAMRQALAHPMSEF 285
Cdd:cd18588 157 LSLLVTPILRRRLEEKFQRGAENQSFLVETVTGIETVKSLAVEPQFQRRW---EELLARYVKasfKTANLSNLASQIVQL 233
|
170
....*....|....*...
gi 499421346 286 LGTILIVSVLWFGGALIL 303
Cdd:cd18588 234 IQKLTTLAILWFGAYLVM 251
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
386-597 |
1.36e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 80.28 E-value: 1.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 386 KREV--LKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRSLIGNVNqeaILFNDT 463
Cdd:PRK10261 334 TREVhaVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQ---FIFQDP 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 464 FFN-NIAFGVENATMEQV---------IEAAKIANAHDFIMEKPEgyntNIGDRGGKLSGGQRQRVSIARAILKNPPILI 533
Cdd:PRK10261 411 YASlDPRQTVGDSIMEPLrvhgllpgkAAAARVAWLLERVGLLPE----HAWRYPHEFSGGQRQRICIARALALNPKVII 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499421346 534 LDEATSALDTESERLVQEALERLMKTR--TTIAIAHRLSTIKN-ADEICVLYEGEIVERGRHEELLE 597
Cdd:PRK10261 487 ADEAVSALDVSIRGQIINLLLDLQRDFgiAYLFISHDMAVVERiSHRVAVMYLGQIVEIGPRRAVFE 553
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
386-587 |
1.63e-15 |
|
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: 75.38 E-value: 1.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 386 KREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQG---GDITIDGTSIKDVRIADLRSLIGNvNQEailfnD 462
Cdd:cd03233 19 KIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPYKEFAEKYPGEIIYV-SEE-----D 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 463 TFFNNIafgvenaTMEQVIEAAKIANAHDFImekpegyntnigdRGgkLSGGQRQRVSIARAILKNPPILILDEATSALD 542
Cdd:cd03233 93 VHFPTL-------TVRETLDFALRCKGNEFV-------------RG--ISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499421346 543 TESerlvqeALERLMKTRtTIAIAHRLSTI-----------KNADEICVLYEGEIV 587
Cdd:cd03233 151 SST------ALEILKCIR-TMADVLKTTTFvslyqasdeiyDLFDKVLVLYEGRQI 199
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
385-578 |
1.69e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 75.68 E-value: 1.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 385 GKREVLKHVNLTVPKGKTVALVGQSGSGKSTL----VDLLPryhdVQGGDITIDGTSIKDVRIADLRSLIGNVNqeAILF 460
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLlrliAGLLP----PAAGTIKLDGGDIDDPDVAEACHYLGHRN--AMKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 461 NDTFFNNIAF--GVENATMEQVIEAAKIANAHDfIMEKPEGYntnigdrggkLSGGQRQRVSIARAILKNPPILILDEAT 538
Cdd:PRK13539 87 ALTVAENLEFwaAFLGGEELDIAAALEAVGLAP-LAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPT 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 499421346 539 SALDTESERLVQEALERLMKTRTTIAIA-HRLSTIKNADEI 578
Cdd:PRK13539 156 AALDAAAVALFAELIRAHLAQGGIVIAAtHIPLGLPGAREL 196
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
370-587 |
2.18e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 76.07 E-value: 2.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 370 MNDRIEFKDISFSYdGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLL---PRyhdVQGGDITIDGTSIKDVRIAD- 445
Cdd:PRK11614 2 EKVMLSFDKVSAHY-GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLcgdPR---ATSGRIVFDGKDITDWQTAKi 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 446 LRSLIGNVNQEAILFND-TFFNNIAFGVENATMEQVIEaaKIANAHDFImekPEGYNTNIgDRGGKLSGGQRQRVSIARA 524
Cdd:PRK11614 78 MREAVAIVPEGRRVFSRmTVEENLAMGGFFAERDQFQE--RIKWVYELF---PRLHERRI-QRAGTMSGGEQQMLAIGRA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499421346 525 ILKNPPILILDEATSALDTESERLVQEALERLMKTRTTIAIAHRLS--TIKNADEICVLYEGEIV 587
Cdd:PRK11614 152 LMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNAnqALKLADRGYVLENGHVV 216
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
377-605 |
2.67e-15 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 75.70 E-value: 2.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 377 KDISFSYDGKReVLKHVNLTVPKGKTVALVGQSGSGKST----LVDLLPRyhdvQGGDITIDGTSIKDVRI-ADLRSLIG 451
Cdd:PRK10895 7 KNLAKAYKGRR-VVEDVSLTVNSGEIVGLLGPNGAGKTTtfymVVGIVPR----DAGNIIIDDEDISLLPLhARARRGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 452 NVNQEAILFND-TFFNNIAFGVE---NATMEQVIEAAkianahDFIMEkpEGYNTNIGDR-GGKLSGGQRQRVSIARAIL 526
Cdd:PRK10895 82 YLPQEASIFRRlSVYDNLMAVLQirdDLSAEQREDRA------NELME--EFHIEHLRDSmGQSLSGGERRRVEIARALA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 527 KNPPILILDEATSALDTESERLVQEALERLMKTRTTIAIA-HRL-STIKNADEICVLYEGEIVERGRHEELLeLDGYYKR 604
Cdd:PRK10895 154 ANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITdHNVrETLAVCERAYIVSQGHLIAHGTPTEIL-QDEHVKR 232
|
.
gi 499421346 605 L 605
Cdd:PRK10895 233 V 233
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
384-568 |
3.12e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 74.99 E-value: 3.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 384 DGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDgtsIKDVRIADLRSLIgnvnqEAILFNDT 463
Cdd:COG2401 40 VVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD---VPDNQFGREASLI-----DAIGRKGD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 464 FfnniafgveNATMEqVIEAAKIANAHDFIMEKPEgyntnigdrggkLSGGQRQRVSIARAILKNPPILILDEATSALDT 543
Cdd:COG2401 112 F---------KDAVE-LLNAVGLSDAVLWLRRFKE------------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDR 169
|
170 180
....*....|....*....|....*..
gi 499421346 544 ESERLVQEALERLMKTR--TTIAIAHR 568
Cdd:COG2401 170 QTAKRVARNLQKLARRAgiTLVVATHH 196
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
362-595 |
3.13e-15 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 77.07 E-value: 3.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 362 PNPKPLTGMNDRIEFKDISFSY---DGKREVLKHVNLTVPKGKTVALVGQSGSGKS----TLVDLLPRyHDVQGGDITID 434
Cdd:PRK09473 1 TVPLAQQQADALLDVKDLRVTFstpDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAA-NGRIGGSATFN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 435 GTSIKDVRIADLRSLigNVNQEAILFNDTFFN-NIAFGVENATME------------------QVIEAAKIANAHDFIME 495
Cdd:PRK09473 80 GREILNLPEKELNKL--RAEQISMIFQDPMTSlNPYMRVGEQLMEvlmlhkgmskaeafeesvRMLDAVKMPEARKRMKM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 496 KPEgyntnigdrggKLSGGQRQRVSIARAILKNPPILILDEATSALDTESERLVQEALERLMKTRTT--IAIAHRLSTIK 573
Cdd:PRK09473 158 YPH-----------EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaiIMITHDLGVVA 226
|
250 260
....*....|....*....|...
gi 499421346 574 N-ADEICVLYEGEIVERGRHEEL 595
Cdd:PRK09473 227 GiCDKVLVMYAGRTMEYGNARDV 249
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
384-590 |
4.46e-15 |
|
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: 74.88 E-value: 4.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 384 DGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTsikdvriadLRSLIGnvnqeailFNdT 463
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR---------VSSLLG--------LG-G 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 464 FFNNIAFGVENATMEQVI---EAAKIANAHDFIMEKPEgyntnIGDRG----GKLSGGQRQRVSIARAILKNPPILILDE 536
Cdd:cd03220 94 GFNPELTGRENIYLNGRLlglSRKEIDEKIDEIIEFSE-----LGDFIdlpvKTYSSGMKARLAFAIATALEPDILLIDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499421346 537 ATSALDTESERLVQEAL-ERLMKTRTTIAIAHRLSTIKN-ADEICVLYEGEIVERG 590
Cdd:cd03220 169 VLAVGDAAFQEKCQRRLrELLKQGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
370-606 |
5.32e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 75.12 E-value: 5.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 370 MNDRIEFKDISFSY---------------------DGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLL-----Pry 423
Cdd:COG1134 1 MSSMIEVENVSKSYrlyhepsrslkelllrrrrtrREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIagileP-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 424 hdvQGGDITIDGtsikdvRIAdlrSLIGnVNqeailfndTFFNNIAFGVEN----------------ATMEQVIEAAKIa 487
Cdd:COG1134 79 ---TSGRVEVNG------RVS---ALLE-LG--------AGFHPELTGRENiylngrllglsrkeidEKFDEIVEFAEL- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 488 naHDFIMEKPEGYntnigdrggklSGGQRQRVSIARAILKNPPILILDEATSALDTESERLVQEALERLMKTRTTIAIA- 566
Cdd:COG1134 137 --GDFIDQPVKTY-----------SSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVs 203
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 499421346 567 HRLSTIKN-ADEICVLYEGEIVERGRHEELLELdgYYKRLN 606
Cdd:COG1134 204 HSMGAVRRlCDRAIWLEKGRLVMDGDPEEVIAA--YEALLA 242
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
393-595 |
1.15e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 75.55 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 393 VNLTVPKGKTVALVGQSGSGKST-------LVDLLPRyhdVQGGDITIDGTSIKDVRIADLRSLIGNvnQEAILFNDTFF 465
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVsslaimgLIDYPGR---VMAEKLEFNGQDLQRISEKERRNLVGA--EVAMIFQDPMT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 466 N-NIAFGVENatmeQVIEAAKI----------ANAHDFI----MEKPEgynTNIGDRGGKLSGGQRQRVSIARAILKNPP 530
Cdd:PRK11022 101 SlNPCYTVGF----QIMEAIKVhqggnkktrrQRAIDLLnqvgIPDPA---SRLDVYPHQLSGGMSQRVMIAMAIACRPK 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499421346 531 ILILDEATSALDTESERLVQEALERLMKTRTT--IAIAHRLSTI-KNADEICVLYEGEIVERGRHEEL 595
Cdd:PRK11022 174 LLIADEPTTALDVTIQAQIIELLLELQQKENMalVLITHDLALVaEAAHKIIVMYAGQVVETGKAHDI 241
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
391-595 |
1.18e-14 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 75.51 E-value: 1.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 391 KHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDG---TSIKDVRIADLRSLIgnvnqeAILFND----- 462
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGkdlLGMKDDEWRAVRSDI------QMIFQDplasl 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 463 ----TFFNNIAFGVE----NATMEQVIEAAKIanahdfiMEKPEGYNTNIGDR-GGKLSGGQRQRVSIARAILKNPPILI 533
Cdd:PRK15079 112 nprmTIGEIIAEPLRtyhpKLSRQEVKDRVKA-------MMLKVGLLPNLINRyPHEFSGGQCQRIGIARALILEPKLII 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499421346 534 LDEATSALDTESERLVQEALERLMKTR--TTIAIAHRLSTIKN-ADEICVLYEGEIVERGRHEEL 595
Cdd:PRK15079 185 CDEPVSALDVSIQAQVVNLLQQLQREMglSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
511-581 |
2.02e-14 |
|
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: 71.42 E-value: 2.02e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499421346 511 LSGGQRQRVSIARAILKNPPILILDEATSALDTESERLVQEAL-ERLMktrTTIAIAHRLSTIKNADEICVL 581
Cdd:cd03223 92 LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLkELGI---TVISVGHRPSLWKFHDRVLDL 160
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
92-317 |
2.48e-14 |
|
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: 74.03 E-value: 2.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 92 LIFLGLFLALMTLFKTSCYFASSAVMIPLRTGVVRDIRIMVYAKVMRLPMGFFSEERKGDIIARMSGdVGEVENSITSSL 171
Cdd:cd18567 41 LTVLAIGFGLLLLLQALLSALRSWLVLYLSTSLNLQWTSNLFRHLLRLPLSYFEKRHLGDIVSRFGS-LDEIQQTLTTGF 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 172 DMLIKSPIMIILYFITLIATSWKLTLFTVLVLPAMG---WLMGKVGRKLKRQSLEAQGKWSdtmSQLEETLGGLRIIKAF 248
Cdd:cd18567 120 VEALLDGLMAILTLVMMFLYSPKLALIVLAAVALYAllrLALYPPLRRATEEQIVASAKEQ---SHFLETIRGIQTIKLF 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499421346 249 IAEDRmidRFTRCSNELRDAVN---KVAMRQALAHPMSEFLGTILIVSVLWFGGALILGHNSS---LTAptFIFY 317
Cdd:cd18567 197 GREAE---REARWLNLLVDAINadiRLQRLQILFSAANGLLFGLENILVIYLGALLVLDGEFTvgmLFA--FLAY 266
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
370-542 |
3.25e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 72.84 E-value: 3.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 370 MNDRIEFKDISFSYdGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDllpryhdVQGGDITIDGTSIKdvRIADLRsl 449
Cdd:PRK09544 1 MTSLVSLENVSVSF-GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVR-------VVLGLVAPDEGVIK--RNGKLR-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 450 IGNVNQEaILFNDTF------FNNIAFGVENATMEQVIEAAKIANAHDFIMEKpegyntnigdrggkLSGGQRQRVSIAR 523
Cdd:PRK09544 69 IGYVPQK-LYLDTTLpltvnrFLRLRPGTKKEDILPALKRVQAGHLIDAPMQK--------------LSGGETQRVLLAR 133
|
170
....*....|....*....
gi 499421346 524 AILKNPPILILDEATSALD 542
Cdd:PRK09544 134 ALLNRPQLLVLDEPTQGVD 152
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
382-567 |
4.07e-14 |
|
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: 75.36 E-value: 4.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 382 SYDGKREVLKHVNLTVPKGKTVALVGQSGSGKSTL------VDllpryHDVQGGDITIDGTSI------------KDVR- 442
Cdd:TIGR03719 13 VVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLlrimagVD-----KDFNGEARPQPGIKVgylpqepqldptKTVRe 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 443 -----IADLRSLIGNVNQEAILFNDTFFNNIAFGVENATMEQVIEAAkiaNAHDF------IMEK---PEGyNTNIGdrg 508
Cdd:TIGR03719 88 nveegVAEIKDALDRFNEISAKYAEPDADFDKLAAEQAELQEIIDAA---DAWDLdsqleiAMDAlrcPPW-DADVT--- 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499421346 509 gKLSGGQRQRVSIARAILKNPPILILDEATSALDTESERLVQEALERLmkTRTTIAIAH 567
Cdd:TIGR03719 161 -KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEY--PGTVVAVTH 216
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
88-328 |
4.33e-14 |
|
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: 73.00 E-value: 4.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 88 PTTALIFLGLFLALMtlfktscyfaSSAVMIPLRTGVV--------RDIRIMVYAKVMRLPMGFFSEERKGDIIARMSgD 159
Cdd:cd18566 39 PTLQVLVIGVVIAIL----------LESLLRLLRSYILawigarfdHRLSNAAFEHLLSLPLSFFEREPSGAHLERLN-S 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 160 VGEVENSITSSLDMLIKSPIMIILYFITLIATSWKLTLFTVLVLPA---MGWLMGKVGRKLKRQSLEAQgkwSDTMSQLE 236
Cdd:cd18566 108 LEQIREFLTGQALLALLDLPFVLIFLGLIWYLGGKLVLVPLVLLGLfvlVAILLGPILRRALKERSRAD---ERRQNFLI 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 237 ETLGGLRIIKAFIAEDRMIDRFTRCSNELRDAVNKVAMRQALAHPMSEFLGTILIVSVLWFGGALILghNSSLTAPTFIF 316
Cdd:cd18566 185 ETLTGIHTIKAMAMEPQMLRRYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSMVAVVAFGALLVI--NGDLTVGALIA 262
|
250
....*....|..
gi 499421346 317 YMVILYSVINPL 328
Cdd:cd18566 263 CTMLSGRVLQPL 274
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
373-597 |
5.66e-14 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 71.98 E-value: 5.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 373 RIEFKDISFSYdGKREVLKHVNLTVPKGKTVALVGQSGSGKST----LVDLLPryhdVQGGDITIDGTSIKDVRIaDLRS 448
Cdd:COG1137 3 TLEAENLVKSY-GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTtfymIVGLVK----PDSGRIFLDGEDITHLPM-HKRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 449 L--IGNVNQEAILFND-TFFNNIA-----FGVENATMEQVIEA-------AKIANAhdfimekpegyntnigdRGGKLSG 513
Cdd:COG1137 77 RlgIGYLPQEASIFRKlTVEDNILavlelRKLSKKEREERLEElleefgiTHLRKS-----------------KAYSLSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 514 GQRQRVSIARAILKNPPILILDEATSALDTESERLVQEALERLmKTRtTIAIahrLSTIKNADE---IC----VLYEGEI 586
Cdd:COG1137 140 GERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHL-KER-GIGV---LITDHNVREtlgICdrayIISEGKV 214
|
250
....*....|.
gi 499421346 587 VERGRHEELLE 597
Cdd:COG1137 215 LAEGTPEEILN 225
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
352-591 |
1.26e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 73.76 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 352 LKAENNIKEIPNPKPLTGMNDRIEFKDISFSydgKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPryHDVQGGDI 431
Cdd:PLN03211 49 VKFENMKNKGSNIKRILGHKPKISDETRQIQ---ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALA--GRIQGNNF 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 432 TidGTSIKDVRIADLRSL--IGNVNQEAILF-NDTFFNNIAFGVENATMEQVIEAAKIANAHDFIME----KPEgyNTNI 504
Cdd:PLN03211 124 T--GTILANNRKPTKQILkrTGFVTQDDILYpHLTVRETLVFCSLLRLPKSLTKQEKILVAESVISElgltKCE--NTII 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 505 GD---RGgkLSGGQRQRVSIARAILKNPPILILDEATSALD-TESERLVQEALERLMKTRTTIAIAHRLST--IKNADEI 578
Cdd:PLN03211 200 GNsfiRG--ISGGERKRVSIAHEMLINPSLLILDEPTSGLDaTAAYRLVLTLGSLAQKGKTIVTSMHQPSSrvYQMFDSV 277
|
250
....*....|...
gi 499421346 579 CVLYEGEIVERGR 591
Cdd:PLN03211 278 LVLSEGRCLFFGK 290
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
385-554 |
1.35e-13 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 69.69 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 385 GKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVR------IADLRSLIGNVNQEAI 458
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRdephenILYLGHLPGLKPELSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 459 LFNDTFFNNIaFGVENATMEQVIEAAKIANAHDFIMekpegyntnigdrgGKLSGGQRQRVSIARAILKNPPILILDEAT 538
Cdd:TIGR01189 91 LENLHFWAAI-HGGAQRTIEDALAAVGLTGFEDLPA--------------AQLSAGQQRRLALARLWLSRRPLWILDEPT 155
|
170
....*....|....*.
gi 499421346 539 SALDTESERLVQEALE 554
Cdd:TIGR01189 156 TALDKAGVALLAGLLR 171
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
374-590 |
2.29e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 72.89 E-value: 2.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYDGKReVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRSL-IGN 452
Cdd:PRK09700 6 ISMAGIGKSFGPVH-ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 453 VNQEAILFND-TFFNNIAFG------------VENATMEQVIEaakianahdfIMEKPEGYNTNIGDRGGKLSGGQRQRV 519
Cdd:PRK09700 85 IYQELSVIDElTVLENLYIGrhltkkvcgvniIDWREMRVRAA----------MMLLRVGLKVDLDEKVANLSISHKQML 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499421346 520 SIARAILKNPPILILDEATSAL-DTESERLVQeALERLMKTRTTIA-IAHRLSTIKN-ADEICVLYEGEIVERG 590
Cdd:PRK09700 155 EIAKTLMLDAKVIIMDEPTSSLtNKEVDYLFL-IMNQLRKEGTAIVyISHKLAEIRRiCDRYTVMKDGSSVCSG 227
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
385-553 |
2.66e-13 |
|
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: 69.06 E-value: 2.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 385 GKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRSLIGNVNQEAILFNDTF 464
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 465 FNNIAFGVENATMEQVIEAAKIANAHDFimekpegyntniGDRG-GKLSGGQRQRVSIARAILKNPPILILDEATSALDT 543
Cdd:cd03231 91 LENLRFWHADHSDEQVEEALARVGLNGF------------EDRPvAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
170
....*....|
gi 499421346 544 ESERLVQEAL 553
Cdd:cd03231 159 AGVARFAEAM 168
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
386-590 |
3.41e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 73.22 E-value: 3.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 386 KREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLP----RYHDVQGGDITIDGTSIKDVRiadlRSLIGNV--NQEail 459
Cdd:TIGR00956 73 TFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIK----KHYRGDVvyNAE--- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 460 fNDTFFNNIAFG---------------VENATMEQVieAAKIANAHDFIMEKPEGYNTNIGD---RGgkLSGGQRQRVSI 521
Cdd:TIGR00956 146 -TDVHFPHLTVGetldfaarcktpqnrPDGVSREEY--AKHIADVYMATYGLSHTRNTKVGNdfvRG--VSGGERKRVSI 220
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499421346 522 ARAILKNPPILILDEATSALDTESerlvqeALE--RLMKTRTTIAIAHRLSTIKNA--------DEICVLYEGEIVERG 590
Cdd:TIGR00956 221 AEASLGGAKIQCWDNATRGLDSAT------ALEfiRALKTSANILDTTPLVAIYQCsqdayelfDKVIVLYEGYQIYFG 293
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
388-596 |
3.51e-13 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 70.20 E-value: 3.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 388 EVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGT-------SIKDVRIADL----------RSLI 450
Cdd:PRK15112 27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHplhfgdySYRSQRIRMIfqdpstslnpRQRI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 451 GNVNQEAILFNDTFFNNIAFGVENATMEQVIEAAKIANAHDFImekpegyntnigdrggkLSGGQRQRVSIARAILKNPP 530
Cdd:PRK15112 107 SQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHM-----------------LAPGQKQRLGLARALILRPK 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499421346 531 ILILDEATSALD-TESERLVQEALERLMKTRTT-IAIAHRLSTIKN-ADEICVLYEGEIVERGRHEELL 596
Cdd:PRK15112 170 VIIADEALASLDmSMRSQLINLMLELQEKQGISyIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVL 238
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
375-588 |
5.13e-13 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 71.74 E-value: 5.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 375 EFKDISFSYDGKReVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLL----PryHDVQGGDITIDGtsiKDVRIADLRSL- 449
Cdd:NF040905 3 EMRGITKTFPGVK-ALDDVNLSVREGEIHALCGENGAGKSTLMKVLsgvyP--HGSYEGEILFDG---EVCRFKDIRDSe 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 450 ---IGNVNQE-AILFNDTFFNNIAFGVENATM------EQVIEAAKIanahdfiMEK---PEGYNTNIGDRGGklsgGQR 516
Cdd:NF040905 77 algIVIIHQElALIPYLSIAENIFLGNERAKRgvidwnETNRRAREL-------LAKvglDESPDTLVTDIGV----GKQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499421346 517 QRVSIARAILKNPPILILDEATSAL-DTESERLvqeaLERLMKTR----TTIAIAHRLSTI-KNADEICVLYEGEIVE 588
Cdd:NF040905 146 QLVEIAKALSKDVKLLILDEPTAALnEEDSAAL----LDLLLELKaqgiTSIIISHKLNEIrRVADSITVLRDGRTIE 219
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
340-554 |
5.17e-13 |
|
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: 71.89 E-value: 5.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 340 KGLASMERVDKILKAENNIKE------IPNPKPLTgmNDRIEFKDISFSYdGKREVLKHVNLTVPKGKTVALVGQSGSGK 413
Cdd:TIGR03719 285 KSKARLARYEELLSQEFQKRNetaeiyIPPGPRLG--DKVIEAENLTKAF-GDKLLIDDLSFKLPPGGIVGVIGPNGAGK 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 414 STLVDLLPRYHDVQGGDITIdGTSIKdvriadlrslIGNVNQ--EAILFNDTFFNNIAFGVEnatmeqVIEAAKIA-NAH 490
Cdd:TIGR03719 362 STLFRMITGQEQPDSGTIEI-GETVK----------LAYVDQsrDALDPNKTVWEEISGGLD------IIKLGKREiPSR 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499421346 491 DFImekpEGYNTNIGD---RGGKLSGGQRQRVSIARAILKNPPILILDEATSALDTESERLVQEALE 554
Cdd:TIGR03719 425 AYV----GRFNFKGSDqqkKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALL 487
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
124-348 |
5.31e-13 |
|
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: 70.14 E-value: 5.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 124 VVRDIRIMVYAKVMRLPMGFFSEERKGDIIARMSGDVGEVENSITSSLDMLIKSPIMIILYFITLIATSWKLTLFTVLVL 203
Cdd:cd18554 77 ILYDIRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIF 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 204 PAMGWLMGKVGRKLKRQSLEAQGKWSDTMSQLEETLGGLRIIKAFIAEDRMIDRFTRCSNELRDAVNKVAMRQALAHPMS 283
Cdd:cd18554 157 PFYILAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTRWNAKTFSAV 236
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499421346 284 EFLGTILIVSVLWFGGALILghNSSLTAPTFIFYMVILYSVINPLKDFAKAGYNIPKGLASMERV 348
Cdd:cd18554 237 NTITDLAPLLVIGFAAYLVI--EGNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDRV 299
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
85-348 |
1.04e-12 |
|
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: 69.05 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 85 DNGPTTALIFLGLFLALMTLFKTSC----YFASSAVMIPLRTGVVRdiriMVYAKVMRLPMGFFSEERKGDIIARMSGDV 160
Cdd:cd18579 31 PDEPLSEGYLLALALFLVSLLQSLLlhqyFFLSFRLGMRVRSALSS----LIYRKALRLSSSARQETSTGEIVNLMSVDV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 161 GEVENSITsSLDMLIKSPIMIILYFITLIATSWKLTL----FTVLVLPAMGWLMGKVGRKLKRQSleaqgKWSDT-MSQL 235
Cdd:cd18579 107 QRIEDFFL-FLHYLWSAPLQIIVALYLLYRLLGWAALaglgVLLLLIPLQAFLAKLISKLRKKLM-----KATDErVKLT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 236 EETLGGLRIIKAFIAEDRMIDRFTRC-SNELRdAVNKVAMRQALAhpMSEFLGTILIVSVLWFGGALILGHnsSLTAPTf 314
Cdd:cd18579 181 NEILSGIKVIKLYAWEKPFLKRIEELrKKELK-ALRKFGYLRALN--SFLFFSTPVLVSLATFATYVLLGN--PLTAAK- 254
|
250 260 270
....*....|....*....|....*....|....*
gi 499421346 315 IFYMVILYSVI-NPLKDFAKAGYNIPKGLASMERV 348
Cdd:cd18579 255 VFTALSLFNLLrFPLLMLPQAISSLIEALVSLKRI 289
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
370-593 |
1.47e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 68.37 E-value: 1.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 370 MNDRIEFKDISFSYDGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSikdVRIADLRSL 449
Cdd:PRK15056 3 QQAGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQP---TRQALQKNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 450 IGNVNQEAILfndtffnNIAFGVenaTMEQVIEAAKIAnaHDFIMEKPEGYNTNIGDRG--------------GKLSGGQ 515
Cdd:PRK15056 80 VAYVPQSEEV-------DWSFPV---LVEDVVMMGRYG--HMGWLRRAKKRDRQIVTAAlarvdmvefrhrqiGELSGGQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499421346 516 RQRVSIARAILKNPPILILDEATSALDTESE-RLVQEALERLMKTRTTIAIAHRLSTIKNADEICVLYEGEIVERGRHE 593
Cdd:PRK15056 148 KKRVFLARAIAQQGQVILLDEPFTGVDVKTEaRIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTE 226
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
99-317 |
1.67e-12 |
|
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: 68.27 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 99 LALMTLFKTSCYFASSAVMIPLRTGVVRDIRIMVYAKVMRLPMGFFSEERKGDIIARMSGDVGEVENSITSSLDMLIKSP 178
Cdd:cd18589 42 MSLLTIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 179 IMIILYFITLIATSWKLTLFTVLVLPAMgWLMGKVGRKLKrQSLEAQGKWSDT-MSQLE-ETLGGLRIIKAFIAEDRMID 256
Cdd:cd18589 122 ARGLFLFIFMLWLSPKLALLTALGLPLL-LLVPKFVGKFQ-QSLAVQVQKSLArANQVAvETFSAMKTVRSFANEEGEAQ 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499421346 257 RFTRCSNELRDAVNKVAMRQALAHPMSEFLGTILIVSVLWFGGALIL-GHNSSLTAPTFIFY 317
Cdd:cd18589 200 RYRQRLQKTYRLNKKEAAAYAVSMWTSSFSGLALKVGILYYGGQLVTaGTVSSGDLVTFVLY 261
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
19-308 |
2.01e-12 |
|
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: 68.30 E-value: 2.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 19 IGWAILLNILSAVFNVFSFTllipILDIlfktgennkvyeymeWGTAGFKDVAINNFYYYvsqmiqdngpttaLIFLGLF 98
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNI----WLDW---------------WSSDWSSSPNSSSGYYL-------------GVYAALL 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 99 LALMTLFKTSCYFASSAVMIplRTGvvrdIRI--MVYAKVMRLPMGFFSEERKGDIIARMSGDVGEVENSITSSLDMLIK 176
Cdd:cd18580 49 VLASVLLVLLRWLLFVLAGL--RAS----RRLhdKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQ 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 177 SPIMIILYFITLIATSWKLTLFTVLVLPAMGWLM---GKVGRKLKRQSLEAQgkwSDTMSQLEETLGGLRIIKAFIAEDR 253
Cdd:cd18580 123 SLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLLQryyLRTSRQLRRLESESR---SPLYSHFSETLSGLSTIRAFGWQER 199
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499421346 254 MIDRFTRCSNE------LRDAVNK-VAMRqalahpmSEFLGTILIVSVLWFggALILGHNSS 308
Cdd:cd18580 200 FIEENLRLLDAsqrafyLLLAVQRwLGLR-------LDLLGALLALVVALL--AVLLRSSIS 252
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
371-598 |
2.80e-12 |
|
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: 69.45 E-value: 2.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 371 NDRIEFKDISFSYDG-KREVLKHVN---LTVPKGKTVALVGQSGSGKSTLVDLL-----PRYHD--VQGGDITIDGTSIK 439
Cdd:TIGR03269 277 EPIIKVRNVSKRYISvDRGVVKAVDnvsLEVKEGEIFGIVGTSGAGKTTLSKIIagvlePTSGEvnVRVGDEWVDMTKPG 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 440 DVRIADLRSLIGNVNQEAILF-NDTFFNNI--AFGVENATMEQVIEAAKIANAHDFIMEKPEgyntNIGDR-GGKLSGGQ 515
Cdd:TIGR03269 357 PDGRGRAKRYIGILHQEYDLYpHRTVLDNLteAIGLELPDELARMKAVITLKMVGFDEEKAE----EILDKyPDELSEGE 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 516 RQRVSIARAILKNPPILILDEATSALDTESERLVQEAlerLMKTR-----TTIAIAHRLSTIKN-ADEICVLYEGEIVER 589
Cdd:TIGR03269 433 RHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHS---ILKAReemeqTFIIVSHDMDFVLDvCDRAALMRDGKIVKI 509
|
....*....
gi 499421346 590 GRHEELLEL 598
Cdd:TIGR03269 510 GDPEEIVEE 518
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
393-594 |
2.84e-12 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 68.36 E-value: 2.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 393 VNLTVP-KGKTvALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGT----SIKDVRIADLRSLIGNVNQEAILF-NDTFFN 466
Cdd:PRK11144 17 VNLTLPaQGIT-AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfdAEKGICLPPEKRRIGYVFQDARLFpHYKVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 467 NIAFGVENATMEQV--------IEAakianahdfimekpegyntnIGDR-GGKLSGGQRQRVSIARAILKNPPILILDEA 537
Cdd:PRK11144 96 NLRYGMAKSMVAQFdkivallgIEP--------------------LLDRyPGSLSGGEKQRVAIGRALLTAPELLLMDEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 538 TSALDTESERLVQEALERLMKTRTT--IAIAHRLSTI-KNADEICVLYEGEIVERGRHEE 594
Cdd:PRK11144 156 LASLDLPRKRELLPYLERLAREINIpiLYVSHSLDEIlRLADRVVVLEQGKVKAFGPLEE 215
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
135-349 |
3.79e-12 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350049 [Multi-domain] Cd Length: 300 Bit Score: 67.55 E-value: 3.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 135 KVMRLPMGFFSEERKGDIIARMSGDVGEVENSITSSLDMLIKSPIMIILYFI-TLIATSWKLTLFTVLVLpaMGWLMGKV 213
Cdd:cd18605 84 SILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVvICYQLPWLLLLLLPLAF--IYYRIQRY 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 214 ----GRKLKRQSLEAQGKwsdTMSQLEETLGGLRIIKAFIAEDRMIDRFTRCsneLRDAVNKVAMRQALAHPMS---EFL 286
Cdd:cd18605 162 yratSRELKRLNSVNLSP---LYTHFSETLKGLVTIRAFRKQERFLKEYLEK---LENNQRAQLASQAASQWLSirlQLL 235
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499421346 287 GTILIVSVLWFGgalILGHNSSLTAPTFIFYMVILYS--VINPLKDFAKAGYNIPKGLASMERVD 349
Cdd:cd18605 236 GVLIVTFVALTA---VVQHFFGLSIDAGLIGLALSYAlpITGLLSGLLNSFTETEKEMVSVERVR 297
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
389-542 |
6.45e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 65.57 E-value: 6.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 389 VLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSI----KDVRiADLRSL-IGNVNQEAILFNDt 463
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLhqmdEEAR-AKLRAKhVGFVFQSFMLIPT- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 464 fFNniafGVENATMEQVIEAAKIANAHDFIMEKPEgyNTNIGDR----GGKLSGGQRQRVSIARAILKNPPILILDEATS 539
Cdd:PRK10584 103 -LN----ALENVELPALLRGESSRQSRNGAKALLE--QLGLGKRldhlPAQLSGGEQQRVALARAFNGRPDVLFADEPTG 175
|
...
gi 499421346 540 ALD 542
Cdd:PRK10584 176 NLD 178
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
374-601 |
6.87e-12 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 65.97 E-value: 6.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYDGKrEVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHD--VQGGDITIDGtsiKDVRIADLRSLIG 451
Cdd:PRK09580 2 LSIKDLHVSVEDK-AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDyeVTGGTVEFKG---KDLLELSPEDRAG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 452 nvnqEAILF-----------NDTFFNNIAFGVENATMEQviEAAKIANAHDFIMEK------PEGYNT---NIGdrggkL 511
Cdd:PRK09580 78 ----EGIFMafqypveipgvSNQFFLQTALNAVRSYRGQ--EPLDRFDFQDLMEEKiallkmPEDLLTrsvNVG-----F 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 512 SGGQRQRVSIARAILKNPPILILDEATSALDTESERLVQEALERLMK-TRTTIAIAH--RLSTIKNADEICVLYEGEIVE 588
Cdd:PRK09580 147 SGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDgKRSFIIVTHyqRILDYIKPDYVHVLYQGRIVK 226
|
250
....*....|....*
gi 499421346 589 RGRHE--ELLELDGY 601
Cdd:PRK09580 227 SGDFTlvKQLEEQGY 241
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
388-590 |
9.07e-12 |
|
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: 65.43 E-value: 9.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 388 EVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRSL---IGNVNQEA--ILFND 462
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIgvvFGQKTQLWwdLPVID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 463 TF-FNNIAFGVENA----TMEQVIEAAKIANahdfIMEKPEgyntnigdRggKLSGGQRQRVSIARAILKNPPILILDEA 537
Cdd:cd03267 115 SFyLLAAIYDLPPArfkkRLDELSELLDLEE----LLDTPV--------R--QLSLGQRMRAEIAAALLHEPEILFLDEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499421346 538 TSALDTESERLVQEALERLMKTR--TTIAIAHRLSTI-KNADEICVLYEGEIVERG 590
Cdd:cd03267 181 TIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIeALARRVLVIDKGRLLYDG 236
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
375-599 |
9.62e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 67.63 E-value: 9.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 375 EFKDISFSYDGKReVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIAD-LRSLIGNV 453
Cdd:PRK11288 6 SFDGIGKTFPGVK-ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAaLAAGVAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 454 NQEAILFND-TFFNNI-------AFGVENAtmEQVIEAAKIANAH---DFIMEKPEGYntnigdrggkLSGGQRQRVSIA 522
Cdd:PRK11288 85 YQELHLVPEmTVAENLylgqlphKGGIVNR--RLLNYEAREQLEHlgvDIDPDTPLKY----------LSIGQRQMVEIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 523 RAILKNPPILILDEATSALDT-ESERL--VQEALERlmKTRTTIAIAHRLSTI-KNADEICVLYEGEIVErgRHEELLEL 598
Cdd:PRK11288 153 KALARNARVIAFDEPTSSLSArEIEQLfrVIRELRA--EGRVILYVSHRMEEIfALCDAITVFKDGRYVA--TFDDMAQV 228
|
.
gi 499421346 599 D 599
Cdd:PRK11288 229 D 229
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
84-323 |
9.94e-12 |
|
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: 66.15 E-value: 9.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 84 QDNGPTTALIFLGLFLALMTLFKTSCYFASSAVMIplrtgVVRDIRIMVYAKVMRLPMGFFSEERKGDIIARMSGDVGEV 163
Cdd:cd18558 55 EEEMTLYAYYYLIIGAIVLITAYIQGSFWGLAAGR-----QTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKI 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 164 ENSITSSLDMLIKSPIMIILYFITLIATSWKLTLFTVLVLPAMGWLMGKVGRKLKRQSLEAQGKWSDTMSQLEETLGGLR 243
Cdd:cd18558 130 NEGIGDKIGVIFQNIATFGTGFIIGFIRGWKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFR 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 244 IIKAFIAEDRMIDRFtrcSNELRDAvNKVAMRQALAHPMSEFLGTILI----VSVLWFGGALILGHNSSLTAPTFIFYMV 319
Cdd:cd18558 210 TVIAFGGQQKEETRY---AQNLEIA-KRNGIKKAITFNISMGAAFLLIyasyALAFWYGTYLVTQQEYSIGEVLTVFFSV 285
|
....
gi 499421346 320 ILYS 323
Cdd:cd18558 286 LIGA 289
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
78-262 |
1.59e-11 |
|
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: 65.57 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 78 YVSQMIQDNGPTTALIFLGLFLALMTLFkTSCYFASSAVMIplrTGVVRDIRI----MVYAkVMRLPMGFFSEERKGDII 153
Cdd:cd18604 29 YETSSALPPSEVSVLYYLGIYALISLLS-VLLGTLRYLLFF---FGSLRASRKlherLLHS-VLRAPLRWLDTTPVGRIL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 154 ARMSGDVGEVENSITSSLDMLIKSPIMIILYFITLIATSWKLTLFTVLVLpAMGWLMG----KVGRKLKRqsLEAQGKwS 229
Cdd:cd18604 104 NRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLA-ALYVYIGrlylRASRELKR--LESVAR-S 179
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 499421346 230 DTMSQLEETLGGLRIIKAFIAEDR-------MIDRFTRCS 262
Cdd:cd18604 180 PILSHFGETLAGLVTIRAFGAEERfieemlrRIDRYSRAF 219
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
127-321 |
2.74e-11 |
|
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: 64.81 E-value: 2.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 127 DIRIMVYAKVMRLPMGFFSEERKGDIIARMSGDVGEVEN----SITSSLDMLIKSPIMIIlyFITLIatSWKLTLFTVLV 202
Cdd:cd18585 69 NLRVWFYRKLEPLAPARLQKYRSGDLLNRIVADIDTLDNlylrVLSPPVVALLVILATIL--FLAFF--SPALALILLAG 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 203 LPAMG----WLMGKVGRKLKRQSLEAQGKWSdtmSQLEETLGGLRIIKAFIAEDRMIDRFTRCSNELRDAVNKVAMRQAL 278
Cdd:cd18585 145 LLLAGvvipLLFYRLGKKIGQQLVQLRAELR---TELVDGLQGMAELLIFGALERQRQQLEQLSDALIKEQRRLARLSGL 221
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499421346 279 AHPMSEFLGTILIVSVLWFGGALIlgHNSSLTAPTFIfyMVIL 321
Cdd:cd18585 222 SQALMILLSGLTVWLVLWLGAPLV--QNGALDGALLA--MLVF 260
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
383-567 |
3.93e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 65.91 E-value: 3.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 383 YDGKREVLKHVNLTVPKGKTVALVGQSGSGKSTL------VDllpryHDVQGGDITIDGTSI------------KDVRia 444
Cdd:PRK11819 16 VPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLlrimagVD-----KEFEGEARPAPGIKVgylpqepqldpeKTVR-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 445 dlrsliGNVnQEAilFNDTF-----FNNI--AFGVENATMEQVIE-----AAKI--ANAHDF------IMEK---PEGyN 501
Cdd:PRK11819 89 ------ENV-EEG--VAEVKaaldrFNEIyaAYAEPDADFDALAAeqgelQEIIdaADAWDLdsqleiAMDAlrcPPW-D 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499421346 502 TNIGdrggKLSGGQRQRVSIARAILKNPPILILDEATSALDTESerlVqEALERLMKTR--TTIAIAH 567
Cdd:PRK11819 159 AKVT----KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES---V-AWLEQFLHDYpgTVVAVTH 218
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
373-587 |
4.26e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 65.43 E-value: 4.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 373 RIEFKDISFSYDGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRSL-IG 451
Cdd:COG3845 257 VLEVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 452 NVNQE-----AILfndtffnniAFGV-ENATMEQ----------VIEAAKI-ANAHDFImekpEGYN---TNIGDRGGKL 511
Cdd:COG3845 337 YIPEDrlgrgLVP---------DMSVaENLILGRyrrppfsrggFLDRKAIrAFAEELI----EEFDvrtPGPDTPARSL 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 512 SGGQRQRVSIARAILKNPPILILDEATSALDTES-----ERLVQEA------------LERLMktrttiAIAHRlstikn 574
Cdd:COG3845 404 SGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAiefihQRLLELRdagaavllisedLDEIL------ALSDR------ 471
|
250
....*....|...
gi 499421346 575 adeICVLYEGEIV 587
Cdd:COG3845 472 ---IAVMYEGRIV 481
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
374-606 |
7.89e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 64.64 E-value: 7.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYDGKReVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGtsiKDVRIADLRSL---- 449
Cdd:PRK10762 5 LQLKGIDKAFPGVK-ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLG---KEVTFNGPKSSqeag 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 450 IGNVNQEAILF-NDTFFNNIAFGVENATMEQVIEAAKIANAHDFIMEKpegYNTNIGDRG--GKLSGGQRQRVSIARAIL 526
Cdd:PRK10762 81 IGIIHQELNLIpQLTIAENIFLGREFVNRFGRIDWKKMYAEADKLLAR---LNLRFSSDKlvGELSIGEQQMVEIAKVLS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 527 KNPPILILDEATSAL-DTESERLVQEALERLMKTRTTIAIAHRLSTIKnadEIC----VLYEGE-IVERG----RHEELL 596
Cdd:PRK10762 158 FESKVIIMDEPTDALtDTETESLFRVIRELKSQGRGIVYISHRLKEIF---EICddvtVFRDGQfIAEREvadlTEDSLI 234
|
250
....*....|....*.
gi 499421346 597 E------LDGYYKRLN 606
Cdd:PRK10762 235 EmmvgrkLEDQYPRLD 250
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
378-596 |
2.05e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 61.95 E-value: 2.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 378 DISFSYDGKrEVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRiadlRSLIGNVNQEA 457
Cdd:PRK13638 6 DLWFRYQDE-PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSK----RGLLALRQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 458 ILFND----TFF----NNIAFGVENATMEQ------VIEAAKIANAHDFIMEKPEGyntnigdrggkLSGGQRQRVSIAR 523
Cdd:PRK13638 81 TVFQDpeqqIFYtdidSDIAFSLRNLGVPEaeitrrVDEALTLVDAQHFRHQPIQC-----------LSHGQKKRVAIAG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499421346 524 AILKNPPILILDEATSALDTESERLVQEALERLMKTRTTIAI-AHRLSTIKN-ADEICVLYEGEIVERGRHEELL 596
Cdd:PRK13638 150 ALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIIsSHDIDLIYEiSDAVYVLRQGQILTHGAPGEVF 224
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
386-605 |
2.75e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 62.03 E-value: 2.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 386 KREV--LKHVNLTVPKGKTVALVGQSGSGKSTLVDLL-----PryhdvQGGDITIDGTSIKDVRIADLRSlIGNV----N 454
Cdd:COG4586 32 YREVeaVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLtgilvP-----TSGEVRVLGYVPFKRRKEFARR-IGVVfgqrS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 455 QeaiLF-----NDTF-FNNIAFGVENA----TMEQVIEAAKIANahdfIMEKPEgyntnigdRggKLSGGQRQRVSIARA 524
Cdd:COG4586 106 Q---LWwdlpaIDSFrLLKAIYRIPDAeykkRLDELVELLDLGE----LLDTPV--------R--QLSLGQRMRCELAAA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 525 ILKNPPILILDEATSALDTESERLVQEALERLMKTR-TTIAIA-HRLSTIKN-ADEICVLYEGEIVERGRHEELLELDGY 601
Cdd:COG4586 169 LLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERgTTILLTsHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKERFGP 248
|
....
gi 499421346 602 YKRL 605
Cdd:COG4586 249 YKTI 252
|
|
| ABC_6TM_NHLM_bacteriocin |
cd18569 |
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ... |
135-348 |
3.12e-10 |
|
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: 61.34 E-value: 3.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 135 KVMRLPMGFFSEERKGDIIARMSGDvGEVENSITSSLDMLIKSPIMIILYFITLIATSWKLTLFTVLVLPAMGWLMGKVG 214
Cdd:cd18569 84 HVLRLPVEFFSQRYAGDIASRVQSN-DRVANLLSGQLATTVLNLVMAVFYALLMLQYDVPLTLIGIAIALLNLLVLRLVS 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 215 RKLK---RQSLEAQGKWSDTmsqleeTLGGLRII---KAFIAEDrmiDRFTRCSNELRDAVN---KVAMRQALAHPMSEF 285
Cdd:cd18569 163 RKRVdlnRRLLQDSGKLTGT------TMSGLQMIetlKASGAES---DFFSRWAGYQAKVLNaqqELGRTNQLLGALPTL 233
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499421346 286 LGTILIVSVLWFGGALILghNSSLTAPTFIFYMVILYSVINPLKDFAKAGYNIPKGLASMERV 348
Cdd:cd18569 234 LSALTNAAILGLGGLLVM--DGALTIGMLVAFQSLMASFLAPVNSLVGLGGTLQEMRGDMERL 294
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
387-590 |
3.49e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 61.00 E-value: 3.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 387 REVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLL---------PRYHDVQgGDITIDG---TSIKDVRIADLRSLIGNVN 454
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALagdltgggaPRGARVT-GDVTLNGeplAAIDAPRLARLRAVLPQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 455 QEAILFN-DTF-----FNNIAFGVENATMEQVIEAAKIANAhdfimekpeGYNTNIGDRGGKLSGGQRQRVSIARAILK- 527
Cdd:PRK13547 93 QPAFAFSaREIvllgrYPHARRAGALTHRDGEIAWQALALA---------GATALVGRDVTTLSGGELARVQFARVLAQl 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499421346 528 --------NPPILILDEATSALDTESERLVQEALERLMK--TRTTIAIAHRLS-TIKNADEICVLYEGEIVERG 590
Cdd:PRK13547 164 wpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARdwNLGVLAIVHDPNlAARHADRIAMLADGAIVAHG 237
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
77-270 |
4.84e-10 |
|
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: 60.81 E-value: 4.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 77 YYVSQMI-------QDNGPTTALIFLGLFLAlmtlfktscyfaSSAVMIPLRTGV--------VRDIRIMVYAKVMRLPM 141
Cdd:cd18590 17 YYTGRVIdilggeyQHNAFTSAIGLMCLFSL------------GSSLSAGLRGGLfmctlsrlNLRLRHQLFSSLVQQDI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 142 GFFSEERKGDIIARMSGDVGEVENSITSSLDMLIKSPIMIILYFITLIATSWKLTLFTVLVLPaMGWLMGKV----GRKL 217
Cdd:cd18590 85 GFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMP-LTAIAQKVyntyHQKL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499421346 218 KRQSLEAQGKWSDTMSqleETLGGLRIIKAFIAEDRMIDRFtrcSNELRDAVN 270
Cdd:cd18590 164 SQAVQDSIAKAGELAR---EAVSSIRTVRSFKAEEEEACRY---SEALERTYN 210
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
390-578 |
8.22e-10 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 59.94 E-value: 8.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 390 LKHVNLTVPKGKTVALVGQSGSGKSTLV-DLL--------------PRYHDVQGGDITIDgtsiKDVRIAdlRSLIGNvN 454
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLInDTLypalarrlhlkkeqPGNHDRIEGLEHID----KVIVID--QSPIGR-T 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 455 QEAI-------------LFND----TFFN-----------NIAfGVENATMEQVIE----AAKIANAHDFIMEKPEGYNT 502
Cdd:cd03271 84 PRSNpatytgvfdeireLFCEvckgKRYNretlevrykgkSIA-DVLDMTVEEALEffenIPKIARKLQTLCDVGLGYIK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 503 nIGDRGGKLSGGQRQRVSIARAILK---NPPILILDEATSALDTESERLVQEALERLM-KTRTTIAIAHRLSTIKNADEI 578
Cdd:cd03271 163 -LGQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVdKGNTVVVIEHNLDVIKCADWI 241
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
373-600 |
8.60e-10 |
|
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: 61.69 E-value: 8.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 373 RIEFKDISFSYDGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDgtsiKDVRI--------A 444
Cdd:TIGR00954 451 GIKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKP----AKGKLfyvpqrpyM 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 445 DLRSLignvnQEAILFNDTFFNNIAFGVENATMEQVIEAAKIanahDFIMEKPEGYNTnIGDRGGKLSGGQRQRVSIARA 524
Cdd:TIGR00954 527 TLGTL-----RDQIIYPDSSEDMKRRGLSDKDLEQILDNVQL----THILEREGGWSA-VQDWMDVLSGGEKQRIAMARL 596
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499421346 525 ILKNPPILILDEATSALDTESERLVQEALERlmKTRTTIAIAHRLSTIKnadeicvlyegeivergRHEELLELDG 600
Cdd:TIGR00954 597 FYHKPQFAILDECTSAVSVDVEGYMYRLCRE--FGITLFSVSHRKSLWK-----------------YHEYLLYMDG 653
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
393-596 |
1.31e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 59.18 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 393 VNLTVPKGKTVALVGQSGSGKSTLVD----LLPryhdvQGGDITIDGTSIKDVRIADL---RSLIgnVNQEAILFNDTFF 465
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLArmagLLP-----GSGSIQFAGQPLEAWSAAELarhRAYL--SQQQTPPFAMPVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 466 NNIAF--------GVENATMEQVIEAAKIAnahDFImekpegyNTNIGdrggKLSGGQRQRVSIARAILK-----NP--P 530
Cdd:PRK03695 88 QYLTLhqpdktrtEAVASALNEVAEALGLD---DKL-------GRSVN----QLSGGEWQRVRLAAVVLQvwpdiNPagQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499421346 531 ILILDEATSALDTESerlvQEALERLMKT--RTTIAI---AHRLS-TIKNADEICVLYEGEIVERGRHEELL 596
Cdd:PRK03695 154 LLLLDEPMNSLDVAQ----QAALDRLLSElcQQGIAVvmsSHDLNhTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
352-585 |
1.41e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 60.95 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 352 LKAEN------NIK-EIPNPKPLTGMNDRIEFKDISFSYDGKRevlkhvnLTVPKGK-----TVALVGQSGSGKSTLVDL 419
Cdd:COG1245 313 LPEENvrirdePIEfEVHAPRREKEEETLVEYPDLTKSYGGFS-------LEVEGGEiregeVLGIVGPNGIGKTTFAKI 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 420 LpryhdvqGGDITIDGTSI-KDVRIA------------DLRSLIGNVNQEAilFNDTFFNniafgvenatmEQVIEAAKI 486
Cdd:COG1245 386 L-------AGVLKPDEGEVdEDLKISykpqyispdydgTVEEFLRSANTDD--FGSSYYK-----------TEIIKPLGL 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 487 anahDFIMEKpegyntNIGDrggkLSGGQRQRVSIARAILKNPPILILDEATSALDTESERLVQEALERLMKTR--TTIA 564
Cdd:COG1245 446 ----EKLLDK------NVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRgkTAMV 511
|
250 260
....*....|....*....|..
gi 499421346 565 IAHRLSTIKN-ADEICVlYEGE 585
Cdd:COG1245 512 VDHDIYLIDYiSDRLMV-FEGE 532
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
390-590 |
1.68e-09 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 57.33 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 390 LKHVNLTVPKGKTVALVGQSGSGKSTLVDllpryhdvqggditidgTSIKDVRIADLRSLIGNVNQEAILFNDTFFNNIA 469
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN-----------------EGLYASGKARLISFLPKFSRNKLIFIDQLQFLID 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 470 FGVENATMEQVIeaakianahdfimekpegyntnigdrgGKLSGGQRQRVSIARAILKNPP--ILILDEATSALDTESER 547
Cdd:cd03238 74 VGLGYLTLGQKL---------------------------STLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDIN 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499421346 548 LVQEALERLM-KTRTTIAIAHRLSTIKNADEICVL------YEGEIVERG 590
Cdd:cd03238 127 QLLEVIKGLIdLGNTVILIEHNLDVLSSADWIIDFgpgsgkSGGKVVFSG 176
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
372-590 |
2.71e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 58.40 E-value: 2.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 372 DRIEFKDISFS-YDGkrEVLkhvnltvpkgktvALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADL---- 446
Cdd:PRK11701 18 PRKGCRDVSFDlYPG--EVL-------------GIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseae 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 447 -----RSLIGNVNQ---EAILFNDTFFNNI-----AFGVEN-----ATMEQVIEAAKIANAHdfimekpegyntnIGDRG 508
Cdd:PRK11701 83 rrrllRTEWGFVHQhprDGLRMQVSAGGNIgerlmAVGARHygdirATAGDWLERVEIDAAR-------------IDDLP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 509 GKLSGGQRQRVSIARAILKNPPILILDEATSALDTEserlVQEALERLMKTRTT------------IAIAHRLstiknAD 576
Cdd:PRK11701 150 TTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVS----VQARLLDLLRGLVRelglavvivthdLAVARLL-----AH 220
|
250
....*....|....
gi 499421346 577 EICVLYEGEIVERG 590
Cdd:PRK11701 221 RLLVMKQGRVVESG 234
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
91-328 |
2.71e-09 |
|
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: 58.68 E-value: 2.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 91 ALIFLGLFLALMTLFKTScyfassaVMIPLRTGVvrDIRIM--VYAKVMRLPMGFFSEERKGDIIARMSGDVgEVENSIT 168
Cdd:cd18555 47 GILILFLLYGLFSFLRGY-------IIIKLQTKL--DKSLMsdFFEHLLKLPYSFFENRSSGDLLFRANSNV-YIRQILS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 169 SSLDMLIKSPIMIILYFITLIATSWKLTLFTVL---VLPAMGWLMGKVGRKLKRQSLEAQGKwsdTMSQLEETLGGLRII 245
Cdd:cd18555 117 NQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLlglLIVLLLLLTRKKIKKLNQEEIVAQTK---VQSYLTETLYGIETI 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 246 KAFIAEDRMIDRFTRCSNELRDAVNKVAMRQALAHPMSEFLGTILIVSVLWFGGALILGHNssLTAPTFIFYMVILYSVI 325
Cdd:cd18555 194 KSLGSEKNIYKKWENLFKKQLKAFKKKERLSNILNSISSSIQFIAPLLILWIGAYLVINGE--LTLGELIAFSSLAGSFL 271
|
...
gi 499421346 326 NPL 328
Cdd:cd18555 272 TPI 274
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
387-586 |
2.79e-09 |
|
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: 60.41 E-value: 2.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 387 REVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIkDVRIADLRSLIGNVNQEAILFND-TFF 465
Cdd:TIGR01257 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHlTVA 1021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 466 NNIAF-------GVENATMEqvIEAakianahdfiMEKPEGYNTNIGDRGGKLSGGQRQRVSIARAILKNPPILILDEAT 538
Cdd:TIGR01257 1022 EHILFyaqlkgrSWEEAQLE--MEA----------MLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPT 1089
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499421346 539 SALDTESERLVQEALERLMKTRTTIAIAHRLSTIKN-ADEICVLYEGEI 586
Cdd:TIGR01257 1090 SGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLlGDRIAIISQGRL 1138
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
396-585 |
2.98e-09 |
|
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: 57.80 E-value: 2.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 396 TVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIK----------DVRIADLRSLIGNvnqeaILFNDTFF 465
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSykpqyikadyEGTVRDLLSSITK-----DFYTHPYF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 466 NNiafgvenatmeQVIEAAKIanahDFIMEK--PEgyntnigdrggkLSGGQRQRVSIARAILKNPPILILDEATSALDT 543
Cdd:cd03237 96 KT-----------EIAKPLQI----EQILDRevPE------------LSGGELQRVAIAACLSKDADIYLLDEPSAYLDV 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499421346 544 ESERLVQEALERLM--KTRTTIAIAHRLSTIKN-ADEICVlYEGE 585
Cdd:cd03237 149 EQRLMASKVIRRFAenNEKTAFVVEHDIIMIDYlADRLIV-FEGE 192
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
387-587 |
3.46e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 59.26 E-value: 3.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 387 REVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGT--SIKDVRIAdLRSLIGNV----NQEAILF 460
Cdd:COG1129 265 GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvRIRSPRDA-IRAGIAYVpedrKGEGLVL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 461 NDTFFNNIA---------FGV-----ENATMEQVIEAAKIanahdfimeKPEGYNTNIGDrggkLSGGQRQRVSIARAIL 526
Cdd:COG1129 344 DLSIRENITlasldrlsrGGLldrrrERALAEEYIKRLRI---------KTPSPEQPVGN----LSGGNQQKVVLAKWLA 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499421346 527 KNPPILILDEATSALD--TESE--RLVQEA-------------LERLmktrttIAIAHRlstiknadeICVLYEGEIV 587
Cdd:COG1129 411 TDPKVLILDEPTRGIDvgAKAEiyRLIRELaaegkavivisseLPEL------LGLSDR---------ILVMREGRIV 473
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
377-587 |
4.14e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 59.36 E-value: 4.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 377 KDISFSYDGKReVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSI--KDVRIAdLRSLIGNVN 454
Cdd:PRK10982 2 SNISKSFPGVK-ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfKSSKEA-LENGISMVH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 455 QEAILFND-TFFNNIAFGvENATMEQVIEAAKIANAHDFIMEKpEGYNTNIGDRGGKLSGGQRQRVSIARAILKNPPILI 533
Cdd:PRK10982 80 QELNLVLQrSVMDNMWLG-RYPTKGMFVDQDKMYRDTKAIFDE-LDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499421346 534 LDEATSALdteSERLVQEALERLMKTRT----TIAIAHRLSTI-KNADEICVLYEGEIV 587
Cdd:PRK10982 158 MDEPTSSL---TEKEVNHLFTIIRKLKErgcgIVYISHKMEEIfQLCDEITILRDGQWI 213
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
395-582 |
6.47e-09 |
|
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: 56.99 E-value: 6.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 395 LTVPK-GKTVALVGQSGSGKSTLVDLLP--------RYHDVQGGDITID---GTSIKD----VRIADLRSLIG--NVNQE 456
Cdd:cd03236 20 LPVPReGQVLGLVGPNGIGKSTALKILAgklkpnlgKFDDPPDWDEILDefrGSELQNyftkLLEGDVKVIVKpqYVDLI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 457 AILFNDTFFNNIAFGVENATMEQVIEAAKIANahdfIMEKpegyntNIGDrggkLSGGQRQRVSIARAILKNPPILILDE 536
Cdd:cd03236 100 PKAVKGKVGELLKKKDERGKLDELVDQLELRH----VLDR------NIDQ----LSGGELQRVAIAAALARDADFYFFDE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499421346 537 ATSALDT----ESERLVQEALErlmKTRTTIAIAHRLSTIKN-ADEICVLY 582
Cdd:cd03236 166 PSSYLDIkqrlNAARLIRELAE---DDNYVLVVEHDLAVLDYlSDYIHCLY 213
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
399-572 |
6.95e-09 |
|
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: 55.07 E-value: 6.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 399 KGKTVALVGQSGSGKSTLVDLLPRYHDVQGGD-ITIDGTSIKDVRIADLRslignvnqeailfndtffnniafgvenatm 477
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLL------------------------------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 478 eqvieaakianahdfimekpegyNTNIGDRGGKLSGGQRQRVSIARAILKNPPILILDEATSALDTESERLVQEALERLM 557
Cdd:smart00382 51 -----------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRL 107
|
170 180
....*....|....*....|..
gi 499421346 558 KTR-------TTIAIAHRLSTI 572
Cdd:smart00382 108 LLLlkseknlTVILTTNDEKDL 129
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
340-554 |
6.95e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 58.59 E-value: 6.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 340 KGLASMERVDKILKAENNIKE------IPNPKPLtGmNDRIEFKDISFSYdGKREVLKHVNLTVPKGKTVALVGQSGSGK 413
Cdd:PRK11819 287 KSKARLARYEELLSEEYQKRNetneifIPPGPRL-G-DKVIEAENLSKSF-GDRLLIDDLSFSLPPGGIVGIIGPNGAGK 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 414 STLVDLLPRYHDVQGGDITIdGTSIKdvriadlrslIGNVNQ--EAILFNDTFFNNIAFGVENATMEQViEAAKIANAHD 491
Cdd:PRK11819 364 STLFKMITGQEQPDSGTIKI-GETVK----------LAYVDQsrDALDPNKTVWEEISGGLDIIKVGNR-EIPSRAYVGR 431
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499421346 492 FimekpegyNTNIGD---RGGKLSGGQRQRVSIARaILK---NppILILDEATSALDTESERLVQEALE 554
Cdd:PRK11819 432 F--------NFKGGDqqkKVGVLSGGERNRLHLAK-TLKqggN--VLLLDEPTNDLDVETLRALEEALL 489
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
373-576 |
7.21e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 58.49 E-value: 7.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 373 RIEFKDISFSYDGKReVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDvQG--GDITIDGTSikdvR-----IAD 445
Cdd:PRK10938 260 RIVLNNGVVSYNDRP-ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHP-QGysNDLTLFGRR----RgsgetIWD 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 446 LRSLIGNVN-------------QEAILfnDTFFNNIafGVENATMEQvieAAKIANAHDFIMekpeGYNTNIGDRG-GKL 511
Cdd:PRK10938 334 IKKHIGYVSsslhldyrvstsvRNVIL--SGFFDSI--GIYQAVSDR---QQKLAQQWLDIL----GIDKRTADAPfHSL 402
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499421346 512 SGGQRQRVSIARAILKNPPILILDEATSALDTESERLVQEALERLM-KTRTTI------------AIAHRLSTIKNAD 576
Cdd:PRK10938 403 SWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIsEGETQLlfvshhaedapaCITHRLEFVPDGD 480
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
91-260 |
8.82e-09 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350043 [Multi-domain] Cd Length: 313 Bit Score: 57.19 E-value: 8.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 91 ALIFLGLFLALM--TLFKTSCYfassaVMIPLRtgVVRDIRIMVYAKVMRLPMGFFSEERKGDIIARMSGDVGEVENSIT 168
Cdd:cd18599 61 QLVYGGSILVILllSLIRGFVF-----VKVTLR--ASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLP 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 169 SSLDMLIKSPIMIILYFITLIATSWKLTLFTVLVLPAMGWL--MGKVG-RKLKRQSLEAQgkwSDTMSQLEETLGGLRII 245
Cdd:cd18599 134 FTLENFLQNVLLVVFSLIIIAIVFPWFLIALIPLAIIFVFLskIFRRAiRELKRLENISR---SPLFSHLTATIQGLSTI 210
|
170
....*....|....*
gi 499421346 246 KAFIAEDRMIDRFTR 260
Cdd:cd18599 211 HAFNKEKEFLSKFKK 225
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
384-570 |
1.27e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 58.32 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 384 DGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLP--RYHDVQGGDITIDGTSIKD---VRIA------DLRSLIGN 452
Cdd:PLN03140 890 EDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAgrKTGGYIEGDIRISGFPKKQetfARISgyceqnDIHSPQVT 969
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 453 VnQEAILFNDTFFNNIAFGVENATM--EQVIEAAKIANAHDFIMEKPegyntniGDRGgkLSGGQRQRVSIARAILKNPP 530
Cdd:PLN03140 970 V-RESLIYSAFLRLPKEVSKEEKMMfvDEVMELVELDNLKDAIVGLP-------GVTG--LSTEQRKRLTIAVELVANPS 1039
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 499421346 531 ILILDEATSALDTESERLVQEALERLMKT-RTTIAIAHRLS 570
Cdd:PLN03140 1040 IIFMDEPTSGLDARAAAIVMRTVRNTVDTgRTVVCTIHQPS 1080
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
379-587 |
1.54e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 57.65 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 379 ISFSYdgkREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLpryhdvqGGDITIDGTSI---KDVRIADL-----RSLI 450
Cdd:PRK11147 11 LSFSD---APLLDNAELHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDDGRIiyeQDLIVARLqqdppRNVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 451 GNVnqeailfndtfFNNIAFGVENAT------------------------MEQVIEAAKIANAHDF---IMEKPEGYNTN 503
Cdd:PRK11147 81 GTV-----------YDFVAEGIEEQAeylkryhdishlvetdpseknlneLAKLQEQLDHHNLWQLenrINEVLAQLGLD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 504 IGDRGGKLSGGQRQRVSIARAILKNPPILILDEATSALDTESerlvQEALERLMKT--RTTIAIAHRLSTIKN-ADEICV 580
Cdd:PRK11147 150 PDAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIET----IEWLEGFLKTfqGSIIFISHDRSFIRNmATRIVD 225
|
....*..
gi 499421346 581 LYEGEIV 587
Cdd:PRK11147 226 LDRGKLV 232
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
352-591 |
1.58e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.51 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 352 LKAEN------NIK-EIPNPKPLTGMNDRIEFKDISFSYDG-KREVLKHvnlTVPKGKTVALVGQSGSGKSTLVDLLpry 423
Cdd:PRK13409 312 LPEENmrirpePIEfEERPPRDESERETLVEYPDLTKKLGDfSLEVEGG---EIYEGEVIGIVGPNGIGKTTFAKLL--- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 424 hdvqGGDITIDGTSI-KDVRIA------------DLRSLIGNVNQEailFNDTFFNNiafgvenatmeqviEAAKIANAH 490
Cdd:PRK13409 386 ----AGVLKPDEGEVdPELKISykpqyikpdydgTVEDLLRSITDD---LGSSYYKS--------------EIIKPLQLE 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 491 DfIMEKpegyntNIGDrggkLSGGQRQRVSIARAILKNPPILILDEATSALDTEsERL-VQEALERLMKTR--TTIAIAH 567
Cdd:PRK13409 445 R-LLDK------NVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE-QRLaVAKAIRRIAEEReaTALVVDH 512
|
250 260
....*....|....*....|....*
gi 499421346 568 RLSTIKN-ADEICVlYEGEIVERGR 591
Cdd:PRK13409 513 DIYMIDYiSDRLMV-FEGEPGKHGH 536
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
90-348 |
1.58e-08 |
|
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents the 6-transmembrane (6TM) domain of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides.
Pssm-ID: 350003 [Multi-domain] Cd Length: 290 Bit Score: 56.45 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 90 TALIFLGLFLALMTLFKTScyFASSAVMIPLRTGVVRDirimVYAKVMRLPMGFFSEERKGDIIARMSGDVGEVENSITS 169
Cdd:cd18559 41 LSVLGALAILQGITVFQYS--MAVSIGGIFASRAVHLD----LYHKALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 170 SLDMLIKSPIMII-LYFITLIATSwkltlfTVLVLPAMGWLMGKVGR-----KLKRQSLEAQGKwSDTMSQLEETLGGLR 243
Cdd:cd18559 115 VIKMWMGPLQNVIgLYLLILLAGP------MAAVGIPLGLLYVPVNRvyaasSRQLKRLESVSK-DPRYKLFNETLLGIS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 244 IIKAFIAEDRMIDRFTRCSNELRDAVNKVAMRQALAhpMSEFLGTILIVSVLWFGGALILGHNSSLTApTFIFYMVILYS 323
Cdd:cd18559 188 VIKAFEWEEAFIRQVDAKRDNELAYLPSIVYLRALA--VRLWCVGPCIVLFASFFAYVSRHSLAGLVA-LKVFYSLALTT 264
|
250 260
....*....|....*....|....*.
gi 499421346 324 VIN-PLKDFAKAGYNIPKGLASMERV 348
Cdd:cd18559 265 YLNwPLNMSPEVITNIVAAEVSLERS 290
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
375-585 |
2.42e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.88 E-value: 2.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 375 EFKDISFSYDGKrEVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIdGTSIK----DVRIADL---R 447
Cdd:PRK11147 321 EMENVNYQIDGK-QLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKLEvayfDQHRAELdpeK 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 448 SLIGNV---NQEaILFNdtffnniafGVENATMEQVieaakianaHDFIMEkPEGYNTNIGdrggKLSGGQRQRVSIARA 524
Cdd:PRK11147 399 TVMDNLaegKQE-VMVN---------GRPRHVLGYL---------QDFLFH-PKRAMTPVK----ALSGGERNRLLLARL 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499421346 525 ILKNPPILILDEATSALDTESERLVQEALERLmkTRTTIAIAHRLSTIKNADEICVLYEGE 585
Cdd:PRK11147 455 FLKPSNLLILDEPTNDLDVETLELLEELLDSY--QGTVLLVSHDRQFVDNTVTECWIFEGN 513
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
378-576 |
3.50e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 54.19 E-value: 3.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 378 DISFSYDgKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRSL--IGN--- 452
Cdd:PRK13540 6 ELDFDYH-DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLcfVGHrsg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 453 VNQEAILFNDTFFnNIAFGVENATMEQVIEAAKIANAHDFIMekpegyntnigdrgGKLSGGQRQRVSIARAILKNPPIL 532
Cdd:PRK13540 85 INPYLTLRENCLY-DIHFSPGAVGITELCRLFSLEHLIDYPC--------------GLLSSGQKRQVALLRLWMSKAKLW 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499421346 533 ILDEATSALDTES-ERLVQEALERLMKTRTTIAIAHRLSTIKNAD 576
Cdd:PRK13540 150 LLDEPLVALDELSlLTIITKIQEHRAKGGAVLLTSHQDLPLNKAD 194
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
510-596 |
3.50e-08 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 55.58 E-value: 3.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 510 KLSGGQRQRVSIARAILKNPPILILDEATSALDTESERLVQEALERLMKTR-TTI-AIAHRLSTI-KNADEICVLYEGEI 586
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNnTTIlLISHDLQMLsQWADKINVLYCGQT 237
|
90
....*....|
gi 499421346 587 VERGRHEELL 596
Cdd:PRK15093 238 VETAPSKELV 247
|
|
| ABC_6TM_PglK_like |
cd18553 |
Six-transmembrane helical domain of the ABC transporter PglK and similar proteins; This group ... |
73-322 |
3.56e-08 |
|
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: 55.24 E-value: 3.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 73 NNFYYYVSQMIQDNGPTTALIFLGLFLALMTLFKTSCYFASSAVMIPLRTGVVRDIRIMVYAKVMRLPMGFFSEERKGDI 152
Cdd:cd18553 34 NKYYKFIYNFFGFSSPVNFVIFFGIILIGFYIFRSLYNIFYTYLLNRFSFGRYHSIAYRLFKNYLKLNYQDFTNKNSSDL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 153 IARMSGDVGEVENSITSSLDMLIKSPIMIILYFItLIATSWKLTLFTVLVLPAMGWLMGK-VGRKLKRQSL---EAQGKW 228
Cdd:cd18553 114 SKSIINEASNLSQVIQSFLFILSEIFVILFIYSL-LLYVNWKITLVLTLFLGLNVFFITKiVSKKIKKQGKkreESQKKF 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 229 SDTMSqleETLGGLRIIKAFIAEDRMIDRFTRCSNELRDAVNKVAMRQALAHPMSEFLGTILIVSVLWFggALILGHNSS 308
Cdd:cd18553 193 YKILS---ETFGNFKIIKLKSNEKEILKNFSQASLKFAKANIINQTLQTVPRLILETIGFSLLILIVLY--ILYKYSDAS 267
|
250
....*....|....
gi 499421346 309 LTAPTFIFYMVILY 322
Cdd:cd18553 268 AVLPIISMYALALY 281
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
390-608 |
3.82e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 56.05 E-value: 3.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 390 LKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTsikdvriADLRSLIGNVNQEAILFNDTFFNNIA 469
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS-------AALIAISSGLNGQLTGIENIELKGLM 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 470 FGVENATME----QVIEAAKIANahdFIMEKPEGYntnigdrggklSGGQRQRVSIARAILKNPPILILDEATSALD-TE 544
Cdd:PRK13545 113 MGLTKEKIKeiipEIIEFADIGK---FIYQPVKTY-----------SSGMKSRLGFAISVHINPDILVIDEALSVGDqTF 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499421346 545 SERLVQEALERLMKTRTTIAIAHRLSTIKNadeICV----LYEGEIVERGRHEELL-ELDGYYKRLNDM 608
Cdd:PRK13545 179 TKKCLDKMNEFKEQGKTIFFISHSLSQVKS---FCTkalwLHYGQVKEYGDIKEVVdHYDEFLKKYNQM 244
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
135-260 |
3.95e-08 |
|
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group represents the six-transmembrane domain 2 (TMD2) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and belong to the ABCC subfamily. The ATP-sensitive (K-ATP) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Thus, in contrast to other ABC transporters, the SUR serves as the regulatory subunit of an ion channel. Mutations and deficiencies in the SUR proteins have been observed in patients with hyperinsulinemic hypoglycemia of infancy, an autosomal recessive disorder of unregulated and high insulin secretion. Mutations have also been associated with non-insulin-dependent diabetes mellitus type 2, an autosomal dominant disease of defective insulin secretion.
Pssm-ID: 350046 [Multi-domain] Cd Length: 307 Bit Score: 55.30 E-value: 3.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 135 KVMRLPMGFFSEERKGDIIARMSGDVGEVENSITSSLDMLIKSPIMIILYFI-TLIATSWkltlFTVLVLPAMG--WLMG 211
Cdd:cd18602 92 NIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIvNAIVTPY----FLIALIPIIIvyYFLQ 167
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 499421346 212 KVGRKLKR--QSLEAQGKwSDTMSQLEETLGGLRIIKAFIAEDRMIDRFTR 260
Cdd:cd18602 168 KFYRASSRelQRLDNITK-SPVFSHFSETLGGLTTIRAFRQQARFTQQMLE 217
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
385-555 |
4.20e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 53.65 E-value: 4.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 385 GKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADLRSL--IGNVNqeAIlfND 462
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLlyLGHQP--GI--KT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 463 --TFFNNIAFgveNATMEQVIEAAKIANAhdfiMEKpegyntnIGDRG------GKLSGGQRQRVSIARAILKNPPILIL 534
Cdd:PRK13538 88 elTALENLRF---YQRLHGPGDDEALWEA----LAQ-------VGLAGfedvpvRQLSAGQQRRVALARLWLTRAPLWIL 153
|
170 180
....*....|....*....|....*
gi 499421346 535 DEATSALDTES----ERLVQEALER 555
Cdd:PRK13538 154 DEPFTAIDKQGvarlEALLAQHAEQ 178
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
91-348 |
4.36e-08 |
|
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: 55.19 E-value: 4.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 91 ALIFLGLFLAlmTLFKTSCYFASSAVMIPLRTGVVrdirIMVYAKVMRLPMGFFSEERK-------------------GD 151
Cdd:cd18596 43 LLLFLGPLLS--SLLDQQYLWIGRRLSVRLRAILT----QLIFEKALRRRDKSGSSKSSeskkkdkeededekssasvGK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 152 IIARMSGDVGEVENsITSSLDMLIKSPIMIILYFITLIATSWKLTLFTVLVLPAMGWLMGKVGRKLKRqsleAQGKWSDT 231
Cdd:cd18596 117 INNLMSVDANRISE-FAAFLHLLVSAPLQIVIAIVFLYRLLGWSALVGLAVMVLLLPLNGYLAKRYSR----AQKELMKA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 232 ----MSQLEETLGGLRIIKAFIAEDRMIDRFtrcsNELRD----AVNKVAMRQALAHPMSEFLGTILIVSVLWFggaLIL 303
Cdd:cd18596 192 rdarVQLVTEVLQGIRMIKFFAWERKWEERI----LEAREeelkWLRKRFLLDLLLSLLWFLIPILVTVVTFAT---YTL 264
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 499421346 304 GHNSSLTAPTfIFYMVILYSVI-NPLKDFAKAGYNIPKGLASMERV 348
Cdd:cd18596 265 VMGQELTASV-AFTSLALFNMLrGPLNVLPELITQLLQAKVSLDRI 309
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
390-595 |
4.81e-08 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 56.17 E-value: 4.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 390 LKHVNLTVPKGKTVALVGQSGSGKSTLVD--LLP--------------RYHDVQGGD-----ITIDGTSI-KDVR----- 442
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLINdtLYPalanrlngaktvpgRYTSIEGLEhldkvIHIDQSPIgRTPRsnpat 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 443 ----IADLRSLIGNVNQEAIL--------FN-----------------------DTF----------FN----------- 466
Cdd:TIGR00630 704 ytgvFDEIRELFAETPEAKVRgytpgrfsFNvkggrceacqgdgvikiemhflpDVYvpcevckgkrYNretlevkykgk 783
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 467 NIAfGVENATMEQVIE----AAKIANAHDFIMEKPEGYNTnIGDRGGKLSGGQRQRVSIARAILK---NPPILILDEATS 539
Cdd:TIGR00630 784 NIA-DVLDMTVEEAYEffeaVPSISRKLQTLCDVGLGYIR-LGQPATTLSGGEAQRIKLAKELSKrstGRTLYILDEPTT 861
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499421346 540 ALDTESERLVQEALERLM-KTRTTIAIAHRLSTIKNADEICVL------YEGEIVERGRHEEL 595
Cdd:TIGR00630 862 GLHFDDIKKLLEVLQRLVdKGNTVVVIEHNLDVIKTADYIIDLgpeggdGGGTVVASGTPEEV 924
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
388-586 |
4.83e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 55.83 E-value: 4.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 388 EVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIADlRSLIGNV-----NQEAILFND 462
Cdd:PRK15439 277 EGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ-RLARGLVylpedRQSSGLYLD 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 463 T---------FFNNIAF----GVENATMEQVIEAAKIANAHdfiMEKPegyntnigdrGGKLSGGQRQRVSIARAILKNP 529
Cdd:PRK15439 356 AplawnvcalTHNRRGFwikpARENAVLERYRRALNIKFNH---AEQA----------ARTLSGGNQQKVLIAKCLEASP 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499421346 530 PILILDEATSALDTESERLVQEALERLMKTRTTIA-IAHRLSTI-KNADEICVLYEGEI 586
Cdd:PRK15439 423 QLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLfISSDLEEIeQMADRVLVMHQGEI 481
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
385-572 |
5.55e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 56.27 E-value: 5.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 385 GKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRyhDVQGGDITiDGTSIKDVRIAD---LRSlIGNVNQ------ 455
Cdd:TIGR00956 774 EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAE--RVTTGVIT-GGDRLVNGRPLDssfQRS-IGYVQQqdlhlp 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 456 -----EAILFNDTFF--NNIAFGVENATMEQVIEaakianahdfIMEKPEGYNTNIGDRGGKLSGGQRQRVSIARAILKN 528
Cdd:TIGR00956 850 tstvrESLRFSAYLRqpKSVSKSEKMEYVEEVIK----------LLEMESYADAVVGVPGEGLNVEQRKRLTIGVELVAK 919
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499421346 529 PPILI-LDEATSALDTESERLVQEALERLMKTRTTIaiahrLSTI 572
Cdd:TIGR00956 920 PKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAI-----LCTI 959
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
340-550 |
7.23e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 55.64 E-value: 7.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 340 KGLASMERVDKILKAENNIKEIPNPkpltgmNDR-----IEFKDISFSYDGKREVLKHVNLTVPKGKTVALVGQSGSGKS 414
Cdd:PLN03073 476 KALDRLGHVDAVVNDPDYKFEFPTP------DDRpgppiISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKS 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 415 TLVDLLpryhdvqGGDIT-IDGTSIKD--VRIADLrslignvNQEAILFNDTFFNNIAFGVEnaTMEQVIEAAKIANAHD 491
Cdd:PLN03073 550 TILKLI-------SGELQpSSGTVFRSakVRMAVF-------SQHHVDGLDLSSNPLLYMMR--CFPGVPEQKLRAHLGS 613
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499421346 492 FimekpeGYNTNIGDRGG-KLSGGQRQRVSIARAILKNPPILILDEATSALDTES-ERLVQ 550
Cdd:PLN03073 614 F------GVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAvEALIQ 668
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
128-338 |
8.66e-08 |
|
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: 54.21 E-value: 8.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 128 IRIMVYAKVMRLPMGFFSEERKGDIIARMSGDVGEVENSITSSLDMLIKS---PIMIILYFITLIATSWKLTLFTVLVLP 204
Cdd:cd18561 71 LRRRLFAKLLKLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVAllgPLLILIYLFFLDPLVALILLVFALLIP 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 205 AMGWLMGKVGRKLKRQSLEAQGKWSdtmSQLEETLGGLRIIKAFIAEDRMIDRFTRCSNELRDAVNKVAMRQALAHPMSE 284
Cdd:cd18561 151 LSPALWDRLAKDTGRRHWAAYGRLS---AQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSLLSSGIMG 227
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499421346 285 FLGTILIVSVLWFGGALILGhnSSLTAPTFIFYMVILYSVINPLKDFAK---AGYNI 338
Cdd:cd18561 228 LATALGTALALGVGALRVLG--GQLTLSSLLLILFLSREFFRPLRDLGAywhAGYQG 282
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
92-294 |
8.85e-08 |
|
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: 54.02 E-value: 8.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 92 LIFLGLFLALMTLFktsCYFASsavmiplrtgvvRDIRIMVYAKVMRLPMGFFSEERKGDIIARMSGDVGEVENSITSSL 171
Cdd:cd18606 49 AIFLFLFGLLLAYL---GIRAS------------KRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 172 DMLIKSPIMIILYFITLIATswkLTLFTVLVLPAMG--WLMGKV----GRKLKRqsLEAQGKwSDTMSQLEETLGGLRII 245
Cdd:cd18606 114 RMFLYTLSSIIGTFILIIIY---LPWFAIALPPLLVlyYFIANYyrasSRELKR--LESILR-SFVYANFSESLSGLSTI 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499421346 246 KAFiaedRMIDRFTRCSNELRDAVNK-----VAMRQALAHPMsEFLGTILIVSV 294
Cdd:cd18606 188 RAY----GAQDRFIKKNEKLIDNMNRayfltIANQRWLAIRL-DLLGSLLVLIV 236
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
89-333 |
9.67e-08 |
|
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: 54.06 E-value: 9.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 89 TTALIFLGLFLALmtLFKTSCYFASSAVMIPLRTGVvrDIRI--MVYAKVMRLPMGFFSEERKGDIIARMSgDVGEVENS 166
Cdd:cd18783 40 TLYVLTIGVVIAL--LFEGILGYLRRYLLLVATTRI--DARLalRTFDRLLSLPIDFFERTPAGVLTKHMQ-QIERIRQF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 167 ITSSLDMLIKSPIMIILYFITLIATSWKLTL----FTVLVLPAMGWLMGKVGRKLKRqSLEAQGKWSdtmSQLEETLGGL 242
Cdd:cd18783 115 LTGQLFGTLLDATSLLVFLPVLFFYSPTLALvvlaFSALIALIILAFLPPFRRRLQA-LYRAEGERQ---AFLVETVHGI 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 243 RIIKAFIAED---RMIDRFTRCSNELRDAVNKVAmrqALAHPMSEFLGTILIVSVLWFGGALILGhnSSLTAPTFIFYMV 319
Cdd:cd18783 191 RTVKSLALEPrqrREWDERVARAIRARFAVGRLS---NWPQTLTGPLEKLMTVGVIWVGAYLVFA--GSLTVGALIAFNM 265
|
250
....*....|....
gi 499421346 320 ILYSVINPLKDFAK 333
Cdd:cd18783 266 LAGRVAGPLVQLAG 279
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
374-547 |
1.69e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 54.36 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYdGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDV--------RIA- 444
Cdd:NF033858 2 ARLEGVSHRY-GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADArhrravcpRIAy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 445 -----------DLrSLIGNVNqeailfndtFFNNIaFGVENATMEQVIEA-AKIANAHDFimekpegyntniGDR-GGKL 511
Cdd:NF033858 81 mpqglgknlypTL-SVFENLD---------FFGRL-FGQDAAERRRRIDElLRATGLAPF------------ADRpAGKL 137
|
170 180 190
....*....|....*....|....*....|....*.
gi 499421346 512 SGGQRQRVSIARAILKNPPILILDEATSALDTESER 547
Cdd:NF033858 138 SGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRR 173
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
367-569 |
3.83e-07 |
|
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: 53.48 E-value: 3.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 367 LTGMN--DRIEFKDISFSYDGKRE-VLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKdVRI 443
Cdd:TIGR01257 1929 ISGGNktDILRLNELTKVYSGTSSpAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL-TNI 2007
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 444 ADLRSLIGNVNQ-EAIlfndtffNNIAFGVENATMEQVI------EAAKIANAHDfimeKPEGYNTNIGDRGGKLSGGQR 516
Cdd:TIGR01257 2008 SDVHQNMGYCPQfDAI-------DDLLTGREHLYLYARLrgvpaeEIEKVANWSI----QSLGLSLYADRLAGTYSGGNK 2076
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499421346 517 QRVSIARAILKNPPILILDEATSALDTESERLVQEALERLMKT-RTTIAIAHRL 569
Cdd:TIGR01257 2077 RKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREgRAVVLTSHSM 2130
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
510-585 |
4.30e-07 |
|
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: 50.26 E-value: 4.30e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499421346 510 KLSGGQRQRVSIARAILKNPPILILDEATSALDTESERLVQEALERLMK--TRTTIAIAHRLSTIKNADEICVLYEGE 585
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEegKKTALVVEHDLAVLDYLSDRIHVFEGE 148
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
394-585 |
5.09e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.50 E-value: 5.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 394 NLTVPK-GKTVALVGQSGSGKSTLVDLL-----P---RYHDVQGGDITID---GTSI---------KDVRIA------DL 446
Cdd:PRK13409 92 GLPIPKeGKVTGILGPNGIGKTTAVKILsgeliPnlgDYEEEPSWDEVLKrfrGTELqnyfkklynGEIKVVhkpqyvDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 447 --RSLIGNVNqEAILFNDtffnniafgvENATMEQVIEAAKIANahdfIMEKPegyntnIGDrggkLSGGQRQRVSIARA 524
Cdd:PRK13409 172 ipKVFKGKVR-ELLKKVD----------ERGKLDEVVERLGLEN----ILDRD------ISE----LSGGELQRVAIAAA 226
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499421346 525 ILKNPPILILDEATSALDTEsERL-VQEALERLMKTRTTIAIAHRLSTIKN-ADEICVLYeGE 585
Cdd:PRK13409 227 LLRDADFYFFDEPTSYLDIR-QRLnVARLIRELAEGKYVLVVEHDLAVLDYlADNVHIAY-GE 287
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
374-554 |
2.40e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 50.28 E-value: 2.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 374 IEFKDISFSYDGkREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLpryhdvqGGDITIDGTSIKDVRIADlrslIGNV 453
Cdd:PRK15064 320 LEVENLTKGFDN-GPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTL-------VGELEPDSGTVKWSENAN----IGYY 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 454 NQ--EAILFND-TFFNNIAFGVENATMEQVIEAA--KIANAHDFIMEKPEgyntnigdrggKLSGGQRQRVSIARAILKN 528
Cdd:PRK15064 388 AQdhAYDFENDlTLFDWMSQWRQEGDDEQAVRGTlgRLLFSQDDIKKSVK-----------VLSGGEKGRMLFGKLMMQK 456
|
170 180
....*....|....*....|....*.
gi 499421346 529 PPILILDEATSALDTESERLVQEALE 554
Cdd:PRK15064 457 PNVLVMDEPTNHMDMESIESLNMALE 482
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
135-294 |
5.59e-06 |
|
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: 48.63 E-value: 5.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 135 KVMRLPMGFFSEERKGDIIARMSGDVGEVENSITSSLDMLIKSPIMIIlyfITLIATSWKLTLFTVLVLP--AMGWLMGK 212
Cdd:cd18603 83 NILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVI---STLVVISISTPIFLVVIIPlaILYFFIQR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 213 V----GRKLKRqsLEAQGKwSDTMSQLEETLGGLRIIKAFiaedRMIDRFTRCSNELRDAVNKV-----------AMRqa 277
Cdd:cd18603 160 FyvatSRQLKR--LESVSR-SPIYSHFSETLQGASTIRAY----GVQERFIRESDRRVDENQRAyypsivsnrwlAVR-- 230
|
170
....*....|....*..
gi 499421346 278 lahpmSEFLGTILIVSV 294
Cdd:cd18603 231 -----LEFLGNLIVLFA 242
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
394-585 |
6.78e-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: 49.01 E-value: 6.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 394 NLTVPK-GKTVALVGQSGSGKSTLVDLL-----P---RYHDVQGGDITID---GTSIKD---------VRIA------DL 446
Cdd:COG1245 92 GLPVPKkGKVTGILGPNGIGKSTALKILsgelkPnlgDYDEEPSWDEVLKrfrGTELQDyfkklangeIKVAhkpqyvDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 447 --RSLIGNVNqEAILFNDtffnniafgvENATMEQVIEAAKIANahdfIMEKpegyntNIGDrggkLSGGQRQRVSIARA 524
Cdd:COG1245 172 ipKVFKGTVR-ELLEKVD----------ERGKLDELAEKLGLEN----ILDR------DISE----LSGGELQRVAIAAA 226
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499421346 525 ILKNPPILILDEATSALD----TESERLVQEALErlmKTRTTIAIAHRLSTI-KNADEICVLYeGE 585
Cdd:COG1245 227 LLRDADFYFFDEPSSYLDiyqrLNVARLIRELAE---EGKYVLVVEHDLAILdYLADYVHILY-GE 288
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
392-595 |
7.11e-06 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 47.68 E-value: 7.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 392 HVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIK---DVRIAdlRSLIGNVNQEAILFNDTFFnni 468
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEglpGHQIA--RMGVVRTFQHVRLFREMTV--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 469 afgVEN---ATMEQV----------------IEAAKIANAHDFImekpEGYN-TNIGDR-GGKLSGGQRQRVSIARAILK 527
Cdd:PRK11300 98 ---IENllvAQHQQLktglfsgllktpafrrAESEALDRAATWL----ERVGlLEHANRqAGNLAYGQQRRLEIARCMVT 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499421346 528 NPPILILDEATSALDTESERLVQEALERLMKTR--TTIAIAHRLSTIKN-ADEICVLYEGEIVERGRHEEL 595
Cdd:PRK11300 171 QPEILMLDEPAAGLNPKETKELDELIAELRNEHnvTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
386-542 |
1.29e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 48.00 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 386 KREVLKHVNLTVPKGKTVALVGQSGSGKSTLVD-LLPRYHDVQGGDITIDGTSIKDVRIAD-LRSLIGNVNQE------- 456
Cdd:PRK13549 274 HIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQcLFGAYPGRWEGEIFIDGKPVKIRNPQQaIAQGIAMVPEDrkrdgiv 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 457 -----------AILFNDTFFNNIAFGVENATMEQVIEAAKIANAHDFImekpegyntnigdRGGKLSGGQRQRVSIARAI 525
Cdd:PRK13549 354 pvmgvgknitlAALDRFTGGSRIDDAAELKTILESIQRLKVKTASPEL-------------AIARLSGGNQQKAVLAKCL 420
|
170
....*....|....*..
gi 499421346 526 LKNPPILILDEATSALD 542
Cdd:PRK13549 421 LLNPKILILDEPTRGID 437
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
511-596 |
1.31e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.09 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 511 LSGGQRQRVSIARAILKNPPILILDEATSALDTESERLVQEALERLMKTRTTIA-IAHRLSTIKN-ADEICVLYEGEIVE 588
Cdd:PRK10938 136 LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVlVLNRFDEIPDfVQFAGVLADCTLAE 215
|
....*...
gi 499421346 589 RGRHEELL 596
Cdd:PRK10938 216 TGEREEIL 223
|
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
118-348 |
1.57e-05 |
|
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: 47.14 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 118 IPLRTGVVRDIRIMVYAKVMRLPMGFFSEERKGDIIARMSGdvgevENSITSSLDMLIKSPI-MIILYFITLIATSWKLT 196
Cdd:cd18583 62 IPVEQYSYRALSTAAFNHVMNLSMDFHDSKKSGEVLKAIEQ-----GSSINDLLEQILFQIVpMIIDLVIAIVYLYYLFD 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 197 LFTVLVLPAMGWL-------MGKVGRKLKRQSLEAQGKWSDTMSqleETLGGLRIIKAFIAEDRMIDRFtrcsnelRDAV 269
Cdd:cd18583 137 PYMGLIVAVVMVLyvwstikLTSWRTKLRRDMIDADREERSILT---ESLLNWETVKYFNREPYEKERY-------REAV 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 270 NKVaMRQALAHPMSEFLGT---ILIVSVLWFGGALILGHN-SSLTAP-----TFIFYMVILYSvinPLKDFAKAGYNIPK 340
Cdd:cd18583 207 KNY-QKAERKYLFSLNLLNavqSLILTLGLLAGCFLAAYQvSQGQATvgdfvTLLTYWAQLSG---PLNFFATLYRSIQS 282
|
....*...
gi 499421346 341 GLASMERV 348
Cdd:cd18583 283 DLIDAERL 290
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
505-595 |
1.83e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 47.04 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 505 GDRGGKLSGGQRQRVSIARAILKNPPILILDEATSALDTESERLVQEALERLMKTRTTIAIAHRL--STIKNADEICVLY 582
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYmeEAEQLAHELTVID 218
|
90
....*....|...
gi 499421346 583 EGEIVERGRHEEL 595
Cdd:NF000106 219 RGRVIADGKVDEL 231
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
510-578 |
1.84e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 45.43 E-value: 1.84e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499421346 510 KLSGGQRQRVSIARAI----LKNPPILILDEATSALDTESERLVQEAL-ERLMKTRTTIAIAHRLSTIKNADEI 578
Cdd:cd03227 77 QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAIlEHLVKGAQVIVITHLPELAELADKL 150
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
509-542 |
2.67e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 46.92 E-value: 2.67e-05
10 20 30
....*....|....*....|....*....|....
gi 499421346 509 GKLSGGQRQRVSIARAILKNPPILILDEATSALD 542
Cdd:PRK10762 394 GLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
375-588 |
3.83e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 46.70 E-value: 3.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 375 EFKDISfSYDGKRevLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTSIKDVRIAD-LRSLIGNV 453
Cdd:PRK09700 267 EVRNVT-SRDRKK--VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDaVKKGMAYI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 454 NQEAilFNDTFFNNI-------------------AFGVENATMEQvieaaKIA-NAHDFIMEKPEGYNTNIGDrggkLSG 513
Cdd:PRK09700 344 TESR--RDNGFFPNFsiaqnmaisrslkdggykgAMGLFHEVDEQ-----RTAeNQRELLALKCHSVNQNITE----LSG 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499421346 514 GQRQRVSIARAILKNPPILILDEATSALDTESERLVQEALERLMKT-RTTIAIAHRLSTIKNA-DEICVLYEGEIVE 588
Cdd:PRK09700 413 GNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELPEIITVcDRIAVFCEGRLTQ 489
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
390-578 |
4.22e-05 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 45.33 E-value: 4.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 390 LKHVNLTVPKGKTVALVGQSGSGKSTL-------------VDLLPRYHDVQGGDI------TIDGTS----IKDVRIA-D 445
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqrryVESLSAYARQFLGQMdkpdvdSIEGLSpaiaIDQKTTSrN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 446 LRSLIGNVNQeailFNDTF---FNNIAfgvenatmeqvieaakIANAHDFIMEKPEGYNTnIGDRGGKLSGGQRQRVSIA 522
Cdd:cd03270 91 PRSTVGTVTE----IYDYLrllFARVG----------------IRERLGFLVDVGLGYLT-LSRSAPTLSGGEAQRIRLA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499421346 523 RAILKN--PPILILDEATSALdteSERLVQEALERLMKTR----TTIAIAHRLSTIKNADEI 578
Cdd:cd03270 150 TQIGSGltGVLYVLDEPSIGL---HPRDNDRLIETLKRLRdlgnTVLVVEHDEDTIRAADHV 208
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
390-609 |
4.29e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 45.58 E-value: 4.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 390 LKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGtsikDVR-IADLRSLIGNVnqeailfndTFFNNI 468
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG----EVSvIAISAGLSGQL---------TGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 469 AFGVE---------NATMEQVIEAAKIAnahDFIMEKPEGYntnigdrggklSGGQRQRVSIARAILKNPPILILDEATS 539
Cdd:PRK13546 107 EFKMLcmgfkrkeiKAMTPKIIEFSELG---EFIYQPVKKY-----------SSGMRAKLGFSINITVNPDILVIDEALS 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499421346 540 ALD-TESERLVQEALERLMKTRTTIAIAHRLSTIKnadEICVlyEGEIVERGRHEELLELDG----YYKRLNDMQ 609
Cdd:PRK13546 173 VGDqTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVR---QFCT--KIAWIEGGKLKDYGELDDvlpkYEAFLNDFK 242
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
387-542 |
4.56e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 46.32 E-value: 4.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 387 REVLKHVNLTVPKGKTVALVGQSGSGKSTL-VDLLPR-YHDVQGGDITIDGtsiKDVRIADLRSLIGN------------ 452
Cdd:NF040905 273 RKVVDDVSLNVRRGEIVGIAGLMGAGRTELaMSVFGRsYGRNISGTVFKDG---KEVDVSTVSDAIDAglayvtedrkgy 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 453 --VNQEAILFNDTFFN--NIA-FGVENATMEqvieaAKIAnahdfimekpEGYNT-------NIGDRGGKLSGGQRQRVS 520
Cdd:NF040905 350 glNLIDDIKRNITLANlgKVSrRGVIDENEE-----IKVA----------EEYRKkmniktpSVFQKVGNLSGGNQQKVV 414
|
170 180
....*....|....*....|..
gi 499421346 521 IARAILKNPPILILDEATSALD 542
Cdd:NF040905 415 LSKWLFTDPDVLILDEPTRGID 436
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
364-553 |
4.65e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 46.32 E-value: 4.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 364 PKPLTGMndriefKDISFSYdGKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIdGTSIKdvri 443
Cdd:PRK10636 309 PNPLLKM------EKVSAGY-GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-AKGIK---- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 444 adlrslIGNVNQEAILF---NDTFFNNIAFGVENATMEQVieaakianaHDFImekpEGYNTN---IGDRGGKLSGGQRQ 517
Cdd:PRK10636 377 ------LGYFAQHQLEFlraDESPLQHLARLAPQELEQKL---------RDYL----GGFGFQgdkVTEETRRFSGGEKA 437
|
170 180 190
....*....|....*....|....*....|....*.
gi 499421346 518 RVSIARAILKNPPILILDEATSALDTESERLVQEAL 553
Cdd:PRK10636 438 RLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEAL 473
|
|
| ABC_6TM_peptidase_like |
cd18571 |
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and ... |
134-253 |
4.84e-05 |
|
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: 45.51 E-value: 4.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 134 AKVMRLPMGFFSEERKGDIIARMsGDVGEVENSITSSLDMLIKSPIMIILYFITLIATSWKL-TLFTVLVLPAMGWLMG- 211
Cdd:cd18571 83 IKLMRLPISFFDTKMTGDILQRI-NDHSRIESFLTSSSLSILFSLLNLIVFSIVLAYYNLTIfLIFLIGSVLYILWILLf 161
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 499421346 212 -KVGRKL--KRQSLEAQGKwsdtmSQLEETLGGLRIIKAFIAEDR 253
Cdd:cd18571 162 lKKRKKLdyKRFDLSSENQ-----SKLIELINGMQEIKLNNSERQ 201
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
95-248 |
6.14e-05 |
|
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350041 [Multi-domain] Cd Length: 293 Bit Score: 45.14 E-value: 6.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 95 LGLFLALM--TLFKTSCYFASSAVMIPLRTGVVRdiriMVYAKVMRLpmgffSEERK-----GDIIARMSGDVGEVENSI 167
Cdd:cd18597 47 IGLFLLQLlsSLLLNHFFYRSMLTGAQVRAALTK----AIYRKSLRL-----SGKSRhefpnGKITNLMSTDLSRIDFAL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 168 tSSLDMLIKSPIMIILYFITLIatsWKLT--------LFtVLVLPAMGWLMGKVGRKLKRQSleaqgKWSDT-MSQLEET 238
Cdd:cd18597 118 -GFFHFLWTAPIQIIIAIALLI---VNLGpsalvgigVL-ILSIPLQGFLMKKLFKLRKKAN-----KITDKrVKLTQEI 187
|
170
....*....|
gi 499421346 239 LGGLRIIKAF 248
Cdd:cd18597 188 LQGIRVIKFY 197
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
509-542 |
7.85e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 45.89 E-value: 7.85e-05
10 20 30
....*....|....*....|....*....|....
gi 499421346 509 GKLSGGQRQRVSIARAILKNPPILILDEATSALD 542
Cdd:NF033858 396 DSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
349-602 |
8.14e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.49 E-value: 8.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 349 DKILKAENNIKEIPNpkpLTGMNdRIEFKDISFSydgkrevlkhvnltVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQG 428
Cdd:PRK10982 241 DKENKPGEVILEVRN---LTSLR-QPSIRDVSFD--------------LHKGEILGIAGLVGAKRTDIVETLFGIREKSA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 429 GDITIDGTSIKD-----------VRIADLRSLIGNVNQEAILFN------DTFFNNIAFgVENATMEQ----VIEAAKIa 487
Cdd:PRK10982 303 GTITLHGKKINNhnaneainhgfALVTEERRSTGIYAYLDIGFNslisniRNYKNKVGL-LDNSRMKSdtqwVIDSMRV- 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 488 nahdfimeKPEGYNTNIGdrggKLSGGQRQRVSIARAILKNPPILILDEATSALDTESE-RLVQEALERLMKTRTTIAIA 566
Cdd:PRK10982 381 --------KTPGHRTQIG----SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKfEIYQLIAELAKKDKGIIIIS 448
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 499421346 567 HRLSTIKN-ADEICVLYEGE---IVERGR--HEELLELDGYY 602
Cdd:PRK10982 449 SEMPELLGiTDRILVMSNGLvagIVDTKTttQNEILRLASLH 490
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
385-567 |
1.03e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.16 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 385 GKREVLKHVNLTVPKGKTVALVGQSGSGKSTLVDLLPryhdvqgGDITIDGTSIkdvriadlrSLIGN-----VNQEAIL 459
Cdd:PRK10636 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLK-------NEISADGGSY---------TFPGNwqlawVNQETPA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 460 FNDTFFNNIAFG-VENATMEQVIEAAK-------IANAH---DFIMEkpegynTNIGDRGGKL----------------- 511
Cdd:PRK10636 76 LPQPALEYVIDGdREYRQLEAQLHDANerndghaIATIHgklDAIDA------WTIRSRAASLlhglgfsneqlerpvsd 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499421346 512 -SGGQRQRVSIARAILKNPPILILDEATSALDTESERLvqeaLERLMK--TRTTIAIAH 567
Cdd:PRK10636 150 fSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIW----LEKWLKsyQGTLILISH 204
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
348-420 |
1.04e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 45.45 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 348 VDKILKAENNI--------KEIPNPKPLTGMNDR-IEFKdisfsydGKRE-VLKHVNLTVPKGKTVALVGQSGSGKSTLV 417
Cdd:PRK00349 580 PEEIMKNPNSLtgqylsgkKKIEVPKERRKGNGKfLKLK-------GAREnNLKNVDVEIPLGKFTCVTGVSGSGKSTLI 652
|
....
gi 499421346 418 -DLL 420
Cdd:PRK00349 653 nETL 656
|
|
| RsgA |
COG1162 |
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis]; |
399-420 |
1.12e-04 |
|
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440776 [Multi-domain] Cd Length: 300 Bit Score: 44.33 E-value: 1.12e-04
10 20
....*....|....*....|..
gi 499421346 399 KGKTVALVGQSGSGKSTLVDLL 420
Cdd:COG1162 165 KGKTSVLVGQSGVGKSTLINAL 186
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
348-417 |
1.46e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 45.02 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 348 VDKILKAENNI--------KEIPNPKPL-TGMNDRIEFKdisfsydGKREV-LKHVNLTVPKGKTVALVGQSGSGKSTLV 417
Cdd:COG0178 576 PEEILKNPDSLtgqylsgrKRIPVPKKRrKGNGKFLTIK-------GARENnLKNVDVEIPLGVLTCVTGVSGSGKSTLV 648
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
88-347 |
1.54e-04 |
|
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group represents the Atm1/ABCB7/HMT1/ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster.
Pssm-ID: 350004 [Multi-domain] Cd Length: 292 Bit Score: 44.14 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 88 PTTALIFLGLFLALMTLFKTscyfASSAVMIPLRTGVVRDIRIMVYAKVMRLPMGFFSEERKGDIIARMSGDVGEVeNSI 167
Cdd:cd18560 37 AVTLILLYALLRFSSKLLKE----LRSLLYRRVQQNAYRELSLKTFAHLHSLSLDWHLSKKTGEVVRIMDRGTESA-NTL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 168 TSSLDMLIkSP-----IMIILYFITLIatSWKLTLFTVLVLPAMGWLMGKVGRKLKRQSLEAQGKWSDTMSQLEETLGGL 242
Cdd:cd18560 112 LSYLVFYL-VPtllelIVVSVVFAFHF--GAWLALIVFLSVLLYGVFTIKVTEWRTKFRRAANKKDNEAHDIAVDSLLNF 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 243 RIIKAFIAEDRMIDRFTRCSNELRDAVNKVAMRQALAHPMSEFLGTILIVSVLWFGGALILGHNssLTAPTFIFYMVILY 322
Cdd:cd18560 189 ETVKYFTNEKYEVDRYGEAVKEYQKSSVKVQASLSLLNVGQQLIIQLGLTLGLLLAGYRVVDGG--LSVGDFVAVNTYIF 266
|
250 260
....*....|....*....|....*.
gi 499421346 323 SVINPLkDFAKAGYN-IPKGLASMER 347
Cdd:cd18560 267 QLFQPL-NFLGTIYRmIIQSLTDMEN 291
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
386-586 |
1.62e-04 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 44.43 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 386 KREVLKHVNLTVPKGKTVALVGQSGSGKSTLVD-LLPRYHDVQGGDITIDGTSIkDVR------------IADLRSLIGN 452
Cdd:TIGR02633 272 HRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQaLFGAYPGKFEGNVFINGKPV-DIRnpaqairagiamVPEDRKRHGI 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 453 VNQEAILFNDTF--FNNIAF--GVENATMEQVIEAA----KIANAHDFIMEkpegyntnigdrgGKLSGGQRQRVSIARA 524
Cdd:TIGR02633 351 VPILGVGKNITLsvLKSFCFkmRIDAAAELQIIGSAiqrlKVKTASPFLPI-------------GRLSGGNQQKAVLAKM 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499421346 525 ILKNPPILILDEATSALDT----ESERLVQEALERLMktrTTIAIAHRLSTIKN-ADEICVLYEGEI 586
Cdd:TIGR02633 418 LLTNPRVLILDEPTRGVDVgakyEIYKLINQLAQEGV---AIIVVSSELAEVLGlSDRVLVIGEGKL 481
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
399-420 |
1.95e-04 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 43.16 E-value: 1.95e-04
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
370-416 |
2.43e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 44.29 E-value: 2.43e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 499421346 370 MNDRIEFKdisfsydGKRE-VLKHVNLTVPKGKTVALVGQSGSGKSTL 416
Cdd:PRK00349 2 MMDKIIIR-------GAREhNLKNIDLDIPRDKLVVFTGLSGSGKSSL 42
|
|
| Zeta_toxin |
pfam06414 |
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is ... |
401-495 |
2.67e-04 |
|
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is thought to be part of a postregulational killing system in bacteria. It relies on antitoxin/toxin systems that secure stable inheritance of low and medium copy number plasmids during cell division and kill cells that have lost the plasmid.
Pssm-ID: 428926 Cd Length: 192 Bit Score: 42.35 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 401 KTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDGTsikdvriaDLRSLIGNVNqeAILFNDTFFNNIAFGVENATM-EQ 479
Cdd:pfam06414 12 KAILLGGQPGAGKTELARALLDELGRQGNVVRIDPD--------DFRELHPHYR--ELQAADPKTASEYTQPDASRWvEK 81
|
90
....*....|....*.
gi 499421346 480 VIEAAkIANAHDFIME 495
Cdd:pfam06414 82 LLQHA-IENGYNIILE 96
|
|
| ABC_6TM_PrtD_like |
cd18586 |
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ... |
86-306 |
5.40e-04 |
|
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: 42.21 E-value: 5.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 86 NGPTTALIFLGLFLALMTLFKTScyFASSAVMIplRTGVVRDIRI--MVYAKVMRLPMgffsEERKGDIIARMSGDVGEV 163
Cdd:cd18586 37 SLSTLLGLTLGMVVLLAFDGLLR--QVRSRILQ--RVGLRLDVELgrRVFRAVLELPL----ESRPSGYWQQLLRDLDTL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 164 ENSITSSLDMLIK----SPIMIILYFI--TLIATswkLTLFTVLVLPAMGWLMGKVGRKLKRQSLEAQGKWSdtmSQLEE 237
Cdd:cd18586 109 RNFLTGPSLFAFFdlpwAPLFLAVIFLihPPLGW---VALVGAPVLVGLAWLNHRATRKPLGEANEAQAARD---ALAAE 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499421346 238 TLGGLRIIKAFIAEDRMIDRFTRCSNELRDAVNKVAMRQALAHPMSEFLGTILIVSVLWFGGALILGHN 306
Cdd:cd18586 183 TLRNAETIKALGMLGNLRRRWEARHAETLELQIRASDLAGAISAIGKTLRMALQSLILGVGAYLVIDGE 251
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
73-264 |
6.44e-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: 42.31 E-value: 6.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 73 NNFYYYVSqmiqdNGPTTALIFLGLFLALMTLFKTSCyfASsavmiplrtgvvRDIRIMVYAKVMRLPMGFFSEERKGDI 152
Cdd:cd18601 58 RDFNLGIY-----AGLTAATFVFGFLRSLLFFHVAVS--AS------------KNLHNKMFASVLRAPIRFFDTNPIGRI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 153 IARMSGDVGEVENSITSSLDMLIKSPIMIILYFITLIATS-WKLTLFTVLVLpAMGWLMG---KVGRKLKRqsLEAQGKw 228
Cdd:cd18601 119 LNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVVNpWVLIPVIPLVI-LFLFLRRyylKTSREVKR--IEGTTR- 194
|
170 180 190
....*....|....*....|....*....|....*.
gi 499421346 229 SDTMSQLEETLGGLRIIKAFIAEDRMIDRFTRCSNE 264
Cdd:cd18601 195 SPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDL 230
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
399-420 |
6.60e-04 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 42.23 E-value: 6.60e-04
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
377-567 |
6.68e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.92 E-value: 6.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 377 KDI---SFSYD-GKREVLKHVNLTVPKGKTVALVGQSGSGKSTL--------VDLLPR-------YHDVQGGDIT----I 433
Cdd:PLN03073 176 KDIhmeNFSISvGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFlrymamhaIDGIPKncqilhvEQEVVGDDTTalqcV 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 434 DGTSIKDVRIadLRSLIGNVNQEAILFNDTFFNNIAfGVENATMEQVIEAAKIANAHDFiMEKPEGYNTNigDRGGKL-- 511
Cdd:PLN03073 256 LNTDIERTQL--LEEEAQLVAQQRELEFETETGKGK-GANKDGVDKDAVSQRLEEIYKR-LELIDAYTAE--ARAASIla 329
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499421346 512 ----------------SGGQRQRVSIARAILKNPPILILDEATSALDTESERLVQEALERLMKtrTTIAIAH 567
Cdd:PLN03073 330 glsftpemqvkatktfSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPK--TFIVVSH 399
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
393-582 |
7.11e-04 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 41.30 E-value: 7.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 393 VNLTVPKGKTvALVGQSGSGKSTLVDLLpRYhdVQGGditidgTSIKDVRIADLRSLIgnvnqeailFNDT--------- 463
Cdd:cd03278 16 TTIPFPPGLT-AIVGPNGSGKSNIIDAI-RW--VLGE------QSAKSLRGEKMSDVI---------FAGSetrkpanfa 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 464 ----FFNNIAfGVENatmeqVIEAAKIANahdfIMEKPEGYNTNIGdrggKLSGGQRQRVSIAR--AILK-NP-PILILD 535
Cdd:cd03278 77 evtlTFDNSD-GRYS-----IISQGDVSE----IIEAPGKKVQRLS----LLSGGEKALTALALlfAIFRvRPsPFCVLD 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499421346 536 EATSALDTE-SERLVqEALERLMKTRTTIAIAHRLSTIKNADeicVLY 582
Cdd:cd03278 143 EVDAALDDAnVERFA-RLLKEFSKETQFIVITHRKGTMEAAD---RLY 186
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
92-331 |
7.34e-04 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350042 [Multi-domain] Cd Length: 288 Bit Score: 41.77 E-value: 7.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 92 LIFLGLFLA--LMTLFKTSCYFASSAVMIPLRTGVVrdirIMVYAKVMRLPMGFFSEERKGDIIARMSGDVGEVENsITS 169
Cdd:cd18598 39 LYALGLVLSslLGALLSSHYNFQMNKVSLKVRAALV----TAVYRKALRVRSSSLSKFSTGEIVNLMSTDADRIVN-FCP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 170 SLDMLIKSPIMII-----LY------FITLIAtswkltlFTVLVLPAMGWLMGKVGrKLKRQSLEAQGKWSDTMSqleET 238
Cdd:cd18598 114 SFHDLWSLPLQIIvalylLYqqvgvaFLAGLV-------FALVLIPINKWIAKRIG-ALSEKMMKHKDARVKLMT---EI 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 239 LGGLRIIKAFIAEDRMIDRFtrcsNELRDA-VNKVAMRQALAHPMSEFLGTI-LIVSVLWFGGALILGHnsSLTAPTFIF 316
Cdd:cd18598 183 LSGIRVIKLLAWERIFKQKI----EELRAKeLKALKGRKYLDALCVYFWATTpVLISILTFATYVLMGN--TLTAAKVFT 256
|
250
....*....|....*
gi 499421346 317 YMVILYSVINPLKDF 331
Cdd:cd18598 257 SLALFNMLIGPLNAF 271
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
443-576 |
7.89e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.74 E-value: 7.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 443 IADLRSLIGNVNQEA-ILFNDTF------FNNI---AFGVENATMEqVIEAAKIANAHDFIMEKPEGY-NTNIGdrggKL 511
Cdd:TIGR02168 1016 KETLEEAIEEIDREArERFKDTFdqvnenFQRVfpkLFGGGEAELR-LTDPEDLLEAGIEIFAQPPGKkNQNLS----LL 1090
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499421346 512 SGGQRQRVSIAR--AILK-NP-PILILDEATSALD-TESERLVQeaLERLMKTRTT-IAIAHRLSTIKNAD 576
Cdd:TIGR02168 1091 SGGEKALTALALlfAIFKvKPaPFCILDEVDAPLDdANVERFAN--LLKEFSKNTQfIVITHNKGTMEVAD 1159
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
393-594 |
8.00e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 42.21 E-value: 8.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 393 VNLTVPKGKTVALVGQSGSGKSTLVDLLPRYHDVQGGDITIDG--TSIKDVR------------------IADLRSLIGN 452
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpIDIRSPRdairagimlcpedrkaegIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 453 VNQEAILFNDTFFNNIAFGVENATMEQVIEAAKI--ANAHDFIMekpegyntnigdrggKLSGGQRQRVSIARAILKNPP 530
Cdd:PRK11288 352 INISARRHHLRAGCLINNRWEAENADRFIRSLNIktPSREQLIM---------------NLSGGNQQKAILGRWLSEDMK 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499421346 531 ILILDEATSALDTESERLVQEALERLMKT-RTTIAIAHRL-STIKNADEICVLYEGEIVERGRHEE 594
Cdd:PRK11288 417 VILLDEPTRGIDVGAKHEIYNVIYELAAQgVAVLFVSSDLpEVLGVADRIVVMREGRIAGELAREQ 482
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
79-272 |
9.09e-04 |
|
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: 41.63 E-value: 9.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 79 VSQMIQDNGPTTALIFLGLFLALMTLFKTSCYFASSAVMIPLRTGVVRDIRIMVYAKVMRLPMGFFSEERKGDIIARMSG 158
Cdd:cd18584 23 IAGVFLEGAGLAALLPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLLARLLALGPALLRRQSSGELATLLTE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 159 DVGEVENSITSSLDMLIKS---PIMIILYfitLIATSWK---LTLFTVLVLPAMGWLMGKVGRKLKRQSLEAQGKWSdtm 232
Cdd:cd18584 103 GVDALDGYFARYLPQLVLAaivPLLILVA---VFPLDWVsalILLVTAPLIPLFMILIGKAAQAASRRQWAALSRLS--- 176
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 499421346 233 SQLEETLGGLRIIKAFIAEDRMIDRFTRCSNELRDAVNKV 272
Cdd:cd18584 177 GHFLDRLRGLPTLKLFGRARAQAARIARASEDYRRRTMKV 216
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
501-597 |
1.55e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 41.76 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499421346 501 NTNIGD---RGgkLSGGQRQRVSIARAILKNPPILILDEATSALDTESERLVQEALERLMK-TRTTIAIahrlSTIKNA- 575
Cdd:PLN03140 326 DTIVGDemiRG--ISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHlTEATVLM----SLLQPAp 399
|
90 100
....*....|....*....|....*...
gi 499421346 576 ------DEICVLYEGEIVERGRHEELLE 597
Cdd:PLN03140 400 etfdlfDDIILLSEGQIVYQGPRDHILE 427
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
399-420 |
2.04e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 39.45 E-value: 2.04e-03
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
390-417 |
2.70e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.78 E-value: 2.70e-03
10 20
....*....|....*....|....*...
gi 499421346 390 LKHVNLTVPKGKTVALVGQSGSGKSTLV 417
Cdd:COG0178 16 LKNIDVDIPRNKLVVITGLSGSGKSSLA 43
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
509-560 |
3.57e-03 |
|
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: 39.13 E-value: 3.57e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 499421346 509 GKLSGGQRQ------RVSIARAILKNPPILILDEATSALDTESerlVQEALERLMKTR 560
Cdd:cd03240 114 GRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEEN---IEESLAEIIEER 168
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
511-578 |
3.75e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.58 E-value: 3.75e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499421346 511 LSGGQRQRVSIARAIL---KNPPILILDEATSALDTESERLVQEALERLM-KTRTTIAIAHRLSTIKNADEI 578
Cdd:PRK00635 810 LSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHTHDIKALIYVLQSLThQGHTVVIIEHNMHVVKVADYV 881
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
511-578 |
7.88e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 39.29 E-value: 7.88e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499421346 511 LSGGQRQRVSIARAILKNP---PILILDEATSALDTESERLVQEALERLM-KTRTTIAIAHRLSTIKNADEI 578
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRStgkTLYILDEPTTGLHFEDIRKLLEVLHRLVdKGNTVVVIEHNLDVIKTADWI 902
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
398-418 |
9.49e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 34.88 E-value: 9.49e-03
|
| |
