|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
12-610 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 562.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 12 SSKETFKNIISYLKHDSKKLYLGIFFSFCHSIFYVIGSFLIGYIFQQYFANYiasssksdfNVKSFSIWLVILGLVFIAY 91
Cdd:COG1132 4 SPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGG---------DLSALLLLLLLLLGLALLR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 92 GFFRYFDAYMYIKVSYQTSSRMRKEAMHKLIKMPISYYDKQKAGNLISTLINDINNVSNTMYNTINQFFSSIFNVLLSII 171
Cdd:COG1132 75 ALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 172 AMMFVASFITLIVVPLALFLFFISLIVIKKAQPYFVKVQNLFGDLNAFVEENLANTKVMNAFDQQDNIFNEFKKITRGIK 251
Cdd:COG1132 155 VLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 252 LTSFKAdaiARSSEPWFGITSGIANLCVAVLAVsfyiykipvggIGGLGTNpDGTATSGLIVTFISLNWNFMGPFQNLLN 331
Cdd:COG1132 235 RANLRA---ARLSALFFPLMELLGNLGLALVLL-----------VGGLLVL-SGSLTVGDLVAFILYLLRLFGPLRQLAN 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 332 INFSFQMGLASSSRVFKILNLDTKKPHVED-ITIDKIDGLIEFKNVSFKYDinSKKYQLYNASFVAKPGQTVAIVGPTGA 410
Cdd:COG1132 300 VLNQLQRALASAERIFELLDEPPEIPDPPGaVPLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGS 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 411 GKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNLREHMSVVLQDTFMFNDTIENNIKLGDKNATKEDVERAANLSNAIH 490
Cdd:COG1132 378 GKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHE 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 491 FIKTLPNGFQTQIENNGQNLSQGQRQLIAIARAVLANKSILILDEATSNIDSSTEEIIQASLLKIMESKTSFVIAHRLST 570
Cdd:COG1132 458 FIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLST 537
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 502819783 571 IKTADLIIVVNNGEIIEIGTHKNLIQLDGFYSNLYNSQFK 610
Cdd:COG1132 538 IRNADRILVLDDGRIVEQGTHEELLARGGLYARLYRLQFG 577
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
13-608 |
8.81e-139 |
|
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: 420.39 E-value: 8.81e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 13 SKETFKNIISYLKHDSKKLYLGIFFSFCHSIFYVIGSFLIGYIFqqyfaNYIASSsksdfnvKSFSIWLVILGLVFIAYG 92
Cdd:COG2274 140 KPFGLRWFLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVI-----DRVLPN-------QDLSTLWVLAIGLLLALL 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 93 F---FRYFDAYMYIKVSYQTSSRMRKEAMHKLIKMPISYYDKQKAGNLIStLINDINNVSNTMYNTINQFFSSIFNVLLS 169
Cdd:COG2274 208 FeglLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLAS-RFRDVESIREFLTGSLLTALLDLLFVLIF 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 170 IIAMMFVASFITLIVVPLALFLFFISLIVIKKAQPYFVKVQNLFGDLNAFVEENLAN---TKVMNAfdqQDNIFNEFKKI 246
Cdd:COG2274 287 LIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGietIKALGA---ESRFRRRWENL 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 247 TRGIKLTSFKADAIARSSEPWFGITSGIANLCVAVLAVSFYIykipvggigglgtnpDGTATSGLIVTFISLNWNFMGPF 326
Cdd:COG2274 364 LAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVI---------------DGQLTLGQLIAFNILSGRFLAPV 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 327 QNLLNINFSFQMGLASSSRVFKILNLDT-KKPHVEDITIDKIDGLIEFKNVSFKYDiNSKKYQLYNASFVAKPGQTVAIV 405
Cdd:COG2274 429 AQLIGLLQRFQDAKIALERLDDILDLPPeREEGRSKLSLPRLKGDIELENVSFRYP-GDSPPVLDNISLTIKPGERVAIV 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 406 GPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNLREHMSVVLQDTFMFNDTIENNIKLGDKNATKEDVERAANL 485
Cdd:COG2274 508 GRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARL 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 486 SNAIHFIKTLPNGFQTQIENNGQNLSQGQRQLIAIARAVLANKSILILDEATSNIDSSTEEIIQASLLKIMESKTSFVIA 565
Cdd:COG2274 588 AGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIA 667
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 502819783 566 HRLSTIKTADLIIVVNNGEIIEIGTHKNLIQLDGFYSNLYNSQ 608
Cdd:COG2274 668 HRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQ 710
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
16-610 |
5.56e-130 |
|
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: 393.31 E-value: 5.56e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 16 TFKNIISYLKHDSKKLYLGIFFSFchsIFYVIGSFLIGYIfqQYFANyiASSSKSDFNVksfsIWLVILGLVFIAY--GF 93
Cdd:TIGR02203 1 TFRRLWSYVRPYKAGLVLAGVAMI---LVAATESTLAALL--KPLLD--DGFGGRDRSV----LWWVPLVVIGLAVlrGI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 94 FRYFDAYMYIKVSYQTSSRMRKEAMHKLIKMPISYYDKQKAGNLISTLINDINNVSNTMYNTINQFFSSIFNVLLSIIAM 173
Cdd:TIGR02203 70 CSFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 174 MFVASFITLIVVPLALFLFFISLIVIKKAQPYFVKVQNLFGDLNAFVEENLANTKVMNAFDQQDNIFNEFKKITRGIKLT 253
Cdd:TIGR02203 150 LYYSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 254 SFKAdAIARSsepwfgITSGIANLCVAV-LAVSFYIYKIPVGgigglgtnpDGTATSGLIVTFISLNWNFMGPFQNLLNI 332
Cdd:TIGR02203 230 AMKM-TSAGS------ISSPITQLIASLaLAVVLFIALFQAQ---------AGSLTAGDFTAFITAMIALIRPLKSLTNV 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 333 NFSFQMGLASSSRVFKILN----LDTKKPHveditIDKIDGLIEFKNVSFKYDINSKKyQLYNASFVAKPGQTVAIVGPT 408
Cdd:TIGR02203 294 NAPMQRGLAAAESLFTLLDsppeKDTGTRA-----IERARGDVEFRNVTFRYPGRDRP-ALDSISLVIEPGETVALVGRS 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 409 GAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNLREHMSVVLQDTFMFNDTIENNIKLGD-KNATKEDVERAANLSN 487
Cdd:TIGR02203 368 GSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRtEQADRAEIERALAAAY 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 488 AIHFIKTLPNGFQTQIENNGQNLSQGQRQLIAIARAVLANKSILILDEATSNIDSSTEEIIQASLLKIMESKTSFVIAHR 567
Cdd:TIGR02203 448 AQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHR 527
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 502819783 568 LSTIKTADLIIVVNNGEIIEIGTHKNLIQLDGFYSNLYNSQFK 610
Cdd:TIGR02203 528 LSTIEKADRIVVMDDGRIVERGTHNELLARNGLYAQLHNMQFR 570
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
76-609 |
3.92e-115 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 355.10 E-value: 3.92e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 76 SFSIW--LVILGLVFIAyGFFRYFDAYMYIKVSYQTSSRMRKEAMHKLIKMPISYYDKQKAGNLISTLINDINNVSNTMY 153
Cdd:PRK11176 62 SVLKWmpLVVIGLMILR-GITSFISSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSS 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 154 N---TINQFFSSIfnvlLSIIAMMFVASF-ITLIVVPLALFLFFISLIVIKKAQPYFVKVQNLFGDLNAFVEENLANTKV 229
Cdd:PRK11176 141 GaliTVVREGASI----IGLFIMMFYYSWqLSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 230 MNAFDQQDNIFNEFKKIT-----RGIKLTSfkADAIarsSEPwfgITSGIANLcvaVLAVSFYIYKIPvggigglgtNPD 304
Cdd:PRK11176 217 VLIFGGQEVETKRFDKVSnrmrqQGMKMVS--ASSI---SDP---IIQLIASL---ALAFVLYAASFP---------SVM 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 305 GTATSGLIVTFISLNWNFMGPFQNLLNINFSFQMGLASSSRVFKILNLDTKKphveDI---TIDKIDGLIEFKNVSFKYD 381
Cdd:PRK11176 277 DTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFAILDLEQEK----DEgkrVIERAKGDIEFRNVTFTYP 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 382 iNSKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNLREHMSVVLQDTFMFND 461
Cdd:PRK11176 353 -GKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFND 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 462 TIENNIKLGDKNA-TKEDVERAANLSNAIHFIKTLPNGFQTQIENNGQNLSQGQRQLIAIARAVLANKSILILDEATSNI 540
Cdd:PRK11176 432 TIANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSAL 511
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502819783 541 DSSTEEIIQASLLKIMESKTSFVIAHRLSTIKTADLIIVVNNGEIIEIGTHKNLIQLDGFYSNLYNSQF 609
Cdd:PRK11176 512 DTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQLHKMQF 580
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
369-599 |
2.65e-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: 329.96 E-value: 2.65e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 369 GLIEFKNVSFKYdiNSKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNLREH 448
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 449 MSVVLQDTFMFNDTIENNIKLGDKNATKEDVERAANLSNAIHFIKTLPNGFQTQIENNGQNLSQGQRQLIAIARAVLANK 528
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502819783 529 SILILDEATSNIDSSTEEIIQASLLKIMESKTSFVIAHRLSTIKTADLIIVVNNGEIIEIGTHKNLIQLDG 599
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
371-605 |
4.72e-108 |
|
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: 324.57 E-value: 4.72e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 371 IEFKNVSFKYDiNSKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNLREHMS 450
Cdd:cd03251 1 VEFKNVTFRYP-GDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 451 VVLQDTFMFNDTIENNIKLGDKNATKEDVERAANLSNAIHFIKTLPNGFQTQIENNGQNLSQGQRQLIAIARAVLANKSI 530
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502819783 531 LILDEATSNIDSSTEEIIQASLLKIMESKTSFVIAHRLSTIKTADLIIVVNNGEIIEIGTHKNLIQLDGFYSNLY 605
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
18-599 |
7.89e-99 |
|
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: 312.46 E-value: 7.89e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 18 KNIISYLKHDSKKLYLGIFFSFCHSIFYVIGSFLIGYIFQQYFANYIASSSksdfnvksFSIWLVILGLVFIAYGFFRYF 97
Cdd:COG4988 6 KRLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIIGGAPLSA--------LLPLLGLLLAVLLLRALLAWL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 98 DAYMYIKVSYQTSSRMRKEAMHKLIKMPISYYDKQKAGNLISTLINDINNVSNTMYNTINQFFSSIFN--VLLSIIAMM- 174
Cdd:COG4988 78 RERAAFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVplLILVAVFPLd 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 175 FVASFITLIVVPLA-LFLFFISLIVIKKAQPYFVKVQNLFGDlnaFVE--ENLANTKVMNAFDQQDNIFNE----FKKIT 247
Cdd:COG4988 158 WLSGLILLVTAPLIpLFMILVGKGAAKASRRQWRALARLSGH---FLDrlRGLTTLKLFGRAKAEAERIAEasedFRKRT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 248 RGIkLTsfkadaIA-RSSepwfGITSGIANLCVAVLAVSFyiykipvgGIGGLGTNPdgTATSGLIVTFISlnwnfmgP- 325
Cdd:COG4988 235 MKV-LR------VAfLSS----AVLEFFASLSIALVAVYI--------GFRLLGGSL--TLFAALFVLLLA-------Pe 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 326 -FQNLLNINFSF---QMGLASSSRVFKILNLDTKKPHVEDITIDKIDGL-IEFKNVSFKYDinSKKYQLYNASFVAKPGQ 400
Cdd:COG4988 287 fFLPLRDLGSFYharANGIAAAEKIFALLDAPEPAAPAGTAPLPAAGPPsIELEDVSFSYP--GGRPALDGLSLTIPPGE 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 401 TVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNLREHMSVVLQDTFMFNDTIENNIKLGDKNATKEDVE 480
Cdd:COG4988 365 RVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELE 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 481 RAANLSNAIHFIKTLPNGFQTQIENNGQNLSQGQRQLIAIARAVLANKSILILDEATSNIDSSTEEIIQASLLKIMESKT 560
Cdd:COG4988 445 AALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRT 524
|
570 580 590
....*....|....*....|....*....|....*....
gi 502819783 561 SFVIAHRLSTIKTADLIIVVNNGEIIEIGTHKNLIQLDG 599
Cdd:COG4988 525 VILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
116-609 |
3.36e-98 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 311.51 E-value: 3.36e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 116 EAMHKLIKMPISYYDKQKAGNLISTLINdinnVSNTMYNTINQFFSSIFNVLLSIIAMMFVASFI----TLIVVPLALFL 191
Cdd:PRK13657 94 EYFERIIQLPLAWHSQRGSGRALHTLLR----GTDALFGLWLEFMREHLATLVALVVLLPLALFMnwrlSLVLVVLGIVY 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 192 FFISLIVIKKAQPYFVKVQNLFGDLNAFVEENLANTKVMNAFdqqdnifNEFKKITRGIKltsFKADAIARSSEP---WF 268
Cdd:PRK13657 170 TLITTLVMRKTKDGQAAVEEHYHDLFAHVSDAIGNVSVVQSY-------NRIEAETQALR---DIADNLLAAQMPvlsWW 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 269 GITSGI--ANLCVAVLAVsFYIykipvggigGLGTNPDGTATSGLIVTFISlnwnfmgpFQNLL------NINFSFQ--M 338
Cdd:PRK13657 240 ALASVLnrAASTITMLAI-LVL---------GAALVQKGQLRVGEVVAFVG--------FATLLigrldqVVAFINQvfM 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 339 GLASSSRVFKILnlDTKkPHVED----ITIDKIDGLIEFKNVSFKYDinSKKYQLYNASFVAKPGQTVAIVGPTGAGKTT 414
Cdd:PRK13657 302 AAPKLEEFFEVE--DAV-PDVRDppgaIDLGRVKGAVEFDDVSFSYD--NSRQGVEDVSFEAKPGQTVAIVGPTGAGKST 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 415 IINLLGKFYDYNSGSIKIDGYELRNIKTNNLREHMSVVLQDTFMFNDTIENNIKLGDKNATKEDVERAANLSNAIHFIKT 494
Cdd:PRK13657 377 LINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIER 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 495 LPNGFQTQIENNGQNLSQGQRQLIAIARAVLANKSILILDEATSNIDSSTEEIIQASLLKIMESKTSFVIAHRLSTIKTA 574
Cdd:PRK13657 457 KPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNA 536
|
490 500 510
....*....|....*....|....*....|....*
gi 502819783 575 DLIIVVNNGEIIEIGTHKNLIQLDGFYSNLYNSQF 609
Cdd:PRK13657 537 DRILVFDNGRVVESGSFDELVARGGRFAALLRAQG 571
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
371-608 |
2.41e-95 |
|
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: 291.83 E-value: 2.41e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 371 IEFKNVSFKYDINSKkyQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNLREHMS 450
Cdd:cd03253 1 IEFENVTFAYDPGRP--VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 451 VVLQDTFMFNDTIENNIKLGDKNATKEDVERAANLSNaIH-FIKTLPNGFQTQIENNGQNLSQGQRQLIAIARAVLANKS 529
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQ-IHdKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502819783 530 ILILDEATSNIDSSTEEIIQASLLKIMESKTSFVIAHRLSTIKTADLIIVVNNGEIIEIGTHKNLIQLDGFYSNLYNSQ 608
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
371-608 |
5.01e-92 |
|
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: 283.28 E-value: 5.01e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 371 IEFKNVSFKYDINSKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNLREHMS 450
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 451 VVLQDTFMFNDTIENNIKLGDKNATKEDVERAANLSNAIHFIKTLPNGFQTQIENNGQNLSQGQRQLIAIARAVLANKSI 530
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502819783 531 LILDEATSNIDSSTEEIIQASLLKIMESKTSFVIAHRLSTIKTADLIIVVNNGEIIEIGTHKNLIQLDGFYSNLYNSQ 608
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
20-604 |
2.16e-91 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 297.02 E-value: 2.16e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 20 IISYLKHDSKKLYLGIFFSFCHSIfyvigsfliGYIFQQYFANYIASSSKSDFNVKSFSIWLVILGLVFIAYGFFRYFDA 99
Cdd:TIGR00958 152 LLGLSGRDWPWLISAFVFLTLSSL---------GEMFIPFYTGRVIDTLGGDKGPPALASAIFFMCLLSIASSVSAGLRG 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 100 YMYIKVSYQTSSRMRKEAMHKLIKMPISYYDKQKAGNLISTLINDINNVSNTMYNTINQFFSSIFNVLLSIIAMMFVA-- 177
Cdd:TIGR00958 223 GSFNYTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSpr 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 178 -SFITLIVVPLalfLFFISLIVIKKAQPYFVKVQNLFGDLNAFVEENLANTKVMNAFDQQDNIFNEFK-KITRGIKLTsf 255
Cdd:TIGR00958 303 lTMVTLINLPL---VFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKeALEETLQLN-- 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 256 KADAIARSSEPWfgITSGIANLC-VAVLAVSFYIYKipvggigglgtnpDGTATSGLIVTFISLNWNFMGPFQNLLNINF 334
Cdd:TIGR00958 378 KRKALAYAGYLW--TTSVLGMLIqVLVLYYGGQLVL-------------TGKVSSGNLVSFLLYQEQLGEAVRVLSYVYS 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 335 SFQMGLASSSRVFKILNLDTKKPHVEDITIDKIDGLIEFKNVSFKYDINSKKYQLYNASFVAKPGQTVAIVGPTGAGKTT 414
Cdd:TIGR00958 443 GMMQAVGASEKVFEYLDRKPNIPLTGTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKST 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 415 IINLLGKFYDYNSGSIKIDGYELRNIKTNNLREHMSVVLQDTFMFNDTIENNIKLGDKNATKEDVERAANLSNAIHFIKT 494
Cdd:TIGR00958 523 VAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIME 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 495 LPNGFQTQIENNGQNLSQGQRQLIAIARAVLANKSILILDEATSNIDSSTEEIIQASllKIMESKTSFVIAHRLSTIKTA 574
Cdd:TIGR00958 603 FPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES--RSRASRTVLLIAHRLSTVERA 680
|
570 580 590
....*....|....*....|....*....|
gi 502819783 575 DLIIVVNNGEIIEIGTHKNLIQLDGFYSNL 604
Cdd:TIGR00958 681 DQILVLKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
339-608 |
2.60e-91 |
|
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: 294.04 E-value: 2.60e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 339 GLASSSRVFKILNldtKKPHVEDI----TIDKIDGLIEFKNVSFKYDINSKKyqLYNASFVAKPGQTVAIVGPTGAGKTT 414
Cdd:COG5265 325 ALADMERMFDLLD---QPPEVADApdapPLVVGGGEVRFENVSFGYDPERPI--LKGVSFEVPAGKTVAIVGPSGAGKST 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 415 IINLLGKFYDYNSGSIKIDGYELRNIKTNNLREHMSVVLQDTFMFNDTIENNIKLGDKNATKEDVERAANLSNaIH-FIK 493
Cdd:COG5265 400 LARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQ-IHdFIE 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 494 TLPNGFQTQIENNGQNLSQGQRQLIAIARAVLANKSILILDEATSNIDSSTEEIIQASLLKIMESKTSFVIAHRLSTIKT 573
Cdd:COG5265 479 SLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVD 558
|
250 260 270
....*....|....*....|....*....|....*
gi 502819783 574 ADLIIVVNNGEIIEIGTHKNLIQLDGFYSNLYNSQ 608
Cdd:COG5265 559 ADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQ 593
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
68-609 |
2.55e-88 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 285.44 E-value: 2.55e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 68 SKSDFNVKSFSIWLVILGLVFIAYG-FFRYfdaYMYIKVSYQTSSRMRKEAMHKLIKMPISYYDKQKAGNLISTLINDIN 146
Cdd:TIGR02204 50 SKDSSGLLNRYFAFLLVVALVLALGtAARF---YLVTWLGERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTT 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 147 NVSNTMYNTINQFFSSIFNVLLSIIaMMFVASF----ITLIVVPLALF-LFFISLIVIKKAqpyfVKVQNLFGDLNAFVE 221
Cdd:TIGR02204 127 LLQSVIGSSLSMALRNALMCIGGLI-MMFITSPkltsLVLLAVPLVLLpILLFGRRVRKLS----RESQDRIADAGSYAG 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 222 ENLANTKVMNAFDQQDNIFNEF------------KKITRGIKLTS------FKADAIARssepWFGITSGIANLCVAVLA 283
Cdd:TIGR02204 202 ETLGAIRTVQAFGHEDAERSRFggavekayeaarQRIRTRALLTAivivlvFGAIVGVL----WVGAHDVIAGKMSAGTL 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 284 VSFYIYKIPVGGigGLGTnpdgtatsglivtfISLNWNfmgpfqnllninfSFQMGLASSSRVFKILNL--DTKKPHVED 361
Cdd:TIGR02204 278 GQFVFYAVMVAG--SIGT--------------LSEVWG-------------ELQRAAGAAERLIELLQAepDIKAPAHPK 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 362 ITIDKIDGLIEFKNVSFKYDINSKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIK 441
Cdd:TIGR02204 329 TLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLD 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 442 TNNLREHMSVVLQDTFMFNDTIENNIKLGDKNATKEDVERAANLSNAIHFIKTLPNGFQTQIENNGQNLSQGQRQLIAIA 521
Cdd:TIGR02204 409 PAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIA 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 522 RAVLANKSILILDEATSNIDSSTEEIIQASLLKIMESKTSFVIAHRLSTIKTADLIIVVNNGEIIEIGTHKNLIQLDGFY 601
Cdd:TIGR02204 489 RAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLY 568
|
....*...
gi 502819783 602 SNLYNSQF 609
Cdd:TIGR02204 569 ARLARLQF 576
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
89-606 |
2.01e-80 |
|
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: 264.32 E-value: 2.01e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 89 IAYGFFRYFDAYmyikVSYQTS----SRMRKEAMHKLIKMPISYYDKQKAGNLISTLINDINNVSNTMYNTINQFFSSif 164
Cdd:COG4987 66 IGRTVFRYLERL----VSHDATlrllADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRVLLPLLVA-- 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 165 nvLLSIIAMMFVASFIT-----LIVVPLALFLFFISLIVIKKAQPYFVKVQNLFGDLNAFVEENLANTKVMNAFDQQDni 239
Cdd:COG4987 140 --LLVILAAVAFLAFFSpalalVLALGLLLAGLLLPLLAARLGRRAGRRLAAARAALRARLTDLLQGAAELAAYGALD-- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 240 fnefkKITRGIKLTSFKADAIARSSEPWFGITSGIANLCVAVLAVSFYIYKIPVGGIGGLgtnpDGTATSGLIVTFISLn 319
Cdd:COG4987 216 -----RALARLDAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGAL----SGPLLALLVLAALAL- 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 320 wnfmgpFQNLLNINFSFQ-MG--LASSSRVFKILNLDTKKPHVEDITIDKIDGLIEFKNVSFKYDiNSKKYQLYNASFVA 396
Cdd:COG4987 286 ------FEALAPLPAAAQhLGrvRAAARRLNELLDAPPAVTEPAEPAPAPGGPSLELEDVSFRYP-GAGRPVLDGLSLTL 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 397 KPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNLREHMSVVLQDTFMFNDTIENNIKLGDKNATK 476
Cdd:COG4987 359 PPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATD 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 477 EDVERAANLSNAIHFIKTLPNGFQTQIENNGQNLSQGQRQLIAIARAVLANKSILILDEATSNIDSSTEEIIQASLLKIM 556
Cdd:COG4987 439 EELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEAL 518
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 502819783 557 ESKTSFVIAHRLSTIKTADLIIVVNNGEIIEIGTHKNLIQLDGFYSNLYN 606
Cdd:COG4987 519 AGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQLYQ 568
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
371-608 |
3.47e-73 |
|
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: 234.69 E-value: 3.47e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 371 IEFKNVSFKYDINSKkYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNLREHMS 450
Cdd:cd03252 1 ITFEHVRFRYKPDGP-VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 451 VVLQDTFMFNDTIENNIKLGDKNATKEDVERAANLSNAIHFIKTLPNGFQTQIENNGQNLSQGQRQLIAIARAVLANKSI 530
Cdd:cd03252 80 VVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502819783 531 LILDEATSNIDSSTEEIIQASLLKIMESKTSFVIAHRLSTIKTADLIIVVNNGEIIEIGTHKNLIQLDGFYSNLYNSQ 608
Cdd:cd03252 160 LIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
116-604 |
7.36e-73 |
|
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: 244.80 E-value: 7.36e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 116 EAMHKLIKMPISYYDKQKAGNLISTLINDINNVSNTMYNTINQFFSSIFNVLLSIIAMMFVASFITLIVVPLALFLFFIS 195
Cdd:TIGR01192 94 EAFGRIISMPLSWHQQRGTSNALHTLLRATETLFGLWLEFMRQHLATFVALFLLIPTAFAMDWRLSIVLMVLGILYILIA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 196 LIVIKKAQPYFVKVQNLFGDLNAFVEENLANTKVMNAFDQQDNIFNEFKKITRgiKLTSFKADAIArssepWFGITSG-- 273
Cdd:TIGR01192 174 KLVMQRTKNGQAAVEHHYHNVFKHVSDSISNVSVVHSYNRIEAETSALKQFTN--NLLSAQYPVLD-----WWALASGln 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 274 -----IANLCVAVLAVSFYIykipvggigglgtnpDGTATSGLIVTFISLNWNFMGPFQNL---LNINFSFQMGLASssr 345
Cdd:TIGR01192 247 rmastISMMCILVIGTVLVI---------------KGELSVGEVIAFIGFANLLIGRLDQMsgfITQIFEARAKLED--- 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 346 vFKILN---LDTKKPhVEDITIDKIDGLIEFKNVSFKYDiNSKKyQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKF 422
Cdd:TIGR01192 309 -FFDLEdsvFQREEP-ADAPELPNVKGAVEFRHITFEFA-NSSQ-GVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRV 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 423 YDYNSGSIKIDGYELRNIKTNNLREHMSVVLQDTFMFNDTIENNIKLGDKNATKEDVERAANLSNAIHFIKTLPNGFQTQ 502
Cdd:TIGR01192 385 YDPTVGQILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTL 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 503 IENNGQNLSQGQRQLIAIARAVLANKSILILDEATSNIDSSTEEIIQASLLKIMESKTSFVIAHRLSTIKTADLIIVVNN 582
Cdd:TIGR01192 465 VGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQ 544
|
490 500
....*....|....*....|..
gi 502819783 583 GEIIEIGTHKNLIQLDGFYSNL 604
Cdd:TIGR01192 545 GRLIEKGSFQELIQKDGRFYKL 566
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
371-584 |
3.00e-72 |
|
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: 229.58 E-value: 3.00e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 371 IEFKNVSFKYDiNSKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNLREHMS 450
Cdd:cd03228 1 IEFKNVSFSYP-GRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 451 VVLQDTFMFNDTIENNIklgdknatkedveraanlsnaihfiktlpngfqtqienngqnLSQGQRQLIAIARAVLANKSI 530
Cdd:cd03228 80 YVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502819783 531 LILDEATSNIDSSTEEIIQASLLKIMESKTSFVIAHRLSTIKTADLIIVVNNGE 584
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
31-346 |
7.36e-71 |
|
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: 230.37 E-value: 7.36e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 31 LYLGIFFSFCHSIFYVIGSFLIGYIFQQYFANYIASSSksdFNVKSFSIWLVILGLVFIAYGFFRYFDAYMYIKVSYQTS 110
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEGLGGGGG---VDFSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 111 SRMRKEAMHKLIKMPISYYDKQKAGNLISTLINDINNVSNTMYNTINQFFSSIFNVLLSIIAMMFVASFITLIVVPLALF 190
Cdd:cd18547 78 YDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 191 LFFISLIVIKKAQPYFVKVQNLFGDLNAFVEENLANTKVMNAFDQQDNIFNEFKKITRGIKLTSFKADAIARSSEPwfgI 270
Cdd:cd18547 158 SLLVTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKAQFYSGLLMP---I 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502819783 271 TSGIANLCVAVLAVsfyiykipVGGIGGLGtnpdGTATSGLIVTFISLNWNFMGPFQNLLNINFSFQMGLASSSRV 346
Cdd:cd18547 235 MNFINNLGYVLVAV--------VGGLLVIN----GALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAERV 298
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
369-590 |
3.00e-67 |
|
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: 218.52 E-value: 3.00e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 369 GLIEFKNVSFKYDINSKkYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNLREH 448
Cdd:cd03244 1 GDIEFKNVSLRYRPNLP-PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 449 MSVVLQDTFMFNDTIENNIKLGDKnATKEDVERAANLSNAIHFIKTLPNGFQTQIENNGQNLSQGQRQLIAIARAVLANK 528
Cdd:cd03244 80 ISIIPQDPVLFSGTIRSNLDPFGE-YSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502819783 529 SILILDEATSNIDSSTEEIIQASLLKIMESKTSFVIAHRLSTIKTADLIIVVNNGEIIEIGT 590
Cdd:cd03244 159 KILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
16-608 |
2.90e-66 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 227.29 E-value: 2.90e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 16 TFKNIISYLKHDSKKLYLGIFFSFCHSIFYVIGSFLIGYIFQQYFAnyiasssksdfnvKSFSIWLVILGLVfIAY---- 91
Cdd:PRK10790 10 TLKRLLAYGSPWRKPLGLAVLMLWVAAAAEVSGPLLISYFIDNMVA-------------KGNLPLGLVAGLA-AAYvglq 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 92 ---GFFRYFDAYMYIKVSYQTSSRMRKEAMHKLIKMPISYYDKQKAGNLISTLINDINNVSNTMYNTINQFFSSIfnvll 168
Cdd:PRK10790 76 llaAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVATVLRSA----- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 169 SIIAMMFVASFI---TLIVVPLALFLFFISLIVI--KKAQPYFVKVQNLFGDLNAFVEENLANTKVMNAFDQQDNiFNE- 242
Cdd:PRK10790 151 ALIGAMLVAMFSldwRMALVAIMIFPAVLVVMVIyqRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQAR-FGEr 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 243 --------FKKITRGIKLTSFkadaIARssePWFGITSGIAnLCVAVLAVSFyiykipvggigglgtNPDGTATSGLIVT 314
Cdd:PRK10790 230 mgeasrshYMARMQTLRLDGF----LLR---PLLSLFSALI-LCGLLMLFGF---------------SASGTIEVGVLYA 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 315 FIslnwNFMG----PFQNLLNINFSFQMGLASSSRVFKILnlDTKKPHVEDITIDKIDGLIEFKNVSFKYDinSKKYQLY 390
Cdd:PRK10790 287 FI----SYLGrlnePLIELTTQQSMLQQAVVAGERVFELM--DGPRQQYGNDDRPLQSGRIDIDNVSFAYR--DDNLVLQ 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 391 NASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNLREHMSVVLQDTFMFNDTIENNIKLG 470
Cdd:PRK10790 359 NINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLG 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 471 dKNATKEDVERAANLSNAIHFIKTLPNGFQTQIENNGQNLSQGQRQLIAIARAVLANKSILILDEATSNIDSSTEEIIQA 550
Cdd:PRK10790 439 -RDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQ 517
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 502819783 551 SLLKIMESKTSFVIAHRLSTIKTADLIIVVNNGEIIEIGTHKNLIQLDGFYSNLYNSQ 608
Cdd:PRK10790 518 ALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQ 575
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
80-608 |
3.27e-66 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 226.52 E-value: 3.27e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 80 WLVILGLVFIAYGFFRYFDAYMYIKVSYQTSSRMRKEAMHKLIKMPISYYDKQKAGNLISTLINDINNVSNTMYNTINQF 159
Cdd:PRK10789 38 WIGTMVLIAVVVYLLRYVWRVLLFGASYQLAVELREDFYRQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 160 FSSIFNVLLSIIAMMFVASF-ITLivvpLALFLFFISLIVIK----KAQPYFVKVQNLFGDLNAFVEENLANTKVMNAF- 233
Cdd:PRK10789 118 VDSLVMGCAVLIVMSTQISWqLTL----LALLPMPVMAIMIKrygdQLHERFKLAQAAFSSLNDRTQESLTSIRMIKAFg 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 234 --DQQDNIFNEFKKITRGIKLTSFKADAiarSSEPWFGITSGIANLcvavLAVSfyiykipvggiGGLGTNPDGTATSGL 311
Cdd:PRK10789 194 leDRQSALFAADAEDTGKKNMRVARIDA---RFDPTIYIAIGMANL----LAIG-----------GGSWMVVNGSLTLGQ 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 312 IVTFI-----------SLNWNFmgpfqnllNInfsFQMGLASSSRVFKILNldtKKPHVED--ITIDKIDGLIEFKNVSF 378
Cdd:PRK10789 256 LTSFVmylglmiwpmlALAWMF--------NI---VERGSAAYSRIRAMLA---EAPVVKDgsEPVPEGRGELDVNIRQF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 379 KYDINSKKyQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNLREHMSVVLQDTFM 458
Cdd:PRK10789 322 TYPQTDHP-ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 459 FNDTIENNIKLGDKNATKEDVERAANLSNAIHFIKTLPNGFQTQIENNGQNLSQGQRQLIAIARAVLANKSILILDEATS 538
Cdd:PRK10789 401 FSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALS 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 539 NIDSSTEEIIQASLLKIMESKTSFVIAHRLSTIKTADLIIVVNNGEIIEIGTHKNLIQLDGFYSNLYNSQ 608
Cdd:PRK10789 481 AVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQ 550
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
369-586 |
1.31e-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: 213.99 E-value: 1.31e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 369 GLIEFKNVSFKYDiNSKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNLREH 448
Cdd:cd03245 1 GRIEFRNVSFSYP-NQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 449 MSVVLQDTFMFNDTIENNIKLGDKNATKEDVERAANLSNAIHFIKTLPNGFQTQIENNGQNLSQGQRQLIAIARAVLANK 528
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502819783 529 SILILDEATSNIDSSTEEIIQASLLKIMESKTSFVIAHRLSTIKTADLIIVVNNGEII 586
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIV 217
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
103-604 |
4.44e-63 |
|
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: 220.97 E-value: 4.44e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 103 IKVSYQTSSRMrkeaMHKLIKMPISYYDKQKAGNLISTL-INDinNVSNTMYNTINQFFSSIFNVLLSIIAMMFVASFIT 181
Cdd:TIGR03796 223 IKLAVGMSARF----LWHILRLPVRFFAQRHAGDIASRVqLND--QVAEFLSGQLATTALDAVMLVFYALLMLLYDPVLT 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 182 LIVVPLALFLFFISLIVIKKAQPYFVKVQNLFGDLNAFVEENLANTKVMNAFDQQDNIFNEFkkitrgiklTSFKADAIa 261
Cdd:TIGR03796 297 LIGIAFAAINVLALQLVSRRRVDANRRLQQDAGKLTGVAISGLQSIETLKASGLESDFFSRW---------AGYQAKLL- 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 262 rSSEPWFGITSGIANLCVAVLAVsfyIYKIPVGGIGGLGTNpDGTATSGLIVTFISLNWNFMGPFQNLLNINFSFQMGLA 341
Cdd:TIGR03796 367 -NAQQELGVLTQILGVLPTLLTS---LNSALILVVGGLRVM-EGQLTIGMLVAFQSLMSSFLEPVNNLVGFGGTLQELEG 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 342 SSSRVFKILNLDTKKPHVEDITID-------KIDGLIEFKNVSFKYDInSKKYQLYNASFVAKPGQTVAIVGPTGAGKTT 414
Cdd:TIGR03796 442 DLNRLDDVLRNPVDPLLEEPEGSAatsepprRLSGYVELRNITFGYSP-LEPPLIENFSLTLQPGQRVALVGGSGSGKST 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 415 IINLLGKFYDYNSGSIKIDGYELRNIKTNNLREHMSVVLQDTFMFNDTIENNIKLGDKNATKEDVERAANlSNAIH-FIK 493
Cdd:TIGR03796 521 IAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPTIPDADLVRACK-DAAIHdVIT 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 494 TLPNGFQTQIENNGQNLSQGQRQLIAIARAVLANKSILILDEATSNIDSSTEEIIQASLLKimESKTSFVIAHRLSTIKT 573
Cdd:TIGR03796 600 SRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLRR--RGCTCIIVAHRLSTIRD 677
|
490 500 510
....*....|....*....|....*....|.
gi 502819783 574 ADLIIVVNNGEIIEIGTHKNLIQLDGFYSNL 604
Cdd:TIGR03796 678 CDEIIVLERGKVVQRGTHEELWAVGGAYARL 708
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
29-580 |
3.35e-59 |
|
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: 206.75 E-value: 3.35e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 29 KKLYLGIFFSFCHSIFYVIGSFLIGYIFQQYFANYIASSSksdfnvksFSIWLVILGLVFIAYGFFRYFDAYMYIKVSYQ 108
Cdd:TIGR02857 3 RALALLALLGVLGALLIIAQAWLLARVVDGLISAGEPLAE--------LLPALGALALVLLLRALLGWLQERAAARAAAA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 109 TSSRMRKEAMHKLIKMPISYYDKQKAGNLISTLINDINNVSNTMYNTINQFFSSIFnVLLSIIAMMFVASFITLIVVPLA 188
Cdd:TIGR02857 75 VKSQLRERLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFARYLPQLVLAVI-VPLAILAAVFPQDWISGLILLLT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 189 LFLFFISLIVI-KKAQPYFVKVQNLFGDLNAFVEENLANTKVMNAFDQQDNifnefkkitrgikltsfKADAIARSSEPW 267
Cdd:TIGR02857 154 APLIPIFMILIgWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKA-----------------QAAAIRRSSEEY 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 268 FGIT---------SG-----IANLCVAVLAVsfYIykipvgGIGGLGtnPDGTATSGLIVtfISLNWNFMGPFQNLlniN 333
Cdd:TIGR02857 217 RERTmrvlriaflSSavlelFATLSVALVAV--YI------GFRLLA--GDLDLATGLFV--LLLAPEFYLPLRQL---G 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 334 FSF---QMGLASSSRVFKILNLDTK-KPHVEDITIDKIDGlIEFKNVSFKYdiNSKKYQLYNASFVAKPGQTVAIVGPTG 409
Cdd:TIGR02857 282 AQYharADGVAAAEALFAVLDAAPRpLAGKAPVTAAPASS-LEFSGVSVAY--PGRRPALRPVSFTVPPGERVALVGPSG 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 410 AGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNLREHMSVVLQDTFMFNDTIENNIKLGDKNATKEDVERAANLSNAI 489
Cdd:TIGR02857 359 AGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLD 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 490 HFIKTLPNGFQTQIENNGQNLSQGQRQLIAIARAVLANKSILILDEATSNIDSSTEEIIQASLLKIMESKTSFVIAHRLS 569
Cdd:TIGR02857 439 EFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLA 518
|
570
....*....|.
gi 502819783 570 TIKTADLIIVV 580
Cdd:TIGR02857 519 LAALADRIVVL 529
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
29-606 |
9.43e-56 |
|
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: 200.74 E-value: 9.43e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 29 KKLYLGIFFSfchSIFYVIGSFLIGYIFQQYFANYIASSSKSdfnvksfSIWLVILGLVFiAYGF---FRYFDAYMYIKV 105
Cdd:TIGR01193 155 KKLIVNIVIA---AIIVTLISIAGSYYLQKIIDTYIPHKMMG-------TLGIISIGLII-AYIIqqiLSYIQIFLLNVL 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 106 SYQTSSRMRKEAMHKLIKMPISYYDKQKAGNLISTlindinnvsntmYNTINQFFSSIFNVLLSIIAMMFVASFITLIVV 185
Cdd:TIGR01193 224 GQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSR------------FTDASSIIDALASTILSLFLDMWILVIVGLFLV 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 186 PLALFLFFISLIVIKKAQPYFVKVQNLFGDLNAFVEENLA--NTKVMNAFDQQDNIFNEFKKITRGIKLTSFKADAIARS 263
Cdd:TIGR01193 292 RQNMLLFLLSLLSIPVYAVIIILFKRTFNKLNHDAMQANAvlNSSIIEDLNGIETIKSLTSEAERYSKIDSEFGDYLNKS 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 264 SEpwFGITSGIANLCVAVLAVSFYIYKIPVGGIGGLgtnpDGTATSGLIVTFISLNWNFMGPFQNLLNINFSFQMGLASS 343
Cdd:TIGR01193 372 FK--YQKADQGQQAIKAVTKLILNVVILWTGAYLVM----RGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVAN 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 344 SRVFKILNLDTKKPHVEDIT-IDKIDGLIEFKNVSFKYDINSKKyqLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKF 422
Cdd:TIGR01193 446 NRLNEVYLVDSEFINKKKRTeLNNLNGDIVINDVSYSYGYGSNI--LSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGF 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 423 YDYNSGSIKIDGYELRNIKTNNLREHMSVVLQDTFMFNDTIENNIKLGDK-NATKEDVERAANLSNAIHFIKTLPNGFQT 501
Cdd:TIGR01193 524 FQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAKeNVSQDEIWAACEIAEIKDDIENMPLGYQT 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 502 QIENNGQNLSQGQRQLIAIARAVLANKSILILDEATSNIDSSTEEIIQASLLKIMEsKTSFVIAHRLSTIKTADLIIVVN 581
Cdd:TIGR01193 604 ELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD-KTIIFVAHRLSVAKQSDKIIVLD 682
|
570 580
....*....|....*....|....*
gi 502819783 582 NGEIIEIGTHKNLIQLDGFYSNLYN 606
Cdd:TIGR01193 683 HGKIIEQGSHDELLDRNGFYASLIH 707
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
365-585 |
2.11e-55 |
|
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: 187.29 E-value: 2.11e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 365 DKIDGLIEFKNVSFKYDINSKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNN 444
Cdd:cd03248 6 DHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 445 LREHMSVVLQDTFMFNDTIENNIKLGDKNATKEDVERAANLSNAIHFIKTLPNGFQTQIENNGQNLSQGQRQLIAIARAV 524
Cdd:cd03248 86 LHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502819783 525 LANKSILILDEATSNIDSSTEEIIQASLLKIMESKTSFVIAHRLSTIKTADLIIVVNNGEI 585
Cdd:cd03248 166 IRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
50-608 |
3.31e-55 |
|
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: 199.03 E-value: 3.31e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 50 FLIGYIFQqyfaNYIASSSKSdfnvKSFSIWLVILGLVFIAyGFFRYFDAYMYIKVSYQTSSRMRKEAMHKLIKMPISYY 129
Cdd:TIGR03797 157 IATGILIG----TAIPDADRS----LLVQIALALLAAAVGA-AAFQLAQSLAVLRLETRMDASLQAAVWDRLLRLPVSFF 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 130 DKQKAGNLISTlINDINNVSNTMYN-TINQFFSSIFNVLlsIIAMMFVASF------ITLIVVPLALFLFfISLIVIKKA 202
Cdd:TIGR03797 228 RQYSTGDLASR-AMGISQIRRILSGsTLTTLLSGIFALL--NLGLMFYYSWklalvaVALALVAIAVTLV-LGLLQVRKE 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 203 QPyfvkVQNLFGDLNAFV--------------EENLANTKVMNAFDQQDNIFNEFKKItrGIKLTSFKAdaiarssepwf 268
Cdd:TIGR03797 304 RR----LLELSGKISGLTvqlingisklrvagAENRAFARWAKLFSRQRKLELSAQRI--ENLLTVFNA----------- 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 269 gitsGIANLCVAVLavsFYIykipvggIGGLGTNpdGTATSGLIVTFISLNWNFMGPFQNLLNINFSFQMGLASSSRVFK 348
Cdd:TIGR03797 367 ----VLPVLTSAAL---FAA-------AISLLGG--AGLSLGSFLAFNTAFGSFSGAVTQLSNTLISILAVIPLWERAKP 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 349 ILnldTKKPHVEDITID--KIDGLIEFKNVSFKYDINSKKYqLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYN 426
Cdd:TIGR03797 431 IL---EALPEVDEAKTDpgKLSGAIEVDRVTFRYRPDGPLI-LDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPE 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 427 SGSIKIDGYELRNIKTNNLREHMSVVLQDTFMFNDTIENNIkLGDKNATKEDVERAANLSNAIHFIKTLPNGFQTQIENN 506
Cdd:TIGR03797 507 SGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENI-AGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEG 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 507 GQNLSQGQRQLIAIARAVLANKSILILDEATSNIDSSTEEIIQASLLKImeSKTSFVIAHRLSTIKTADLIIVVNNGEII 586
Cdd:TIGR03797 586 GGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERL--KVTRIVIAHRLSTIRNADRIYVLDAGRVV 663
|
570 580
....*....|....*....|..
gi 502819783 587 EIGTHKNLIQLDGFYSNLYNSQ 608
Cdd:TIGR03797 664 QQGTYDELMAREGLFAQLARRQ 685
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
33-602 |
1.18e-54 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 201.33 E-value: 1.18e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 33 LGIFFSFCHSIFYV---IGSFLIGYIFQQYFANYIASSSKSDFNVKsfsiwLVILGLVFIAYGFFrYFDAYMYIKVS-YQ 108
Cdd:TIGR00957 962 IGLFITFLSIFLFVcnhVSALASNYWLSLWTDDPMVNGTQNNTSLR-----LSVYGALGILQGFA-VFGYSMAVSIGgIQ 1035
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 109 TSSRMRKEAMHKLIKMPISYYDKQKAGNLISTLINDINNVSNTMYNTINQFFSSIFNVLLSIIAMMFVASFITLIVVPLA 188
Cdd:TIGR00957 1036 ASRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLG 1115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 189 LFLFFIslivikkaQPYFVKVQNLFGDLNAF--------VEENLANTKVMNAFDQQDnifnefkkitRGIKLTSFKADAI 260
Cdd:TIGR00957 1116 LLYFFV--------QRFYVASSRQLKRLESVsrspvyshFNETLLGVSVIRAFEEQE----------RFIHQSDLKVDEN 1177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 261 ARSSEP------WFGITSGIANLCVAVLAVSFYIykipvggIGGLGTNPD--GTATS-GLIVTFiSLNWnfmgpfqnLLN 331
Cdd:TIGR00957 1178 QKAYYPsivanrWLAVRLECVGNCIVLFAALFAV-------ISRHSLSAGlvGLSVSySLQVTF-YLNW--------LVR 1241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 332 INFSFQMGLASSSRVFKILNLDTKKPHVEDITIDKID----GLIEFKNVSFKY--DINskkYQLYNASFVAKPGQTVAIV 405
Cdd:TIGR00957 1242 MSSEMETNIVAVERLKEYSETEKEAPWQIQETAPPSGwpprGRVEFRNYCLRYreDLD---LVLRHINVTIHGGEKVGIV 1318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 406 GPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNLREHMSVVLQDTFMFNDTIENNIKLGDKnATKEDVERAANL 485
Cdd:TIGR00957 1319 GRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQ-YSDEEVWWALEL 1397
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 486 SNAIHFIKTLPNGFQTQIENNGQNLSQGQRQLIAIARAVLANKSILILDEATSNIDSSTEEIIQASLLKIMESKTSFVIA 565
Cdd:TIGR00957 1398 AHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIA 1477
|
570 580 590
....*....|....*....|....*....|....*...
gi 502819783 566 HRLSTIKTADLIIVVNNGEIIEIGTHKNLIQLDG-FYS 602
Cdd:TIGR00957 1478 HRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGiFYS 1515
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
323-608 |
5.99e-51 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 185.03 E-value: 5.99e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 323 MGPFQNLLNINFSFQ-MG--LASSSRVFKILNL--DTKKPHVEDITIDKidGLIEFKNVSFKYDiNSKKYQLYNASFVAK 397
Cdd:PRK11160 288 LAAFEALMPVAGAFQhLGqvIASARRINEITEQkpEVTFPTTSTAAADQ--VSLTLNNVSFTYP-DQPQPVLKGLSLQIK 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 398 PGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNLREHMSVVLQDTFMFNDTIENNIKLGDKNATKE 477
Cdd:PRK11160 365 AGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDE 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 478 ---DVERAANLSNAIhfikTLPNGFQTQIENNGQNLSQGQRQLIAIARAVLANKSILILDEATSNIDSSTEEIIQASLLK 554
Cdd:PRK11160 445 aliEVLQQVGLEKLL----EDDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAE 520
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 502819783 555 IMESKTSFVIAHRLSTIKTADLIIVVNNGEIIEIGTHKNLIQLDGFYSNLYNSQ 608
Cdd:PRK11160 521 HAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLKQRL 574
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
348-606 |
9.99e-51 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 184.66 E-value: 9.99e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 348 KILNLDTKKPHVEDITIDKIDGL-IEFKNVS-FKYDinsKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDY 425
Cdd:PRK11174 326 TFLETPLAHPQQGEKELASNDPVtIEAEDLEiLSPD---GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 426 NsGSIKIDGYELRNIKTNNLREHMSVVLQDTFMFNDTIENNIKLGDKNATKEDVERAANLSNAIHFIKTLPNGFQTQIEN 505
Cdd:PRK11174 403 Q-GSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGD 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 506 NGQNLSQGQRQLIAIARAVLANKSILILDEATSNIDSSTEEIIQASLLKIMESKTSFVIAHRLSTIKTADLIIVVNNGEI 585
Cdd:PRK11174 482 QAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQI 561
|
250 260
....*....|....*....|.
gi 502819783 586 IEIGTHKNLIQLDGFYSNLYN 606
Cdd:PRK11174 562 VQQGDYAELSQAGGLFATLLA 582
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
368-590 |
3.75e-48 |
|
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: 167.20 E-value: 3.75e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 368 DGLIEFKNVSFKYDINSKKYqLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNLRE 447
Cdd:cd03369 4 HGEIEVENLSVRYAPDLPPV-LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 448 HMSVVLQDTFMFNDTIENNIKLGDKnatKEDVERAANLSnaihfiktlpngfqtqIENNGQNLSQGQRQLIAIARAVLAN 527
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNLDPFDE---YSDEEIYGALR----------------VSEGGLNLSQGQRQLLCLARALLKR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502819783 528 KSILILDEATSNIDSSTEEIIQASLLKIMESKTSFVIAHRLSTIKTADLIIVVNNGEIIEIGT 590
Cdd:cd03369 144 PRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
75-599 |
7.48e-45 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 172.08 E-value: 7.48e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 75 KSFS--IWLVILGLVFIAYGFFRYFDAYMYIKVSYQTSSRMRKEAMHKLIKMPISYYDKQKAGNLISTLINDINNVSNTM 152
Cdd:PLN03232 945 KSYSpgFYIVVYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNV 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 153 YNTINQFFSSIFNvLLSIIAMMFVASFITLIVVPLALFLFFISLIVIKKAQPYFVKVQN--------LFGD-LNAfveen 223
Cdd:PLN03232 1025 ANLMNMFMNQLWQ-LLSTFALIGTVSTISLWAIMPLLILFYAAYLYYQSTSREVRRLDSvtrspiyaQFGEaLNG----- 1098
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 224 LANTKVMNAFDQQDNIfnEFKKITRGIKLTsfkadAIARSSEPWFGITSGIANLCVAVLAVSFYIYKipvggiGGLGTNP 303
Cdd:PLN03232 1099 LSSIRAYKAYDRMAKI--NGKSMDNNIRFT-----LANTSSNRWLTIRLETLGGVMIWLTATFAVLR------NGNAENQ 1165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 304 DGTA-TSGLIVTFISlnwNFMGPFQNLLNINFSFQMGLASSSRVFKILNLDTKKPHVED----ITIDKIDGLIEFKNVSF 378
Cdd:PLN03232 1166 AGFAsTMGLLLSYTL---NITTLLSGVLRQASKAENSLNSVERVGNYIDLPSEATAIIEnnrpVSGWPSRGSIKFEDVHL 1242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 379 KYDINSKKYqLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNLREHMSVVLQDTFM 458
Cdd:PLN03232 1243 RYRPGLPPV-LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVL 1321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 459 FNDTIENNIklgDKNATKEDveraANLSNAIH------FIKTLPNGFQTQIENNGQNLSQGQRQLIAIARAVLANKSILI 532
Cdd:PLN03232 1322 FSGTVRFNI---DPFSEHND----ADLWEALErahikdVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILV 1394
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502819783 533 LDEATSNIDSSTEEIIQASLLKIMESKTSFVIAHRLSTIKTADLIIVVNNGEIIEIGTHKNLIQLDG 599
Cdd:PLN03232 1395 LDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDT 1461
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
81-596 |
4.67e-44 |
|
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: 165.21 E-value: 4.67e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 81 LVILGLVFiAYGFFRYFDAYMYIKVSYQTSSRMRKEAMHKLIKMPISyydkqkAGNLIST-LINDINNVSNTMY-NTINQ 158
Cdd:TIGR01842 50 VLALGLYL-FLGLLDALRSFVLVRIGEKLDGALNQPIFAASFSATLR------RGSGDGLqALRDLDQLRQFLTgPGLFA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 159 FFSS-IFNVLLSIIAMM-----FVASFITLIVVPLALFLFFISLIVIKKAQPYFVKVQNLfgdlnafVEENLANTKVMNA 232
Cdd:TIGR01842 123 FFDApWMPIYLLVCFLLhpwigILALGGAVVLVGLALLNNRATKKPLKEATEASIRANNL-------ADSALRNAEVIEA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 233 FDQQDNIFNEFKKitrgikltsFKADAIArssepWFGITSGIANLCVAVLAVSFYIYKIPVGGIGGLgTNPDGTATSGLI 312
Cdd:TIGR01842 196 MGMMGNLTKRWGR---------FHSKYLS-----AQSAASDRAGMLSNLSKYFRIVLQSLVLGLGAY-LAIDGEITPGMM 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 313 VTFISLNWNFMGPFQNLLNINFSFQMGLASSSRVFKIL-NLDTKKPHVEditIDKIDGLIEFKNVSFKYDiNSKKYQLYN 391
Cdd:TIGR01842 261 IAGSILVGRALAPIDGAIGGWKQFSGARQAYKRLNELLaNYPSRDPAMP---LPEPEGHLSVENVTIVPP-GGKKPTLRG 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 392 ASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNLREHMSVVLQDTFMFNDTIENNIKLGD 471
Cdd:TIGR01842 337 ISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIARFG 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 472 KNATKEDVERAANLSNAIHFIKTLPNGFQTQIENNGQNLSQGQRQLIAIARAVLANKSILILDEATSNIDSSTEEIIQAS 551
Cdd:TIGR01842 417 ENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANA 496
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 502819783 552 LLKIMESK-TSFVIAHRLSTIKTADLIIVVNNGEIIEIGTHKNLIQ 596
Cdd:TIGR01842 497 IKALKARGiTVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLA 542
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
369-604 |
1.05e-42 |
|
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: 154.30 E-value: 1.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 369 GLIEFKNVSFKYDiNSKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNLREH 448
Cdd:cd03288 18 GEIKIHDLCVRYE-NNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 449 MSVVLQDTFMFNDTIENNIKlGDKNATKEDVERAANLSNAIHFIKTLPNGFQTQIENNGQNLSQGQRQLIAIARAVLANK 528
Cdd:cd03288 97 LSIILQDPILFSGSIRFNLD-PECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKS 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502819783 529 SILILDEATSNIDSSTEEIIQASLLKIMESKTSFVIAHRLSTIKTADLIIVVNNGEIIEIGTHKNLI-QLDGFYSNL 604
Cdd:cd03288 176 SILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaQEDGVFASL 252
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
33-346 |
4.88e-42 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 153.48 E-value: 4.88e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 33 LGIFFSFCHSIFYVIGSFLIGYIFQQYFANyiasssksdFNVKSFSIWLVILGLVFIAYGFFRYFDAYMYIKVSYQTSSR 112
Cdd:cd07346 3 LALLLLLLATALGLALPLLTKLLIDDVIPA---------GDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 113 MRKEAMHKLIKMPISYYDKQKAGNLISTLINDINNVSNTMYNTINQFFSSIFNVLLSIIAMMFVASFITLIVVPLALFLF 192
Cdd:cd07346 74 LRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 193 FISLIVIKKAQPYFVKVQNLFGDLNAFVEENLANTKVMNAFDQQDNIFNEFKKITRGIKLTSFKADAIARSSEPWFGITS 272
Cdd:cd07346 154 LILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLT 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502819783 273 GIANLCVAVLAVSFYIykipvggigglgtnpDGTATSGLIVTFISLNWNFMGPFQNLLNINFSFQMGLASSSRV 346
Cdd:cd07346 234 ALGTALVLLYGGYLVL---------------QGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
371-585 |
1.34e-41 |
|
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: 148.13 E-value: 1.34e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 371 IEFKNVSFKYDiNSKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNLREHMS 450
Cdd:cd03246 1 LEVENVSFRYP-GAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 451 VVLQDTFMFNDTIENNIklgdknatkedveraanlsnaihfiktlpngfqtqienngqnLSQGQRQLIAIARAVLANKSI 530
Cdd:cd03246 80 YLPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502819783 531 LILDEATSNIDSSTEEIIQASLLKI-MESKTSFVIAHRLSTIKTADLIIVVNNGEI 585
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
367-601 |
2.01e-41 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 161.35 E-value: 2.01e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 367 IDGLIEFKNVSFKYdINSKKYQLY-NASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDY-------------------- 425
Cdd:PTZ00265 1162 IKGKIEIMDVNFRY-ISRPNVPIYkDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfknehtndmtneq 1240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 426 ----------------------------------NSGSIKIDGYELRNIKTNNLREHMSVVLQDTFMFNDTIENNIKLGD 471
Cdd:PTZ00265 1241 dyqgdeeqnvgmknvnefsltkeggsgedstvfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGK 1320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 472 KNATKEDVERAANLSNAIHFIKTLPNGFQTQIENNGQNLSQGQRQLIAIARAVLANKSILILDEATSNIDSSTEEIIQAS 551
Cdd:PTZ00265 1321 EDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKT 1400
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 502819783 552 LLKIMES--KTSFVIAHRLSTIKTADLIIVVNN----GEIIEI-GTHKNLIQL-DGFY 601
Cdd:PTZ00265 1401 IVDIKDKadKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQAhGTHEELLSVqDGVY 1458
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
369-590 |
8.74e-41 |
|
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: 156.06 E-value: 8.74e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 369 GLIEFKNVSFKYDiNSKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNLREH 448
Cdd:COG4618 329 GRLSVENLTVVPP-GSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRH 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 449 MSVVLQDTFMFNDTIENNI-KLGDknATKEDVERAANLSNAIHFIKTLPNGFQTQIENNGQNLSQGQRQLIAIARAVLAN 527
Cdd:COG4618 408 IGYLPQDVELFDGTIAENIaRFGD--ADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGD 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502819783 528 KSILILDEATSNIDSSTEEIIQASLLKIMESKTS-FVIAHRLSTIKTADLIIVVNNGEIIEIGT 590
Cdd:COG4618 486 PRLVVLDEPNSNLDDEGEAALAAAIRALKARGATvVVITHRPSLLAAVDKLLVLRDGRVQAFGP 549
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
89-568 |
8.23e-39 |
|
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: 150.20 E-value: 8.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 89 IAYGFFRYFDAYMYIKVSYQTSSRMRKEAMHKLIKMPISYYDKQKAGNLISTLINDINNVSNTMYNTInqfFSSIFNVLL 168
Cdd:TIGR02868 64 IGRAVFRYLERLVGHDAALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVI---VPAGVALVV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 169 SIIAMMFVASF-----ITLIVVpLALFLFFISLIVIKKAQPYFVKVQNLFGDLNAFVEENLANTKVMNAFDQQDnifnef 243
Cdd:TIGR02868 141 GAAAVAAIAVLsvpaaLILAAG-LLLAGFVAPLVSLRAARAAEQALARLRGELAAQLTDALDGAAELVASGALP------ 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 244 kKITRGIKLTSFKADAIARSSEPWFGITSGIANLcVAVLAVsfyIYKIPVGGIGGLGTNPDGTATSGLIVTFISLnWNFM 323
Cdd:TIGR02868 214 -AALAQVEEADRELTRAERRAAAATALGAALTLL-AAGLAV---LGALWAGGPAVADGRLAPVTLAVLVLLPLAA-FEAF 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 324 GPFQNLLNinfSFQMGLASSSRVFKILnlDTKK-------PHVEDITIDKIDglIEFKNVSFKYDINSKkyQLYNASFVA 396
Cdd:TIGR02868 288 AALPAAAQ---QLTRVRAAAERIVEVL--DAAGpvaegsaPAAGAVGLGKPT--LELRDLSAGYPGAPP--VLDGVSLDL 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 397 KPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNLREHMSVVLQDTFMFNDTIENNIKLGDKNATK 476
Cdd:TIGR02868 359 PPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATD 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 477 EDVERAANLSNAIHFIKTLPNGFQTQIENNGQNLSQGQRQLIAIARAVLANKSILILDEATSNIDSSTEEIIQASLLKIM 556
Cdd:TIGR02868 439 EELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAAL 518
|
490
....*....|..
gi 502819783 557 ESKTSFVIAHRL 568
Cdd:TIGR02868 519 SGRTVVLITHHL 530
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
371-589 |
3.07e-38 |
|
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: 139.37 E-value: 3.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 371 IEFKNVSFKYDINSKKYqLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKtNNLREHMS 450
Cdd:cd03247 1 LSINNVSFSYPEQEQQV-LKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 451 VVLQDTFMFNDTIENNIklgdknatkedveraanlsnaihfiktlpngfqtqiennGQNLSQGQRQLIAIARAVLANKSI 530
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502819783 531 LILDEATSNIDSSTEEIIQASLLKIMESKTSFVIAHRLSTIKTADLIIVVNNGEIIEIG 589
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
31-346 |
1.91e-37 |
|
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: 140.60 E-value: 1.91e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 31 LYLGIFFSFCHSIFYVIGSFLIGYIFQQYFANYiasssksDFNVKSFSIWLVILGLVFIAYGFFRYFDAYMYIKVSYQTS 110
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIDDYIVPG-------QGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRII 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 111 SRMRKEAMHKLIKMPISYYDKQKAGNLISTLINDINNVSNTMYNTINQFFSSIFnVLLSIIAMMFVAS----FITLIVVP 186
Cdd:cd18544 74 YDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLL-LLIGILIAMFLLNwrlaLISLLVLP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 187 lalFLFFISLIVIKKAQPYFVKVQNLFGDLNAFVEENLANTKVMNAFDQQDNIFNEFKKITRGIKLTSFK---ADAIARS 263
Cdd:cd18544 153 ---LLLLATYLFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKsikLFALFRP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 264 sepwfgITSGIANLCVAVLavsfyIYkipVGGIGGLgtnpDGTATSGLIVTFISLNWNFMGPFQNL---LNInfsFQMGL 340
Cdd:cd18544 230 ------LVELLSSLALALV-----LW---YGGGQVL----SGAVTLGVLYAFIQYIQRFFRPIRDLaekFNI---LQSAM 288
|
....*.
gi 502819783 341 ASSSRV 346
Cdd:cd18544 289 ASAERI 294
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
98-599 |
6.73e-37 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 147.96 E-value: 6.73e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 98 DAYMYIKVSYQTSSRMRKEAMHKLIKMPISYYDKQKAGNLISTLINDINNVSNTMYNTINQFFSSIFNvLLSIIAMMFVA 177
Cdd:PLN03130 973 NSYWLIMSSLYAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFLGQIFQ-LLSTFVLIGIV 1051
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 178 SFITLIVVpLALFLFFISLIVIKKAQPYFVK---------VQNLFGD-LNAfveenLANTKVMNAFDQQDNIFNefKKIT 247
Cdd:PLN03130 1052 STISLWAI-MPLLVLFYGAYLYYQSTAREVKrldsitrspVYAQFGEaLNG-----LSTIRAYKAYDRMAEING--RSMD 1123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 248 RGIKLTsfkadAIARSSEPWFGI----TSGIANLCVAVLAVSfyiykipvggIGGLGTNPDGTA-TSGLIvtfISLNWNF 322
Cdd:PLN03130 1124 NNIRFT-----LVNMSSNRWLAIrletLGGLMIWLTASFAVM----------QNGRAENQAAFAsTMGLL---LSYALNI 1185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 323 MGPFQNLLNINFSFQMGLASSSRVFKILNLDTKKPHVedITIDK------IDGLIEFKNVSFKYDINSKKYqLYNASFVA 396
Cdd:PLN03130 1186 TSLLTAVLRLASLAENSLNAVERVGTYIDLPSEAPLV--IENNRpppgwpSSGSIKFEDVVLRYRPELPPV-LHGLSFEI 1262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 397 KPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNLREHMSVVLQDTFMFNDTIENNIK-LGDKNAT 475
Cdd:PLN03130 1263 SPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDpFNEHNDA 1342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 476 K--EDVERAaNLSNAIhfiKTLPNGFQTQIENNGQNLSQGQRQLIAIARAVLANKSILILDEATSNIDSSTEEIIQASLL 553
Cdd:PLN03130 1343 DlwESLERA-HLKDVI---RRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIR 1418
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 502819783 554 KIMESKTSFVIAHRLSTIKTADLIIVVNNGEIIEIGTHKNLIQLDG 599
Cdd:PLN03130 1419 EEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEG 1464
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
371-590 |
1.16e-36 |
|
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: 136.69 E-value: 1.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 371 IEFKNVSFKYdiNSKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNLREHMS 450
Cdd:COG1122 1 IELENLSFSY--PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 451 VVLQ--DTFMFNDTIENNIKLGDKN------ATKEDVERAANLSNAIHFIKTLPngfqtqienngQNLSQGQRQLIAIAr 522
Cdd:COG1122 79 LVFQnpDDQLFAPTVEEDVAFGPENlglpreEIRERVEEALELVGLEHLADRPP-----------HELSGGQKQRVAIA- 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502819783 523 AVLANK-SILILDEATSNID-SSTEEIIQAsLLKIMESKTSFVIA-HRLSTI-KTADLIIVVNNGEIIEIGT 590
Cdd:COG1122 147 GVLAMEpEVLVLDEPTAGLDpRGRRELLEL-LKRLNKEGKTVIIVtHDLDLVaELADRVIVLDDGRIVADGT 217
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
372-584 |
1.67e-36 |
|
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: 135.67 E-value: 1.67e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 372 EFKNVSFKYDiNSKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNLREHMSV 451
Cdd:cd03225 1 ELKNLSFSYP-DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 452 VLQ--DTFMFNDTIENNIKLGDKNA------TKEDVERAANLSNAIHFIKTLPngfqtqienngQNLSQGQRQLIAIArA 523
Cdd:cd03225 80 VFQnpDDQFFGPTVEEEVAFGLENLglpeeeIEERVEEALELVGLEGLRDRSP-----------FTLSGGQKQRVAIA-G 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502819783 524 VLA-NKSILILDEATSNIDSSTEEIIQASLLKIMESKTSFVIA-HRLSTIKT-ADLIIVVNNGE 584
Cdd:cd03225 148 VLAmDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVtHDLDLLLElADRVIVLEDGK 211
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
82-584 |
1.23e-34 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 140.93 E-value: 1.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 82 VILGLVFIayGFFRYFDAYMYIKVSYQTSSRMRKEAMHKLIKmPISYYDKQ-KAGNLISTLINDINNVSNTMYNTINQFF 160
Cdd:PTZ00265 99 IIFSLVLI--GIFQFILSFISSFCMDVVTTKILKTLKLEFLK-SVFYQDGQfHDNNPGSKLTSDLDFYLEQVNAGIGTKF 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 161 SSIFNVLLSIIAMMFVASF----ITLIVVPLALFLFFISLIVIKKAQpyFVKVQNLFGDLN--AFVEENLANTKVMNAFD 234
Cdd:PTZ00265 176 ITIFTYASAFLGLYIWSLFknarLTLCITCVFPLIYICGVICNKKVK--INKKTSLLYNNNtmSIIEEALVGIRTVVSYC 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 235 QQDNIFNEFKKITRGIKLTSFKADAIARSSepwFGITSGianLCVAVLAVSF-YIYKIPVGGIGGLGTNPD---GTATSG 310
Cdd:PTZ00265 254 GEKTILKKFNLSEKLYSKYILKANFMESLH---IGMING---FILASYAFGFwYGTRIIISDLSNQQPNNDfhgGSVISI 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 311 LIVTFISLnwnFMGPFQnLLNINfSFQMGLASSSRVFKILNldtKKPHVED----ITIDKIDGlIEFKNVSFKYDiNSKK 386
Cdd:PTZ00265 328 LLGVLISM---FMLTII-LPNIT-EYMKSLEATNSLYEIIN---RKPLVENnddgKKLKDIKK-IQFKNVRFHYD-TRKD 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 387 YQLY-NASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKI-DGYELRNIKTNNLREHMSVVLQDTFMFNDTIE 464
Cdd:PTZ00265 398 VEIYkDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIK 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 465 NNIKLG----------------DKNATKEDVER--------AANLSNAIH------------------------------ 490
Cdd:PTZ00265 478 NNIKYSlyslkdlealsnyyneDGNDSQENKNKrnscrakcAGDLNDMSNttdsneliemrknyqtikdsevvdvskkvl 557
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 491 ---FIKTLPNGFQTQIENNGQNLSQGQRQLIAIARAVLANKSILILDEATSNIDSSTEEIIQASL--LKIMESKTSFVIA 565
Cdd:PTZ00265 558 ihdFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTInnLKGNENRITIIIA 637
|
570
....*....|....*....
gi 502819783 566 HRLSTIKTADLIIVVNNGE 584
Cdd:PTZ00265 638 HRLSTIRYANTIFVLSNRE 656
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
370-590 |
2.27e-34 |
|
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: 136.96 E-value: 2.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 370 LIEFKNVSFKYDINSKKYQ--LYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNLRE 447
Cdd:COG1123 260 LLEVRNLSKRYPVRGKGGVraVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 448 ---HMSVVLQDTF-MFN--DTIENNI-------KLGDKNATKEDVERAANLSNaihfiktLPNGFqtqIENNGQNLSQGQ 514
Cdd:COG1123 340 lrrRVQMVFQDPYsSLNprMTVGDIIaeplrlhGLLSRAERRERVAELLERVG-------LPPDL---ADRYPHELSGGQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 515 RQLIAIARAVLANKSILILDEATSNIDSSteeiIQASLLKIM-----ESKTSFV-IAHRLSTIKT-ADLIIVVNNGEIIE 587
Cdd:COG1123 410 RQRVAIARALALEPKLLILDEPTSALDVS----VQAQILNLLrdlqrELGLTYLfISHDLAVVRYiADRVAVMYDGRIVE 485
|
...
gi 502819783 588 IGT 590
Cdd:COG1123 486 DGP 488
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
371-584 |
4.00e-34 |
|
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: 128.74 E-value: 4.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 371 IEFKNVSFKYDINSK--KYQLYNASFVAKPGQTVAIVGPTGAGKTTIIN-LLGKFyDYNSGSIKIDGyelrniktnnlre 447
Cdd:cd03250 1 ISVEDASFTWDSGEQetSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSaLLGEL-EKLSGSVSVPG------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 448 HMSVVLQDTFMFNDTIENNIKLGDK-NATK-EDVERAANLSNAIhfiKTLPNGFQTQIENNGQNLSQGQRQLIAIARAVL 525
Cdd:cd03250 67 SIAYVSQEPWIQNGTIRENILFGKPfDEERyEKVIKACALEPDL---EILPDGDLTEIGEKGINLSGGQKQRISLARAVY 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502819783 526 ANKSILILDEATSNIDSSTEE-IIQASLLKI-MESKTSFVIAHRLSTIKTADLIIVVNNGE 584
Cdd:cd03250 144 SDADIYLLDDPLSAVDAHVGRhIFENCILGLlLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
31-346 |
6.89e-34 |
|
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: 130.63 E-value: 6.89e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 31 LYLGIFFSFCHSIFYVIGSFLIGYIFQQYFANYIASSsksdfnvksfsIWLVILGLVFIA--YGFFRYFDAYMYIKVSYQ 108
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRIIDSVIGGGLREL-----------LWLLALLILGVAllRGVFRYLQGYLAEKASQK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 109 TSSRMRKEAMHKLIKMPISYYDKQKAGNLISTLINDINNVSNTMYNTINQFFSSIFNVLLSIIAMMFVASFITLIVVPLA 188
Cdd:cd18542 70 VAYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAII 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 189 LFLFFISLIVIKKAQPYFVKVQNLFGDLNAFVEENLANTKVMNAFDQQDNIFNEFKKITRGIKLTSFKAdaiARSSEPWF 268
Cdd:cd18542 150 PFIALFSYVFFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKL---AKLLAKYW 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502819783 269 GITSGIANLCVAVLAVsfyiykipVGGIGGLgtnpDGTATSGLIVTFISLNWNFMGPFQNLLNINFSFQMGLASSSRV 346
Cdd:cd18542 227 PLMDFLSGLQIVLVLW--------VGGYLVI----NGEITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAERI 292
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
371-585 |
1.54e-32 |
|
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: 124.52 E-value: 1.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 371 IEFKNVSFKYDINSKKYQ-LYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNL---- 445
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQaLKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 446 REHMSVVLQDTFMFND-TIENNIKLG---DKNATKEDVERAANLSNAI---HFIKTLPNgfqtqienngqNLSQGQRQLI 518
Cdd:cd03255 81 RRHIGFVFQSFNLLPDlTALENVELPlllAGVPKKERRERAEELLERVglgDRLNHYPS-----------ELSGGQQQRV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502819783 519 AIARAVLANKSILILDEATSNIDSSTEEIIQASLLKIM-ESKTSFVIA-HRLSTIKTADLIIVVNNGEI 585
Cdd:cd03255 150 AIARALANDPKIILADEPTGNLDSETGKEVMELLRELNkEAGTTIVVVtHDPELAEYADRIIELRDGKI 218
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
391-538 |
2.54e-32 |
|
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: 121.60 E-value: 2.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 391 NASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNLREHMSVVLQDTFMFND-TIENNIKL 469
Cdd:pfam00005 3 NVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENLRL 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502819783 470 G------DKNATKEDVERAANLSNAIHFIKTLpngfqtqIENNGQNLSQGQRQLIAIARAVLANKSILILDEATS 538
Cdd:pfam00005 83 GlllkglSKREKDARAEEALEKLGLGDLADRP-------VGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
370-587 |
3.89e-32 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 124.00 E-value: 3.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 370 LIEFKNVSFKYDINSKKYQ-LYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNL--- 445
Cdd:COG1136 4 LLELRNLTKSYGTGEGEVTaLRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 446 -REHMSVVLQDTFMFND-TIENNIKLG---DKNATKEDVERAANLSNAI---HFIKTLPNgfqtqienngqNLSQGQRQL 517
Cdd:COG1136 84 rRRHIGFVFQFFNLLPElTALENVALPlllAGVSRKERRERARELLERVglgDRLDHRPS-----------QLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502819783 518 IAIARAVLANKSILILDEATSNIDSSTEEIIQASLLKIM-ESKTSFVIA-HRLSTIKTADLIIVVNNGEIIE 587
Cdd:COG1136 153 VAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNrELGTTIVMVtHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
372-584 |
5.96e-32 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 120.81 E-value: 5.96e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 372 EFKNVSFKYDinsKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNLREHMSV 451
Cdd:cd00267 1 EIENLSFRYG---GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 452 VLQdtfmfndtienniklgdknatkedveraanlsnaihfiktlpngfqtqienngqnLSQGQRQLIAIARAVLANKSIL 531
Cdd:cd00267 78 VPQ-------------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502819783 532 ILDEATSNIDSSTEEIIQASLLKIMESKTSFVIA-HRLSTIKTA-DLIIVVNNGE 584
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRELAEEGRTVIIVtHDPELAELAaDRVIVLKDGK 157
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
370-589 |
1.05e-31 |
|
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: 122.61 E-value: 1.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 370 LIEFKNVSFKYDINSKKYQ-LYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKT---NNL 445
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRrlrKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 446 REHMSVVLQDTF------MfndTIENNIK-----LGDKNATKEDVERAANLSNAIHFIKTLPNGFQTQienngqnLSQGQ 514
Cdd:cd03257 81 RKEIQMVFQDPMsslnprM---TIGEQIAeplriHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHE-------LSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 515 RQLIAIARAVLANKSILILDEATSNIDSSTeeiiQASLLKIM-----ESKTSFV-IAHRLSTIK-TADLIIVVNNGEIIE 587
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALDVSV----QAQILDLLkklqeELGLTLLfITHDLGVVAkIADRVAVMYAGKIVE 226
|
..
gi 502819783 588 IG 589
Cdd:cd03257 227 EG 228
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
22-568 |
1.50e-31 |
|
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: 131.19 E-value: 1.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 22 SYLKHDSKKLYLGIFFSFCHSIFY------VIGSFLIG-------YIFQQYFANYIASSSKSDF--NVKSFSIWLVILGL 86
Cdd:TIGR01271 855 TYLRYITTNRNLVFVLIFCLVIFLaevaasLLGLWLITdnpsapnYVDQQHANASSPDVQKPVIitPTSAYYIFYIYVGT 934
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 87 V--FIAYGFFRyfdAYMYIKVSYQTSSRMRKEAMHKLIKMPISYYDKQKAGNLISTLINDINNVSNTMYNTINQFFSSIF 164
Cdd:TIGR01271 935 AdsVLALGFFR---GLPLVHTLLTVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTL 1011
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 165 NVLLSIIAMMFVASFITLIVVPLALFlfFISLivikkaQPYFVKVQNLFGDLNAFVEE--------NLANTKVMNAFDQQ 236
Cdd:TIGR01271 1012 IVLGAIFVVSVLQPYIFIAAIPVAVI--FIML------RAYFLRTSQQLKQLESEARSpifshlitSLKGLWTIRAFGRQ 1083
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 237 DNIFNEFKKitrgikltsfkadAIARSSEPWFGITSGIANLCVAVLAVsFYIYKIPVGGIGgLGTNPDGTATSGLIVTfi 316
Cdd:TIGR01271 1084 SYFETLFHK-------------ALNLHTANWFLYLSTLRWFQMRIDII-FVFFFIAVTFIA-IGTNQDGEGEVGIILT-- 1146
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 317 sLNWNFMGPFQNLLNINFSFQMGLASSSRVFKILNLDTKKPH---------------VEDITIDKI---DGLIEFKNVSF 378
Cdd:TIGR01271 1147 -LAMNILSTLQWAVNSSIDVDGLMRSVSRVFKFIDLPQEEPRpsggggkyqlstvlvIENPHAQKCwpsGGQMDVQGLTA 1225
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 379 KYDINSKKYqLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDyNSGSIKIDGYELRNIKTNNLREHMSVVLQDTFM 458
Cdd:TIGR01271 1226 KYTEAGRAV-LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFI 1303
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 459 FNDTIENNIklgDKNATKEDVE--RAANLSNAIHFIKTLPNGFQTQIENNGQNLSQGQRQLIAIARAVLANKSILILDEA 536
Cdd:TIGR01271 1304 FSGTFRKNL---DPYEQWSDEEiwKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEP 1380
|
570 580 590
....*....|....*....|....*....|..
gi 502819783 537 TSNIDSSTEEIIQASLLKIMESKTSFVIAHRL 568
Cdd:TIGR01271 1381 SAHLDPVTLQIIRKTLKQSFSNCTVILSEHRV 1412
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
370-590 |
1.94e-31 |
|
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: 122.27 E-value: 1.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 370 LIEFKNVSFKYDinsKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRnIKTNNLREHM 449
Cdd:COG4555 1 MIEVENLSKKYG---KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVR-KEPREARRQI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 450 SVVLQDTFMF-NDTIENNIKL--------GDKNATK-EDVERAANLSNAIHFiKTlpngfqtqienngQNLSQGQRQLIA 519
Cdd:COG4555 77 GVLPDERGLYdRLTVRENIRYfaelyglfDEELKKRiEELIELLGLEEFLDR-RV-------------GELSTGMKKKVA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502819783 520 IARAVLANKSILILDEATSNIDSSTEEIIQASLLKIMESKTSFVIA-HRLSTI-KTADLIIVVNNGEIIEIGT 590
Cdd:COG4555 143 LARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSsHIMQEVeALCDRVVILHKGKVVAQGS 215
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
31-346 |
3.04e-31 |
|
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: 123.30 E-value: 3.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 31 LYLGIFFSFCHSIFYVIGSFLIGYIFQQYFANYiasssksdfnvKSFSIWLVILGLV--FIAYGFFRYFDAYMYIKVSYQ 108
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEK-----------DLEALLLVPLAIIglFLLRGLASYLQTYLMAYVGQR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 109 TSSRMRKEAMHKLIKMPISYYDKQKAGNLISTLINDINNVSNTMYNTINQFFSSIFNVLLSIIAMMFVA---SFITLIVV 185
Cdd:cd18552 70 VVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDwklTLIALVVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 186 PLAlflFFISLIVIKKAQPYFVKVQNLFGDLNAFVEENLANTKVMNAFDQQDNIFNEFKKITRGIKLTSFKadaIARSSE 265
Cdd:cd18552 150 PLA---ALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMK---IARARA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 266 pwfgITSGIANLcVAVLAVSFYIYkipVGGIGGLgtnpDGTATSGLIVTFISLNWNFMGPFQNLLNINFSFQMGLASSSR 345
Cdd:cd18552 224 ----LSSPLMEL-LGAIAIALVLW---YGGYQVI----SGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAER 291
|
.
gi 502819783 346 V 346
Cdd:cd18552 292 I 292
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
31-326 |
8.61e-31 |
|
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: 121.60 E-value: 8.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 31 LYLGIFFSFCHSIFYVIGSFLIGYIFQqyfaNYIASSSKSDFNVKSFSIWLVILGLVFIAYGFFRyfdAYMYIKVSYQTS 110
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILD----VLLPDGDPETQALNVYSLALLLLGLAQFILSFLQ---SYLLNHTGERLS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 111 SRMRKEAMHKLIKMPISYYDKQKAGNLISTLINDINNVSNTMYNTINQFFSSIFNVLLSIIAMMFVASFITLIVVPLALF 190
Cdd:pfam00664 74 RRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 191 LFFISLIVIKKAQPYFVKVQNLFGDLNAFVEENLANTKVMNAFDQQDNIFNEFKKITRGIKLTSFKADAIARSSepwFGI 270
Cdd:pfam00664 154 YILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLS---FGI 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 502819783 271 TSGIANLCVavlAVSFYIykipvggigGLGTNPDGTATSGLIVTFISLNWNFMGPF 326
Cdd:pfam00664 231 TQFIGYLSY---ALALWF---------GAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
371-596 |
1.31e-30 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 119.78 E-value: 1.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 371 IEFKNVSFKYDinsKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNiKTNNLREHMS 450
Cdd:COG1131 1 IEVRGLTKRYG---DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 451 VVLQDTFMFND-TIENNIKL------GDKNATKEDVERA---ANLSNAIH-FIKTlpngfqtqienngqnLSQGQRQLIA 519
Cdd:COG1131 77 YVPQEPALYPDlTVRENLRFfarlygLPRKEARERIDELlelFGLTDAADrKVGT---------------LSGGMKQRLG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 520 IARAVLANKSILILDEATSNID-SSTEEIIQAsLLKIMESKTSFVIA-HRLSTI-KTADLIIVVNNGEIIEIGTHKNLIQ 596
Cdd:COG1131 142 LALALLHDPELLILDEPTSGLDpEARRELWEL-LRELAAEGKTVLLStHYLEEAeRLCDRVAIIDKGRIVADGTPDELKA 220
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
371-587 |
3.79e-30 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 118.23 E-value: 3.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 371 IEFKNVSFKYDinSKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNN---LRE 447
Cdd:COG2884 2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipyLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 448 HMSVVLQDT-FMFNDTIENNIKLG------DKNATKEDVERAANLSNAIHFIKTLPNgfqtqienngqNLSQGQRQLIAI 520
Cdd:COG2884 80 RIGVVFQDFrLLPDRTVYENVALPlrvtgkSRKEIRRRVREVLDLVGLSDKAKALPH-----------ELSGGEQQRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 521 ARAVLANKSILILDEATSNIDSST-EEIIQAsLLKIMESKTSFVIA-HRLSTIKTADL-IIVVNNGEIIE 587
Cdd:COG2884 149 ARALVNRPELLLADEPTGNLDPETsWEIMEL-LEEINRRGTTVLIAtHDLELVDRMPKrVLELEDGRLVR 217
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
33-346 |
5.31e-30 |
|
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: 119.82 E-value: 5.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 33 LGIFFSFCHSIFYVIGSFLIGYIFqqyfaNYIASSSKSDFNVKSFSIWLVILGLVfiaYGFFRYFDAYMYIKVSYQTSSR 112
Cdd:cd18541 3 LGILFLILVDLLQLLIPRIIGRAI-----DALTAGTLTASQLLRYALLILLLALL---IGIFRFLWRYLIFGASRRIEYD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 113 MRKEAMHKLIKMPISYYDKQKAGNLISTLINDINNVSNTMYNTINQFFSSIFNVLLSIIAMMFVASFITLIVVPLALFLF 192
Cdd:cd18541 75 LRNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 193 FISLIVIKKAQPYFVKVQNLFGDLNAFVEENLANTKVMNAFDQQDNIFNEFKKITRGIKLTSFKadaIARSSEPWFGITS 272
Cdd:cd18541 155 LLVYRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLR---LARVDALFFPLIG 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502819783 273 GIANLCVAVLAvsfyiykipvgGIGGLGTNpDGTATSGLIVTFIS----LNWNFMGpFQNLLNInfsFQMGLASSSRV 346
Cdd:cd18541 232 LLIGLSFLIVL-----------WYGGRLVI-RGTITLGDLVAFNSylgmLIWPMMA-LGWVINL---IQRGAASLKRI 293
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
35-346 |
3.38e-29 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 117.57 E-value: 3.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 35 IFFSFCHSIFYVIGSFLIGYIFQQYFANYIASSsksdfNVKSFSIWLVILGLVFIAYGFFRYFDAYMYIKVSYQTSSRMR 114
Cdd:cd18545 2 LLLALLLMLLSTAASLAGPYLIKIAIDEYIPNG-----DLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 115 KEAMHKLIKMPISYYDKQKAGNLISTLINDINNVSNTMYNTINQFFSSIFNvLLSIIAMMFVASF----ITLIVVPlalF 190
Cdd:cd18545 77 QDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLT-LVGIVIIMFSLNVrlalVTLAVLP---L 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 191 LFFISLIVIKKAQPYFVKVQNLFGDLNAFVEENLANTKVMNAFDQQDNIFNEFKKITRGIKLTSFKADAIARSSEPWFGI 270
Cdd:cd18545 153 LVLVVFLLRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVEL 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502819783 271 TSGIANLCVavlavsfYIYkipvgGIGGLGtnpDGTATSGLIVTFISLNWNFMGPFQNLLNINFSFQMGLASSSRV 346
Cdd:cd18545 233 ISALGTALV-------YWY-----GGKLVL---GGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASAERI 293
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
370-595 |
4.07e-29 |
|
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: 115.37 E-value: 4.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 370 LIEFKNVSFKYDINSKKYQ-LYNASFVAKPGQTVAIVGPTGAGKTT---IINLLGKfydYNSGSIKIDGYE---LRNIKT 442
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTaLKDVSLSVPKGEIFGIIGRSGAGKSTlirCINGLER---PTSGSVLVDGTDltlLSGKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 443 NNLREHMSVVLQDTFMFND-TIENNIKLGDKNATKEDVERAANLSNAIHFIktlpnGFQTQIENNGQNLSQGQRQLIAIA 521
Cdd:cd03258 78 RKARRRIGMIFQHFNLLSSrTVFENVALPLEIAGVPKAEIEERVLELLELV-----GLEDKADAYPAQLSGGQKQRVGIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502819783 522 RAVLANKSILILDEATSNIDSSTEEIIQASLLKIMESK--TSFVIAHRLSTIKT-ADLIIVVNNGEIIEIGTHKNLI 595
Cdd:cd03258 153 RALANNPKVLLCDEATSALDPETTQSILALLRDINRELglTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVF 229
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
367-594 |
5.19e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 116.75 E-value: 5.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 367 IDGLIEFKNVSFKYDINSKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNLR 446
Cdd:PRK13650 1 MSNIIEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 447 EHMSVVLQ--DTFMFNDTIENNIKLGDKNA------TKEDVERAANLSNAIHFIKTLPngfqtqienngQNLSQGQRQLI 518
Cdd:PRK13650 81 HKIGMVFQnpDNQFVGATVEDDVAFGLENKgipheeMKERVNEALELVGMQDFKEREP-----------ARLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502819783 519 AIARAVLANKSILILDEATSNIDSSTE-EIIQaSLLKIMESK--TSFVIAHRLSTIKTADLIIVVNNGEIIEIGTHKNL 594
Cdd:PRK13650 150 AIAGAVAMRPKIIILDEATSMLDPEGRlELIK-TIKGIRDDYqmTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
371-589 |
1.74e-28 |
|
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: 113.43 E-value: 1.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 371 IEFKNVSFKYDinsKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYN-----SGSIKIDGYELRNIKTN-- 443
Cdd:cd03260 1 IELRDLNVYYG---DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdEGEVLLDGKDIYDLDVDvl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 444 NLREHMSVVLQDTFMFNDTIENNIKLG-------DKNATKEDVERAanLSNAihfikTLPNGFQTQIenNGQNLSQGQRQ 516
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGlrlhgikLKEELDERVEEA--LRKA-----ALWDEVKDRL--HALGLSGGQQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502819783 517 LIAIARAvLANK-SILILDEATSNIDSSTEEIIQASLLKIMESKTSFVIAHRLSTIK-TADLIIVVNNGEIIEIG 589
Cdd:cd03260 149 RLCLARA-LANEpEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAArVADRTAFLLNGRLVEFG 222
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
369-595 |
5.82e-28 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 120.27 E-value: 5.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 369 GLIEFKNVSFKYDiNSKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNLREH 448
Cdd:PTZ00243 1307 GSLVFEGVQMRYR-EGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQ 1385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 449 MSVVLQDTFMFNDTIENNIklgDK--NATKEDVERAANLSNAIHFIKTLPNGFQTQIENNGQNLSQGQRQLIAIARAVLA 526
Cdd:PTZ00243 1386 FSMIPQDPVLFDGTVRQNV---DPflEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLK 1462
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 527 NKSILIL-DEATSNIDSSTEEIIQASLLKIMESKTSFVIAHRLSTIKTADLIIVVNNGEIIEIGTHKNLI 595
Cdd:PTZ00243 1463 KGSGFILmDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELV 1532
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
370-598 |
9.74e-28 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 112.80 E-value: 9.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 370 LIEFKNVSFKYDiNSKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNLREHM 449
Cdd:PRK13635 5 IIRVEHISFRYP-DAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 450 SVVLQ--DTFMFNDTIENNIKLGDKN---ATKEDVER---AANLSNAIHFIKTLPNgfqtqienngqNLSQGQRQLIAIA 521
Cdd:PRK13635 84 GMVFQnpDNQFVGATVQDDVAFGLENigvPREEMVERvdqALRQVGMEDFLNREPH-----------RLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502819783 522 RAVLANKSILILDEATSNID-SSTEEIIQA-SLLKIMESKTSFVIAHRLSTIKTADLIIVVNNGEIIEIGTHKNLIQLD 598
Cdd:PRK13635 153 GVLALQPDIIILDEATSMLDpRGRREVLETvRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSG 231
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
371-584 |
1.02e-27 |
|
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: 109.97 E-value: 1.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 371 IEFKNVSFKYdinSKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELR--NIKTNNLREH 448
Cdd:cd03229 1 LELKNVSKRY---GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTdlEDELPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 449 MSVVLQD-TFMFNDTIENNIKLGdknatkedveraanlsnaihfiktlpngfqtqienngqnLSQGQRQLIAIARAVLAN 527
Cdd:cd03229 78 IGMVFQDfALFPHLTVLENIALG---------------------------------------LSGGQQQRVALARALAMD 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 528 KSILILDEATSNIDSSTEEIIQASLLKIMES--KTSFVIAHRLSTIKT-ADLIIVVNNGE 584
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
33-346 |
7.04e-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: 350051 [Multi-domain] Cd Length: 293 Bit Score: 110.70 E-value: 7.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 33 LGIFFSFCHSIFYVIGSFLIGYIFQQyfanyIASSSKSdfnvKSFSIWLVILGL-VFIAYGFFRYFDAYMYIKVSYQTSS 111
Cdd:cd18778 3 LTLLCALLSTLLGLVPPWLIRELVDL-----VTIGSKS----LGLLLGLALLLLgAYLLRALLNFLRIYLNHVAEQKVVA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 112 RMRKEAMHKLIKMPISYYDKQKAGNLISTLINDINNVSNTMYNTINQFFSSIFnVLLSIIAMMFVAS----FITLIVVPl 187
Cdd:cd18778 74 DLRSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVL-TLVGVAIILFSINpklaLLTLIPIP- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 188 alFLFFISLIVIKKAQPYFVKVQNLFGDLNAFVEENLANTKVMNAFDQQDNIFNEFKKITRGIKLTSFKADAIARSSEPW 267
Cdd:cd18778 152 --FLALGAWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPL 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502819783 268 FGITSGIANlcVAVLAvsfyiykipVGGIGGLgtnpDGTATSGLIVTFISLNWNFMGPFQNLLNINFSFQMGLASSSRV 346
Cdd:cd18778 230 MEFLTSLGT--VLVLG---------FGGRLVL----AGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGAERV 293
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
371-588 |
2.51e-26 |
|
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: 107.17 E-value: 2.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 371 IEFKNVSFKYDINSKKYQ-LYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELrniktNNLREHM 449
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTaLEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPV-----TGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 450 SVVLQDTFMFN-DTIENNIKLGDK---NATKEDVERAANLSNAI---HFIKTLPngfqtqienngQNLSQGQRQLIAIAR 522
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLElqgVPKAEARERAEELLELVglsGFENAYP-----------HQLSGGMRQRVALAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502819783 523 AVLANKSILILDEATSNIDSSTEEIIQASLLKIMES--KTSFVIAHRLS-TIKTADLIIVVNN--GEIIEI 588
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIWREtgKTVLLVTHDIDeAVFLADRVVVLSArpGRIVAE 215
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
382-595 |
2.75e-26 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 107.42 E-value: 2.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 382 INSKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNnlREHMSVVLQDTFMF-N 460
Cdd:cd03299 8 KDWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 461 DTIENNIKLGDKNATKEDVERAANLSNAIHFIktlpnGFQTQIENNGQNLSQGQRQLIAIARAVLANKSILILDEATSNI 540
Cdd:cd03299 86 MTVYKNIAYGLKKRKVDKKEIERKVLEIAEML-----GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSAL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502819783 541 DSSTEEIIQASLLKIM-ESKTSFV-IAHRLSTIKT-ADLIIVVNNGEIIEIGTHKNLI 595
Cdd:cd03299 161 DVRTKEKLREELKKIRkEFGVTVLhVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVF 218
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
371-590 |
4.20e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 108.15 E-value: 4.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 371 IEFKNVSFKYDiNSKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNLREHMS 450
Cdd:PRK13632 8 IKVENVSFSYP-NSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 451 VVLQ--DTFMFNDTIENNIKLG------DKNATKEDVERAANLSNAIHFIKTLPngfqtqienngQNLSQGQRQLIAIAr 522
Cdd:PRK13632 87 IIFQnpDNQFIGATVEDDIAFGlenkkvPPKKMKDIIDDLAKKVGMEDYLDKEP-----------QNLSGGQKQRVAIA- 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502819783 523 AVLA-NKSILILDEATSNIDSSTEEIIQASLLKIME--SKTSFVIAHRLSTIKTADLIIVVNNGEIIEIGT 590
Cdd:PRK13632 155 SVLAlNPEIIIFDESTSMLDPKGKREIKKIMVDLRKtrKKTLISITHDMDEAILADKVIVFSEGKLIAQGK 225
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
370-590 |
5.18e-26 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 111.92 E-value: 5.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 370 LIEFKNVSFKYDiNSKKYQLYNASFVAKPGQTVAIVGPTGAGKTT----IINLLGKFYDYnSGSIKIDGYELRNIKTNNL 445
Cdd:COG1123 4 LLEVRDLSVRYP-GGDVPAVDGVSLTIAPGETVALVGESGSGKSTlalaLMGLLPHGGRI-SGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 446 REHMSVVLQD--TFMFNDTIENNIKLG------DKNATKEDVERAANLSNAIHFIKTLPngfqtqienngQNLSQGQRQL 517
Cdd:COG1123 82 GRRIGMVFQDpmTQLNPVTVGDQIAEAlenlglSRAEARARVLELLEAVGLERRLDRYP-----------HQLSGGQRQR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502819783 518 IAIARAVLANKSILILDEATSNIDSSTEEIIQASL--LKIMESKTSFVIAHRLSTI-KTADLIIVVNNGEIIEIGT 590
Cdd:COG1123 151 VAIAMALALDPDLLIADEPTTALDVTTQAEILDLLreLQRERGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGP 226
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
371-589 |
6.18e-26 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 105.68 E-value: 6.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 371 IEFKNVSFKYDinsKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNnlREHMS 450
Cdd:cd03259 1 LELKGLSKTYG---SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 451 VVLQDTFMF-NDTIENNIKLGDKNATKEDVERAANLSNAI------HFIKTLPNGfqtqienngqnLSQGQRQLIAIARA 523
Cdd:cd03259 76 MVFQDYALFpHLTVAENIAFGLKLRGVPKAEIRARVRELLelvgleGLLNRYPHE-----------LSGGQQQRVALARA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502819783 524 VLANKSILILDEATSNIDSSTEEIIQASLLKIMES--KTSFVIAHRLS-TIKTADLIIVVNNGEIIEIG 589
Cdd:cd03259 145 LAREPSLLLLDEPLSALDAKLREELREELKELQRElgITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
370-590 |
9.65e-26 |
|
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: 106.43 E-value: 9.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 370 LIEFKNVSFKYDINSKKYQ-LYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNLREH 448
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPvLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 449 MSVVLQDT-------FMFNDTIENNIKLGDKNATKEDVERAANLSNaihfiktLPNGFQTQIennGQNLSQGQRQLIAIA 521
Cdd:COG1124 81 VQMVFQDPyaslhprHTVDRILAEPLRIHGLPDREERIAELLEQVG-------LPPSFLDRY---PHQLSGGQRQRVAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502819783 522 RAVLANKSILILDEATSNIDSSTE-EIIQasLLKIM--ESKTSFV-IAHRLSTIKT-ADLIIVVNNGEIIEIGT 590
Cdd:COG1124 151 RALILEPELLLLDEPTSALDVSVQaEILN--LLKDLreERGLTYLfVSHDLAVVAHlCDRVAVMQNGRIVEELT 222
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
371-585 |
1.28e-25 |
|
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: 103.63 E-value: 1.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 371 IEFKNVSFKYDinsKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNiKTNNLREHMS 450
Cdd:cd03230 1 IEVRNLSKRYG---KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 451 VVLQDTFMFND-TIENNIKlgdknatkedveraanlsnaihfiktlpngfqtqienngqnLSQGQRQLIAIARAVLANKS 529
Cdd:cd03230 77 YLPEEPSLYENlTVRENLK-----------------------------------------LSGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502819783 530 ILILDEATSNIDSSTEEIIQASLLKIM-ESKTSFVIAHRLSTI-KTADLIIVVNNGEI 585
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELKkEGKTILLSSHILEEAeRLCDRVAILNNGRI 173
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
374-586 |
1.79e-25 |
|
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: 104.26 E-value: 1.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 374 KNVSFKYdiNSKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGyelRNIKTNNLREHMSVVL 453
Cdd:cd03226 3 ENISFSY--KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 454 QDT--FMFNDTIENNIKLGDKNATkEDVERAANLsnaihfIKTL-PNGFQtqiENNGQNLSQGQRQLIAIARAVLANKSI 530
Cdd:cd03226 78 QDVdyQLFTDSVREELLLGLKELD-AGNEQAETV------LKDLdLYALK---ERHPLSLSGGQKQRLAIAAALLSGKDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502819783 531 LILDEATSNIDSSTEEIIQASLLKIM-ESKTSFVIAHRLSTI-KTADLIIVVNNGEII 586
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGELIRELAaQGKAVIVITHDYEFLaKVCDRVLLLANGAIV 205
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
371-595 |
1.83e-25 |
|
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: 105.46 E-value: 1.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 371 IEFKNVSFKYdiNSKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNLREHMS 450
Cdd:cd03295 1 IEFENVTKRY--GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 451 VVLQDTFMF-NDTIENNIKL-----GDKNATKEdvERAANLsnaIHFIKTLPNGFQtqiENNGQNLSQGQRQLIAIARAV 524
Cdd:cd03295 79 YVIQQIGLFpHMTVEENIALvpkllKWPKEKIR--ERADEL---LALVGLDPAEFA---DRYPHELSGGQQQRVGVARAL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502819783 525 LANKSILILDEATSNIDSSTEEIIQASLLKIMES--KTSFVIAHRL-STIKTADLIIVVNNGEIIEIGTHKNLI 595
Cdd:cd03295 151 AADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElgKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
371-590 |
3.21e-25 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 104.51 E-value: 3.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 371 IEFKNVSFKYDinsKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDG---YELRNIKTNNLRE 447
Cdd:cd03261 1 IELRGLTKSFG---GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGediSGLSEAELYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 448 HMSVVLQDTFMFND-TIENNIKLGDKNATKEDVER----------AANLSNAIHFiktLPNgfqtqienngqNLSQGQRQ 516
Cdd:cd03261 78 RMGMLFQSGALFDSlTVFENVAFPLREHTRLSEEEireivlekleAVGLRGAEDL---YPA-----------ELSGGMKK 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502819783 517 LIAIARAVLANKSILILDEATSNIDSSTEEIIQASLLKIMESK--TSFVIAHRLSTI-KTADLIIVVNNGEIIEIGT 590
Cdd:cd03261 144 RVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELglTSIMVTHDLDTAfAIADRIAVLYDGKIVAEGT 220
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
371-586 |
7.36e-25 |
|
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: 102.24 E-value: 7.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 371 IEFKNVSFKYDINSKKYQ---LYNASFVAKPGQTVAIVGPTGAGKTTIINLL-GKFYDYN-SGSIKIDGyelRNIKTNNL 445
Cdd:cd03213 4 LSFRNLTVTVKSSPSKSGkqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALaGRRTGLGvSGEVLING---RPLDKRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 446 REHMSVVLQ-DTFMFNDTIEnniklgdknatkEDVERAANLsnaihfiktlpngfqtqienngQNLSQGQRQLIAIARAV 524
Cdd:cd03213 81 RKIIGYVPQdDILHPTLTVR------------ETLMFAAKL----------------------RGLSGGERKRVSIALEL 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502819783 525 LANKSILILDEATSNIDSSTEEIIqASLLKIM--ESKTSFVIAHRLST--IKTADLIIVVNNGEII 586
Cdd:cd03213 127 VSNPSLLFLDEPTSGLDSSSALQV-MSLLRRLadTGRTIICSIHQPSSeiFELFDKLLLLSQGRVI 191
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
371-586 |
3.12e-24 |
|
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: 101.88 E-value: 3.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 371 IEFKNVSFKYdiNSKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNLRE--- 447
Cdd:cd03256 1 IEVENLSKTY--PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQlrr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 448 HMSVVLQDtfmFN-----DTIEN--NIKLGDKNA--------TKEDVERAANLSNAIhfiktlpnGFQTQIENNGQNLSQ 512
Cdd:cd03256 79 QIGMIFQQ---FNlierlSVLENvlSGRLGRRSTwrslfglfPKEEKQRALAALERV--------GLLDKAYQRADQLSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502819783 513 GQRQLIAIARAVLANKSILILDEATSNIDSSTEEIIQASLLKIMESKTSFVIA--HRLSTIKT-ADLIIVVNNGEII 586
Cdd:cd03256 148 GQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVslHQVDLAREyADRIVGLKDGRIV 224
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
369-585 |
3.36e-24 |
|
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: 102.63 E-value: 3.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 369 GLIEFKNVSFKYdINSKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYdYNSGSIKIDGYELRNIKTNNLREH 448
Cdd:cd03289 1 GQMTVKDLTAKY-TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL-NTEGDIQIDGVSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 449 MSVVLQDTFMFNDTIENNIklgDKNATKEDVE--RAANLSNAIHFIKTLPNGFQTQIENNGQNLSQGQRQLIAIARAVLA 526
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKNL---DPYGKWSDEEiwKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502819783 527 NKSILILDEATSNIDSSTEEIIQASLLKIMESKTSFVIAHRLSTIKTADLIIVVNNGEI 585
Cdd:cd03289 156 KAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKV 214
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
371-604 |
1.75e-23 |
|
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: 106.18 E-value: 1.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 371 IEFKNVSFKYdINSKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGyelrniktnnlreHMS 450
Cdd:TIGR00957 637 ITVHNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-------------SVA 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 451 VVLQDTFMFNDTIENNIKLG---DKNATKEDVERAANLSNaihfIKTLPNGFQTQIENNGQNLSQGQRQLIAIARAVLAN 527
Cdd:TIGR00957 703 YVPQQAWIQNDSLRENILFGkalNEKYYQQVLEACALLPD----LEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSN 778
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 528 KSILILDEATSNIDSSTEEIIQASLL---KIMESKTSFVIAHRLSTIKTADLIIVVNNGEIIEIGTHKNLIQLDGFYSNL 604
Cdd:TIGR00957 779 ADIYLFDDPLSAVDAHVGKHIFEHVIgpeGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEF 858
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
370-590 |
3.27e-23 |
|
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: 98.96 E-value: 3.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 370 LIEFKNVSFKYDinsKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNLREHM 449
Cdd:COG1120 1 MLEAENLSVGYG---GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 450 SVVLQDTFM-FNDTIENNIKLG-------DKNATKEDVERAANlsnAIHfiktlpngfQTQIEN----NGQNLSQGQRQL 517
Cdd:COG1120 78 AYVPQEPPApFGLTVRELVALGryphlglFGRPSAEDREAVEE---ALE---------RTGLEHladrPVDELSGGERQR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 518 IAIARAVLANKSILILDEATSNIDssteeiI--QASLLKIM------ESKTSFVIAHRLS-TIKTADLIIVVNNGEIIEI 588
Cdd:COG1120 146 VLIARALAQEPPLLLLDEPTSHLD------LahQLEVLELLrrlareRGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQ 219
|
..
gi 502819783 589 GT 590
Cdd:COG1120 220 GP 221
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
371-585 |
4.18e-23 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 97.86 E-value: 4.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 371 IEFKNVSFKYDINSKKyqLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNN---LRE 447
Cdd:cd03292 1 IEFINVTKTYPNGTAA--LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipyLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 448 HMSVVLQDT-FMFNDTIENNIKL-------GDKNATKEdVERAANLSNAIHFIKTLPNGfqtqienngqnLSQGQRQLIA 519
Cdd:cd03292 79 KIGVVFQDFrLLPDRNVYENVAFalevtgvPPREIRKR-VPAALELVGLSHKHRALPAE-----------LSGGEQQRVA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502819783 520 IARAVLANKSILILDEATSNIDSSTEEIIQASLLKIMESKTSFVIAHRLSTI--KTADLIIVVNNGEI 585
Cdd:cd03292 147 IARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELvdTTRHRVIALERGKL 214
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
371-590 |
4.37e-23 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 98.29 E-value: 4.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 371 IEFKNVSFKYDinskkYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYEL-------RNIKT- 442
Cdd:COG3840 2 LRLDDLTYRYG-----DFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLtalppaeRPVSMl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 443 ---NNLREHMSVvlqdtfmfndtiENNIKLG---DKNATKED---VERAANLSNAIHFIKTLPngfqtqiennGQnLSQG 513
Cdd:COG3840 77 fqeNNLFPHLTV------------AQNIGLGlrpGLKLTAEQraqVEQALERVGLAGLLDRLP----------GQ-LSGG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 514 QRQLIAIARAVLANKSILILDEATSNIDSS-TEEIIQasLLKIMESK---TSFVIAHRLSTIKT-ADLIIVVNNGEIIEI 588
Cdd:COG3840 134 QRQRVALARCLVRKRPILLLDEPFSALDPAlRQEMLD--LVDELCRErglTVLMVTHDPEDAARiADRVLLVADGRIAAD 211
|
..
gi 502819783 589 GT 590
Cdd:COG3840 212 GP 213
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
368-590 |
6.82e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 99.10 E-value: 6.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 368 DGLIEFKNVSFKYDiNSKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFY---DYNSGSIKIDGYELRNIKTNN 444
Cdd:PRK13640 3 DNIVEFKHVSFTYP-DSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 445 LREHMSVVLQ--DTFMFNDTIENNIKLGDKN------ATKEDVERAANLSNAIHFIKTLPngfqtqienngQNLSQGQRQ 516
Cdd:PRK13640 82 IREKVGIVFQnpDNQFVGATVGDDVAFGLENravprpEMIKIVRDVLADVGMLDYIDSEP-----------ANLSGGQKQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502819783 517 LIAIARAVLANKSILILDEATSNIDSSTEEIIQASLLKIMESK--TSFVIAHRLSTIKTADLIIVVNNGEIIEIGT 590
Cdd:PRK13640 151 RVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGS 226
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
80-346 |
7.03e-23 |
|
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: 99.04 E-value: 7.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 80 WLVILGLVFIAYGFFRYFDAYMYIKVSYQTSSRMRKEAMHKLIKMPISYYDKQKAGNLISTLINDINNVSNTMYNTINQF 159
Cdd:cd18551 38 LLALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 160 FSSIFNVLLSIIAMMF---VASFITLIVVPLAlflFFISLIVIKKAQPYFVKVQNLFGDLNAFVEENLANTKVMNAFDQQ 236
Cdd:cd18551 118 VTGVLTVVGAVVLMFLldwVLTLVTLAVVPLA---FLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAE 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 237 DNIFNEFKKITRGIKLTSFKAdaiARssepWFGITSGIANLCV-AVLAVSFyiykipvgGIGGLGTNpDGTATSGLIVTF 315
Cdd:cd18551 195 ERETKRGGEAAERLYRAGLKA---AK----IEALIGPLMGLAVqLALLVVL--------GVGGARVA-SGALTVGTLVAF 258
|
250 260 270
....*....|....*....|....*....|.
gi 502819783 316 ISLNWNFMGPFQNLLNINFSFQMGLASSSRV 346
Cdd:cd18551 259 LLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
371-595 |
8.88e-23 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 103.66 E-value: 8.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 371 IEFKNVSFKYDINSKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIIN-LLGKFYDYNSGSIKIDGyelrniktnnlreHM 449
Cdd:PLN03130 615 ISIKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRG-------------TV 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 450 SVVLQDTFMFNDTIENNIKLG-DKNATKedVERAANLSNAIHFIKTLPNGFQTQIENNGQNLSQGQRQLIAIARAVLANK 528
Cdd:PLN03130 682 AYVPQVSWIFNATVRDNILFGsPFDPER--YERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNS 759
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502819783 529 SILILDEATSNIDSST-EEIIQASLLKIMESKTSFVIAHRLSTIKTADLIIVVNNGEIIEIGTHKNLI 595
Cdd:PLN03130 760 DVYIFDDPLSALDAHVgRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELS 827
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
43-346 |
1.36e-22 |
|
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: 98.35 E-value: 1.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 43 IFYVIGSF--LIGYIFQQYFANYIASSSKSDFNVKSFSIWLVILGLVFIAYGFFRYFDAYMYIKVSYQTSSRMRKEAMHK 120
Cdd:cd18563 6 LLMLLGTAlgLVPPYLTKILIDDVLIQLGPGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLRRDLYEH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 121 LIKMPISYYDKQKAGNLISTLINDINNVSNTMYNTINQFFSSIFNvLLSIIAMMFVASF----ITLIVVPlalFLFFISL 196
Cdd:cd18563 86 LQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILM-IIGIGVVLFSLNWklalLVLIPVP---LVVWGSY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 197 IVIKKAQPYFVKVQNLFGDLNAFVEENLANTKVMNAFDQQDNIFNEFKKITRGIKLTSFKADAIARSSEPWFGITSGIAN 276
Cdd:cd18563 162 FFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFLTSLGT 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 277 LCVAVlavsfyiykipVGGIGGLGtnpdGTATSGLIVTFISLNWNFMGPFQNLLNINFSFQMGLASSSRV 346
Cdd:cd18563 242 LIVWY-----------FGGRQVLS----GTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
371-590 |
4.30e-22 |
|
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: 95.38 E-value: 4.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 371 IEFKNVSFKYDinsKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNnlREHMS 450
Cdd:cd03300 1 IELENVSKFYG---GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 451 VVLQDTFMFND-TIENNIKLG------DKNATKEDVERAANLSNAIHFIKTLPNgfqtqienngqNLSQGQRQLIAIARA 523
Cdd:cd03300 76 TVFQNYALFPHlTVFENIAFGlrlkklPKAEIKERVAEALDLVQLEGYANRKPS-----------QLSGGQQQRVAIARA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 524 VLANKSILILDEATSNIDSSTEEIIQASLLKIMES-KTSFV-IAHRLSTIKT-ADLIIVVNNGEIIEIGT 590
Cdd:cd03300 145 LVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKElGITFVfVTHDQEEALTmSDRIAVMNKGKIQQIGT 214
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
372-589 |
4.78e-22 |
|
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: 93.65 E-value: 4.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 372 EFKNVSFKYDinsKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNLREHMSV 451
Cdd:cd03214 1 EVENLSVGYG---GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 452 VLQdtfmfndtienniklgdknatkedverAANLSNAIHFIKtlpNGFQTqienngqnLSQGQRQLIAIARAVLANKSIL 531
Cdd:cd03214 78 VPQ---------------------------ALELLGLAHLAD---RPFNE--------LSGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502819783 532 ILDEATSNID----SSTEEIIQAslLKIMESKTSFVIAHRLS-TIKTADLIIVVNNGEIIEIG 589
Cdd:cd03214 120 LLDEPTSHLDiahqIELLELLRR--LARERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
371-585 |
5.58e-22 |
|
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: 94.52 E-value: 5.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 371 IEFKNVSFKYdinSKKYQLYNASFVAKPGQTVAIVGPTGAGKTTI---INLLGKfydYNSGSIKIDGYELRNIKTN--NL 445
Cdd:cd03262 1 IEIKNLHKSF---GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLlrcINLLEE---PDSGTIIIDGLKLTDDKKNinEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 446 REHMSVVLQDTFMF-NDTIENNIKLGDKNATKEDVERAANLsnAIHFIKTLpnGFQTQIENNGQNLSQGQRQLIAIARAV 524
Cdd:cd03262 75 RQKVGMVFQQFNLFpHLTVLENITLAPIKVKGMSKAEAEER--ALELLEKV--GLADKADAYPAQLSGGQQQRVAIARAL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502819783 525 LANKSILILDEATSNIDSsteEIIQaSLLKIM-----ESKTSFVIAHRLSTI-KTADLIIVVNNGEI 585
Cdd:cd03262 151 AMNPKVMLFDEPTSALDP---ELVG-EVLDVMkdlaeEGMTMVVVTHEMGFArEVADRVIFMDDGRI 213
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
367-587 |
6.95e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 95.93 E-value: 6.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 367 IDGLIEFKNVSFKYDINSKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNLR 446
Cdd:PRK13642 1 MNKILEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 447 EHMSVVLQ--DTFMFNDTIENNIKLGDKNATKEDVERAANLSNAIHFIKTLpnGFQTQienNGQNLSQGQRQLIAIARAV 524
Cdd:PRK13642 81 RKIGMVFQnpDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNML--DFKTR---EPARLSGGQKQRVAVAGII 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502819783 525 LANKSILILDEATSNIDSSTEEIIQASLLKIMESK--TSFVIAHRLSTIKTADLIIVVNNGEIIE 587
Cdd:PRK13642 156 ALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIK 220
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
370-590 |
8.51e-22 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 94.66 E-value: 8.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 370 LIEFKNVSFKYDinsKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKT---NNLR 446
Cdd:COG1127 5 MIEVRNLTKSFG---DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEkelYELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 447 EHMSVVLQDTFMFND-TIENNIKLG---DKNATKEDVERAA-------NLSNAIHFiktLPNgfqtqiEnngqnLSQGQR 515
Cdd:COG1127 82 RRIGMLFQGGALFDSlTVFENVAFPlreHTDLSEAEIRELVleklelvGLPGAADK---MPS------E-----LSGGMR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 516 QLIAIARAVLANKSILILDEATSNID--SSTEeiIQASLLKIMESK--TSFVIAHRLSTIKT-ADLIIVVNNGEIIEIGT 590
Cdd:COG1127 148 KRVALARALALDPEILLYDEPTAGLDpiTSAV--IDELIRELRDELglTSVVVTHDLDSAFAiADRVAVLADGKIIAEGT 225
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
370-590 |
8.82e-22 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 97.09 E-value: 8.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 370 LIEFKNVSFKYDinsKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNnlREHM 449
Cdd:COG3842 5 ALELENVSKRYG---DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE--KRNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 450 SVVLQD----TFMfndTIENNIKLG------DKNATKEDVERAANLSNAIHFIKTLPNgfqtqienngqNLSQGQRQLIA 519
Cdd:COG3842 80 GMVFQDyalfPHL---TVAENVAFGlrmrgvPKAEIRARVAELLELVGLEGLADRYPH-----------QLSGGQQQRVA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502819783 520 IARAvLANK-SILILDEATSNIDSSTEEIIQASLLKIM-ESKTSFVIA-HRLS---TIktADLIIVVNNGEIIEIGT 590
Cdd:COG3842 146 LARA-LAPEpRVLLLDEPLSALDAKLREEMREELRRLQrELGITFIYVtHDQEealAL--ADRIAVMNDGRIEQVGT 219
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
44-594 |
9.44e-22 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 100.44 E-value: 9.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 44 FYVIGSFLIGYIFQQY-----FANYIASSSKSDFN-VKSFSIWLVILGLVFIAYGFFRYFDAYMyiKVSYQTSSRMRKEA 117
Cdd:PLN03232 303 FWLGGIFKIGHDLSQFvgpviLSHLLQSMQEGDPAwVGYVYAFLIFFGVTFGVLCESQYFQNVG--RVGFRLRSTLVAAI 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 118 MHKLIKMP---ISYYDKQKAGNLISTLINDINNVSNTMYNtinqFFSSIFNVLLSII--------AMMFvASFITLIVVP 186
Cdd:PLN03232 381 FHKSLRLTheaRKNFASGKVTNMITTDANALQQIAEQLHG----LWSAPFRIIVSMVllyqqlgvASLF-GSLILFLLIP 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 187 LALFLFFISLIVIKKAQPYFVKVQNLfgdlnafVEENLANTKVMNAFDQQDNIFNEFKKItRGIKLTSFkadaiaRSSEP 266
Cdd:PLN03232 456 LQTLIVRKMRKLTKEGLQWTDKRVGI-------INEILASMDTVKCYAWEKSFESRIQGI-RNEELSWF------RKAQL 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 267 WFGITSGIAN-LCVAVLAVSFYIYKIpvggiggLGtnpdGTATSGLIVTFISLNWNFMGPFQ---NLL----NINFSFQm 338
Cdd:PLN03232 522 LSAFNSFILNsIPVVVTLVSFGVFVL-------LG----GDLTPARAFTSLSLFAVLRSPLNmlpNLLsqvvNANVSLQ- 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 339 glasssRVFKILnLDTKKPHVEDITIDKIDGLIEFKNVSFKYDINSKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIIN- 417
Cdd:PLN03232 590 ------RIEELL-LSEERILAQNPPLQPGAPAISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISa 662
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 418 LLGKFYDYNSGSIKIDGyelrniktnnlreHMSVVLQDTFMFNDTIENNIKLGDKNATkEDVERAANLSNAIHFIKTLPN 497
Cdd:PLN03232 663 MLGELSHAETSSVVIRG-------------SVAYVPQVSWIFNATVRENILFGSDFES-ERYWRAIDVTALQHDLDLLPG 728
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 498 GFQTQIENNGQNLSQGQRQLIAIARAVLANKSILILDEATSNIDSSTEEIIQASLLKI-MESKTSFVIAHRLSTIKTADL 576
Cdd:PLN03232 729 RDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDeLKGKTRVLVTNQLHFLPLMDR 808
|
570
....*....|....*...
gi 502819783 577 IIVVNNGEIIEIGTHKNL 594
Cdd:PLN03232 809 IILVSEGMIKEEGTFAEL 826
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
370-590 |
1.06e-21 |
|
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: 96.28 E-value: 1.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 370 LIEFKNVSFKYDINSKKYQ-LYNASFVAKPGQTVAIVGPTGAGKTT----IINLLgKFYDYNSGSIKIDGYELRNIKTNN 444
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKaVDGVSFDVRRGETLGLVGESGSGKSTlaraILGLL-PPPGITSGEILFDGEDLLKLSEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 445 LRE----HMSVVLQDTFM-FN----------DTIENNIKLGDKNATKEDVE--RAANLSNAIHFIKTLPngFQtqienng 507
Cdd:COG0444 80 LRKirgrEIQMIFQDPMTsLNpvmtvgdqiaEPLRIHGGLSKAEARERAIEllERVGLPDPERRLDRYP--HE------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 508 qnLSQGQRQLIAIARAVLANKSILILDEATSNIDSSteeiIQASLLKIM-----ESKTSFV-IAHRLSTIK-TADLIIVV 580
Cdd:COG0444 151 --LSGGMRQRVMIARALALEPKLLIADEPTTALDVT----IQAQILNLLkdlqrELGLAILfITHDLGVVAeIADRVAVM 224
|
250
....*....|
gi 502819783 581 NNGEIIEIGT 590
Cdd:COG0444 225 YAGRIVEEGP 234
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
371-590 |
1.59e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 95.11 E-value: 1.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 371 IEFKNVSFKYDINS--KKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYEL--RNIKTNNLR 446
Cdd:PRK13637 3 IKIENLTHIYMEGTpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 447 EHMSVVLQ--DTFMFNDTIENNIKLGDKNATKEDVERAANLSNAIHFIKTLPNGFQtqiENNGQNLSQGQRQLIAIARAV 524
Cdd:PRK13637 83 KKVGLVFQypEYQLFEETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYEDYK---DKSPFELSGGQKRRVAIAGVV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502819783 525 LANKSILILDEATSNIDSSTEEIIQASLLKIMESK--TSFVIAHRLSTI-KTADLIIVVNNGEIIEIGT 590
Cdd:PRK13637 160 AMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYnmTIILVSHSMEDVaKLADRIIVMNKGKCELQGT 228
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
59-345 |
1.63e-21 |
|
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: 95.21 E-value: 1.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 59 YFANYIASSSKSDFNVKSFSIWLVILGLVFIAYGFFRYFDAY----MYIKVSYqtssRMRKEAMHKLIKMPISYYDKQKA 134
Cdd:cd18549 23 LIVRYIIDDLLPSKNLRLILIIGAILLALYILRTLLNYFVTYwghvMGARIET----DMRRDLFEHLQKLSFSFFDNNKT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 135 GNLISTLINDINNVSNTMYNTINQFFSSIFNVLLSIIAMMFVASFITLIVVPLALFLFFISLIVIKKAQPYFVKVQNLFG 214
Cdd:cd18549 99 GQLMSRITNDLFDISELAHHGPEDLFISIITIIGSFIILLTINVPLTLIVFALLPLMIIFTIYFNKKMKKAFRRVREKIG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 215 DLNAFVEENLANTKVMNAFDQQDNIFNEFKKIT---RGIKLTSFKADAIarssepWFGITSGIANLC-VAVLAV-SFYIY 289
Cdd:cd18549 179 EINAQLEDSLSGIRVVKAFANEEYEIEKFDEGNdrfLESKKKAYKAMAY------FFSGMNFFTNLLnLVVLVAgGYFII 252
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 502819783 290 KipvggigglgtnpdGTATSGLIVTFISLNWNFMGPFQNLLNINFSFQMGLASSSR 345
Cdd:cd18549 253 K--------------GEITLGDLVAFLLYVNVFIKPIRRLVNFTEQYQKGMAGFER 294
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
31-287 |
2.23e-21 |
|
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: 94.85 E-value: 2.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 31 LYLGIFFSFCHSIFYVIGSFLIGYIFQQYFANYIASSSKSDF--NVKSFSIWLVILGlvfIAYGFFRYFDAYMYIKVSYQ 108
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFTDFGSGESSPDEFldDVNKYALYFVYLG---IGSFVLSYIQTACWTITGER 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 109 TSSRMRKEAMHKLIKMPISYYDKQKAGNLISTLINDInnvsntmyNTINQFFSSIFNVLLSIIAmMFVASFI-------- 180
Cdd:cd18577 78 QARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDT--------NLIQDGIGEKLGLLIQSLS-TFIAGFIiafiyswk 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 181 -TLIVVPLALFLFFISLIVIKKAQPYFVKVQNLFGDLNAFVEENLANTKVMNAFDQQDNIFNEFKKITRgikltsfKADA 259
Cdd:cd18577 149 lTLVLLATLPLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALE-------KARK 221
|
250 260
....*....|....*....|....*....
gi 502819783 260 IARSSEPWFGITSGIANLCV-AVLAVSFY 287
Cdd:cd18577 222 AGIKKGLVSGLGLGLLFFIIfAMYALAFW 250
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
368-588 |
4.53e-21 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 93.23 E-value: 4.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 368 DGLIEFKNVSFKYDINSKKYQ-LYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRniktnNLR 446
Cdd:COG1116 5 APALELRGVSKRFPTGGGGVTaLDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT-----GPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 447 EHMSVVLQDtfmfnD------TIENNIKLG---DKNATKEDVERAANLSNAI---HFIKTLPNgfqtqienngqNLSQGQ 514
Cdd:COG1116 80 PDRGVVFQE-----PallpwlTVLDNVALGlelRGVPKAERRERARELLELVglaGFEDAYPH-----------QLSGGM 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 515 RQLIAIARAVLANKSILILDEATSNIDSSTEEIIQASLLKIMES--KTSFVIAH------RLstiktADLIIVVNN--GE 584
Cdd:COG1116 144 RQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQEtgKTVLFVTHdvdeavFL-----ADRVVVLSArpGR 218
|
....
gi 502819783 585 IIEI 588
Cdd:COG1116 219 IVEE 222
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
372-583 |
6.62e-21 |
|
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: 91.44 E-value: 6.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 372 EFKNVSFKYDinsKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIktnnlREHMSV 451
Cdd:cd03235 1 EVEDLTVSYG---GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 452 VLQDT---FMFNDTIENNIKLG----------DKNATKEDVERAANLSNAIHFIKTlpngfqtQIenngQNLSQGQRQLI 518
Cdd:cd03235 73 VPQRRsidRDFPISVRDVVLMGlyghkglfrrLSKADKAKVDEALERVGLSELADR-------QI----GELSGGQQQRV 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502819783 519 AIARAVLANKSILILDEATSNIDSSTEEIIqASLLK--IMESKTSFVIAHRLSTIKT-ADLIIVVNNG 583
Cdd:cd03235 142 LLARALVQDPDLLLLDEPFAGVDPKTQEDI-YELLRelRREGMTILVVTHDLGLVLEyFDRVLLLNRT 208
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
43-346 |
8.56e-21 |
|
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: 93.01 E-value: 8.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 43 IFYVIGSFLIGYIFQQYFANYI--ASSSKSDFNVKSFSIWLVILGLVFIAYGFFRYfdaYMYIKVSYQTSSRMRKEAMHK 120
Cdd:cd18557 2 LLFLLISSAAQLLLPYLIGRLIdtIIKGGDLDVLNELALILLAIYLLQSVFTFVRY---YLFNIAGERIVARLRRDLFSS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 121 LIKMPISYYDKQKAGNLISTLINDINNVSNTMYNTINQFFSSIFNVLLSIIaMMFVASF-ITLIVVPLALFLFFISLIVI 199
Cdd:cd18557 79 LLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLI-ILFILSWkLTLVLLLVIPLLLIASKIYG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 200 KKAQPYFVKVQNLFGDLNAFVEENLANTKVMNAFDQQDNIFNEFKKITRGIKLTSFKAdAIARSSepWFGITSGIANLcv 279
Cdd:cd18557 158 RYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKK-ALANAL--FQGITSLLIYL-- 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502819783 280 AVLAVSFYiykipvggiGGLGTNpDGTATSGLIVTFISLNWNFMGPFQNLLNINFSFQMGLASSSRV 346
Cdd:cd18557 233 SLLLVLWY---------GGYLVL-SGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
370-590 |
1.17e-20 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 91.30 E-value: 1.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 370 LIEFKNVSFKYDinsKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNiktnnLREHM 449
Cdd:COG1121 6 AIELENLTVSYG---GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR-----ARRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 450 SVVLQdTFMFND----TIENNIKLG-------DKNATKEDVERAAN-LS--NAIHFIKTlpngfqtQIennGQnLSQGQR 515
Cdd:COG1121 78 GYVPQ-RAEVDWdfpiTVRDVVLMGrygrrglFRRPSRADREAVDEaLErvGLEDLADR-------PI---GE-LSGGQQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502819783 516 QLIAIARAVLANKSILILDEATSNIDSSTEEIIqASLLKIM--ESKTSFVIAHRLSTIKT-ADLIIVVnNGEIIEIGT 590
Cdd:COG1121 146 QRVLLARALAQDPDLLLLDEPFAGVDAATEEAL-YELLRELrrEGKTILVVTHDLGAVREyFDRVLLL-NRGLVAHGP 221
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
368-590 |
1.73e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 91.74 E-value: 1.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 368 DGLIEFKNVSFKYDiNSKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNLRE 447
Cdd:PRK13648 5 NSIIVFKNVSFQYQ-SDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 448 HMSVVLQ--DTFMFNDTIENNIKLGDKN---ATKEDVERAANLSNAIHFIKtlpngfqtQIENNGQNLSQGQRQLIAIAR 522
Cdd:PRK13648 84 HIGIVFQnpDNQFVGSIVKYDVAFGLENhavPYDEMHRRVSEALKQVDMLE--------RADYEPNALSGGQKQRVAIAG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 523 AVLANKSILILDEATSNIDSSTEEIIQASLLKIMESK--TSFVIAHRLSTIKTADLIIVVNNGEIIEIGT 590
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGT 225
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
84-535 |
4.89e-20 |
|
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: 93.71 E-value: 4.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 84 LGLVFIAYGFFRYFDAYMyIKVSYQTSSRMRKEAMHKLIKMPISYYDKQKAGNLISTLINDINNVSNTmyntINQFFSSI 163
Cdd:COG4615 55 AGLLVLLLLSRLASQLLL-TRLGQHAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQA----FVRLPELL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 164 FNVLLSIIAMMFVAS------FITLIVVPLALFLFFISLiviKKAQPYFVKVQnlfgdlnafveenlantkvmnafDQQD 237
Cdd:COG4615 130 QSVALVLGCLAYLAWlspplfLLTLVLLGLGVAGYRLLV---RRARRHLRRAR-----------------------EAED 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 238 NIFNEFKKITRGIK-LT-------SFKADAIARSSEP----------WFGITSGIANLCV-AVLAVSFYIykipvggIGG 298
Cdd:COG4615 184 RLFKHFRALLEGFKeLKlnrrrrrAFFDEDLQPTAERyrdlriradtIFALANNWGNLLFfALIGLILFL-------LPA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 299 LGTNPDGTATS-GLIVTFIslnwnfMGPFQNLLNINFSFQMGLASSSRVFKI-LNLDTKKPHVEDITIDKIDGL---IEF 373
Cdd:COG4615 257 LGWADPAVLSGfVLVLLFL------RGPLSQLVGALPTLSRANVALRKIEELeLALAAAEPAAADAAAPPAPADfqtLEL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 374 KNVSFKY--DINSKKYQL--YNASFvaKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNLREHM 449
Cdd:COG4615 331 RGVTYRYpgEDGDEGFTLgpIDLTI--RRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLF 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 450 SVVLQDTFMFNDTiennikLGDKNAtkEDVERAANLsnaihfIKTLPNGFQTQIENNG---QNLSQGQRQLIAIARAVLA 526
Cdd:COG4615 409 SAVFSDFHLFDRL------LGLDGE--ADPARAREL------LERLELDHKVSVEDGRfstTDLSQGQRKRLALLVALLE 474
|
....*....
gi 502819783 527 NKSILILDE 535
Cdd:COG4615 475 DRPILVFDE 483
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
371-590 |
6.09e-20 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 91.29 E-value: 6.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 371 IEFKNVSFKYDINSKKYQ-LYNASFVAKPGQTVAIVGPTGAGKTT---IINLLGKfydYNSGSIKIDGYELRNIKTNNLR 446
Cdd:COG1135 2 IELENLSKTFPTKGGPVTaLDDVSLTIEKGEIFGIIGYSGAGKSTlirCINLLER---PTSGSVLVDGVDLTALSERELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 447 E---HMSVVLQDtfmFN----DTIENNIKL-----G-DKNATKEdveRAANLsnaIHFI------KTLPNgfqtqienng 507
Cdd:COG1135 79 AarrKIGMIFQH---FNllssRTVAENVALpleiaGvPKAEIRK---RVAEL---LELVglsdkaDAYPS---------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 508 qNLSQGQRQLIAIARAvLANK-SILILDEATSNID-SSTEEIIQasLLKIMESK---TSFVIAHRLSTIKT-ADLIIVVN 581
Cdd:COG1135 140 -QLSGGQKQRVGIARA-LANNpKVLLCDEATSALDpETTRSILD--LLKDINRElglTIVLITHEMDVVRRiCDRVAVLE 215
|
....*....
gi 502819783 582 NGEIIEIGT 590
Cdd:COG1135 216 NGRIVEQGP 224
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
21-355 |
8.19e-20 |
|
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: 90.59 E-value: 8.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 21 ISYLKHDSKKLYLGIFFSFCHSIFYVIGSFLIGYIFQQYFA-NYIASSSKSDFnvksFSIWLVILGLV-FIAYGFFRYFD 98
Cdd:cd18578 1 LKLNKPEWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLpDDDELRSEANF----WALMFLVLAIVaGIAYFLQGYLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 99 AYMyikvSYQTSSRMRKEAMHKLIKMPISYYDKQK--AGNLISTLINDINNVSNTMYNTINQFFSSIFNVLLSIIAMMFV 176
Cdd:cd18578 77 GIA----GERLTRRLRKLAFRAILRQDIAWFDDPEnsTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 177 A---SFITLIVVPLALFLFFISLIVIKKAQpyfVKVQNLFGDLNAFVEENLANTKVMNAFDQQDNIFNEFKKITRGIKLT 253
Cdd:cd18578 153 GwklALVGLATVPLLLLAGYLRMRLLSGFE---EKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 254 SFKAdAIARSSepWFGITSGIANLCVAVLavsFYiykipVGGIggLGTNpDGTATSGLIVTFISLNWNFMGpfqnlLNIN 333
Cdd:cd18578 230 GLRR-ALISGL--GFGLSQSLTFFAYALA---FW-----YGGR--LVAN-GEYTFEQFFIVFMALIFGAQS-----AGQA 290
|
330 340
....*....|....*....|....*.
gi 502819783 334 FSF--QMGLA--SSSRVFKILNLDTK 355
Cdd:cd18578 291 FSFapDIAKAkaAAARIFRLLDRKPE 316
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
399-589 |
8.34e-20 |
|
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: 88.32 E-value: 8.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 399 GQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNnlREHMSVVLQDTFMFND-TIENNIKLG---DKNA 474
Cdd:cd03298 24 GEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFAHlTVEQNVGLGlspGLKL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 475 TKED---VERAANLSNAIHFIKTLPNgfqtqienngqNLSQGQRQLIAIARAVLANKSILILDEATSNIDSSTEEIIQAS 551
Cdd:cd03298 102 TAEDrqaIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 502819783 552 LLKIMESK--TSFVIAHRLSTI-KTADLIIVVNNGEIIEIG 589
Cdd:cd03298 171 VLDLHAETkmTVLMVTHQPEDAkRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
33-346 |
1.24e-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: 350009 [Multi-domain] Cd Length: 313 Bit Score: 89.93 E-value: 1.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 33 LGIFFSFCHSIFYVIGSFLIGYIFQQYFANyiaSSSKSDFNVKSFSI-------WLVIlGLVFIAYGF---FRYFDAYMY 102
Cdd:cd18565 3 LGLLASILNRLFDLAPPLLIGVAIDAVFNG---EASFLPLVPASLGPadprgqlWLLG-GLTVAAFLLeslFQYLSGVLW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 103 IKVSYQTSSRMRKEAMHKLIKMPISYYDKQKAGNLISTLINDINNVSNTMYNTINQfFSSIFNVLLSIIAMMFVAS---- 178
Cdd:cd18565 79 RRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANS-IIRVVVTVLGIGAILFYLNwqla 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 179 FITLIVVPLalfLFFISLIVIKKAQPYFVKVQNLFGDLNAFVEENLANTKVMNAFDQQDnifnefkkitrgikltsFKAD 258
Cdd:cd18565 158 LVALLPVPL---IIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAED-----------------FERE 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 259 AIARSSEP-----WFGITSGIANLCVAVLAVSF-YIYKIPVGG---IGGlGTNPDGTATSGLIVTFISLNWNFMGPFQNL 329
Cdd:cd18565 218 RVADASEEyrdanWRAIRLRAAFFPVIRLVAGAgFVATFVVGGywvLDG-PPLFTGTLTVGTLVTFLFYTQRLLWPLTRL 296
|
330
....*....|....*..
gi 502819783 330 LNINFSFQMGLASSSRV 346
Cdd:cd18565 297 GDLIDQYQRAMASAKRV 313
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
81-346 |
1.57e-19 |
|
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: 89.38 E-value: 1.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 81 LVILGLVFIAYgFFRYFDAYMYIKVSYQTSSRMRKEAMHKLIKMPISYYDKQKAGNLISTLINDINNVSNTMYNTINQFF 160
Cdd:cd18548 43 LLMLLLALLGL-IAGILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 161 SSIFNVLLSIIAMMFVASFITLIVVPLALFLFFISLIVIKKAQPYFVKVQNLFGDLNAFVEENLANTKVMNAFDQQDNIF 240
Cdd:cd18548 122 RAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEE 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 241 NEFKKITRGIKLTSFKADAIARSSEPwfgITSGIANLCVAVLavsfyIYkipvggIGGLGTNpDGTATSGLIVTFISLNW 320
Cdd:cd18548 202 ERFDKANDDLTDTSLKAGRLMALLNP---LMMLIMNLAIVAI-----LW------FGGHLIN-AGSLQVGDLVAFINYLM 266
|
250 260
....*....|....*....|....*.
gi 502819783 321 NFMGPFQNLLNINFSFQMGLASSSRV 346
Cdd:cd18548 267 QILMSLMMLSMVFVMLPRASASAKRI 292
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
79-346 |
2.58e-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: 350008 [Multi-domain] Cd Length: 307 Bit Score: 89.11 E-value: 2.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 79 IWLVILGLVFIAY--GFFRYFDAYMYIKVSYQTSSRMRKEAMHKLIKMPISYYDKQKAGNLISTLINDINNVSNTMYNTI 156
Cdd:cd18564 53 LLLAAAALVGIALlrGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 157 NQFFSSIFnVLLSIIAMMFVA----SFITLIVVPlaLFLFFISLIV--IKKAqpyFVKVQNLFGDLNAFVEENLANTKVM 230
Cdd:cd18564 133 LPLLTNLL-TLVGMLGVMFWLdwqlALIALAVAP--LLLLAARRFSrrIKEA---SREQRRREGALASVAQESLSAIRVV 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 231 NAFDQQDNIFNEFKKITRGikltSFKADAIARSSEPWFG-ITSGIANLCVA-VLAvsfyiykipVGGIGGLgtnpDGTAT 308
Cdd:cd18564 207 QAFGREEHEERRFARENRK----SLRAGLRAARLQALLSpVVDVLVAVGTAlVLW---------FGAWLVL----AGRLT 269
|
250 260 270
....*....|....*....|....*....|....*...
gi 502819783 309 SGLIVTFISLNWNFMGPFQNLLNINFSFQMGLASSSRV 346
Cdd:cd18564 270 PGDLLVFLAYLKNLYKPVRDLAKLTGRIAKASASAERV 307
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
389-596 |
6.38e-19 |
|
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: 86.93 E-value: 6.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 389 LYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNLRE----HMSVVLQDTFMF-NDTI 463
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLpHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 464 ENNIKLG------DKNATKEDVERAANLSNAIHFIKTLPNgfqtqienngqNLSQGQRQLIAIARAVLANKSILILDEAT 537
Cdd:cd03294 120 LENVAFGlevqgvPRAEREERAAEALELVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502819783 538 SNIDSSTEEIIQASLLKI--MESKTSFVIAHRLS-TIKTADLIIVVNNGEIIEIGTHKNLIQ 596
Cdd:cd03294 189 SALDPLIRREMQDELLRLqaELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILT 250
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
389-594 |
6.90e-19 |
|
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: 85.56 E-value: 6.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 389 LYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNN-LREHMSVVLQDTFMFND-TIENN 466
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVPEGRRIFPElTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 467 IKLG----DKNATKEDVERAANLsnaihFiktlPNgFQTQIENNGQNLSQGQRQLIAIARAVLANKSILILDEATSNIDS 542
Cdd:cd03224 96 LLLGayarRRAKRKARLERVYEL-----F----PR-LKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502819783 543 STEEIIQASLLKIMESKTSFVI----AHRLSTIktADLIIVVNNGEIIEIGTHKNL 594
Cdd:cd03224 166 KIVEEIFEAIRELRDEGVTILLveqnARFALEI--ADRAYVLERGRVVLEGTAAEL 219
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
371-589 |
9.19e-19 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 85.00 E-value: 9.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 371 IEFKNVSFKYDinsKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYEL-------RNI--- 440
Cdd:cd03301 1 VELENVTKRFG---NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVtdlppkdRDIamv 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 441 -KTNNLREHMSVVlqdtfmfnDTIENNIKL--GDKNATKEDVERAANLSNAIHFIKTLPngfqtqienngQNLSQGQRQL 517
Cdd:cd03301 78 fQNYALYPHMTVY--------DNIAFGLKLrkVPKDEIDERVREVAELLQIEHLLDRKP-----------KQLSGGQRQR 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502819783 518 IAIARAVLANKSILILDEATSNIDSSTEEIIQASLLKI-MESKTSFV-IAH-RLSTIKTADLIIVVNNGEIIEIG 589
Cdd:cd03301 139 VALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLqQRLGTTTIyVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
399-583 |
1.27e-18 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 85.08 E-value: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 399 GQTVAIVGPTGAGKTTII--------NLLGKFYdYNSGSIKIDGYELRNIKTnnlREHMSVVLQDTFMFNDTIENNIKLG 470
Cdd:cd03290 27 GQLTMIVGQVGCGKSSLLlailgemqTLEGKVH-WSNKNESEPSFEATRSRN---RYSVAYAAQKPWLLNATVEENITFG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 471 ---DKNATKEDVErAANLSNAIHFiktLPNGFQTQIENNGQNLSQGQRQLIAIARAVLANKSILILDEATSNIDSS-TEE 546
Cdd:cd03290 103 spfNKQRYKAVTD-ACSLQPDIDL---LPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlSDH 178
|
170 180 190
....*....|....*....|....*....|....*....
gi 502819783 547 IIQASLLKIM--ESKTSFVIAHRLSTIKTADLIIVVNNG 583
Cdd:cd03290 179 LMQEGILKFLqdDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
42-346 |
1.48e-18 |
|
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: 86.38 E-value: 1.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 42 SIFYVIGSFLIGYIFQQYFANYIASSSKSDFNVKSFSIWLVILGLvFIAYGFFRYFDAYMYIKVSYQTSSRMRKEAMHKL 121
Cdd:cd18576 1 GLILLLLSSAIGLVFPLLAGQLIDAALGGGDTASLNQIALLLLGL-FLLQAVFSFFRIYLFARVGERVVADLRKDLYRHL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 122 IKMPISYYDKQKAGNLISTLINDINNVSNTMYNTINQFFSSIFNVLLSIIAMMFVASFITLIVVPLALFLFFISLIVIKK 201
Cdd:cd18576 80 QRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 202 AQPYFVKVQNLFGDLNAFVEENLANTKVMNAFDQQDNIFNEFKKITRGIKLTSFKAdAIARSsepWFGITSGIAnLCVAV 281
Cdd:cd18576 160 IRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKR-ARIRA---LFSSFIIFL-LFGAI 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502819783 282 LAVSFYiykipvggiGGLGTNpDGTATSGLIVTFISLNWNFMGPFQNLLNINFSFQMGLASSSRV 346
Cdd:cd18576 235 VAVLWY---------GGRLVL-AGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
389-586 |
1.62e-18 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 82.86 E-value: 1.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 389 LYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRniktnnlrehmsvvlqdtfmFNDTIENnIK 468
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS--------------------FASPRDA-RR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 469 LGdknatkedveraanlsnaIHFIktlpngFQtqienngqnLSQGQRQLIAIARAVLANKSILILDEATSNIdsSTEEIi 548
Cdd:cd03216 75 AG------------------IAMV------YQ---------LSVGERQMVEIARALARNARLLILDEPTAAL--TPAEV- 118
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 502819783 549 qASLLKIM----ESKTSFV-IAHRLSTI-KTADLIIVVNNGEII 586
Cdd:cd03216 119 -ERLFKVIrrlrAQGVAVIfISHRLDEVfEIADRVTVLRDGRVV 161
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
34-346 |
1.97e-18 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 86.06 E-value: 1.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 34 GIFFSFCHSIFYVIGSFLIGYIFqqyFAnyiASSSKSDFNVKSFSIWLVILGLVFIAYGFFRyfdAYMYIKVSYQTSSRM 113
Cdd:cd18572 1 AFVFLVVAALSELAIPHYTGAVI---DA---VVADGSREAFYRAVLLLLLLSVLSGLFSGLR---GGCFSYAGTRLVRRL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 114 RKEAMHKLIKMPISYYDKQKAGNLISTLINDINNVSNTMYNTINQFFSSIFnVLLSIIAMMFVASF----ITLIVVPLAL 189
Cdd:cd18572 72 RRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLV-QLVGGLAFMFSLSWrltlLAFITVPVIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 190 FLFFISLIVIKKAQpyfVKVQNLFGDLNAFVEENLANTKVMNAFDQQDNIFNEFKKITRGIKLTSFKaDAIARSSepWFG 269
Cdd:cd18572 151 LITKVYGRYYRKLS---KEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVR-QALAYAG--YVA 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502819783 270 ITSGIANLCVAVlaVSFYiykipvggIGGLGTNpdGTATSGLIVTFIsLNWNFMGP-FQNLLNINFSFQMGLASSSRV 346
Cdd:cd18572 225 VNTLLQNGTQVL--VLFY--------GGHLVLS--GRMSAGQLVTFM-LYQQQLGEaFQSLGDVFSSLMQAVGAAEKV 289
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
391-590 |
2.07e-18 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 87.78 E-value: 2.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 391 NASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNLRE----HMSVVLQD-TFMFNDTIEN 465
Cdd:PRK10070 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSfALMPHMTVLD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 466 NIKLGDKNATKEDVERAANLSNAIHFIktlpnGFQTQIENNGQNLSQGQRQLIAIARAVLANKSILILDEATSNIDSSTE 545
Cdd:PRK10070 126 NTAFGMELAGINAEERREKALDALRQV-----GLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIR 200
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 502819783 546 EIIQASLLKIM--ESKTSFVIAHRL-STIKTADLIIVVNNGEIIEIGT 590
Cdd:PRK10070 201 TEMQDELVKLQakHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGT 248
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
371-590 |
2.16e-18 |
|
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: 84.09 E-value: 2.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 371 IEFKNVSFKYdINSKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNiKTNNLREHMS 450
Cdd:cd03263 1 LQIRNLTKTY-KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 451 VVLQ-DTFMFNDTIENNIKL---------GDKNATKEDVERAANLSnaiHFIKTLPngfqtqienngQNLSQGQRQLIAI 520
Cdd:cd03263 79 YCPQfDALFDELTVREHLRFyarlkglpkSEIKEEVELLLRVLGLT---DKANKRA-----------RTLSGGMKRKLSL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502819783 521 ARAVLANKSILILDEATSNIDSSTEEIIQASLLKIMESKTsfVI--------AHRLstiktADLIIVVNNGEIIEIGT 590
Cdd:cd03263 145 AIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRS--IIltthsmdeAEAL-----CDRIAIMSDGKLRCIGS 215
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
391-587 |
2.45e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 88.15 E-value: 2.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 391 NASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDG--YELRNIKTnNLREHMSVVLQDTFMFND-TIENNI 467
Cdd:COG1129 22 GVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepVRFRSPRD-AQAAGIAIIHQELNLVPNlSVAENI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 468 KLG---------DKNATKEDVERAanlsnaihfIKTLpnGFQ----TQIEnngqNLSQGQRQLIAIARAVLANKSILILD 534
Cdd:COG1129 101 FLGreprrggliDWRAMRRRAREL---------LARL--GLDidpdTPVG----DLSVAQQQLVEIARALSRDARVLILD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502819783 535 EATSNIDSSteEIiqASLLKIM----ESKTSFV-IAHRLSTIKT-ADLIIVVNNGEIIE 587
Cdd:COG1129 166 EPTASLTER--EV--ERLFRIIrrlkAQGVAIIyISHRLDEVFEiADRVTVLRDGRLVG 220
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
370-550 |
2.77e-18 |
|
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: 84.75 E-value: 2.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 370 LIEFKNVSFKYDinsKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKfydYN----SGSIKIDGYELRNIKTNNL 445
Cdd:COG1119 3 LLELRNVTVRRG---GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITG---DLpptyGNDVRLFGERRGGEDVWEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 446 REHMSVV---LQDTFMFNDTIENNIKLG-------DKNATKEDVERAANLSNAI---HFIKTLpngFQTqienngqnLSQ 512
Cdd:COG1119 77 RKRIGLVspaLQLRFPRDETVLDVVLSGffdsiglYREPTDEQRERARELLELLglaHLADRP---FGT--------LSQ 145
|
170 180 190
....*....|....*....|....*....|....*....
gi 502819783 513 GQRQLIAIARAVLANKSILILDEATSNID-SSTEEIIQA 550
Cdd:COG1119 146 GEQRRVLIARALVKDPELLILDEPTAGLDlGARELLLAL 184
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
29-346 |
4.35e-18 |
|
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: 85.22 E-value: 4.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 29 KKLYLGIFFSFCHSIFYVIGSFLIGYIFQQYFANYiasssksdfNVKSFSIWLVILGLVFIAYGFFRYFDAYMYIKVSYQ 108
Cdd:cd18540 2 KLLILLIILMLLVALLDAVFPLLTKYAIDHFITPG---------TLDGLTGFILLYLGLILIQALSVFLFIRLAGKIEMG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 109 TSSRMRKEAMHKLIKMPISYYDKQKAGNLISTLINDINNVSNTMYNTINQFFSSIFNVLLSIIAMMFVA---SFITLIVV 185
Cdd:cd18540 73 VSYDLRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNwklALIVLAVV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 186 PlalFLFFISLIVIKKAQPYFVKVQNLFGDLNAFVEENLANTKVMNAFDQQDNIFNEFKKITRGIKLTSFKAdaiARSSE 265
Cdd:cd18540 153 P---VLAVVSIYFQKKILKAYRKVRKINSRITGAFNEGITGAKTTKTLVREEKNLREFKELTEEMRRASVRA---ARLSA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 266 PWFGITSGIANLCVAVLAVsfyiykipVGGIGGLgtnpDGTATSGLIVTFISLNWNFMGPFQNLLNINFSFQMGLASSSR 345
Cdd:cd18540 227 LFLPIVLFLGSIATALVLW--------YGGILVL----AGAITIGTLVAFISYATQFFEPIQQLARVLAELQSAQASAER 294
|
.
gi 502819783 346 V 346
Cdd:cd18540 295 V 295
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
29-346 |
4.95e-18 |
|
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: 84.80 E-value: 4.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 29 KKLYLGIFF-SFCHSIFYVIGSFLIGYIFQQYFANYiasssksdfNVKSFSIWLVILGLVFIAYGFFRYFDAYMYIKVSY 107
Cdd:cd18570 1 KKLLILILLlSLLITLLGIAGSFFFQILIDDIIPSG---------DINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 108 QTSSRMRKEAMHKLIKMPISYYDKQKAGNLISTLiNDINNVSNTMYNTINQFFSSIFNVLLSIIAMMFVASFITLIVVPL 187
Cdd:cd18570 72 KLDIRLILGYFKHLLKLPLSFFETRKTGEIISRF-NDANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 188 ALFLFFISLIVIKKAQPYFVKVQNLFGDLNAFVEENLANTKVMNAFDQQDNIFNEFKKITRGIKLTSFKADAIARSSEPW 267
Cdd:cd18570 151 IPLYILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSI 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502819783 268 FGITSGIANLCVAVLAVSFYIykipvggigglgtnpDGTATSGLIVTFISLNWNFMGPFQNLLNINFSFQMGLASSSRV 346
Cdd:cd18570 231 KGLISLIGSLLILWIGSYLVI---------------KGQLSLGQLIAFNALLGYFLGPIENLINLQPKIQEAKVAADRL 294
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
389-594 |
7.98e-18 |
|
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: 83.11 E-value: 7.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 389 LYNASFVAKPGQTVAIVGPTGAGKTT----IINLLGKFydynSGSIKIDGYELRNIKTNNL-REHMSVVLQDTFMFND-T 462
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTllkaISGLLPPR----SGSIRFDGEDITGLPPHRIaRLGIGYVPEGRRIFPSlT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 463 IENNIKLG-----DKNATKEDVERAANLsnaihfiktlpngF---QTQIENNGQNLSQGQRQLIAIARAVLANKSILILD 534
Cdd:COG0410 95 VEENLLLGayarrDRAEVRADLERVYEL-------------FprlKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502819783 535 EATS----NIdssTEEIIQAsLLKIMESKTSFVI----AHRLSTIktADLIIVVNNGEIIEIGTHKNL 594
Cdd:COG0410 162 EPSLglapLI---VEEIFEI-IRRLNREGVTILLveqnARFALEI--ADRAYVLERGRIVLEGTAAEL 223
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
64-301 |
1.96e-17 |
|
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: 82.95 E-value: 1.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 64 IASSSKSDFNVKSFSIW--LVILGLVFIAYGFFRYFDAYMYIKVSYQTSSRMRKEAMHKLIKMPISYYDKQKAGNLISTL 141
Cdd:cd18573 25 VASKESGDIEIFGLSLKtfALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFDKNKTGELVSRL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 142 INDINNVSNTMYNTINQFFSSIFNVLLSIIAMMFV----ASFITLIVVPLALFLFFISLiVIKKAQpyfVKVQNLFGDLN 217
Cdd:cd18573 105 SSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYIspklTLVMLLVVPPIAVGAVFYGR-YVRKLS---KQVQDALADAT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 218 AFVEENLANTKVMNAFDQQDNIFNEFKKITRGIKLTSFKaDAIARSSepWFGITSGIANLcvAVLAV------------- 284
Cdd:cd18573 181 KVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKK-EALASGL--FFGSTGFSGNL--SLLSVlyyggslvasgel 255
|
250 260
....*....|....*....|....
gi 502819783 285 ------SFYIYKIPVG-GIGGLGT 301
Cdd:cd18573 256 tvgdltSFLMYAVYVGsSVSGLSS 279
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
371-594 |
2.01e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 82.91 E-value: 2.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 371 IEFKNVSFKYDINS--KKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNiKTNN---- 444
Cdd:PRK13646 3 IRFDNVSYTYQKGTpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITH-KTKDkyir 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 445 -LREHMSVVLQ--DTFMFNDTIENNIKLGDKNaTKEDVERAANLSnaihFIKTLPNGFQTQI-ENNGQNLSQGQRQLIAI 520
Cdd:PRK13646 82 pVRKRIGMVFQfpESQLFEDTVEREIIFGPKN-FKMNLDEVKNYA----HRLLMDLGFSRDVmSQSPFQMSGGQMRKIAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502819783 521 ARAVLANKSILILDEATSNIDSSTEEIIQASL--LKIMESKTSFVIAHRLSTI-KTADLIIVVNNGEIIEIGTHKNL 594
Cdd:PRK13646 157 VSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLksLQTDENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKEL 233
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
371-589 |
2.15e-17 |
|
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: 81.09 E-value: 2.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 371 IEFKNVSFKYDinsKKYQLYNASFVAKPGQTvAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKtNNLREHMS 450
Cdd:cd03264 1 LQLENLTKRYG---KKRALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQP-QKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 451 VVLQDtFMF--NDTIENNIK----LGDKNATKED--VERAANLSNAIHFIKTLPNGfqtqienngqnLSQGQRQLIAIAR 522
Cdd:cd03264 76 YLPQE-FGVypNFTVREFLDyiawLKGIPSKEVKarVDEVLELVNLGDRAKKKIGS-----------LSGGMRRRVGIAQ 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502819783 523 AVLANKSILILDEATSNIDSStEEIIQASLL-KIMESKTSFVIAHRLSTIK-TADLIIVVNNGEIIEIG 589
Cdd:cd03264 144 ALVGDPSILIVDEPTAGLDPE-ERIRFRNLLsELGEDRIVILSTHIVEDVEsLCNQVAVLNKGKLVFEG 211
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
393-541 |
5.85e-17 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 80.40 E-value: 5.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 393 SFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNikTNNLREHMSVVLQDTFMFND-TIENNIKLG- 470
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTT--TPPSRRPVSMLFQENNLFSHlTVAQNIGLGl 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502819783 471 --------DKNATKEDVERAANLSNaihFIKTLPngfqtqiennGQnLSQGQRQLIAIARAVLANKSILILDEATSNID 541
Cdd:PRK10771 97 npglklnaAQREKLHAIARQMGIED---LLARLP----------GQ-LSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
391-589 |
6.45e-17 |
|
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: 79.65 E-value: 6.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 391 NASFVAkPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYEL----RNIKTNNLREHMSVVLQDTFMF-NDTIEN 465
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsrKKINLPPQQRKIGLVFQQYALFpHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 466 NIKLGDK-NATKEDVERAANLSNAIHFiktlpngfqTQIENNG-QNLSQGQRQLIAIARAVLANKSILILDEATSNIDSS 543
Cdd:cd03297 95 NLAFGLKrKRNREDRISVDELLDLLGL---------DHLLNRYpAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 502819783 544 TEEIIQASLLKIMES--KTSFVIAHRLSTIKT-ADLIIVVNNGEIIEIG 589
Cdd:cd03297 166 LRLQLLPELKQIKKNlnIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
371-590 |
6.79e-17 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 82.50 E-value: 6.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 371 IEFKNVSFKYDinskKYQ-LYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGyelRNIKTN-NLRE- 447
Cdd:COG1118 3 IEVRNISKRFG----SFTlLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNG---RDLFTNlPPREr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 448 HMSVVLQDTFMF-NDTIENNIKLG------DKNATKEDVERAANLSNAIHFIKTLPNgfqtqienngqNLSQGQRQLIAI 520
Cdd:COG1118 76 RVGFVFQHYALFpHMTVAENIAFGlrvrppSKAEIRARVEELLELVQLEGLADRYPS-----------QLSGGQRQRVAL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502819783 521 ARAvLANK-SILILDEATSNIDSSTEEIIQASLLKI---MESKTSFVI-----AHRLstiktADLIIVVNNGEIIEIGT 590
Cdd:COG1118 145 ARA-LAVEpEVLLLDEPFGALDAKVRKELRRWLRRLhdeLGGTTVFVThdqeeALEL-----ADRVVVMNQGRIEQVGT 217
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
391-590 |
7.44e-17 |
|
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: 80.17 E-value: 7.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 391 NASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGyelRNIktNNLREH------MSVVLQDTFMFND-TI 463
Cdd:cd03219 18 DVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDG---EDI--TGLPPHeiarlgIGRTFQIPRLFPElTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 464 ENNIKLG-------------DKNATKEDVERAANLsnaIHFIktlpnGFQTQIENNGQNLSQGQRQLIAIARAVLANKSI 530
Cdd:cd03219 93 LENVMVAaqartgsglllarARREEREARERAEEL---LERV-----GLADLADRPAGELSYGQQRRLEIARALATDPKL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502819783 531 LILDEATSNIDSS-TEEIIQAsLLKIMESKTSFV-IAHRLSTIKT-ADLIIVVNNGEIIEIGT 590
Cdd:cd03219 165 LLLDEPAAGLNPEeTEELAEL-IRELRERGITVLlVEHDMDVVMSlADRVTVLDQGRVIAEGT 226
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
79-346 |
7.60e-17 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 81.37 E-value: 7.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 79 IWLVILGL-VFIAYGFFRYFDAYMYIKVSYQTSSRMRKEAMHKLIKMPISYYDKQKAGNLISTLINDINNVSNTMYNTIN 157
Cdd:cd18550 39 VLLALGMVaVAVASALLGVVQTYLSARIGQGVMYDLRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 158 QFFSSIFNVLLSIIAMMFVASFITLIVVPLALFLFFISLIVIKKAQPYFVKVQNLFGDLNAFVEENLANTKVMNA--FDQ 235
Cdd:cd18550 119 SVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPTRRVGRRRRKLTREQQEKLAELNSIMQETLSVSGALLVklFGR 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 236 QDNIFNEFKKITRGIKLTSFKADAIARssepWFGITSGIANLCVAVLavsfyIYkipvgGIGGLGTnPDGTATSGLIVTF 315
Cdd:cd18550 199 EDDEAARFARRSRELRDLGVRQALAGR----WFFAALGLFTAIGPAL-----VY-----WVGGLLV-IGGGLTIGTLVAF 263
|
250 260 270
....*....|....*....|....*....|.
gi 502819783 316 ISLNWNFMGPFQNLLNINFSFQMGLASSSRV 346
Cdd:cd18550 264 TALLGRLYGPLTQLLNIQVDLMTSLALFERI 294
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
391-590 |
1.05e-16 |
|
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: 83.20 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 391 NASFVAKPGQTVAIVGPTGAGKTT----IINLLGkfydyNSGSIKIDGYELRNIKTNN---LREHMSVVLQDTF-MFN-- 460
Cdd:COG4172 304 GVSLTLRRGETLGLVGESGSGKSTlglaLLRLIP-----SEGEIRFDGQDLDGLSRRAlrpLRRRMQVVFQDPFgSLSpr 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 461 ----DTIENNIKLGDKNATKEDVERAAnlsnaihfIKTL-------------PNGFqtqienngqnlSQGQRQLIAIARA 523
Cdd:COG4172 379 mtvgQIIAEGLRVHGPGLSAAERRARV--------AEALeevgldpaarhryPHEF-----------SGGQRQRIAIARA 439
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502819783 524 VLANKSILILDEATSNIDSSteeiIQA---SLLKIMESKT--SFV-IAHRLSTIKT-ADLIIVVNNGEIIEIGT 590
Cdd:COG4172 440 LILEPKLLVLDEPTSALDVS----VQAqilDLLRDLQREHglAYLfISHDLAVVRAlAHRVMVMKDGKVVEQGP 509
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
370-589 |
1.07e-16 |
|
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: 79.33 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 370 LIEFKNVSFKYDINSKKYQ-LYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELrniktnnLREH 448
Cdd:cd03266 1 MITADALTKRFRDVKKTVQaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDV-------VKEP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 449 MSVVLQDTFMFNDTienniKLGDKNATKEDVERAANL----SNAIH-----FIKTLpnGFQTQIENNGQNLSQGQRQLIA 519
Cdd:cd03266 74 AEARRRLGFVSDST-----GLYDRLTARENLEYFAGLyglkGDELTarleeLADRL--GMEELLDRRVGGFSTGMRQKVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502819783 520 IARAVLANKSILILDEATSNID-SSTEEIIQASLLKIMESKTSFVIAHRLSTIKT-ADLIIVVNNGEIIEIG 589
Cdd:cd03266 147 IARALVHDPPVLLLDEPTTGLDvMATRALREFIRQLRALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
370-590 |
1.23e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 80.62 E-value: 1.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 370 LIEFKNVSFKYdiNSKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNLREHM 449
Cdd:PRK13652 3 LIETRDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 450 SVVLQ--DTFMFNDTIENNIKLGDKNATKEDVERAANLSNAIHFIktlpnGFQTQIENNGQNLSQGQRQLIAIARAVLAN 527
Cdd:PRK13652 81 GLVFQnpDDQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHML-----GLEELRDRVPHHLSGGEKKRVAIAGVIAME 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502819783 528 KSILILDEATSNIDSSTEEIIQASLLKIMESKTSFVI--AHRLSTI-KTADLIIVVNNGEIIEIGT 590
Cdd:PRK13652 156 PQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIfsTHQLDLVpEMADYIYVMDKGRIVAYGT 221
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
371-594 |
1.27e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 80.64 E-value: 1.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 371 IEFKNVSFKYDINS--KKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELrNIKTNN---- 444
Cdd:PRK13641 3 IKFENVDYIYSPGTpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHI-TPETGNknlk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 445 -LREHMSVVLQ--DTFMFNDTIENNIKLGDKN--ATKEDVEraanlSNAIHFIKTLpnGFQTQIENNGQ-NLSQGQRQLI 518
Cdd:PRK13641 82 kLRKKVSLVFQfpEAQLFENTVLKDVEFGPKNfgFSEDEAK-----EKALKWLKKV--GLSEDLISKSPfELSGGQMRRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502819783 519 AIArAVLANK-SILILDEATSNID-SSTEEIIQASLLKIMESKTSFVIAHRLSTI-KTADLIIVVNNGEIIEIGTHKNL 594
Cdd:PRK13641 155 AIA-GVMAYEpEILCLDEPAAGLDpEGRKEMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKEI 232
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
386-596 |
1.47e-16 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 84.06 E-value: 1.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 386 KYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIkidgYELRNIktnnlrehmSVVLQDTFMFNDTIEN 465
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV----WAERSI---------AYVPQQAWIMNATVRG 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 466 NIKLGDKnatkedvERAANLSNAIHF------IKTLPNGFQTQIENNGQNLSQGQRQLIAIARAVLANKSILILDEATSN 539
Cdd:PTZ00243 740 NILFFDE-------EDAARLADAVRVsqleadLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSA 812
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502819783 540 IDSST-EEIIQASLLKIMESKTSFVIAHRLSTIKTADLIIVVNNGEIIEIGTHKNLIQ 596
Cdd:PTZ00243 813 LDAHVgERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMR 870
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
371-590 |
1.54e-16 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 81.27 E-value: 1.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 371 IEFKNVSFKYDinsKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGyelRNIktNNLRE--- 447
Cdd:COG3839 4 LELENVSKSYG---GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGG---RDV--TDLPPkdr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 448 -------------HMSVvlqdtfmfndtiENNIKLG------DKNATKEDVERAA---NLSnaiHFIKTLPngfqtqien 505
Cdd:COG3839 76 niamvfqsyalypHMTV------------YENIAFPlklrkvPKAEIDRRVREAAellGLE---DLLDRKP--------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 506 ngQNLSQGQRQLIAIARAVLANKSILILDEATSNIDSST-----EEIiqASLLKimESKTSFVIA-HRLS---TIktADL 576
Cdd:COG3839 132 --KQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLrvemrAEI--KRLHR--RLGTTTIYVtHDQVeamTL--ADR 203
|
250
....*....|....
gi 502819783 577 IIVVNNGEIIEIGT 590
Cdd:COG3839 204 IAVMNDGRIQQVGT 217
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
371-586 |
1.84e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 79.74 E-value: 1.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 371 IEFKNVS--FKYDINSKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGyelRNIktNNLREH 448
Cdd:COG1101 2 LELKNLSktFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDG---KDV--TKLPEY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 449 -----MSVVLQDTFM---FNDTIENNIKLGDKNATKEDVERAANLSNAIHF---IKTLPNGFQTQIENNGQNLSQGQRQL 517
Cdd:COG1101 77 krakyIGRVFQDPMMgtaPSMTIEENLALAYRRGKRRGLRRGLTKKRRELFrelLATLGLGLENRLDTKVGLLSGGQRQA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502819783 518 IAIARAVLANKSILILDEATSNIDSSTEEiiqasllKIMESKTSFVIAHRLST----------IKTADLIIVVNNGEII 586
Cdd:COG1101 157 LSLLMATLTKPKLLLLDEHTAALDPKTAA-------LVLELTEKIVEENNLTTlmvthnmeqaLDYGNRLIMMHEGRII 228
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
384-587 |
2.14e-16 |
|
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: 78.03 E-value: 2.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 384 SKKYQ----LYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDG-YELRNIKTNNlreHMSVVLQD-TF 457
Cdd:cd03268 7 TKTYGkkrvLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGkSYQKNIEALR---RIGALIEApGF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 458 MFNDTIENNIK-----LGDKNATKEDVERAANLSNAIHF-IKTlpngfqtqienngqnLSQGQRQLIAIARAVLANKSIL 531
Cdd:cd03268 84 YPNLTARENLRllarlLGIRKKRIDEVLDVVGLKDSAKKkVKG---------------FSLGMKQRLGIALALLGNPDLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502819783 532 ILDEATSNIDSSTEEIIQASLLKIMESKTSFVIA-HRLSTI-KTADLIIVVNNGEIIE 587
Cdd:cd03268 149 ILDEPTNGLDPDGIKELRELILSLRDQGITVLISsHLLSEIqKVADRIGIINKGKLIE 206
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
370-592 |
2.46e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 79.35 E-value: 2.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 370 LIEFKNVSFKYDINSKKyqLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTN--NLRE 447
Cdd:PRK13639 1 ILETRDLKYSYPDGTEA--LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSllEVRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 448 HMSVVLQ--DTFMFNDTIENNIKLGDKNA--TKEDVERaaNLSNAIHFIKTlpNGFQtqiENNGQNLSQGQRQLIAIARA 523
Cdd:PRK13639 79 TVGIVFQnpDDQLFAPTVEEDVAFGPLNLglSKEEVEK--RVKEALKAVGM--EGFE---NKPPHHLSGGQKKRVAIAGI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502819783 524 VLANKSILILDEATSNIDSSTEEIIQASLLKIMESKTSFVIA-HRLSTIKT-ADLIIVVNNGEIIEIGTHK 592
Cdd:PRK13639 152 LAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIIStHDVDLVPVyADKVYVMSDGKIIKEGTPK 222
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
367-589 |
2.56e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 79.39 E-value: 2.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 367 IDGLIEFKNVSFKYDINSKKyqLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNLR 446
Cdd:PRK13647 1 MDNIIEVEDLHFRYKDGTKA--LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 447 EHMSVVLQ--DTFMFNDTIENNIKLGDKNA--TKEDVERAANlsNAIHFIktlpnGFQTQIENNGQNLSQGQRQLIAIAR 522
Cdd:PRK13647 79 SKVGLVFQdpDDQVFSSTVWDDVAFGPVNMglDKDEVERRVE--EALKAV-----RMWDFRDKPPYHLSYGQKKRVAIAG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502819783 523 AVLANKSILILDEATSNIDSSTEEIIQASLLKIMESKTSFVIA-HRLS-TIKTADLIIVVNNGEIIEIG 589
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDlAAEWADQVIVLKEGRVLAEG 220
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
371-596 |
2.77e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 79.68 E-value: 2.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 371 IEFKNVSFKYDINS--KKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNN---- 444
Cdd:PRK13634 3 ITFQKVEHRYQYKTpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKklkp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 445 LREHMSVVLQ--DTFMFNDTIENNIKLGDKN--ATKEDVERAAnlSNAIHFIKtLPNGFQTQienNGQNLSQGQRQLIAI 520
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDICFGPMNfgVSEEDAKQKA--REMIELVG-LPEELLAR---SPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 521 ArAVLA-NKSILILDEATSNIDSSTEEiiqasllKIMEsktSFVIAHR---LSTI----------KTADLIIVVNNGEII 586
Cdd:PRK13634 157 A-GVLAmEPEVLVLDEPTAGLDPKGRK-------EMME---MFYKLHKekgLTTVlvthsmedaaRYADQIVVMHKGTVF 225
|
250
....*....|
gi 502819783 587 EIGTHKNLIQ 596
Cdd:PRK13634 226 LQGTPREIFA 235
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
389-594 |
2.78e-16 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 83.04 E-value: 2.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 389 LYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGyelrniktnnlreHMSVVLQDTFMFNDTIENNIK 468
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKDNII 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 469 LGdknaTKEDVERAANLSNAIHF---IKTLPNGFQTQIENNGQNLSQGQRQLIAIARAVLANKSILILDEATSNIDSSTE 545
Cdd:TIGR01271 509 FG----LSYDEYRYTSVIKACQLeedIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTE 584
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 502819783 546 -EIIQASLLKIMESKTSFVIAHRLSTIKTADLIIVVNNGEIIEIGTHKNL 594
Cdd:TIGR01271 585 kEIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSEL 634
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
397-594 |
2.82e-16 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 79.02 E-value: 2.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 397 KPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYEL---RNIKTN-----NLREHMSVVLQDTFMF-NDTIENNI 467
Cdd:PRK11264 27 KPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtaRSLSQQkglirQLRQHVGFVFQNFNLFpHRTVLENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 468 KLGDKNATKEDVERAANLSNAIhFIKTLPNGFQTQIEnngQNLSQGQRQLIAIARAVLANKSILILDEATSNIDSSTEEI 547
Cdd:PRK11264 107 IEGPVIVKGEPKEEATARAREL-LAKVGLAGKETSYP---RRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGE 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 502819783 548 IQASLLKIMESKTSFVI-AHRLSTIK-TADLIIVVNNGEIIEIGTHKNL 594
Cdd:PRK11264 183 VLNTIRQLAQEKRTMVIvTHEMSFARdVADRAIFMDQGRIVEQGPAKAL 231
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
393-589 |
2.84e-16 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 80.16 E-value: 2.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 393 SFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNLRE---HMSVVLQDTFM-FN------DT 462
Cdd:COG4608 38 SFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPlrrRMQMVFQDPYAsLNprmtvgDI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 463 IENNIKLGDKNATKEDVERAANLSNAI----HFIKTLPNGFqtqienngqnlSQGQRQLIAIARAVLANKSILILDEATS 538
Cdd:COG4608 118 IAEPLRIHGLASKAERRERVAELLELVglrpEHADRYPHEF-----------SGGQRQRIGIARALALNPKLIVCDEPVS 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502819783 539 NIDSSteeiIQASLLKIM-----ESKTSFV-IAHRLSTIK-TADLIIVVNNGEIIEIG 589
Cdd:COG4608 187 ALDVS----IQAQVLNLLedlqdELGLTYLfISHDLSVVRhISDRVAVMYLGKIVEIA 240
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
370-609 |
3.22e-16 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 80.76 E-value: 3.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 370 LIEFKNVSFKYD----INSKKYQLYNASFVAkpgqtvaIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNnl 445
Cdd:PRK09452 14 LVELRGISKSFDgkevISNLDLTINNGEFLT-------LLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 446 REHMSVVLQDTFMF-NDTIENNIKLGDKNATKEDVERAANLSNAIHFIktlpngfqtQIENNGQ----NLSQGQRQLIAI 520
Cdd:PRK09452 85 NRHVNTVFQSYALFpHMTVFENVAFGLRMQKTPAAEITPRVMEALRMV---------QLEEFAQrkphQLSGGQQQRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 521 ARAVLANKSILILDEATSNIDSSTEEIIQaSLLKIMESKTS----FVIAHRLSTIKTADLIIVVNNGEIIEIGTHKNLiq 596
Cdd:PRK09452 156 ARAVVNKPKVLLLDESLSALDYKLRKQMQ-NELKALQRKLGitfvFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI-- 232
|
250
....*....|....*.
gi 502819783 597 ldgfY---SNLYNSQF 609
Cdd:PRK09452 233 ----YeepKNLFVARF 244
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
391-590 |
3.92e-16 |
|
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: 78.54 E-value: 3.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 391 NASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIK--------------TNNLREHMSVvlqdt 456
Cdd:COG0411 22 DVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPphriarlgiartfqNPRLFPELTV----- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 457 fmfndtIEnNIKLGDKNATKEDV------------ERAANLSNAIHFIKTLpnGFQTQIENNGQNLSQGQRQLIAIARAV 524
Cdd:COG0411 97 ------LE-NVLVAAHARLGRGLlaallrlprarrEEREARERAEELLERV--GLADRADEPAGNLSYGQQRRLEIARAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 525 LANKSILILDEATSNIDSS-TEEIIQAsLLKIMESK--TSFVIAHRLSTI-KTADLIIVVNNGEIIEIGT 590
Cdd:COG0411 168 ATEPKLLLLDEPAAGLNPEeTEELAEL-IRRLRDERgiTILLIEHDMDLVmGLADRIVVLDFGRVIAEGT 236
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
370-596 |
4.02e-16 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 78.21 E-value: 4.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 370 LIEFKNVSFKYdinSKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTN--NLRE 447
Cdd:PRK09493 1 MIEFKNVSKHF---GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDerLIRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 448 HMSVVLQDTFMFND-TIENNIKLGD---KNATKEDVERAAnlsnaihfiKTLPN--GFQTQIENNGQNLSQGQRQLIAIA 521
Cdd:PRK09493 78 EAGMVFQQFYLFPHlTALENVMFGPlrvRGASKEEAEKQA---------RELLAkvGLAERAHHYPSELSGGQQQRVAIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 522 RAvLANKSILIL-DEATSNIDSSteeiIQASLLKIM-----ESKTSFVIAHRLS-TIKTADLIIVVNNGEIIEIGTHKNL 594
Cdd:PRK09493 149 RA-LAVKPKLMLfDEPTSALDPE----LRHEVLKVMqdlaeEGMTMVIVTHEIGfAEKVASRLIFIDKGRIAEDGDPQVL 223
|
..
gi 502819783 595 IQ 596
Cdd:PRK09493 224 IK 225
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
43-194 |
4.83e-16 |
|
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: 79.09 E-value: 4.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 43 IFYVIGSFLigYIFQQYFANYIASSSKSDFNVKSFSIWLVILGLVFIAYGFFRYFDAYMYIKVSYQTSSRMRKEAMHKLI 122
Cdd:cd18580 6 LLLLLLAFL--SQFSNIWLDWWSSDWSSSPNSSSGYYLGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLHDKLLRSVL 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502819783 123 KMPISYYDKQKAGNLISTLINDINNVSNTMYNTINQFFSSIFNVLLSIIAMMFVASFITLIVVPLALFLFFI 194
Cdd:cd18580 84 RAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLL 155
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
369-590 |
5.72e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 78.90 E-value: 5.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 369 GLIEFKNVSFKYdinSKKY-----QLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYE----LRN 439
Cdd:PRK13645 5 KDIILDNVSYTY---AKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAipanLKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 440 IK-TNNLREHMSVVLQ--DTFMFNDTIENNIKLGDKNATKEDVERAANLSNAIHFIKtLPNGFqtqIENNGQNLSQGQRQ 516
Cdd:PRK13645 82 IKeVKRLRKEIGLVFQfpEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQ-LPEDY---VKRSPFELSGGQKR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502819783 517 LIAIARAVLANKSILILDEATSNIDSSTEEIIQASLLKIMES--KTSFVIAHRLSTI-KTADLIIVVNNGEIIEIGT 590
Cdd:PRK13645 158 RVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEykKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGS 234
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
389-566 |
7.41e-16 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 77.82 E-value: 7.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 389 LYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGyelrnIKTNNLREHMSVVLQDTFMFN-DTIENNI 467
Cdd:PRK11248 17 LEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDG-----KPVEGPGAERGVVFQNEGLLPwRNVQDNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 468 KLGDKNAtkeDVERAANLSNAIHFIKtlpngfQTQIENNGQ----NLSQGQRQLIAIARAVLANKSILILDEATSNIDSS 543
Cdd:PRK11248 92 AFGLQLA---GVEKMQRLEIAHQMLK------KVGLEGAEKryiwQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAF 162
|
170 180
....*....|....*....|....*
gi 502819783 544 TEEIIQASLLKIME--SKTSFVIAH 566
Cdd:PRK11248 163 TREQMQTLLLKLWQetGKQVLLITH 187
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
371-590 |
7.91e-16 |
|
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: 77.38 E-value: 7.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 371 IEFKNVSFKYDinsKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGyelRNIKTNNLRE-HM 449
Cdd:cd03296 3 IEVRNVSKRFG---DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGG---EDATDVPVQErNV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 450 SVVLQDTFMFND-TIENNIKLG----------DKNATKEDVERAANLSNAIHFIKTLPNgfqtqienngqNLSQGQRQLI 518
Cdd:cd03296 77 GFVFQHYALFRHmTVFDNVAFGlrvkprserpPEAEIRAKVHELLKLVQLDWLADRYPA-----------QLSGGQRQRV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502819783 519 AIARAVLANKSILILDEATSNIDSSTEEIIQASLLKI---MESKTSFVIAHRLSTIKTADLIIVVNNGEIIEIGT 590
Cdd:cd03296 146 ALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLhdeLHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
370-594 |
9.57e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 77.51 E-value: 9.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 370 LIEFKNVSFKYdinSKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYN-----SGSIKIDGYEL--RNIKT 442
Cdd:PRK14239 5 ILQVSDLSVYY---NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIysPRTDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 443 NNLREHMSVVLQDTFMFNDTIENNIKLG-------DKNATKEDVERAanLSNAihfikTLPNGFQTQIENNGQNLSQGQR 515
Cdd:PRK14239 82 VDLRKEIGMVFQQPNPFPMSIYENVVYGlrlkgikDKQVLDEAVEKS--LKGA-----SIWDEVKDRLHDSALGLSGGQQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 516 QLIAIARAVLANKSILILDEATSNIDSSTEEIIQASLLKIMESKTSFVIAHRLSTI-KTADLIIVVNNGEIIEIGTHKNL 594
Cdd:PRK14239 155 QRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQAsRISDRTGFFLDGDLIEYNDTKQM 234
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
371-596 |
9.82e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 77.86 E-value: 9.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 371 IEFKNVSFKYDINS--KKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTN----N 444
Cdd:PRK13649 3 INLQNVSYTYQAGTpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNkdikQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 445 LREHMSVVLQ--DTFMFNDTIENNIKLGDKN--ATKEDVERAANLSNAIHFIKtlpngfQTQIENNGQNLSQGQRQLIAI 520
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQNfgVSQEEAEALAREKLALVGIS------ESLFEKNPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502819783 521 ARAVLANKSILILDEATSNIDSSTEEIIQASLLKIMESKTSFV-IAHRLSTIKT-ADLIIVVNNGEIIEIGTHKNLIQ 596
Cdd:PRK13649 157 AGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVlVTHLMDDVANyADFVYVLEKGKLVLSGKPKDIFQ 234
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
389-594 |
1.09e-15 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 77.59 E-value: 1.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 389 LYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGyelrniktnnlreHMSVVLQDTFMFNDTIENNIK 468
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTIKENII 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 469 LG---DKNATKEdVERAANLSNAIhfiKTLPNGFQTQIENNGQNLSQGQRQLIAIARAVLANKSILILDEATSNIDSSTE 545
Cdd:cd03291 120 FGvsyDEYRYKS-VVKACQLEEDI---TKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTE 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 502819783 546 -EIIQASLLKIMESKTSFVIAHRLSTIKTADLIIVVNNGEIIEIGTHKNL 594
Cdd:cd03291 196 kEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
370-589 |
1.41e-15 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 78.72 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 370 LIEFKNVSFKYDinsKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTnnLREHM 449
Cdd:PRK11607 19 LLEIRNLTKSFD---GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP--YQRPI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 450 SVVLQDTFMF-NDTIENNIKLG---DKNATKEDVERAANLSNAIH---FIKTLPNgfqtqienngqNLSQGQRQLIAIAR 522
Cdd:PRK11607 94 NMMFQSYALFpHMTVEQNIAFGlkqDKLPKAEIASRVNEMLGLVHmqeFAKRKPH-----------QLSGGQRQRVALAR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 523 AVLANKSILILDEATSNIDSSTEEIIQASLLKIME--SKTSFVIAHRLSTIKT-ADLIIVVNNGEIIEIG 589
Cdd:PRK11607 163 SLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILErvGVTCVMVTHDQEEAMTmAGRIAIMNRGKFVQIG 232
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
393-541 |
1.49e-15 |
|
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: 75.59 E-value: 1.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 393 SFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRnIKTNNLREHMSVVLQDTFMFND-TIENNI---- 467
Cdd:COG4133 22 SFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIR-DAREDYRRRLAYLGHADGLKPElTVRENLrfwa 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502819783 468 KLGDKNATKEDVERAA---NLSNAIHfiktLPngfqtqiennGQNLSQGQRQLIAIARAVLANKSILILDEATSNID 541
Cdd:COG4133 101 ALYGLRADREAIDEALeavGLAGLAD----LP----------VRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALD 163
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
370-595 |
2.27e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 76.56 E-value: 2.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 370 LIEFKNVSFKYDINSKKyqLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNI-KTNNLREH 448
Cdd:PRK13644 1 MIRLENVSYSYPDGTPA--LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFsKLQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 449 MSVVLQ--DTFMFNDTIENNIKLGDKNATKEDVERAANLSNAIHFIktlpnGFQTQIENNGQNLSQGQRQLIAIARAVLA 526
Cdd:PRK13644 79 VGIVFQnpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEI-----GLEKYRHRSPKTLSGGQGQCVALAGILTM 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 527 NKSILILDEATSNIDSSTEEIIQASLLKIMES-KTSFVIAHRLSTIKTADLIIVVNNGEIIEIGTHKNLI 595
Cdd:PRK13644 154 EPECLIFDEVTSMLDPDSGIAVLERIKKLHEKgKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
371-596 |
2.36e-15 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 75.82 E-value: 2.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 371 IEFKNVSFKYDINSKkyqLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNN------ 444
Cdd:PRK11124 3 IQLNGINCFYGAHQA---LFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTPSdkaire 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 445 LREHMSVVLQD-------TFMFNdTIENNIK-LG-DKNATKEDveraanlsnAIHFIKTLpngfqtQIENNG----QNLS 511
Cdd:PRK11124 80 LRRNVGMVFQQynlwphlTVQQN-LIEAPCRvLGlSKDQALAR---------AEKLLERL------RLKPYAdrfpLHLS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 512 QGQRQLIAIARAVLANKSILILDEATSNIDSSteeiIQASLLKIMESK-----TSFVIAHRLSTI-KTADLIIVVNNGEI 585
Cdd:PRK11124 144 GGQQQRVAIARALMMEPQVLLFDEPTAALDPE----ITAQIVSIIRELaetgiTQVIVTHEVEVArKTASRVVYMENGHI 219
|
250
....*....|.
gi 502819783 586 IEIGTHKNLIQ 596
Cdd:PRK11124 220 VEQGDASCFTQ 230
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
371-590 |
3.12e-15 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 77.15 E-value: 3.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 371 IEFKNVSFKYDINSKKYQ-LYNASFVAKPGQTVAIVGPTGAGKTT---IINLLGKfydYNSGSIKIDGYELRNIKTNNLR 446
Cdd:PRK11153 2 IELKNISKVFPQGGRTIHaLNNVSLHIPAGEIFGVIGASGAGKSTlirCINLLER---PTSGRVLVDGQDLTALSEKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 447 E---HMSVVLQDtfmFN----DTIENNIKLGDK--NATKEDVERAAN-------LSnaiHFIKTLPngfqtqienngQNL 510
Cdd:PRK11153 79 KarrQIGMIFQH---FNllssRTVFDNVALPLElaGTPKAEIKARVTellelvgLS---DKADRYP-----------AQL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 511 SQGQRQLIAIARAvLANK-SILILDEATSNIDSSTEEIIQASLLKIME--SKTSFVIAHRLSTIK-TADLIIVVNNGEII 586
Cdd:PRK11153 142 SGGQKQRVAIARA-LASNpKVLLCDEATSALDPATTRSILELLKDINRelGLTIVLITHEMDVVKrICDRVAVIDAGRLV 220
|
....
gi 502819783 587 EIGT 590
Cdd:PRK11153 221 EQGT 224
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
370-586 |
3.87e-15 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 78.61 E-value: 3.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 370 LIEFKNVSFKYDINSKKYQ-LYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNL--- 445
Cdd:PRK10535 4 LLELKDIRRSYPSGEEQVEvLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaql 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 446 -REHMSVVLQDTFMFND-TIENNIKLgdkNATKEDVERAANLSNAIHFIKTLpnGFQTQIENNGQNLSQGQRQLIAIARA 523
Cdd:PRK10535 84 rREHFGFIFQRYHLLSHlTAAQNVEV---PAVYAGLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502819783 524 VLANKSILILDEATSNIDS-STEEIIqaSLLKIMESK--TSFVIAHRLSTIKTADLIIVVNNGEII 586
Cdd:PRK10535 159 LMNGGQVILADEPTGALDShSGEEVM--AILHQLRDRghTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
384-569 |
5.31e-15 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 74.85 E-value: 5.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 384 SKKYQ--------LYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNN---LREH-MSV 451
Cdd:PRK11629 12 CKRYQegsvqtdvLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRNQkLGF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 452 VLQDTFMFND--TIEN---NIKLGDKNaTKEDVERAANLSNAIhfiktlpnGFQTQIENNGQNLSQGQRQLIAIARAVLA 526
Cdd:PRK11629 92 IYQFHHLLPDftALENvamPLLIGKKK-PAEINSRALEMLAAV--------GLEHRANHRPSELSGGERQRVAIARALVN 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 502819783 527 NKSILILDEATSNIDSSTEEIIQASLLKI-MESKTSF-VIAHRLS 569
Cdd:PRK11629 163 NPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFlVVTHDLQ 207
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
371-594 |
5.45e-15 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 76.68 E-value: 5.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 371 IEFKNVSFKYDINSkkyQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNlREhMS 450
Cdd:PRK11432 7 VVLKNITKRFGSNT---VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ-RD-IC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 451 VVLQDTFMF-NDTIENNIKLGDKNATKEDVERAANLSNAIHFIKTlpNGFQT----QIenngqnlSQGQRQLIAIARAVL 525
Cdd:PRK11432 82 MVFQSYALFpHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDL--AGFEDryvdQI-------SGGQQQRVALARALI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 526 ANKSILILDEATSNIDssteeiiqASLLKIMESK----------TSFVIAHRLS-TIKTADLIIVVNNGEIIEIGTHKNL 594
Cdd:PRK11432 153 LKPKVLLFDEPLSNLD--------ANLRRSMREKirelqqqfniTSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
393-590 |
9.26e-15 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 75.77 E-value: 9.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 393 SFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRN---IKTNNLREHMSVVLQDTF-MFN------DT 462
Cdd:PRK11308 35 SFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKadpEAQKLLRQKIQIVFQNPYgSLNprkkvgQI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 463 IENNIKLGDKNATKEDVERAANLSNAI----HFIKTLPNGFqtqienngqnlSQGQRQLIAIARAVLANKSILILDEATS 538
Cdd:PRK11308 115 LEEPLLINTSLSAAERREKALAMMAKVglrpEHYDRYPHMF-----------SGGQRQRIAIARALMLDPDVVVADEPVS 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502819783 539 NIDSSteeiIQASLLKIM-----ESKTSFV-IAHRLSTIK-TADLIIVVNNGEIIEIGT 590
Cdd:PRK11308 184 ALDVS----VQAQVLNLMmdlqqELGLSYVfISHDLSVVEhIADEVMVMYLGRCVEKGT 238
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
371-590 |
1.04e-14 |
|
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: 77.15 E-value: 1.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 371 IEFKNVSFKYDinsKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDY--NSGSI------------------ 430
Cdd:TIGR03269 1 IEVKNLTKKFD---GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYepTSGRIiyhvalcekcgyverpsk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 431 ---------------KIDGYELRNIKTNNLREHMSVVLQDTFMF--NDTIENNI-----KLGDKNatKEDVERAANLSNA 488
Cdd:TIGR03269 78 vgepcpvcggtlepeEVDFWNLSDKLRRRIRKRIAIMLQRTFALygDDTVLDNVlealeEIGYEG--KEAVGRAVDLIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 489 IHFiktlpngfQTQIENNGQNLSQGQRQLIAIARAVLANKSILILDEATSNIDSSTEEIIQASLLK-IMESKTSFVIAHR 567
Cdd:TIGR03269 156 VQL--------SHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEaVKASGISMVLTSH 227
|
250 260
....*....|....*....|....*
gi 502819783 568 LSTI--KTADLIIVVNNGEIIEIGT 590
Cdd:TIGR03269 228 WPEVieDLSDKAIWLENGEIKEEGT 252
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
81-346 |
1.11e-14 |
|
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: 74.83 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 81 LVILGLVFIAYGFFRYFDAYMYIKVSYQTSSRM----RKEAMHKLIKMPISYYDKQKAGNLISTLINDINNVSNTMYNTI 156
Cdd:cd18546 38 LLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLlydlRLRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 157 NQFFSSIFNvLLSIIAMMFVASF----ITLIVVPLalfLFFISLIVIKKAQPYFVKVQNLFGDLNAFVEENLANTKVMNA 232
Cdd:cd18546 118 VQLVVSLLT-LVGIAVVLLVLDPrlalVALAALPP---LALATRWFRRRSSRAYRRARERIAAVNADLQETLAGIRVVQA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 233 FDQQD---NIFNEFKKITRGIKLTSFKADAIarssepWFGITSGIANLCVAVlavsfyiykipVGGIGGLGTNpDGTATS 309
Cdd:cd18546 194 FRRERrnaERFAELSDDYRDARLRAQRLVAI------YFPGVELLGNLATAA-----------VLLVGAWRVA-AGTLTV 255
|
250 260 270
....*....|....*....|....*....|....*..
gi 502819783 310 GLIVTFISLNWNFMGPFQNLLNINFSFQMGLASSSRV 346
Cdd:cd18546 256 GVLVAFLLYLRRFFAPIQQLSQVFDSYQQARAALEKI 292
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
81-346 |
1.17e-14 |
|
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: 74.83 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 81 LVILGLVFIAYGFF---RYFDAymyiKVSYQTSSRMRKEAMHKLIKMPISYYDKQKAGNLISTLINDInnvsntmyNTIN 157
Cdd:cd18543 43 LLLLALGVAEAVLSflrRYLAG----RLSLGVEHDLRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDL--------SLVQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 158 QFFS-------SIFNVLLSIIAMMFVASFITLIVVPLALFLFFISLIVIKKAQPYFVKVQNLFGDLNAFVEENLANTKVM 230
Cdd:cd18543 111 RFLAfgpfllgNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFRRRYFPASRRAQDQAGDLATVVEESVTGIRVV 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 231 NAFDQQDNIFNEFKKITRGIKLTSF-KADAIARSSePWFGITSGIANlcVAVLAVsfyiykipvggiGGLGTnPDGTATS 309
Cdd:cd18543 191 KAFGRERRELDRFEAAARRLRATRLrAARLRARFW-PLLEALPELGL--AAVLAL------------GGWLV-ANGSLTL 254
|
250 260 270
....*....|....*....|....*....|....*..
gi 502819783 310 GLIVTFISLNWNFMGPFQNLLNINFSFQMGLASSSRV 346
Cdd:cd18543 255 GTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
370-586 |
1.22e-14 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 73.76 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 370 LIEFKNVSFKYdinSKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNN-LREH 448
Cdd:PRK11614 5 MLSFDKVSAHY---GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 449 MSVVLQDTFMFND-TIENNIKLG----DKNATKEDVERAANLsnaihfiktLPNGFQTQIENNGqNLSQGQRQLIAIARA 523
Cdd:PRK11614 82 VAIVPEGRRVFSRmTVEENLAMGgffaERDQFQERIKWVYEL---------FPRLHERRIQRAG-TMSGGEQQMLAIGRA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502819783 524 VLANKSILILDEATSNIdssTEEIIQASLLKIM----ESKTSFVIAHRLS-TIKTADLIIVVNNGEII 586
Cdd:PRK11614 152 LMSQPRLLLLDEPSLGL---APIIIQQIFDTIEqlreQGMTIFLVEQNANqALKLADRGYVLENGHVV 216
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
370-596 |
1.22e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 74.77 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 370 LIEFKNVSFKYDINS--KKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNN--- 444
Cdd:PRK13643 1 MIKFEKVNYTYQPNSpfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeik 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 445 -LREHMSVVLQ--DTFMFNDTIENNIKLGDKN--ATKEDVERAAnlSNAIHFIktlpnGFQTQI-ENNGQNLSQGQRQLI 518
Cdd:PRK13643 81 pVRKKVGVVFQfpESQLFEETVLKDVAFGPQNfgIPKEKAEKIA--AEKLEMV-----GLADEFwEKSPFELSGGQMRRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 519 AIARAVLANKSILILDEATSNIDSSTeeiiQASLLKIMES-----KTSFVIAHRLSTIKT-ADLIIVVNNGEIIEIGTHK 592
Cdd:PRK13643 154 AIAGILAMEPEVLVLDEPTAGLDPKA----RIEMMQLFESihqsgQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPS 229
|
....
gi 502819783 593 NLIQ 596
Cdd:PRK13643 230 DVFQ 233
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
371-594 |
1.25e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 74.30 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 371 IEFKNVSFKYDinSKKYqLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYnSGSIKIDG---------YElRNIK 441
Cdd:PRK14258 8 IKVNNLSFYYD--TQKI-LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNEL-ESEVRVEGrveffnqniYE-RRVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 442 TNNLREHMSVVLQDTFMFNDTIENNIKLGDK----------NATKEDVERAANLSNAIhfiktlpngfQTQIENNGQNLS 511
Cdd:PRK14258 83 LNRLRRQVSMVHPKPNLFPMSVYDNVAYGVKivgwrpkleiDDIVESALKDADLWDEI----------KHKIHKSALDLS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 512 QGQRQLIAIARAVLANKSILILDEATSNIDSST----EEIIQASLLKimESKTSFVIAHRLSTI-KTADLIIVVNN---- 582
Cdd:PRK14258 153 GGQQQRLCIARALAVKPKVLLMDEPCFGLDPIAsmkvESLIQSLRLR--SELTMVIVSHNLHQVsRLSDFTAFFKGnenr 230
|
250
....*....|...
gi 502819783 583 -GEIIEIGTHKNL 594
Cdd:PRK14258 231 iGQLVEFGLTKKI 243
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
371-588 |
2.42e-14 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 75.78 E-value: 2.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 371 IEFKNVSFKYDINSkkYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNLREHMS 450
Cdd:PRK10522 323 LELRNVTFAYQDNG--FSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFS 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 451 VVLQDTFMFNDTIENniklGDKNATKEDVERaanlsnaihFIKTLPNGFQTQIENN---GQNLSQGQRQLIAIARAVLAN 527
Cdd:PRK10522 401 AVFTDFHLFDQLLGP----EGKPANPALVEK---------WLERLKMAHKLELEDGrisNLKLSKGQKKRLALLLALAEE 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502819783 528 KSILILDEATSNIDSSTEEIIQASLLKIMES--KTSFVIAHRLSTIKTADLIIVVNNGEIIEI 588
Cdd:PRK10522 468 RDILLLDEWAADQDPHFRREFYQVLLPLLQEmgKTIFAISHDDHYFIHADRLLEMRNGQLSEL 530
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
371-590 |
4.95e-14 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 73.96 E-value: 4.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 371 IEFKNVSfKYDINSKkyQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNlrEHMS 450
Cdd:PRK10851 3 IEIANIK-KSFGRTQ--VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 451 VVLQDTFMFND-TIENNIKLG----------DKNATKEDVERAANLSNAIHfiktLPNGFQTQienngqnLSQGQRQLIA 519
Cdd:PRK10851 78 FVFQHYALFRHmTVFDNIAFGltvlprrerpNAAAIKAKVTQLLEMVQLAH----LADRYPAQ-------LSGGQKQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502819783 520 IARAVLANKSILILDEATSNIDSSTEEIIQASLLKIMESK--TS-FVIAHRLSTIKTADLIIVVNNGEIIEIGT 590
Cdd:PRK10851 147 LARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELkfTSvFVTHDQEEAMEVADRVVVMSQGNIEQAGT 220
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
371-586 |
4.99e-14 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 71.98 E-value: 4.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 371 IEFKNVSFKYDINSK--------------KYQLYNA----SFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKI 432
Cdd:cd03267 1 IEVSNLSKSYRVYSKepgligslkslfkrKYREVEAlkgiSFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 433 DG---YELRniktNNLREHMSVVL------------QDTFMFNDTIENNiklgDKNATKEDVERAANLSNAIHFIKTlpn 497
Cdd:cd03267 81 AGlvpWKRR----KKFLRRIGVVFgqktqlwwdlpvIDSFYLLAAIYDL----PPARFKKRLDELSELLDLEELLDT--- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 498 gfqtqienNGQNLSQGQRQLIAIARAVLANKSILILDEATSNIDSSTEEIIQASLLKIMESKTSFVI--AHRLSTI-KTA 574
Cdd:cd03267 150 --------PVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLltSHYMKDIeALA 221
|
250
....*....|..
gi 502819783 575 DLIIVVNNGEII 586
Cdd:cd03267 222 RRVLVIDKGRLL 233
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
371-589 |
1.45e-13 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 70.84 E-value: 1.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 371 IEFKNVSFKYDinsKKYQLYNASFVAKPGQTVAIVGPTGAGKTT---IINLLGKFYDYN--SGSIKIDGYEL--RNIKTN 443
Cdd:COG1117 12 IEVRNLNVYYG---DKQALKDINLDIPENKVTALIGPSGCGKSTllrCLNRMNDLIPGArvEGEILLDGEDIydPDVDVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 444 NLREHMSVVLQDTFMFNDTIENNIKLG-------DKNATKEDVERA---ANLSNaihfiktlpngfqtqiE------NNG 507
Cdd:COG1117 89 ELRRRVGMVFQKPNPFPKSIYDNVAYGlrlhgikSKSELDEIVEESlrkAALWD----------------EvkdrlkKSA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 508 QNLSQGQRQLIAIARAvLANK-SILILDEATSNIDS-ST---EEIIQAslLKimeSKTSFVI-------AHRLSTiKTAd 575
Cdd:COG1117 153 LGLSGGQQQRLCIARA-LAVEpEVLLMDEPTSALDPiSTakiEELILE--LK---KDYTIVIvthnmqqAARVSD-YTA- 224
|
250
....*....|....
gi 502819783 576 liiVVNNGEIIEIG 589
Cdd:COG1117 225 ---FFYLGELVEFG 235
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
383-589 |
1.60e-13 |
|
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: 70.38 E-value: 1.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 383 NSKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLL-GKFYDYN--SGSIKIDGYELRNIKTnnlREHMSVVLQ-DTFM 458
Cdd:cd03234 17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsGRVEGGGttSGQILFNGQPRKPDQF---QKCVAYVRQdDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 459 FNDTIE------NNIKLGDKNATKEDVERAANLSnaihfIKTLPNgfqTQIENNG-QNLSQGQRQLIAIARAVLANKSIL 531
Cdd:cd03234 94 PGLTVRetltytAILRLPRKSSDAIRKKRVEDVL-----LRDLAL---TRIGGNLvKGISGGERRRVSIAVQLLWDPKVL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502819783 532 ILDEATSNIDSSTE-EIIQasLLKIMESKTSFVIA--H--RLSTIKTADLIIVVNNGEIIEIG 589
Cdd:cd03234 166 ILDEPTSGLDSFTAlNLVS--TLSQLARRNRIVILtiHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
386-589 |
1.63e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 73.20 E-value: 1.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 386 KYQLYNASFVAKPGQTVAIVGPTGAGKTT----IINLLGkfydyNSGSIKIDGYELRNIKTNNL---REHMSVVLQDTF- 457
Cdd:PRK15134 299 NVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPNs 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 458 MFN------DTIENNIKLGDKNATKEdvERAANLSNAIHFI-------KTLPNGFqtqienngqnlSQGQRQLIAIARAV 524
Cdd:PRK15134 374 SLNprlnvlQIIEEGLRVHQPTLSAA--QREQQVIAVMEEVgldpetrHRYPAEF-----------SGGQRQRIAIARAL 440
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502819783 525 LANKSILILDEATSNIDSSTEEIIQAsLLKIMESKtsfviaHRLSTIKTA-DL---------IIVVNNGEIIEIG 589
Cdd:PRK15134 441 ILKPSLIILDEPTSSLDKTVQAQILA-LLKSLQQK------HQLAYLFIShDLhvvralchqVIVLRQGEVVEQG 508
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
389-596 |
1.81e-13 |
|
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: 70.25 E-value: 1.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 389 LYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNL-REHMSVVLQDTFMFND-TIENN 466
Cdd:TIGR03410 16 LRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaRAGIAYVPQGREIFPRlTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 467 IKLG---DKNATKEDVERAANLSNAIHFIKTLPNGfqtqienngqNLSQGQRQLIAIARAVLANKSILILDEATSNIDSS 543
Cdd:TIGR03410 96 LLTGlaaLPRRSRKIPDEIYELFPVLKEMLGRRGG----------DLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502819783 544 TEEIIQASLLKIMESK--TSFVIAHRLS-TIKTADLIIVVNNGEIIEIGTHKNLIQ 596
Cdd:TIGR03410 166 IIKDIGRVIRRLRAEGgmAILLVEQYLDfARELADRYYVMERGRVVASGAGDELDE 221
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
368-594 |
1.94e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 70.89 E-value: 1.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 368 DGLIEFKNVSFKY---DINSKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIK-TN 443
Cdd:PRK13633 2 NEMIKCKNVSYKYesnEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 444 NLREHMSVVLQ--DTFMFNDTIENNIKLGDKN------ATKEDVERAANLSNAIHFIKTLPNgfqtqienngqNLSQGQR 515
Cdd:PRK13633 82 DIRNKAGMVFQnpDNQIVATIVEEDVAFGPENlgippeEIRERVDESLKKVGMYEYRRHAPH-----------LLSGGQK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 516 QLIAIArAVLANK-SILILDEATSNID-SSTEEIIqaSLLKIMESK---TSFVIAHRLSTIKTADLIIVVNNGEIIEIGT 590
Cdd:PRK13633 151 QRVAIA-GILAMRpECIIFDEPTAMLDpSGRREVV--NTIKELNKKygiTIILITHYMEEAVEADRIIVMDSGKVVMEGT 227
|
....
gi 502819783 591 HKNL 594
Cdd:PRK13633 228 PKEI 231
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
391-600 |
2.34e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 69.13 E-value: 2.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 391 NASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGyelRNIKTNNLREHMSVV-----LQDTFmfndTIEN 465
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG---GDIDDPDVAEACHYLghrnaMKPAL----TVAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 466 NIKL--GDKNATKEDVERAA---NLSNAIHfiktLPngfqtqiennGQNLSQGQRQLIAIARAVLANKSILILDEATSNI 540
Cdd:PRK13539 93 NLEFwaAFLGGEELDIAAALeavGLAPLAH----LP----------FGYLSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502819783 541 DSSTEEIIQAsllkimesktsfVIAHRLSTiktadliivvnnGEIIEIGTHKNL-------IQLDGF 600
Cdd:PRK13539 159 DAAAVALFAE------------LIRAHLAQ------------GGIVIAATHIPLglpgareLDLGPF 201
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
389-589 |
2.85e-13 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 69.42 E-value: 2.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 389 LYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELrnikTNNLREHMsVVLQDTFMFN-DTIENNI 467
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQI----TEPGPDRM-VVFQNYSLLPwLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 468 KLGDK--NATKEDVERAANLSNAIHFIktlpnGFQTQIENNGQNLSQGQRQLIAIARAVLANKSILILDEATSNIDSSTE 545
Cdd:TIGR01184 76 ALAVDrvLPDLSKSERRAIVEEHIALV-----GLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 502819783 546 EIIQASLLKIMESK--TSFVIAHRL-STIKTADLIIVVNNGEIIEIG 589
Cdd:TIGR01184 151 GNLQEELMQIWEEHrvTVLMVTHDVdEALLLSDRVVMLTNGPAANIG 197
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
370-548 |
3.51e-13 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 69.13 E-value: 3.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 370 LIEFKNVSFKYdiNSKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNN---LR 446
Cdd:PRK10908 1 MIRFEHVSKAY--LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 447 EHMSVVLQDTFMFND-TIENN--IKLGDKNATKEDVERaaNLSNAIHFIktlpnGFQTQIENNGQNLSQGQRQLIAIARA 523
Cdd:PRK10908 79 RQIGMIFQDHHLLMDrTVYDNvaIPLIIAGASGDDIRR--RVSAALDKV-----GLLDKAKNFPIQLSGGEQQRVGIARA 151
|
170 180
....*....|....*....|....*
gi 502819783 524 VLANKSILILDEATSNIDSSTEEII 548
Cdd:PRK10908 152 VVNKPAVLLADEPTGNLDDALSEGI 176
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
391-590 |
3.66e-13 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 69.63 E-value: 3.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 391 NASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNLrEHMSVV--LQDTFMFND--TIEN- 465
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQI-ARMGVVrtFQHVRLFREmtVIENl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 466 ----------NIKLG-DKNATKEDVERAAnLSNAIHFIKTLpnGFQTQIENNGQNLSQGQRQLIAIARAVLANKSILILD 534
Cdd:PRK11300 102 lvaqhqqlktGLFSGlLKTPAFRRAESEA-LDRAATWLERV--GLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502819783 535 EATSNIDSSTEEIIQA--SLLKIMESKTSFVIAHRLSTI-KTADLIIVVNNGEIIEIGT 590
Cdd:PRK11300 179 EPAAGLNPKETKELDEliAELRNEHNVTVLLIEHDMKLVmGISDRIYVVNQGTPLANGT 237
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
370-578 |
4.02e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 68.97 E-value: 4.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 370 LIEFKNVSFKydINSKKYqLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNLREHM 449
Cdd:PRK10247 7 LLQLQNVGYL--AGDAKI-LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 450 SVVLQDTFMFNDTIENNIKLG--------DKNATKEDVERAAnlsnaihfiktLPngfQTQIENNGQNLSQGQRQLIAIA 521
Cdd:PRK10247 84 SYCAQTPTLFGDTVYDNLIFPwqirnqqpDPAIFLDDLERFA-----------LP---DTILTKNIAELSGGEKQRISLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502819783 522 RAVLANKSILILDEATSNIDSSTEEIIQASLLKIMESKTSFVI--AHRLSTIKTADLII 578
Cdd:PRK10247 150 RNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLwvTHDKDEINHADKVI 208
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
389-590 |
4.36e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 71.88 E-value: 4.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 389 LYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNS--GSIKIDGYELR--NIKTNN------------LREHMSvV 452
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEELQasNIRDTEragiaiihqelaLVKELS-V 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 453 LQDTFMFNDTIENNIKlgDKNATkedVERAANLSNAIHfIKTLPNgfqTQIEnngqNLSQGQRQLIAIARAVLANKSILI 532
Cdd:PRK13549 100 LENIFLGNEITPGGIM--DYDAM---YLRAQKLLAQLK-LDINPA---TPVG----NLGLGQQQLVEIAKALNKQARLLI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502819783 533 LDEATSNIDSSTEEIiqasLLKIMES-KTSFV----IAHRLSTIKT-ADLIIVVNNGEiiEIGT 590
Cdd:PRK13549 167 LDEPTASLTESETAV----LLDIIRDlKAHGIaciyISHKLNEVKAiSDTICVIRDGR--HIGT 224
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
368-590 |
5.80e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 70.26 E-value: 5.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 368 DGLIEFKNVSFKYDINSKK--YQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYEL-------- 437
Cdd:PRK13631 19 DIILRVKNLYCVFDEKQENelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIgdkknnhe 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 438 -------RNIKT-NNLREHMSVVLQ--DTFMFNDTIENNIKLGDKnATKEDVERAANLSnAIHFIKT-LPNGFqtqIENN 506
Cdd:PRK13631 99 litnpysKKIKNfKELRRRVSMVFQfpEYQLFKDTIEKDIMFGPV-ALGVKKSEAKKLA-KFYLNKMgLDDSY---LERS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 507 GQNLSQGQRQLIAIARAVLANKSILILDEATSNIDSSTE-EIIQASLLKIMESKTSFVIAHRLSTI-KTADLIIVVNNGE 584
Cdd:PRK13631 174 PFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEhEMMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGK 253
|
....*.
gi 502819783 585 IIEIGT 590
Cdd:PRK13631 254 ILKTGT 259
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
403-589 |
8.75e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 68.72 E-value: 8.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 403 AIVGPTGAGKTTIINLLGKFYDYN-----SGSIKIDGYELRNIKTN--NLREHMSVVLQDTFMF-NDTIENNIKLG---- 470
Cdd:PRK14267 34 ALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDVDpiEVRREVGMVFQYPNPFpHLTIYDNVAIGvkln 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 471 ----DKNATKEDVERAanLSNAihfikTLPNGFQTQIENNGQNLSQGQRQLIAIARAVLANKSILILDEATSNIDSSTEE 546
Cdd:PRK14267 114 glvkSKKELDERVEWA--LKKA-----ALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTA 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 502819783 547 IIQASLLKIMESKTSFVIAHR-LSTIKTADLIIVVNNGEIIEIG 589
Cdd:PRK14267 187 KIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVG 230
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
367-590 |
1.54e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 68.28 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 367 IDGLIEFKNVS--FKYDINSKKYQLYNA----SFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYEL--- 437
Cdd:PRK15112 1 VETLLEVRNLSktFRYRTGWFRRQTVEAvkplSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLhfg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 438 ----RNIKTNNLREHMSVVLQDTFMFNDTIENNIKLgdkNATKEDVERAANLSNAIHFIKTLPNgfqtQIENNGQNLSQG 513
Cdd:PRK15112 81 dysyRSQRIRMIFQDPSTSLNPRQRISQILDFPLRL---NTDLEPEQREKQIIETLRQVGLLPD----HASYYPHMLAPG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 514 QRQLIAIARAVLANKSILILDEATSNIDSSTEEIIQASLLKIMESK-TSFV-IAHRLSTIK-TADLIIVVNNGEIIEIGT 590
Cdd:PRK15112 154 QKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQgISYIyVTQHLGMMKhISDQVLVMHQGEVVERGS 233
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
386-604 |
1.63e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 70.46 E-value: 1.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 386 KYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGkFYDYN----SGSIKIDGY-----ELR-----------NIKTNNL 445
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVLLNGMpidakEMRaisayvqqddlFIPTLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 446 REHMsvvlqdTFMfndtieNNIKLGDKNATKEDVER------AANLSNAIHFIktlpngfqTQIENNGQNLSQGQRQLIA 519
Cdd:TIGR00955 117 REHL------MFQ------AHLRMPRRVTKKEKRERvdevlqALGLRKCANTR--------IGVPGRVKGLSGGERKRLA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 520 IARAVLANKSILILDEATSNIDS-STEEIIQAslLKIMESKTSFVIAhrlsTIK--TADL------IIVVNNGEIIEIGT 590
Cdd:TIGR00955 177 FASELLTDPPLLFCDEPTSGLDSfMAYSVVQV--LKGLAQKGKTIIC----TIHqpSSELfelfdkIILMAEGRVAYLGS 250
|
250
....*....|....
gi 502819783 591 HKNLIQldgFYSNL 604
Cdd:TIGR00955 251 PDQAVP---FFSDL 261
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
375-594 |
1.63e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 67.76 E-value: 1.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 375 NVSFKYDINSKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGY------ELRNIKTNNLREH 448
Cdd:PRK14246 12 NISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 449 MSVVLQDTFMF-NDTIENNIK-------LGDKNATKEDVE---RAANLSNAIHfiktlpngfqTQIENNGQNLSQGQRQL 517
Cdd:PRK14246 92 VGMVFQQPNPFpHLSIYDNIAyplkshgIKEKREIKKIVEeclRKVGLWKEVY----------DRLNSPASQLSGGQQQR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502819783 518 IAIARAVLANKSILILDEATSNIDSSTEEIIQASLLKIMESKTSFVIAHRLSTI-KTADLIIVVNNGEIIEIGTHKNL 594
Cdd:PRK14246 162 LTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEI 239
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
371-558 |
2.22e-12 |
|
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: 66.11 E-value: 2.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 371 IEFKNVSFKYDINSKKYQLY-NASFVAKPGQTVAIVGPTGAGKTTIINLLG--KFYDYNSGSIKIDGYELrniKTNNLRE 447
Cdd:cd03232 4 LTWKNLNYTVPVKGGKRQLLnNISGYVKPGTLTALMGESGAGKTTLLDVLAgrKTAGVITGEILINGRPL---DKNFQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 448 HMSVVLQDTFMFNDTIenniklgdknatKEDVERAANLsnaihfiktlpngfqtqienngQNLSQGQRQLIAIARAVLAN 527
Cdd:cd03232 81 TGYVEQQDVHSPNLTV------------REALRFSALL----------------------RGLSVEQRKRLTIGVELAAK 126
|
170 180 190
....*....|....*....|....*....|.
gi 502819783 528 KSILILDEATSNIDSSTEEIIQASLLKIMES 558
Cdd:cd03232 127 PSILFLDEPTSGLDSQAAYNIVRFLKKLADS 157
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
371-594 |
2.53e-12 |
|
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: 66.62 E-value: 2.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 371 IEFKNVSFKYDINSKkyqLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNiKTNNLREHMS 450
Cdd:cd03265 1 IEVENLVKKYGDFEA---VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 451 VVLQDTFMFND-TIENNIKL-----GDKNAtkEDVERAANLSNAI-------HFIKTLPNGFQTQIEnngqnlsqgqrql 517
Cdd:cd03265 77 IVFQDLSVDDElTGWENLYIharlyGVPGA--ERRERIDELLDFVglleaadRLVKTYSGGMRRRLE------------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 518 iaIARAVLANKSILILDEATSNIDSSTE----EIIQAslLKIMESKTSFVIAHRLSTI-KTADLIIVVNNGEIIEIGTHK 592
Cdd:cd03265 142 --IARSLVHRPEVLFLDEPTIGLDPQTRahvwEYIEK--LKEEFGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPE 217
|
..
gi 502819783 593 NL 594
Cdd:cd03265 218 EL 219
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
73-245 |
3.08e-12 |
|
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: 67.51 E-value: 3.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 73 NVKSFSIWLVILGLVFIAYGFFRYFDAYMYIKVSYQTSSRMRKEAMHKLIKMPISYYDKQKAGNLISTLINDINNVSNTM 152
Cdd:cd18575 31 NTALLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 153 YNTInqffsSIF--NVLLSI--IAMMFVASF----ITLIVVPLALF-LFFISLIVIKKAQpyfvKVQNLFGDLNAFVEEN 223
Cdd:cd18575 111 GSSL-----SIAlrNLLLLIggLVMLFITSPkltlLVLLVIPLVVLpIILFGRRVRRLSR----ASQDRLADLSAFAEET 181
|
170 180
....*....|....*....|..
gi 502819783 224 LANTKVMNAFDQQDNIFNEFKK 245
Cdd:cd18575 182 LSAIKTVQAFTREDAERQRFAT 203
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
389-598 |
3.10e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 69.17 E-value: 3.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 389 LYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNN-LREHMSVVLQDTFMFND-TIENN 466
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAaLAAGVAIIYQELHLVPEmTVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 467 IKLGdknatkedveraaNLSNAIHFI--KTLPNGFQTQIENNGQN---------LSQGQRQLIAIARAVLANKSILILDE 535
Cdd:PRK11288 100 LYLG-------------QLPHKGGIVnrRLLNYEAREQLEHLGVDidpdtplkyLSIGQRQMVEIAKALARNARVIAFDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502819783 536 ATSNIdsSTEEIIQasLLKIM-----ESKTSFVIAHRLSTI-KTADLIIVVNNGEIIEigTHKNLIQLD 598
Cdd:PRK11288 167 PTSSL--SAREIEQ--LFRVIrelraEGRVILYVSHRMEEIfALCDAITVFKDGRYVA--TFDDMAQVD 229
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
385-596 |
3.69e-12 |
|
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: 66.41 E-value: 3.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 385 KKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNN-LREHMSVVLQDTFMFND-T 462
Cdd:cd03218 12 KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKrARLGIGYLPQEASIFRKlT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 463 IENNIKLGDKNATKEDVERaanlsnaIHFIKTLPNGFQ-TQIENN-GQNLSQGQRQLIAIARAVLANKSILILDEATSNI 540
Cdd:cd03218 92 VEENILAVLEIRGLSKKER-------EEKLEELLEEFHiTHLRKSkASSLSGGERRRVEIARALATNPKFLLLDEPFAGV 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502819783 541 DSSTEEIIQASLLKIMESKTSFVIA-HRLS-TIKTADLIIVVNNGEIIEIGTHKNLIQ 596
Cdd:cd03218 165 DPIAVQDIQKIIKILKDRGIGVLITdHNVReTLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
395-553 |
4.77e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 65.96 E-value: 4.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 395 VAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNN---LR-EHMSVVLQdTFMFNDTIenniklg 470
Cdd:PRK10584 32 VVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEArakLRaKHVGFVFQ-SFMLIPTL------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 471 dkNATkEDVERAANL---------SNAIHFIKTLpnGFQTQIENNGQNLSQGQRQLIAIARAVLANKSILILDEATSNID 541
Cdd:PRK10584 104 --NAL-ENVELPALLrgessrqsrNGAKALLEQL--GLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
|
170
....*....|..
gi 502819783 542 SSTEEIIqASLL 553
Cdd:PRK10584 179 RQTGDKI-ADLL 189
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
397-594 |
5.58e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 66.09 E-value: 5.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 397 KPGQTVAIVGPTGAGKTTIINLLGKFYDYN-----SGSIKIDGYELRNIKTNNLREHMSVVLQ-DTFMFNDTIENNIKLG 470
Cdd:PRK14247 27 PDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIELRRRVQMVFQiPNPIPNLSIFENVALG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 471 DK-----NATKEDVERAAN-LSNAihfikTLPNGFQTQIENNGQNLSQGQRQLIAIARAVLANKSILILDEATSNIDSST 544
Cdd:PRK14247 107 LKlnrlvKSKKELQERVRWaLEKA-----QLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPEN 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 502819783 545 EEIIQASLLKIMESKTSFVIAH-RLSTIKTADLIIVVNNGEIIEIGTHKNL 594
Cdd:PRK14247 182 TAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
398-594 |
7.49e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 66.27 E-value: 7.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 398 PGQTV-AIVGPTGAGKTTIINLLGKFYD-----YNSGSIKIDGYELRNIK-TNNLREHMSVVLQDTFMFNDTIENNIKLG 470
Cdd:PRK14271 45 PARAVtSLMGPTGSGKTTFLRTLNRMNDkvsgyRYSGDVLLGGRSIFNYRdVLEFRRRVGMLFQRPNPFPMSIMDNVLAG 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 471 DKNATKEDVERAANLSNAIHFIKTLPNGFQTQIENNGQNLSQGQRQLIAIARAVLANKSILILDEATSNIDSSTEEIIQA 550
Cdd:PRK14271 125 VRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEE 204
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 502819783 551 SLLKIMESKTSFVIAHRLS-TIKTADLIIVVNNGEIIEIGTHKNL 594
Cdd:PRK14271 205 FIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
371-594 |
9.24e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 66.26 E-value: 9.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 371 IEFKNVSFKYDINSKKY--QLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSI-----------KIDGYE- 436
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTElkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkKTKEKEk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 437 -----------LRNIK-TNNLREHMSVVLQ--DTFMFNDTIENNIKLGdknATKEDVERAANLSNAIHFIKT--LPNGFq 500
Cdd:PRK13651 83 vleklviqktrFKKIKkIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFG---PVSMGVSKEEAKKRAAKYIELvgLDESY- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 501 tqIENNGQNLSQGQRQLIAIARAVLANKSILILDEATSNID-SSTEEIiqaslLKIM-----ESKTSFVIAHRL-STIKT 573
Cdd:PRK13651 159 --LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpQGVKEI-----LEIFdnlnkQGKTIILVTHDLdNVLEW 231
|
250 260
....*....|....*....|..
gi 502819783 574 ADLIIVVNNGEIIEIG-THKNL 594
Cdd:PRK13651 232 TKRTIFFKDGKIIKDGdTYDIL 253
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
385-588 |
1.45e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 64.21 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 385 KKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDgyelrnIKTNNLREHMSVvlqdtfmfndtIE 464
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD------VPDNQFGREASL-----------ID 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 465 NNIKLGDKNATKEdVERAANLSNAIHFIKTLPngfqtqienngqNLSQGQRQLIAIARAVLANKSILILDEATSNIDSST 544
Cdd:COG2401 105 AIGRKGDFKDAVE-LLNAVGLSDAVLWLRRFK------------ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQT 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 502819783 545 EEIIQASLLKIM-ESKTSFVIA-HRLSTIKT--ADLIIVVNNGEIIEI 588
Cdd:COG2401 172 AKRVARNLQKLArRAGITLVVAtHHYDVIDDlqPDLLIFVGYGGVPEE 219
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
345-589 |
1.59e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 67.19 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 345 RVFKILNLD---TKKPHVEDITIDKIDGLIEFKNVSFKYDINS--------KKYQLYNASFVAKPGQTVAIVGPTGAGKT 413
Cdd:PRK10261 285 RRFPLISLEhpaKQEPPIEQDTVVDGEPILQVRNLVTRFPLRSgllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKS 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 414 TIINLLGKFYDYNSGSIKIDGYELRNI---KTNNLREHMSVVLQDTFMFND---TIENNI-------KLGDKNATKEDV- 479
Cdd:PRK10261 365 TTGRALLRLVESQGGEIIFNGQRIDTLspgKLQALRRDIQFIFQDPYASLDprqTVGDSImeplrvhGLLPGKAAAARVa 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 480 ---ERAANL-SNAIHFiktlPNGFqtqienngqnlSQGQRQLIAIARAVLANKSILILDEATSNIDSSTEEIIQASLLKI 555
Cdd:PRK10261 445 wllERVGLLpEHAWRY----PHEF-----------SGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDL 509
|
250 260 270
....*....|....*....|....*....|....*..
gi 502819783 556 M-ESKTSFV-IAHRLSTI-KTADLIIVVNNGEIIEIG 589
Cdd:PRK10261 510 QrDFGIAYLfISHDMAVVeRISHRVAVMYLGQIVEIG 546
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
370-590 |
1.80e-11 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 64.79 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 370 LIEFKNVSFKYdinSKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNLREHM 449
Cdd:PRK13548 2 MLEARNLSVRL---GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 450 SVVLQD---TFMFndTIENNIKLG------DKNATKEDVERAANLSNAIHFIKTLpngFQTqienngqnLSQGQRQLIAI 520
Cdd:PRK13548 79 AVLPQHsslSFPF--TVEEVVAMGraphglSRAEDDALVAAALAQVDLAHLAGRD---YPQ--------LSGGEQQRVQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 521 ARaVLAN-------KSILILDEATSNIDssteeiI--QASLLKIMESKTS------FVIAHRLS-TIKTADLIIVVNNGE 584
Cdd:PRK13548 146 AR-VLAQlwepdgpPRWLLLDEPTSALD------LahQHHVLRLARQLAHerglavIVVLHDLNlAARYADRIVLLHQGR 218
|
....*.
gi 502819783 585 IIEIGT 590
Cdd:PRK13548 219 LVADGT 224
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
399-589 |
2.32e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 65.82 E-value: 2.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 399 GQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYEL-------RNI----KTNNLREHMSVVlqdtfmfnDTIENNI 467
Cdd:PRK11000 29 GEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMndvppaeRGVgmvfQSYALYPHLSVA--------ENMSFGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 468 KLG--DKNATKEDVERAANLSNAIHFIKTLPngfqtqienngQNLSQGQRQLIAIARAVLANKSILILDEATSNIDSSTE 545
Cdd:PRK11000 101 KLAgaKKEEINQRVNQVAEVLQLAHLLDRKP-----------KALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALR 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 502819783 546 -----EIiqASLLKIMESKTSFVIAHRLSTIKTADLIIVVNNGEIIEIG 589
Cdd:PRK11000 170 vqmriEI--SRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
371-589 |
2.83e-11 |
|
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: 63.71 E-value: 2.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 371 IEFKNVSFKYDINSKKYQLY-------------------NASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIK 431
Cdd:cd03220 1 IELENVSKSYPTYKGGSSSLkklgilgrkgevgefwalkDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 432 IDGyelrniktnnlrehmSVV----LQDTFMFNDTIENNIKLgdkNAT------KEDVERaanlsnaIHFIKT---LPNG 498
Cdd:cd03220 81 VRG---------------RVSsllgLGGGFNPELTGRENIYL---NGRllglsrKEIDEK-------IDEIIEfseLGDF 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 499 FQTQIenngQNLSQGQRQLIAIARAVLANKSILILDEATSNIDSSTEEIIQASLLKIMESKTSFVIA-HRLSTIK-TADL 576
Cdd:cd03220 136 IDLPV----KTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVsHDPSSIKrLCDR 211
|
250
....*....|...
gi 502819783 577 IIVVNNGEIIEIG 589
Cdd:cd03220 212 ALVLEKGKIRFDG 224
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
370-590 |
3.38e-11 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 66.00 E-value: 3.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 370 LIEFKNVSFKYDinSKKyQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNS--GSIKIDGYEL--RNIKTNNl 445
Cdd:TIGR02633 1 LLEMKGIVKTFG--GVK-ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLkaSNIRDTE- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 446 REHMSVVLQD-TFMFNDTIENNIKLGDKNATKEDVeraANLSNAIHFIKTLPNGFQTQIENNGQNLSQ---GQRQLIAIA 521
Cdd:TIGR02633 77 RAGIVIIHQElTLVPELSVAENIFLGNEITLPGGR---MAYNAMYLRAKNLLRELQLDADNVTRPVGDyggGQQQLVEIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502819783 522 RAVLANKSILILDEATSNIDSSTEEIIqASLLKIMESK--TSFVIAHRLSTIKT-ADLIIVVNNGEiiEIGT 590
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSLTEKETEIL-LDIIRDLKAHgvACVYISHKLNEVKAvCDTICVIRDGQ--HVAT 222
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
393-589 |
7.23e-11 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 64.48 E-value: 7.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 393 SFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNLREHMSVVLQDTFM-FNDTIENNIKLGD 471
Cdd:PRK09536 23 DLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFEFDVRQVVEMGR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 472 K-------NATKED---VERAANLSNAIHFIktlpngfqtqiENNGQNLSQGQRQLIAIARAVLANKSILILDEATSNID 541
Cdd:PRK09536 103 TphrsrfdTWTETDraaVERAMERTGVAQFA-----------DRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502819783 542 SS----TEEIIQaSLLKimESKTSFVIAHRLS-TIKTADLIIVVNNGEIIEIG 589
Cdd:PRK09536 172 INhqvrTLELVR-RLVD--DGKTAVAAIHDLDlAARYCDELVLLADGRVRAAG 221
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
341-567 |
8.47e-11 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 64.83 E-value: 8.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 341 ASSSRV--FKILNLDTKKPHVEDITIDKI-DGLIEFKNVSfkydINSKKYQ--LYNASFVAKPGQTVAIVGPTGAGKTTI 415
Cdd:COG4178 330 ATVDRLagFEEALEAADALPEAASRIETSeDGALALEDLT----LRTPDGRplLEDLSLSLKPGERLLITGPSGSGKSTL 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 416 INLLGKFYDYNSGSIKI-DGyelrniktnnlrEHMSVVLQDTFMFNDTIENNIK--LGDKNATKEDVE---RAANLSnai 489
Cdd:COG4178 406 LRAIAGLWPYGSGRIARpAG------------ARVLFLPQRPYLPLGTLREALLypATAEAFSDAELRealEAVGLG--- 470
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502819783 490 HFIKTLpngfqTQIENNGQNLSQGQRQLIAIARAVLANKSILILDEATSNIDSSTEEIIQASLLKIMESKTSFVIAHR 567
Cdd:COG4178 471 HLAERL-----DEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
391-592 |
1.94e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 63.51 E-value: 1.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 391 NASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRnIKT----NNLR-----EHMSVVlqDTFmfnd 461
Cdd:COG3845 23 DVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVR-IRSprdaIALGigmvhQHFMLV--PNL---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 462 TIENNIKLGDKNA------TKEDVERAANLSNAIHFiKTLPNgfqTQIEnngqNLSQGQRQLIAIARAVLANKSILILDE 535
Cdd:COG3845 96 TVAENIVLGLEPTkggrldRKAARARIRELSERYGL-DVDPD---AKVE----DLSVGEQQRVEILKALYRGARILILDE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502819783 536 ATSNIdsSTEEIiqASLLKIM-----ESKTSFVIAHRLSTIKT-ADLIIVVNNGEIieIGTHK 592
Cdd:COG3845 168 PTAVL--TPQEA--DELFEILrrlaaEGKSIIFITHKLREVMAiADRVTVLRRGKV--VGTVD 224
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
389-587 |
2.13e-10 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 61.63 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 389 LYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNN---LREHMSVVLQDTF-MFN--DT 462
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQrkaFRRDIQMVFQDSIsAVNprKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 463 IENNIK-----LGDKNATkEDVERAANLSNAIHfiktLPNGFQTQIEnngQNLSQGQRQLIAIARAVLANKSILILDEAT 537
Cdd:PRK10419 108 VREIIReplrhLLSLDKA-ERLARASEMLRAVD----LDDSVLDKRP---PQLSGGQLQRVCLARALAVEPKLLILDEAV 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502819783 538 SNIDSsteeIIQASLLKIME-----SKTSFV-IAHRLSTI-KTADLIIVVNNGEIIE 587
Cdd:PRK10419 180 SNLDL----VLQAGVIRLLKklqqqFGTACLfITHDLRLVeRFCQRVMVMDNGQIVE 232
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
371-589 |
2.33e-10 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 60.76 E-value: 2.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 371 IEFKNVSfkydinsKKYQLYNA----SFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGyelrNIKTNNLR 446
Cdd:cd03269 1 LEVENVT-------KRFGRVTAlddiSFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG----KPLDIAAR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 447 EHMSVVLQDTFMFNDT--IENNIKLGD-KNATKEDVERaanlsNAIHFIKTLpnGFQTQIENNGQNLSQGQRQLIAIARA 523
Cdd:cd03269 70 NRIGYLPEERGLYPKMkvIDQLVYLAQlKGLKKEEARR-----RIDEWLERL--ELSEYANKRVEELSKGNQQKVQFIAA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502819783 524 VLANKSILILDEATSNIDSSTEEIIQASLLKIMESKTSFVI-AHRLSTI-KTADLIIVVNNGEIIEIG 589
Cdd:cd03269 143 VIHDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILsTHQMELVeELCDRVLLLNKGRAVLYG 210
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
368-594 |
2.51e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 61.79 E-value: 2.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 368 DGLIEFKNVSFKYdiNSKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDG----YELRNIKtn 443
Cdd:PRK13636 3 DYILKVEELNYNY--SDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpidYSRKGLM-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 444 NLREHMSVVLQ--DTFMFNDTIENNIKLG------DKNATKEDVERAANLSNAIHfIKTLPNgfqtqienngQNLSQGQR 515
Cdd:PRK13636 79 KLRESVGMVFQdpDNQLFSASVYQDVSFGavnlklPEDEVRKRVDNALKRTGIEH-LKDKPT----------HCLSFGQK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 516 QLIAIARAVLANKSILILDEATSNIDS-STEEIIQASLLKIMESKTSFVIA-HRLSTIKT-ADLIIVVNNGEIIEIGTHK 592
Cdd:PRK13636 148 KRVAIAGVLVMEPKVLVLDEPTAGLDPmGVSEIMKLLVEMQKELGLTIIIAtHDIDIVPLyCDNVFVMKEGRVILQGNPK 227
|
..
gi 502819783 593 NL 594
Cdd:PRK13636 228 EV 229
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
371-434 |
4.47e-10 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 60.48 E-value: 4.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 371 IEFKNVSFKYDINSKKYQ-------------------LYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIK 431
Cdd:COG1134 5 IEVENVSKSYRLYHEPSRslkelllrrrrtrreefwaLKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
...
gi 502819783 432 IDG 434
Cdd:COG1134 85 VNG 87
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
371-567 |
5.04e-10 |
|
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: 58.70 E-value: 5.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 371 IEFKNVSFKYDINSKKYQlyNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGyelrniktnnlREHMS 450
Cdd:cd03223 1 IELENLSLATPDGRVLLK--DLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE-----------GEDLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 451 VVLQDTFMfndtienniKLGdknatkedveraaNLSNAIhfIKTLpngfqtqiennGQNLSQGQRQLIAIARAVLANKSI 530
Cdd:cd03223 68 FLPQRPYL---------PLG-------------TLREQL--IYPW-----------DDVLSGGEQQRLAFARLLLHKPKF 112
|
170 180 190
....*....|....*....|....*....|....*....
gi 502819783 531 LILDEATSNIDSSTEeiiqASLLKIMESK-TSFV-IAHR 567
Cdd:cd03223 113 VFLDEATSALDEESE----DRLYQLLKELgITVIsVGHR 147
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
389-587 |
5.17e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 62.11 E-value: 5.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 389 LYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNS--GSIKIDGyELRNIKTNNLREHMSVVL--QD----TFMfn 460
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDG-EVCRFKDIRDSEALGIVIihQElaliPYL-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 461 dTIENNIKLGDKNATKEDVERAANLSNAIHFIKT--LPNGFQTQIENNGqnlsQGQRQLIAIARAVLANKSILILDEATS 538
Cdd:NF040905 94 -SIAENIFLGNERAKRGVIDWNETNRRARELLAKvgLDESPDTLVTDIG----VGKQQLVEIAKALSKDVKLLILDEPTA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502819783 539 --NIDSSteeiiqASLLK-IMESK----TSFVIAHRLSTI-KTADLIIVVNNGEIIE 587
Cdd:NF040905 169 alNEEDS------AALLDlLLELKaqgiTSIIISHKLNEIrRVADSITVLRDGRTIE 219
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
391-596 |
5.92e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 59.91 E-value: 5.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 391 NASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTN-NLREHMSVVLQDTFMFN-----DTIE 464
Cdd:PRK10895 21 DVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHaRARRGIGYLPQEASIFRrlsvyDNLM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 465 NNIKLGDKNATKEDVERAANLSNAIHfIKTLPNgfqtqieNNGQNLSQGQRQLIAIARAVLANKSILILDEATSNIDSST 544
Cdd:PRK10895 101 AVLQIRDDLSAEQREDRANELMEEFH-IEHLRD-------SMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPIS 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502819783 545 EEIIQASLLKIMESKTSFVIA-HRL-STIKTADLIIVVNNGEIIEIGTHKNLIQ 596
Cdd:PRK10895 173 VIDIKRIIEHLRDSGLGVLITdHNVrETLAVCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
371-590 |
8.74e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 60.12 E-value: 8.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 371 IEFKNVSFKYDinSKKYqLYNASFVAKPGQTVAIVGPTGAGKTTII-NLLGkFYDYNSGSIKIDGYELRNIKTNN----- 444
Cdd:COG4152 2 LELKGLTKRFG--DKTA-VDDVSFTVPKGEIFGLLGPNGAGKTTTIrIILG-ILAPDSGEVLWDGEPLDPEDRRRigylp 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 445 ----LREHMSVVLQDTFmfndtiennikLGD-KNATKEDVERAANlsnaiHFIKTLpnGFQTQIENNGQNLSQGQRQLIA 519
Cdd:COG4152 78 eergLYPKMKVGEQLVY-----------LARlKGLSKAEAKRRAD-----EWLERL--GLGDRANKKVEELSKGNQQKVQ 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502819783 520 IARAVLANKSILILDEATSNIDSSTEEIIQASLLKIMESKTSfVI--AHRLSTI-KTADLIIVVNNGEIIEIGT 590
Cdd:COG4152 140 LIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTT-VIfsSHQMELVeELCDRIVIINKGRKVLSGS 212
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
370-583 |
1.21e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 60.95 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 370 LIEFKNVSFKYdinSKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNLREH- 448
Cdd:PRK09700 5 YISMAGIGKSF---GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 449 MSVVLQDTFMFND-TIENNIKLGdKNATK-----------EDVERAAnlsnaihfIKTLPNGFQTQIENNGQNLSQGQRQ 516
Cdd:PRK09700 82 IGIIYQELSVIDElTVLENLYIG-RHLTKkvcgvniidwrEMRVRAA--------MMLLRVGLKVDLDEKVANLSISHKQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502819783 517 LIAIARAVLANKSILILDEATSNIdsSTEEIIQasLLKIM-----ESKTSFVIAHRLSTIK-TADLIIVVNNG 583
Cdd:PRK09700 153 MLEIAKTLMLDAKVIIMDEPTSSL--TNKEVDY--LFLIMnqlrkEGTAIVYISHKLAEIRrICDRYTVMKDG 221
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
375-590 |
1.25e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 61.02 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 375 NVSFKYDiNSKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYEL--RNIKTNNLREH---- 448
Cdd:PRK10261 19 NIAFMQE-QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLrrRSRQVIELSEQsaaq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 449 --------MSVVLQD-------TFMFNDTIENNIKLgDKNATKEDVERAANlsNAIHFIKtLPNGfQTQIENNGQNLSQG 513
Cdd:PRK10261 98 mrhvrgadMAMIFQEpmtslnpVFTVGEQIAESIRL-HQGASREEAMVEAK--RMLDQVR-IPEA-QTILSRYPHQLSGG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 514 QRQLIAIARAVLANKSILILDEATSNIDSSTE-EIIQasLLKIMESKTSF---VIAHRLSTI-KTADLIIVVNNGEIIEI 588
Cdd:PRK10261 173 MRQRVMIAMALSCRPAVLIADEPTTALDVTIQaQILQ--LIKVLQKEMSMgviFITHDMGVVaEIADRVLVMYQGEAVET 250
|
..
gi 502819783 589 GT 590
Cdd:PRK10261 251 GS 252
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
391-541 |
1.33e-09 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 60.85 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 391 NASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDgyelrniktNNLRehMSVVLQDTFMFND-TIENNIKL 469
Cdd:COG0488 16 DVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP---------KGLR--IGYLPQEPPLDDDlTVLDTVLD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 470 GDK----------------NATKEDVERAANLSNAIHF---------IKTLPNGFQTQIENNGQ---NLSQGQRQLIAIA 521
Cdd:COG0488 85 GDAelraleaeleeleaklAEPDEDLERLAELQEEFEAlggweaearAEEILSGLGFPEEDLDRpvsELSGGWRRRVALA 164
|
170 180
....*....|....*....|
gi 502819783 522 RAVLANKSILILDEATSNID 541
Cdd:COG0488 165 RALLSEPDLLLLDEPTNHLD 184
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
389-589 |
1.46e-09 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 59.21 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 389 LYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNN-------------LREHMSVVLQ- 454
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDgqlkvadknqlrlLRTRLTMVFQh 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 455 -DTFMFNDTIENNIK-----LGDKNAtkEDVERAANLSNAIHFIKTLPNGFQTqienngqNLSQGQRQLIAIARAVLANK 528
Cdd:PRK10619 101 fNLWSHMTVLENVMEapiqvLGLSKQ--EARERAVKYLAKVGIDERAQGKYPV-------HLSGGQQQRVSIARALAMEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502819783 529 SILILDEATSNIDSsteEIIqASLLKIM-----ESKTSFVIAHRLSTIK-TADLIIVVNNGEIIEIG 589
Cdd:PRK10619 172 EVLLFDEPTSALDP---ELV-GEVLRIMqqlaeEGKTMVVVTHEMGFARhVSSHVIFLHQGKIEEEG 234
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
371-590 |
1.65e-09 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 58.87 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 371 IEFKNVSFKYdinSKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNLREHMS 450
Cdd:PRK11231 3 LRTENLTVGY---GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 451 -----------VVLQDTFMFNDTIENNI--KLGDKNatKEDVERAANlsnaihfiktlpngfQTQIENNGQ----NLSQG 513
Cdd:PRK11231 80 llpqhhltpegITVRELVAYGRSPWLSLwgRLSAED--NARVNQAME---------------QTRINHLADrrltDLSGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 514 QRQLIAIARAVLANKSILILDEATSNIDSSTeeiiQASLLKIM-----ESKTSFVIAHRLS-TIKTADLIIVVNNGEIIE 587
Cdd:PRK11231 143 QRQRAFLAMVLAQDTPVVLLDEPTTYLDINH----QVELMRLMrelntQGKTVVTVLHDLNqASRYCDHLVVLANGHVMA 218
|
...
gi 502819783 588 IGT 590
Cdd:PRK11231 219 QGT 221
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
400-590 |
1.85e-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: 61.18 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 400 QTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGyelRNIKTN--NLREHMSVVLQDTFMFND-TIENNI----KLGDK 472
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGG---KDIETNldAVRQSLGMCPQHNILFHHlTVAEHIlfyaQLKGR 1033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 473 NATKEDVERAANLSNAihfiktlpnGFQTQIENNGQNLSQGQRQLIAIARAVLANKSILILDEATSNIDSSTEEIIQASL 552
Cdd:TIGR01257 1034 SWEEAQLEMEAMLEDT---------GLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL 1104
|
170 180 190
....*....|....*....|....*....|....*....
gi 502819783 553 LKIMESKTSFVIAHRLSTIKT-ADLIIVVNNGEIIEIGT 590
Cdd:TIGR01257 1105 LKYRSGRTIIMSTHHMDEADLlGDRIAIISQGRLYCSGT 1143
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
393-590 |
1.96e-09 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 60.47 E-value: 1.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 393 SFVAKPGQTVAIVGPTGAGKT----TIINLLGKFYDYNSGSIKIDGYELRNIKTNNLRE----HMSVVLQDTfM--FND- 461
Cdd:COG4172 30 SFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRirgnRIAMIFQEP-MtsLNPl 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 462 -TIENNI--------KLGDKNATKEDVE--RAANLSNAIHFIKTLPngFQtqienngqnLSQGQRQLIAIARAvLANK-S 529
Cdd:COG4172 109 hTIGKQIaevlrlhrGLSGAAARARALEllERVGIPDPERRLDAYP--HQ---------LSGGQRQRVMIAMA-LANEpD 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502819783 530 ILILDEATSNIDSSteeiIQASLLKIM-----ESKTSFV-IAHRLSTI-KTADLIIVVNNGEIIEIGT 590
Cdd:COG4172 177 LLIADEPTTALDVT----VQAQILDLLkdlqrELGMALLlITHDLGVVrRFADRVAVMRQGEIVEQGP 240
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
400-568 |
2.14e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 58.64 E-value: 2.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 400 QTVAIVGPTGAGKTTIINLLGKFYDY-----NSGSIKIDGYEL--RNIKTNNLREHMSVVLQDTFMFNDTIENNIKLGDK 472
Cdd:PRK14243 37 QITAFIGPSGCGKSTILRCFNRLNDLipgfrVEGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPFPKSIYDNIAYGAR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 473 -NATKED----VERAanLSNAIhfiktLPNGFQTQIENNGQNLSQGQRQLIAIARAVLANKSILILDEATSNIDS-ST-- 544
Cdd:PRK14243 117 iNGYKGDmdelVERS--LRQAA-----LWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPiSTlr 189
|
170 180
....*....|....*....|....*
gi 502819783 545 -EEIIQasllKIMESKTSFVIAHRL 568
Cdd:PRK14243 190 iEELMH----ELKEQYTIIIVTHNM 210
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
370-585 |
2.55e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 60.06 E-value: 2.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 370 LIEFKNVSFKYdinSKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIkTNNLREHM 449
Cdd:PRK15439 11 LLCARSISKQY---SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARL-TPAKAHQL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 450 SVVL--QDTFMF-NDTIENNIKLGdKNATKEDVERAANLsnaihfIKTLpnGFQTQIENNGQNLSQGQRQLIAIARAVLA 526
Cdd:PRK15439 87 GIYLvpQEPLLFpNLSVKENILFG-LPKRQASMQKMKQL------LAAL--GCQLDLDSSAGSLEVADRQIVEILRGLMR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502819783 527 NKSILILDEATSNIDSSTEEIIQASLLKIMESKTSFV-IAHRLSTI-KTADLIIVVNNGEI 585
Cdd:PRK15439 158 DSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVfISHKLPEIrQLADRISVMRDGTI 218
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
75-332 |
3.38e-09 |
|
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: 58.36 E-value: 3.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 75 KSFSIWLVILGLVFIAY---GFFRYFDAYMYIKVSYQTSSRMRKEAMHKLIKMPISYYDKQKAGNLISTlINDInnvsnt 151
Cdd:cd18566 36 ESIPTLQVLVIGVVIAIlleSLLRLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLER-LNSL------ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 152 myNTINQFFSSifNVLLSIIAMMFVASFITLI--------VVPLALFLFFISLIVIkkaqpYFVKVQNLFGDLN------ 217
Cdd:cd18566 109 --EQIREFLTG--QALLALLDLPFVLIFLGLIwylggklvLVPLVLLGLFVLVAIL-----LGPILRRALKERSraderr 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 218 -AFVEENLAN---TKVMNAFDQQDNIFNEF--KKITRGIKLTsfKADAIARSSEPWFGITSGIANLCVAVLAVSfyiyki 291
Cdd:cd18566 180 qNFLIETLTGihtIKAMAMEPQMLRRYERLqaNAAYAGFKVA--KINAVAQTLGQLFSQVSMVAVVAFGALLVI------ 251
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 502819783 292 pvggigglgtnpDGTATSGLIVTFISLNWNFMGPFQNLLNI 332
Cdd:cd18566 252 ------------NGDLTVGALIACTMLSGRVLQPLQRAFGL 280
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
398-589 |
3.87e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 58.09 E-value: 3.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 398 PGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTN--NLREHMSVVLQD--TFMFNDTIENNIKLGDKN 473
Cdd:PRK13638 26 LSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGllALRQQVATVFQDpeQQIFYTDIDSDIAFSLRN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 474 ATKEDVERAANLSNAIHFIKTlpNGFQTQienNGQNLSQGQRQLIAIARAVLANKSILILDEATSNIDSSTEEIIQASLL 553
Cdd:PRK13638 106 LGVPEAEITRRVDEALTLVDA--QHFRHQ---PIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIR 180
|
170 180 190
....*....|....*....|....*....|....*...
gi 502819783 554 KIMESKTSFVI-AHRLSTI-KTADLIIVVNNGEIIEIG 589
Cdd:PRK13638 181 RIVAQGNHVIIsSHDIDLIyEISDAVYVLRQGQILTHG 218
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
393-550 |
4.26e-09 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 56.60 E-value: 4.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 393 SFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELrniktNNLREHMSvvlqdtfmfndtiENNIKLGDK 472
Cdd:TIGR01189 20 SFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPL-----AEQRDEPH-------------ENILYLGHL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 473 NATKEDVERAANLsnaiHFIKTLPNGFQTQIEN-------NG------QNLSQGQRQLIAIARAVLANKSILILDEATSN 539
Cdd:TIGR01189 82 PGLKPELSALENL----HFWAAIHGGAQRTIEDalaavglTGfedlpaAQLSAGQQRRLALARLWLSRRPLWILDEPTTA 157
|
170
....*....|.
gi 502819783 540 IDSSTEEIIQA 550
Cdd:TIGR01189 158 LDKAGVALLAG 168
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
83-247 |
4.64e-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: 57.96 E-value: 4.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 83 ILGLVFIAYGFFRYFDAYMYIKVSYQTSSRMRKEAMHKLIKMPISYYDKQKAGNLISTLINDINNVSNTMYNTINQFFSS 162
Cdd:cd18599 63 VYGGSILVILLLSLIRGFVFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQN 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 163 IFNVLLSIIAMMFVASFITLIVVPLALFLFFISLIvIKKAQPYFVKVQN-----LFGDLNAFVEenlaNTKVMNAFDQQD 237
Cdd:cd18599 143 VLLVVFSLIIIAIVFPWFLIALIPLAIIFVFLSKI-FRRAIRELKRLENisrspLFSHLTATIQ----GLSTIHAFNKEK 217
|
170
....*....|
gi 502819783 238 NIFNEFKKIT 247
Cdd:cd18599 218 EFLSKFKKLL 227
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
371-596 |
4.90e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 57.89 E-value: 4.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 371 IEFKNVSFKYDinsKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGyELRNIKTNNLREHMS 450
Cdd:PRK13537 8 IDFRNVEKRYG---DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCG-EPVPSRARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 451 VVLQ-DTFMFNDTIENNIKLGDKNATKEDVERAANLSNAIHFIKtLPNGFQTQIenngQNLSQGQRQLIAIARAVLANKS 529
Cdd:PRK13537 84 VVPQfDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAK-LENKADAKV----GELSGGMKRRLTLARALVNDPD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502819783 530 ILILDEATSNIDSSTEEIIQASLLKIMES-KTSFVIAHRLSTI-KTADLIIVVNNGEIIEIGTHKNLIQ 596
Cdd:PRK13537 159 VLVLDEPTTGLDPQARHLMWERLRSLLARgKTILLTTHFMEEAeRLCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
371-541 |
5.42e-09 |
|
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: 55.15 E-value: 5.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 371 IEFKNVSFKYDinsKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLgkfydynsgsikidgyelrniktnnlrehms 450
Cdd:cd03221 1 IELENLSKTYG---GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLI------------------------------- 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 451 vvlqdtfmfndtiennikLGDKNATKEDVERAANLSNAiHFiktlpngfqtqienngQNLSQGQRQLIAIARAVLANKSI 530
Cdd:cd03221 47 ------------------AGELEPDEGIVTWGSTVKIG-YF----------------EQLSGGEKMRLALAKLLLENPNL 91
|
170
....*....|.
gi 502819783 531 LILDEATSNID 541
Cdd:cd03221 92 LLLDEPTNHLD 102
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
384-586 |
6.01e-09 |
|
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: 56.12 E-value: 6.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 384 SKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYN---SGSIKIDGYELRNIKTNNLREHMSVVLQDTFMFN 460
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHFPT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 461 DTIEnniklgdknatkEDVERAANLsnaihfiktlpngfqtqieNNGQNL---SQGQRQLIAIARAVLANKSILILDEAT 537
Cdd:cd03233 98 LTVR------------ETLDFALRC-------------------KGNEFVrgiSGGERKRVSIAEALVSRASVLCWDNST 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502819783 538 SNIDSSTE-EIIQA--SLLKIMESkTSFVIAHRLS--TIKTADLIIVVNNGEII 586
Cdd:cd03233 147 RGLDSSTAlEILKCirTMADVLKT-TTFVSLYQASdeIYDLFDKVLVLYEGRQI 199
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
398-578 |
7.27e-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: 54.69 E-value: 7.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 398 PGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIdgyelrnIKTNNLREHMSVVLQdtfmfndtienniklgdknatke 477
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY-------IDGEDILEEVLDQLL----------------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 478 dveraanlsnaihfiktlpngfQTQIENNGQNLSQGQRQLIAIARAVLANKSILILDEATSNIDSSTEEIIQASL----- 552
Cdd:smart00382 51 ----------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrll 108
|
170 180
....*....|....*....|....*...
gi 502819783 553 --LKIMESKTSFVIAHRLSTIKTADLII 578
Cdd:smart00382 109 llLKSEKNLTVILTTNDEKDLGPALLRR 136
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
386-598 |
1.10e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 56.53 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 386 KYQLYNASFVAKP-GQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNLREHMSVVLQDTFMFND-TI 463
Cdd:PRK10253 19 KYTVAENLTVEIPdGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDiTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 464 ENNIKLGD-------KNATKEDVERAANLSNAihfiktlpNGFQTQIENNGQNLSQGQRQLIAIARAVLANKSILILDEA 536
Cdd:PRK10253 99 QELVARGRyphqplfTRWRKEDEEAVTKAMQA--------TGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502819783 537 TSNIDSStEEIIQASLLKIMESKTSFVIA---HRLS-TIKTADLIIVVNNGEIIEIGTHKNLIQLD 598
Cdd:PRK10253 171 TTWLDIS-HQIDLLELLSELNREKGYTLAavlHDLNqACRYASHLIALREGKIVAQGAPKEIVTAE 235
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
61-293 |
1.65e-08 |
|
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: 56.38 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 61 ANYIASSSKSDFN-----VKSFSIWLVILGLVFIAYGFFRYFdayMYIKVSYQTSSRMRKEAMHKLIKMPISYYDKQKAG 135
Cdd:cd18605 23 SYWVSHSNNSFFNfindsFNFFLTVYGFLAGLNSLFTLLRAF---LFAYGGLRAARRLHNKLLSSILFAKMSFFDKTPVG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 136 NLISTLINDINNVSNTMYNTINQFFSSIFNVLLSIIAMMFVASFITLIVVPLALFLFFIslivikkaQPYF--------- 206
Cdd:cd18605 100 RILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLLLPLAFIYYRI--------QRYYratsrelkr 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 207 ---VKVQNLFGDLNafveENLANTKVMNAFDQQDNIFNEFKKitrgiKLTSF-KADAIARSSEPWFGI----TSGIANLC 278
Cdd:cd18605 172 lnsVNLSPLYTHFS----ETLKGLVTIRAFRKQERFLKEYLE-----KLENNqRAQLASQAASQWLSIrlqlLGVLIVTF 242
|
250
....*....|....*
gi 502819783 279 VAVLAVSFYIYKIPV 293
Cdd:cd18605 243 VALTAVVQHFFGLSI 257
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
370-587 |
2.19e-08 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 57.00 E-value: 2.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 370 LIEFKNVSFKYDinsKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIdGyelRNIKTNNLREHm 449
Cdd:COG0488 315 VLELEGLSKSYG---DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-G---ETVKIGYFDQH- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 450 svvlQDTFMFNDTIENNIKLGDKNATKEDV----ERaanlsnaihFiktlpnGF-----QTQIEnngqNLSQGQRQLIAI 520
Cdd:COG0488 387 ----QEELDPDKTVLDELRDGAPGGTEQEVrgylGR---------F------LFsgddaFKPVG----VLSGGEKARLAL 443
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502819783 521 ARAVLANKSILILDEATSNIDSSTEEIIQASLLkimesktSF-----VIAH-R--LSTIktADLIIVVNNGEIIE 587
Cdd:COG0488 444 AKLLLSPPNVLLLDEPTNHLDIETLEALEEALD-------DFpgtvlLVSHdRyfLDRV--ATRILEFEDGGVRE 509
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
391-597 |
2.64e-08 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 56.73 E-value: 2.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 391 NASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIK-------IDGYELRNIKTNNLREHMSVVLQDTFMF--ND 461
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdewVDMTKPGPDGRGRAKRYIGILHQEYDLYphRT 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 462 TIEN-----NIKLGDKNATKEdveraanlsnAIHFIKTLpnGFQTQ-----IENNGQNLSQGQRQLIAIARAVLANKSIL 531
Cdd:TIGR03269 382 VLDNlteaiGLELPDELARMK----------AVITLKMV--GFDEEkaeeiLDKYPDELSEGERHRVALAQVLIKEPRIV 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502819783 532 ILDEATSNIDSSTEEIIQASLLKIME--SKTSFVIAHRLSTI-KTADLIIVVNNGEIIEIGTHKNLIQL 597
Cdd:TIGR03269 450 ILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVlDVCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
389-573 |
2.65e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 55.27 E-value: 2.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 389 LYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNLREHMSVVLQDTFMFNDTIENNIK 468
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVPQSEEVDWSFPVLVEDVVM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 469 LGD-------KNATKEDVERaanLSNAIHFIKTLPNGFQtQIennGQnLSQGQRQLIAIARAVLANKSILILDEATSNID 541
Cdd:PRK15056 103 MGRyghmgwlRRAKKRDRQI---VTAALARVDMVEFRHR-QI---GE-LSGGQKKRVFLARAIAQQGQVILLDEPFTGVD 174
|
170 180 190
....*....|....*....|....*....|....
gi 502819783 542 SSTEEIIqASLLKIM--ESKTSFVIAHRLSTIKT 573
Cdd:PRK15056 175 VKTEARI-ISLLRELrdEGKTMLVSTHNLGSVTE 207
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
43-200 |
2.80e-08 |
|
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: 55.55 E-value: 2.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 43 IFYVIGSFLigYIFQQYFANYIASSSKSDFNVKSFSI----WLVILGLVFIAYGFFRYFDAYMYIKVSYQTSSRMRKEAM 118
Cdd:cd18604 6 LLFVLSQLL--SVGQSWWLGIWASAYETSSALPPSEVsvlyYLGIYALISLLSVLLGTLRYLLFFFGSLRASRKLHERLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 119 HKLIKMPISYYDKQKAGNLISTLINDINNVSNTMYNTINQFFSSIFNVLLSIIAMMFVASFITLIVVPLALFLFFISLIV 198
Cdd:cd18604 84 HSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLAALYVYIGRLY 163
|
..
gi 502819783 199 IK 200
Cdd:cd18604 164 LR 165
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
50-194 |
3.25e-08 |
|
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: 55.56 E-value: 3.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 50 FLIGYIFQQYFanYIASS---SK-SDFNVKSFSIW-------LVILGLVFIAYGFFRYFDAYMYIKVSYQTSSRMRKEAM 118
Cdd:cd18603 4 ILLLYLLSQAF--SVGSNiwlSEwSDDPALNGTQDteqrdyrLGVYGALGLGQAIFVFLGSLALALGCVRASRNLHNKLL 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502819783 119 HKLIKMPISYYDKQKAGNLISTLINDINNVSNTMYNTINQFFSSIFNVLLSIIAMMFVASFITLIVVPLALFLFFI 194
Cdd:cd18603 82 HNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVVIIPLAILYFFI 157
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
29-201 |
3.55e-08 |
|
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: 55.21 E-value: 3.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 29 KKLYLGIFFSFCHSIFYVIGSFLIGYIFQQYFANYiasssksdfNVKSFSIWLVILGLVFIAYGFFRYFDAYMYIKVSYQ 108
Cdd:cd18555 2 KLLISILLLSLLLQLLTLLIPILTQYVIDNVIVPG---------NLNLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 109 TSSRMRKEAMHKLIKMPISYYDKQKAGNLISTlINDINNVSNTMYNTINQFFSSIFNVLLSIIAMMFVASFITLIVVPLA 188
Cdd:cd18555 73 LDKSLMSDFFEHLLKLPYSFFENRSSGDLLFR-ANSNVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLG 151
|
170
....*....|...
gi 502819783 189 LFLFFISLIVIKK 201
Cdd:cd18555 152 LLIVLLLLLTRKK 164
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
391-535 |
3.76e-08 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 55.49 E-value: 3.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 391 NASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYEL------RNIKTNnlREHMSVVLQDTFMFND-TI 463
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdsargIFLPPH--RRRIGYVFQEARLFPHlSV 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502819783 464 ENNIKLGDKNATKEdvERAANLSNAI------HFIKTLPngfqtqienngQNLSQGQRQLIAIARAVLANKSILILDE 535
Cdd:COG4148 95 RGNLLYGRKRAPRA--ERRISFDEVVellgigHLLDRRP-----------ATLSGGERQRVAIGRALLSSPRLLLMDE 159
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
81-316 |
4.27e-08 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 54.95 E-value: 4.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 81 LVILGLVFIAYGFFRYFDAYMYIKVSYQTSSRMRKEAMHKLIKMPISYYDKQKAGNLISTLINDINNVSNTMYNTINQFF 160
Cdd:cd18780 45 VLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 161 SSIFNVLLSIIaMMFVASF----ITLIVVPLalfLFFISLIVIKKAQPYFVKVQNLFGDLNAFVEENLANTKVMNAFDQQ 236
Cdd:cd18780 125 RYLVQIIGGLV-FMFTTSWkltlVMLSVVPP---LSIGAVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 237 DNIFNEF-KKITRGIKLtsfkADAIARSSEPWFGITSGIANLcvAVLAVSFYiykipvggiGGLGTNpDGTATSGLIVTF 315
Cdd:cd18780 201 TKEVSRYsEKINESYLL----GKKLARASGGFNGFMGAAAQL--AIVLVLWY---------GGRLVI-DGELTTGLLTSF 264
|
.
gi 502819783 316 I 316
Cdd:cd18780 265 L 265
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
378-589 |
4.51e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 56.66 E-value: 4.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 378 FKYDINSKKYQ-LYNASFVAKPGQTVAIVGPTGAGKTTIINLL-GKFYDYN---SGSIKIDGYELRNIK----------- 441
Cdd:TIGR00956 65 LKKFRDTKTFDiLKPMDGLIKPGELTVVLGRPGSGCSTLLKTIaSNTDGFHigvEGVITYDGITPEEIKkhyrgdvvyna 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 442 -TNNLREHMSVvlQDTFMFN---DTIENNIKLGDKNatkedvERAANLSNAIHFIKTLPNGFQTQIENNG-QNLSQGQRQ 516
Cdd:TIGR00956 145 eTDVHFPHLTV--GETLDFAarcKTPQNRPDGVSRE------EYAKHIADVYMATYGLSHTRNTKVGNDFvRGVSGGERK 216
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502819783 517 LIAIARAVLANKSILILDEATSNIDSSTE-EIIQAslLKIMES---KTSFVIAHRLS--TIKTADLIIVVNNGEIIEIG 589
Cdd:TIGR00956 217 RVSIAEASLGGAKIQCWDNATRGLDSATAlEFIRA--LKTSANildTTPLVAIYQCSqdAYELFDKVIVLYEGYQIYFG 293
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
393-541 |
5.47e-08 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 53.64 E-value: 5.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 393 SFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYN---SGSIKIDGYELRNIKTnnLREHMSVVLQDTFMF-NDTIENNIK 468
Cdd:COG4136 21 SLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPA--EQRRIGILFQDDLLFpHLSVGENLA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 469 LG-----DKNATKEDVERA---ANLSN-AIHFIKTLpngfqtqienngqnlSQGQRQLIAIARAVLANKSILILDEATSN 539
Cdd:COG4136 99 FAlpptiGRAQRRARVEQAleeAGLAGfADRDPATL---------------SGGQRARVALLRALLAEPRALLLDEPFSK 163
|
..
gi 502819783 540 ID 541
Cdd:COG4136 164 LD 165
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
398-541 |
8.34e-08 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 54.50 E-value: 8.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 398 PGQTV-AIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTN-NL---REHMSVVLQDTFMF-NDTIENNIKLGD 471
Cdd:PRK11144 22 PAQGItAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGiCLppeKRRIGYVFQDARLFpHYKVRGNLRYGM 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 472 KNATKEDVERAANLSNAIHFIKTLPngfqtqienngQNLSQGQRQLIAIARAVLANKSILILDEATSNID 541
Cdd:PRK11144 102 AKSMVAQFDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
389-589 |
8.85e-08 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 52.91 E-value: 8.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 389 LYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYN--SGSIKIDGYELRNIKTNNlREHMSVVLqdtfMFNDTIE-N 465
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEvtEGEILFKGEDITDLPPEE-RARLGIFL----AFQYPPEiP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 466 NIKLGDknatkedveraanlsnaihFIKTLPNGFqtqienngqnlSQGQRQLIAIARAVLANKSILILDEATSNIDSSTE 545
Cdd:cd03217 91 GVKNAD-------------------FLRYVNEGF-----------SGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDAL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 502819783 546 EIIQASLLKIMESKTSF-VIAH--RLSTIKTADLIIVVNNGEIIEIG 589
Cdd:cd03217 141 RLVAEVINKLREEGKSVlIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
370-541 |
1.07e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 53.19 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 370 LIEFKNVSFKYdinSKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGyELRnIKTNNLREHM 449
Cdd:PRK09544 4 LVSLENVSVSF---GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG-KLR-IGYVPQKLYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 450 SVVLQDT---FMfndtienNIKLGDKnatKEDVERAANLSNAIHFiktlpngfqtqIENNGQNLSQGQRQLIAIARAVLA 526
Cdd:PRK09544 79 DTTLPLTvnrFL-------RLRPGTK---KEDILPALKRVQAGHL-----------IDAPMQKLSGGETQRVLLARALLN 137
|
170
....*....|....*
gi 502819783 527 NKSILILDEATSNID 541
Cdd:PRK09544 138 RPQLLVLDEPTQGVD 152
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
348-585 |
1.26e-07 |
|
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: 54.45 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 348 KILNLDTKKPHveditiDKIDGLIEFKNVSFKYDINSKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIIN-LLGKFYDYN 426
Cdd:TIGR02633 241 EITSLYPHEPH------EIGDVILEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQaLFGAYPGKF 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 427 SGSIKIDGYELrNIKT--NNLREHMSVVLQDT----FMFNDTIENNIKLG--DKNATKEDVERAANLSNAIHFIKTLP-N 497
Cdd:TIGR02633 315 EGNVFINGKPV-DIRNpaQAIRAGIAMVPEDRkrhgIVPILGVGKNITLSvlKSFCFKMRIDAAAELQIIGSAIQRLKvK 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 498 GFQTQIENNGqnLSQGQRQLIAIARAVLANKSILILDEATSNIDSSTE-EIIQASLLKIMESKTSFVIAHRLSTI-KTAD 575
Cdd:TIGR02633 394 TASPFLPIGR--LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKyEIYKLINQLAQEGVAIIVVSSELAEVlGLSD 471
|
250
....*....|
gi 502819783 576 LIIVVNNGEI 585
Cdd:TIGR02633 472 RVLVIGEGKL 481
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
46-196 |
2.14e-07 |
|
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: 52.86 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 46 VIGSFLIGYIFQQYFANYIASSSKSDFNVKSFSIWLVILGLVFIAYGFFRYFDAYMYIKVSYQTSSRMRKEAMHKLIKMP 125
Cdd:cd18606 3 LLLLLLILSQFAQVFTNLWLSFWTEDFFGLSQGFYIGIYAGLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALKRVLRAP 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502819783 126 ISYYDKQKAGNLISTLINDINNVSNTMYNTINQFFSSIFNVLlSIIAMMFVAS-FITLIVVPLALFLFFISL 196
Cdd:cd18606 83 MSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSII-GTFILIIIYLpWFAIALPPLLVLYYFIAN 153
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
395-541 |
2.19e-07 |
|
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: 52.37 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 395 VAKPGQTVAIVGPTGAGKTTIINLL--------GKFYDYNSGSIKID---GYELRNIKTNNLREHMSVVLQDTFM----- 458
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKSTALKILagklkpnlGKFDDPPDWDEILDefrGSELQNYFTKLLEGDVKVIVKPQYVdlipk 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 459 -FNDTIENNIKLGDKNATKEDVERAANLSNAihfiktlpngfqtqIENNGQNLSQGQRQLIAIARAVLANKSILILDEAT 537
Cdd:cd03236 102 aVKGKVGELLKKKDERGKLDELVDQLELRHV--------------LDRNIDQLSGGELQRVAIAAALARDADFYFFDEPS 167
|
....
gi 502819783 538 SNID 541
Cdd:cd03236 168 SYLD 171
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
399-590 |
3.05e-07 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 52.92 E-value: 3.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 399 GQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGyelRNIktNNL--RE--------------HMSVvlqdtfmfndt 462
Cdd:PRK11650 30 GEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGG---RVV--NELepADrdiamvfqnyalypHMSV----------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 463 iENNIKLGDKNA--TKEDVER----AANLSNAIHFIKTLPngfqtqienngQNLSQGQRQLIAIARAVLANKSILILDEA 536
Cdd:PRK11650 94 -RENMAYGLKIRgmPKAEIEErvaeAARILELEPLLDRKP-----------RELSGGQRQRVAMGRAIVREPAVFLFDEP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502819783 537 TSNIDSSTE-----EI--IQASLlkimeSKTSFVIAH-RLSTIKTADLIIVVNNGEIIEIGT 590
Cdd:PRK11650 162 LSNLDAKLRvqmrlEIqrLHRRL-----KTTSLYVTHdQVEAMTLADRVVVMNGGVAEQIGT 218
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
399-585 |
3.25e-07 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 51.94 E-value: 3.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 399 GQTVAIVGPTGAGKTTIINLLGKFY--DYNSGS--------IKIDGYELRNIKTNnlREHMSVVLQDTFMFND-TIENNI 467
Cdd:PRK09984 30 GEMVALLGPSGSGKSTLLRHLSGLItgDKSAGShiellgrtVQREGRLARDIRKS--RANTGYIFQQFNLVNRlSVLENV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 468 KLGDKNAT--------------KEDVERAANLSNAIHFIktlpngfqtqiENNGQNLSQGQRQLIAIARAVLANKSILIL 533
Cdd:PRK09984 108 LIGALGSTpfwrtcfswftreqKQRALQALTRVGMVHFA-----------HQRVSTLSGGQQQRVAIARALMQQAKVILA 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502819783 534 DEATSNIDSSTEEIIQASLLKIMESK--TSFVIAHRLS-TIKTADLIIVVNNGEI 585
Cdd:PRK09984 177 DEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDyALRYCERIVALRQGHV 231
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
372-541 |
4.45e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 52.62 E-value: 4.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 372 EFKNVSFKYDINSKKYQLYNASFVAKPGQTVAIVGPTGAGKT-TIINLLGKFYDYNSGSIKIDGyelRNIKTNN----LR 446
Cdd:PRK13549 261 EVRNLTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTeLVQCLFGAYPGRWEGEIFIDG---KPVKIRNpqqaIA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 447 EHMSVVLQD-------TFMfndTIENNIKLG--DKNATKEDVERAANLSNAIHFIKTL----PNGFQtQIENngqnLSQG 513
Cdd:PRK13549 338 QGIAMVPEDrkrdgivPVM---GVGKNITLAalDRFTGGSRIDDAAELKTILESIQRLkvktASPEL-AIAR----LSGG 409
|
170 180
....*....|....*....|....*...
gi 502819783 514 QRQLIAIARAVLANKSILILDEATSNID 541
Cdd:PRK13549 410 NQQKAVLAKCLLLNPKILILDEPTRGID 437
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
403-580 |
4.56e-07 |
|
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: 50.68 E-value: 4.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 403 AIVGPTGAGKTTIINLLgKFYDYNSGSikidgyelrniKTNNLREHmsvvLQDTFMFNDTIeNNIKLGDKNATKED--VE 480
Cdd:cd03240 26 LIVGQNGAGKTTIIEAL-KYALTGELP-----------PNSKGGAH----DPKLIREGEVR-AQVKLAFENANGKKytIT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 481 RAAN-LSNAIhFIKTlpNGFQTQIENNGQNLSQGQRQL------IAIARAVLANKSILILDEATSNIDsstEEIIQASLL 553
Cdd:cd03240 89 RSLAiLENVI-FCHQ--GESNWPLLDMRGRCSGGEKVLasliirLALAETFGSNCGILALDEPTTNLD---EENIEESLA 162
|
170 180 190
....*....|....*....|....*....|...
gi 502819783 554 KIMESKTSF------VIAHRLSTIKTADLIIVV 580
Cdd:cd03240 163 EIIEERKSQknfqliVITHDEELVDAADHIYRV 195
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
391-541 |
5.93e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 52.48 E-value: 5.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 391 NASFVAKPGQTVAIVGPTGAGKTTI-INLLGKFYDYN-SGSIKIDGYE--LRNIKT---NNL------REHMSVVLQDTF 457
Cdd:NF040905 278 DVSLNVRRGEIVGIAGLMGAGRTELaMSVFGRSYGRNiSGTVFKDGKEvdVSTVSDaidAGLayvtedRKGYGLNLIDDI 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 458 MFNDTIENNIKLGDKNATKEDVER--AANLSNAIHfIKTlPNGFQTQIenngqNLSQGQRQLIAIARAVLANKSILILDE 535
Cdd:NF040905 358 KRNITLANLGKVSRRGVIDENEEIkvAEEYRKKMN-IKT-PSVFQKVG-----NLSGGNQQKVVLSKWLFTDPDVLILDE 430
|
....*.
gi 502819783 536 ATSNID 541
Cdd:NF040905 431 PTRGID 436
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
393-590 |
6.48e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 51.67 E-value: 6.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 393 SFVAKPGQTVAIVGPTGAGKT----TIINLLgkfyDY----NSGSIKIDGYELRNIKTNNLRE----HMSVVLQD----- 455
Cdd:PRK11022 27 SYSVKQGEVVGIVGESGSGKSvsslAIMGLI----DYpgrvMAEKLEFNGQDLQRISEKERRNlvgaEVAMIFQDpmtsl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 456 --TFMFNDTIENNIKLGDKNATKEDVERAANLSNAIhfikTLPNGfQTQIENNGQNLSQGQRQLIAIARAVLANKSILIL 533
Cdd:PRK11022 103 npCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQV----GIPDP-ASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIA 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502819783 534 DEATSNIDSSteeiIQASLLKIM------ESKTSFVIAHRLSTI-KTADLIIVVNNGEIIEIGT 590
Cdd:PRK11022 178 DEPTTALDVT----IQAQIIELLlelqqkENMALVLITHDLALVaEAAHKIIVMYAGQVVETGK 237
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
394-541 |
7.12e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 50.23 E-value: 7.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 394 FVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGyelRNIKTNNLREHMSVvlqdtfmfndtiennikLGDKN 473
Cdd:PRK13543 32 FHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDG---KTATRGDRSRFMAY-----------------LGHLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 474 ATKEDVERAANLsnaiHFIKTLPNGFQTQIENNG--------------QNLSQGQRQLIAIARAVLANKSILILDEATSN 539
Cdd:PRK13543 92 GLKADLSTLENL----HFLCGLHGRRAKQMPGSAlaivglagyedtlvRQLSAGQKKRLALARLWLSPAPLWLLDEPYAN 167
|
..
gi 502819783 540 ID 541
Cdd:PRK13543 168 LD 169
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
371-596 |
7.57e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 51.24 E-value: 7.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 371 IEFKNVSFKYDINSKKYQLYNA------------------SFVAKPGQTVAIVGPTGAGKTTIINLL-GKFYDyNSGSIK 431
Cdd:COG4586 2 IEVENLSKTYRVYEKEPGLKGAlkglfrreyreveavddiSFTIEPGEIVGFIGPNGAGKSTTIKMLtGILVP-TSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 432 IDGYELRNIKTNNLReHMSVV------------LQDTFMFNDTIeNNIklgDKNATKEDVERAANLSNAIHFIKtlpngf 499
Cdd:COG4586 81 VLGYVPFKRRKEFAR-RIGVVfgqrsqlwwdlpAIDSFRLLKAI-YRI---PDAEYKKRLDELVELLDLGELLD------ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 500 qTQIenngQNLSQGQR---QLIAiarAVLANKSILILDEATSNIDSSTEEIIQASLLKIMESK--TSFVIAHRLSTI-KT 573
Cdd:COG4586 150 -TPV----RQLSLGQRmrcELAA---ALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERgtTILLTSHDMDDIeAL 221
|
250 260
....*....|....*....|...
gi 502819783 574 ADLIIVVNNGEIIEIGTHKNLIQ 596
Cdd:COG4586 222 CDRVIVIDHGRIIYDGSLEELKE 244
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
389-586 |
1.01e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 51.65 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 389 LYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELrNIKTNN--LREHMSVVLQD-TFMFNDTIEN 465
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI-DFKSSKeaLENGISMVHQElNLVLQRSVMD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 466 NIKLGDKNATKEDVERAANLSNAIHFIKTLpnGFQTQIENNGQNLSQGQRQLIAIARAVLANKSILILDEATSNIDSSTE 545
Cdd:PRK10982 93 NMWLGRYPTKGMFVDQDKMYRDTKAIFDEL--DIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEV 170
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 502819783 546 EIIQASLLKIMESKTSFV-IAHRLSTI-KTADLIIVVNNGEII 586
Cdd:PRK10982 171 NHLFTIIRKLKERGCGIVyISHKMEEIfQLCDEITILRDGQWI 213
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
395-544 |
1.20e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 51.42 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 395 VAKPGQTVAIVGPTGAGKTTIINLL-GKFYDYN-SGSIKIDGYELrnikTNNLREHMSVVLQDTFMF-NDTIENNIKLGD 471
Cdd:PLN03211 90 MASPGEILAVLGPSGSGKSTLLNALaGRIQGNNfTGTILANNRKP----TKQILKRTGFVTQDDILYpHLTVRETLVFCS 165
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502819783 472 -----KNATKEDVERAANLSNAIHFIKTLPNgfqTQIENNG-QNLSQGQRQLIAIARAVLANKSILILDEATSNIDSST 544
Cdd:PLN03211 166 llrlpKSLTKQEKILVAESVISELGLTKCEN---TIIGNSFiRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATA 241
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
368-594 |
4.18e-06 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 48.61 E-value: 4.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 368 DGLIEFKNVSFKydiNSKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNL-- 445
Cdd:PRK11831 5 ANLVDMRGVSFT---RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLyt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 446 -REHMSVVLQDTFMFND-TIENNIKLgdknATKEDVERAANLSNAIHFIKTLPNGFQTQIENNGQNLSQGQRQLIAIARA 523
Cdd:PRK11831 82 vRKRMSMLFQSGALFTDmNVFDNVAY----PLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502819783 524 VLANKSILILDEATSNIDSsteeIIQASLLKIMES------KTSFVIAHRL-STIKTADLIIVVNNGEIIEIGTHKNL 594
Cdd:PRK11831 158 IALEPDLIMFDEPFVGQDP----ITMGVLVKLISElnsalgVTCVVVSHDVpEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
370-587 |
8.24e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 48.55 E-value: 8.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 370 LIEFKNVSFKYDINSKKYQLYNA-SFVAKPGQTVAIVGPTGAGKT----TIINLL-GKFYDYNSGSIKIDGYELRNIKTN 443
Cdd:PRK15134 5 LLAIENLSVAFRQQQTVRTVVNDvSLQIEAGETLALVGESGSGKSvtalSILRLLpSPPVVYPSGDIRFHGESLLHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 444 NLR----EHMSVVLQDTFM-FN--DTIENNIK--LGDKNATKEDVERAANLSN----AIHFIKTLPNGFQTQienngqnL 510
Cdd:PRK15134 85 TLRgvrgNKIAMIFQEPMVsLNplHTLEKQLYevLSLHRGMRREAARGEILNCldrvGIRQAAKRLTDYPHQ-------L 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 511 SQGQRQLIAIARAVLANKSILILDEATSNIDSSteeiIQASLLKIM-ESKTS-----FVIAHRLSTI-KTADLIIVVNNG 583
Cdd:PRK15134 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVS----VQAQILQLLrELQQElnmglLFITHNLSIVrKLADRVAVMQNG 233
|
....
gi 502819783 584 EIIE 587
Cdd:PRK15134 234 RCVE 237
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
391-549 |
1.12e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 48.08 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 391 NASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGyelRNIKTNN-------------------------- 444
Cdd:PRK10762 270 DVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDG---HEVVTRSpqdglangivyisedrkrdglvlgms 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 445 LREHMSVVLQDTFmfnDTIENNIKLGDKNATKEDVERAANlsnaihfIKTlPNgfQTQIENNgqnLSQGQRQLIAIARAV 524
Cdd:PRK10762 347 VKENMSLTALRYF---SRAGGSLKHADEQQAVSDFIRLFN-------IKT-PS--MEQAIGL---LSGGNQQKVAIARGL 410
|
170 180
....*....|....*....|....*.
gi 502819783 525 LANKSILILDEATSNID-SSTEEIIQ 549
Cdd:PRK10762 411 MTRPKVLILDEPTRGVDvGAKKEIYQ 436
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
58-194 |
1.24e-05 |
|
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: 47.60 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 58 QYFANYIASSSKSDFNVKSFSIWLVILGLVFIAYGFF-RYFDAYMYIKVSYQTSSRMrkeaMHKLIKMPISYYDKQKAGN 136
Cdd:cd18602 33 ASVVFNITSSSLEDDEVSYYISVYAGLSLGAVILSLVtNLAGELAGLRAARRLHDRM----LRNIVRAPMRFFDTTPIGR 108
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 502819783 137 LISTLINDINNVSNTMYNTINQFFSSIFNVLLSIIAMMFVASFITLIVVPLALFLFFI 194
Cdd:cd18602 109 ILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIALIPIIIVYYFL 166
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
391-589 |
2.17e-05 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 46.23 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 391 NASFVAKPGQTVAIVGPTGAGKT-TIINLLGKF---YDYNSGSIKIDGyelRNIKTNNLR-EHMSVVLQD---TF----- 457
Cdd:PRK10418 21 GVSLTLQRGRVLALVGGSGSGKSlTCAAALGILpagVRQTAGRVLLDG---KPVAPCALRgRKIATIMQNprsAFnplht 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 458 MFNDTIENNIKLG--DKNATKEDVERAANLSNAIHFIKTLPngFQtqienngqnLSQGQRQLIAIARAVLANKSILILDE 535
Cdd:PRK10418 98 MHTHARETCLALGkpADDATLTAALEAVGLENAARVLKLYP--FE---------MSGGMLQRMMIALALLCEAPFIIADE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502819783 536 ATSNIDSsteeIIQASLLKIMESKTS------FVIAHRLSTI-KTADLIIVVNNGEIIEIG 589
Cdd:PRK10418 167 PTTDLDV----VAQARILDLLESIVQkralgmLLVTHDMGVVaRLADDVAVMSHGRIVEQG 223
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
395-580 |
2.71e-05 |
|
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: 47.09 E-value: 2.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 395 VAKPGQTVAIVGPTGAGKTTIINLLgkfydynSGSIK--IDGYELRNIKTNNLREHMSVVLQDtfMFNDTIENNIKLGDK 472
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKIL-------SGELKpnLGDYDEEPSWDEVLKRFRGTELQD--YFKKLANGEIKVAHK 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 473 N------------ATKEDVERAANLSNAIHFIKTLpnGFQTQIENNGQNLSQGQRQLIAIARAVLANKSILILDEATSNI 540
Cdd:COG1245 166 PqyvdlipkvfkgTVRELLEKVDERGKLDELAEKL--GLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYL 243
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 502819783 541 DSStEEIIQASLLKIM--ESKTSFVIAHRLSTI-KTADLIIVV 580
Cdd:COG1245 244 DIY-QRLNVARLIRELaeEGKYVLVVEHDLAILdYLADYVHIL 285
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
101-346 |
4.97e-05 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 45.54 E-value: 4.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 101 MYIKVSYQTSSRMRKEAMHKLIKMPISYYDKQKAGNLISTLINDINNVSNTMYNTINQFFSSIFNVLLSIIAMMFVA--- 177
Cdd:cd18589 59 IYNITMSRIHSRLQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSpkl 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 178 SFITLIVVPLalfLFFISLIVIKKAQPYFVKVQNLFGDLNAFVEENLANTKVMNAFDQQDNIFNEFKKITRGIKLTSfKA 257
Cdd:cd18589 139 ALLTALGLPL---LLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLN-KK 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 258 DAIARSSEPWFGITSGIAnLCVAVLavsFYiykipvGGIggLGTNpdGTATSGLIVTFISLNWNFMGPFQNLLNINFSFQ 337
Cdd:cd18589 215 EAAAYAVSMWTSSFSGLA-LKVGIL---YY------GGQ--LVTA--GTVSSGDLVTFVLYELQFTSAVEVLLSYYPSVM 280
|
....*....
gi 502819783 338 MGLASSSRV 346
Cdd:cd18589 281 KAVGSSEKI 289
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
368-432 |
5.95e-05 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 46.08 E-value: 5.95e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502819783 368 DGLIEFKNVSFKYDinsKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKI 432
Cdd:TIGR03719 320 DKVIEAENLTKAFG---DKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI 381
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
46-236 |
6.31e-05 |
|
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: 45.35 E-value: 6.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 46 VIGSFLIGYIFQQYFANYIASSSKSDF-----NVKSFSIWLVILGL-VFIAYgffrYFDAYMYIKVSYQTSSRMRKEAMH 119
Cdd:cd18558 25 MTDSFTNGGMTNITGNSSGLNSSAGPFekleeEMTLYAYYYLIIGAiVLITA----YIQGSFWGLAAGRQTKKIRYKFFH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 120 KLIKMPISYYDKQKAGNLISTLINDINNVSNTMYNTINQFFSSIFNVLLSIIAMMFVASFITLIVVPLALFLFFISLIVI 199
Cdd:cd18558 101 AIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRGWKLTLVILAISPVLGLSAVVWA 180
|
170 180 190
....*....|....*....|....*....|....*..
gi 502819783 200 KKAQPYFVKVQNLFGDLNAFVEENLANTKVMNAFDQQ 236
Cdd:cd18558 181 KILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQ 217
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
391-541 |
6.58e-05 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 44.63 E-value: 6.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 391 NASFVAKPGQTVAIVGPTGAGKTTIinllgkFY------DYNSGSIKIDGyelRNIkTN---NLREHMSV--VLQDTFMF 459
Cdd:COG1137 21 DVSLEVNQGEIVGLLGPNGAGKTTT------FYmivglvKPDSGRIFLDG---EDI-THlpmHKRARLGIgyLPQEASIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 460 ND-TIENNIK----LGDKNAtKEDVERAANLSNAIHfIKTLPNgfqtqieNNGQNLSQGQRQLIAIARAVLANKSILILD 534
Cdd:COG1137 91 RKlTVEDNILavleLRKLSK-KEREERLEELLEEFG-ITHLRK-------SKAYSLSGGERRRVEIARALATNPKFILLD 161
|
....*..
gi 502819783 535 EATSNID 541
Cdd:COG1137 162 EPFAGVD 168
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
510-575 |
6.86e-05 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 44.15 E-value: 6.86e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502819783 510 LSQGQRQLIAIARAVLANKSILILDEATSNIDSSTEEIIQASLLKIMESKTSFVIA-HRLSTIKTAD 575
Cdd:NF040873 120 LSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHARGATVVVVtHDLELVRRAD 186
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
382-577 |
7.42e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 44.09 E-value: 7.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 382 INSKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIdgyelRNIKTNNLREHMSVVL--QDTFMF 459
Cdd:PRK13541 9 FNIEQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYY-----KNCNINNIAKPYCTYIghNLGLKL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 460 NDTIENNIKLgdknaTKEDVERAANLSNAIHFIKtlpngFQTQIENNGQNLSQGQRQLIAIARAVLANKSILILDEATSN 539
Cdd:PRK13541 84 EMTVFENLKF-----WSEIYNSAETLYAAIHYFK-----LHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETN 153
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 502819783 540 IDSSTEEIIQAslLKIMESKTSFVI---AHRLSTIKTADLI 577
Cdd:PRK13541 154 LSKENRDLLNN--LIVMKANSGGIVllsSHLESSIKSAQIL 192
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
372-588 |
1.08e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 45.16 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 372 EFKNVSFKydiNSKKYQlyNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELR-NIKTNNLREHMS 450
Cdd:PRK09700 267 EVRNVTSR---DRKKVR--DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDAVKKGMA 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 451 VVLQ---DTFMF-------NDTIENNIKLGDKNAT-----KEDVERAANLSNAIHFIKTlpngfqTQIENNGQNLSQGQR 515
Cdd:PRK09700 342 YITEsrrDNGFFpnfsiaqNMAISRSLKDGGYKGAmglfhEVDEQRTAENQRELLALKC------HSVNQNITELSGGNQ 415
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502819783 516 QLIAIARAVLANKSILILDEATSNIDSSTeeiiQASLLKIM-----ESKTSFVIAHRLSTIKTA-DLIIVVNNGEIIEI 588
Cdd:PRK09700 416 QKVLISKWLCCCPEVIIFDEPTRGIDVGA----KAEIYKVMrqladDGKVILMVSSELPEIITVcDRIAVFCEGRLTQI 490
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
391-596 |
1.69e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 44.34 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 391 NASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGYELRNIKTNNLREH-MSVVLQD----------TFMF 459
Cdd:PRK10982 266 DVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINHgFALVTEErrstgiyaylDIGF 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 460 NDTIEN------NIKLGDKNATKEDVERAANLSNaihfIKTlpNGFQTQIenngQNLSQGQRQLIAIARAVLANKSILIL 533
Cdd:PRK10982 346 NSLISNirnyknKVGLLDNSRMKSDTQWVIDSMR----VKT--PGHRTQI----GSLSGGNQQKVIIGRWLLTQPEILML 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502819783 534 DEATSNIDSSTE-EIIQASLLKIMESKTSFVIAHRL-STIKTADLIIVVNNGEIIEIGTHKNLIQ 596
Cdd:PRK10982 416 DEPTRGIDVGAKfEIYQLIAELAKKDKGIIIISSEMpELLGITDRILVMSNGLVAGIVDTKTTTQ 480
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
81-194 |
1.95e-04 |
|
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: 43.60 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 81 LVILGLVFIAYGFFR----YFDAYMYIKVSYQTSSRMRKEAMHKLIKMPISYYDKQKAGNLISTlINDINNVSNTMyntI 156
Cdd:cd18567 41 LTVLAIGFGLLLLLQallsALRSWLVLYLSTSLNLQWTSNLFRHLLRLPLSYFEKRHLGDIVSR-FGSLDEIQQTL---T 116
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 502819783 157 NQFFSSIFNVLLSI---IAMMFVASFITLIVVpLALFLFFI 194
Cdd:cd18567 117 TGFVEALLDGLMAIltlVMMFLYSPKLALIVL-AAVALYAL 156
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
372-548 |
2.30e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 44.33 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 372 EFKNVSFKYDINSKKYQ-LYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFY--------DYNSGSIKID-------GY 435
Cdd:TIGR00956 761 HWRNLTYEVKIKKEKRViLNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVttgvitggDRLVNGRPLDssfqrsiGY 840
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 436 ELRN---IKTNNLREHM--SVVLQDTfmfndtieNNIKLGDKNATKEDVERAANLSNAIHFIKTLPngfqtqiennGQNL 510
Cdd:TIGR00956 841 VQQQdlhLPTSTVRESLrfSAYLRQP--------KSVSKSEKMEYVEEVIKLLEMESYADAVVGVP----------GEGL 902
|
170 180 190
....*....|....*....|....*....|....*....
gi 502819783 511 SQGQRQLIAIARAVLAN-KSILILDEATSNIDSSTEEII 548
Cdd:TIGR00956 903 NVEQRKRLTIGVELVAKpKLLLFLDEPTSGLDSQTAWSI 941
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
370-575 |
3.07e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.46 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 370 LIEFKNVSFKYdiNSKKYqLYNASFVAKPGQTVAIVGPTGAGKTTIINLL---------------GK-------FYD--- 424
Cdd:PRK10938 260 RIVLNNGVVSY--NDRPI-LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLItgdhpqgysndltlfGRrrgsgetIWDikk 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 425 ---YNSGSIKIDgYELrnikTNNLRehmSVVLQDTFmfnDTIenniklGDKNATKEDVERAAN--LSnAIHFIKTLPNG- 498
Cdd:PRK10938 337 higYVSSSLHLD-YRV----STSVR---NVILSGFF---DSI------GIYQAVSDRQQKLAQqwLD-ILGIDKRTADAp 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 499 FQTqienngqnLSQGQRQLIAIARAVLANKSILILDEATSNIDSSTEEIIQaSLLKIM--ESKTS--FV----------I 564
Cdd:PRK10938 399 FHS--------LSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVR-RFVDVLisEGETQllFVshhaedapacI 469
|
250
....*....|.
gi 502819783 565 AHRLSTIKTAD 575
Cdd:PRK10938 470 THRLEFVPDGD 480
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
397-420 |
3.44e-04 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 43.00 E-value: 3.44e-04
10 20
....*....|....*....|....*
gi 502819783 397 KPGQTVAIVGPTGAGKTTIIN-LLG 420
Cdd:PRK01889 193 SGGKTVALLGSSGVGKSTLVNaLLG 217
|
|
| ABC_6TM_NdvA_beta-glucan_exporter_like |
cd18562 |
Six-transmembrane helical domain of the cyclic beta-glucan ABC transporter NdvA, and similar ... |
74-318 |
3.46e-04 |
|
Six-transmembrane helical domain of the cyclic beta-glucan ABC transporter NdvA, and similar proteins; This group represents the six-transmembrane domain of NdvA, an ATP-dependent exporter of cyclic beta glucans, and similar proteins. NdvA is required for nodulation of legume roots and is involved in beta-(1,2)-glucan export to the periplasm. NdvA mutants in Brucella abortus and Sinorhizobium meliloti have been shown to exhibit decreased virulence in mice and inhibit intracellular multiplication in HeLa cells. These results suggest that cyclic beta-(1,2)-glucan is required to transport into the periplasmatic space to function as a virulence factor. 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: 350006 [Multi-domain] Cd Length: 289 Bit Score: 43.00 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 74 VKSFSIWLVILGLVFI--AYGFFRyFDAYMYIKVSY-QTSSRMRKEAMH----KLIKMPISYYDKQKAGNLISTLINDIn 146
Cdd:cd18562 26 VDALSSGGDAFPLLALwaALGLFS-ILAGVLVALLAdRLAHRRRLAVMAsyfeHVITLPLSFHSQRGSGRLLRIMLRGT- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 147 nvsNTMYNTINQFFSSIFNVLLSIIAMMFVASFI----TLIVVPLALFLFFISLIVIKKAQPYFVKVQNLFGDLNAFVEE 222
Cdd:cd18562 104 ---DALFGLWLGFFREHLAALVSLIVLLPVALWMnwrlALLLVVLAAVYAALNRLVMRRTKAGQAAVEEHHSALSGRVGD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 223 NLANTKVMNAFDQQDNIFNEFKKITRGIKLTSFkadaiarsseP---WFGITSGIANLC-----VAVLAVSFYIYKipvg 294
Cdd:cd18562 181 VIGNVTVVQSYTRLAAETSALRGITRRLLAAQY----------PvlnWWALASVLTRAAstltmVAIFALGAWLVQ---- 246
|
250 260
....*....|....*....|....
gi 502819783 295 gigglgtnpDGTATSGLIVTFISL 318
Cdd:cd18562 247 ---------RGELTVGEIVSFVGF 261
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
393-572 |
4.38e-04 |
|
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: 43.20 E-value: 4.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 393 SFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDgyelrniKTNNL-----REHMSV-VLQDTFMFNDTIENN 466
Cdd:TIGR00954 472 SFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKP-------AKGKLfyvpqRPYMTLgTLRDQIIYPDSSEDM 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 467 IklgDKNATKEDVERAANLSNAIHFIKTlpNGFQTQIENNGQNLSQGQRQLIAIARAVLANKSILILDEATSNIDSSTEE 546
Cdd:TIGR00954 545 K---RRGLSDKDLEQILDNVQLTHILER--EGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEG 619
|
170 180
....*....|....*....|....*.
gi 502819783 547 IIqASLLKIMeSKTSFVIAHRLSTIK 572
Cdd:TIGR00954 620 YM-YRLCREF-GITLFSVSHRKSLWK 643
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
45-317 |
6.11e-04 |
|
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: 42.27 E-value: 6.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 45 YVIGSFLIGYIFQQYFANyiasssksdFNVKSFSIWLVILGLVFIAYGFFRYFDAymyiKVSYQTSSR----MRKEAMHK 120
Cdd:cd18561 12 YIAQAWLLARALARIFAG---------GPWEDIMPPLAGIAGVIVLRAALLWLRE----RVAHRAAQRvkqhLRRRLFAK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 121 LIKMPISYYDKQKAGNLISTLINDINNVSNTMYNTINQFFSSIFNVLLSIIAMMFVASFITLIVVPLALFLFFISLIVIK 200
Cdd:cd18561 79 LLKLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLIPLSPALWDR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 201 KAQPYFVKVQNLFGDLNAFVEENLANTKVMNAFDQQDnifnefkkitrgikltsFKADAIARSSEPWFGITsgIANLCVA 280
Cdd:cd18561 159 LAKDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASK-----------------RRGNELAARAEDLRQAT--MKVLAVS 219
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 502819783 281 VLAVSF-----YIYKIPVGGIGGLGTNPDG-TATSGLIVTFIS 317
Cdd:cd18561 220 LLSSGImglatALGTALALGVGALRVLGGQlTLSSLLLILFLS 262
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
354-432 |
6.57e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.80 E-value: 6.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 354 TKKPHVEDITI-------DKIdglIEFKNVSfkydinsKKY---QLY-NASFVAKPGQTVAIVGPTGAGKTTIINLLGKF 422
Cdd:PRK11819 304 QKRNETNEIFIppgprlgDKV---IEAENLS-------KSFgdrLLIdDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQ 373
|
90
....*....|
gi 502819783 423 YDYNSGSIKI 432
Cdd:PRK11819 374 EQPDSGTIKI 383
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
397-564 |
7.77e-04 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 42.69 E-value: 7.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 397 KPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKIDGyelRNIKTNNLREHMSVVLQDTFmfnDTIENNIKLGD----- 471
Cdd:TIGR01257 1963 RPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAG---KSILTNISDVHQNMGYCPQF---DAIDDLLTGREhlyly 2036
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 472 ---KNATKEDVERAANLSnaihfIKTLpnGFQTQIENNGQNLSQGQRQLIAIARAVLANKSILILDEATSNIDSSTEEII 548
Cdd:TIGR01257 2037 arlRGVPAEEIEKVANWS-----IQSL--GLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRML 2109
|
170
....*....|....*.
gi 502819783 549 QASLLKIMESKTSFVI 564
Cdd:TIGR01257 2110 WNTIVSIIREGRAVVL 2125
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
35-199 |
8.23e-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: 8.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 35 IFFSFCHSIFYVIGSFLIGYIFQQYFANYIASSSksdfnvksFSIWLVILGLVFIAYGFFRYFDAYMYIKVSYQTSSRMR 114
Cdd:cd18584 2 VLLGLLAALLIIAQAWLLARIIAGVFLEGAGLAA--------LLPLLLLLLAALLLRALLAWAQERLAARAAARVKAELR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 115 KEAMHKLIKMPISYYDKQKAGNLISTLINDINNVSNtmyntinqFFSSIfnvlLSIIAMMFVASFITLIVV----PLALF 190
Cdd:cd18584 74 RRLLARLLALGPALLRRQSSGELATLLTEGVDALDG--------YFARY----LPQLVLAAIVPLLILVAVfpldWVSAL 141
|
....*....
gi 502819783 191 LFFISLIVI 199
Cdd:cd18584 142 ILLVTAPLI 150
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
371-431 |
9.60e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 42.19 E-value: 9.60e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502819783 371 IEFKNVSFKYDinsKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIK 431
Cdd:PRK15064 320 LEVENLTKGFD---NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK 377
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
76-225 |
1.04e-03 |
|
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: 41.35 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 76 SFSIWLVILGLVFIAYGF---FRYFDAYMYIKVSYQTSSRMRKEAMHKLIKMPISYYDKQKAGNLISTLiNDINNVSNTM 152
Cdd:cd18783 37 SYSTLYVLTIGVVIALLFegiLGYLRRYLLLVATTRIDARLALRTFDRLLSLPIDFFERTPAGVLTKHM-QQIERIRQFL 115
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502819783 153 yntINQFFSSIFNV--LLSIIAMMFVASF-ITLIVVPLALFLFFISLIVIKKAQPYFVKVQNLFGDLNAFVEENLA 225
Cdd:cd18783 116 ---TGQLFGTLLDAtsLLVFLPVLFFYSPtLALVVLAFSALIALIILAFLPPFRRRLQALYRAEGERQAFLVETVH 188
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
391-589 |
1.05e-03 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 41.06 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 391 NASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIkidGYELRNIKTNNL------------REHMSVVLQ---D 455
Cdd:PRK11701 24 DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEV---HYRMRDGQLRDLyalseaerrrllRTEWGFVHQhprD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 456 TFMFNDTIENNI-----KLGDKN-------ATK--EDVERAANLsnaihfIKTLPNGFqtqienngqnlSQGQRQLIAIA 521
Cdd:PRK11701 101 GLRMQVSAGGNIgerlmAVGARHygdiratAGDwlERVEIDAAR------IDDLPTTF-----------SGGMQQRLQIA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502819783 522 RAVLANKSILILDEATSNIDSSteeiIQASLLKIMESKTS------FVIAHRLSTIK-TADLIIVVNNGEIIEIG 589
Cdd:PRK11701 164 RNLVTHPRLVFMDEPTGGLDVS----VQARLLDLLRGLVRelglavVIVTHDLAVARlLAHRLLVMKQGRVVESG 234
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
399-419 |
1.70e-03 |
|
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: 40.07 E-value: 1.70e-03
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
112-233 |
1.72e-03 |
|
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: 40.78 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 112 RMRKEAMHKLIKMPISYYDKQKAGNLISTLINDINNVSNTMYNTINQFFSSIFNVLLSIIAMMFVASFITLIVVPLALFL 191
Cdd:cd18590 70 RLRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLT 149
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 502819783 192 FFISLIVIKKAQPYFVKVQNLFGDLNAFVEENLANTKVMNAF 233
Cdd:cd18590 150 AIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSF 191
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
82-346 |
1.79e-03 |
|
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: 40.87 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 82 VILGLVFIAYGFFR----YFDAYMYIKVSYQTSSRMRKEAMHKLIKMPISYYDKQKAGNLISTLINDINNVSNTMYNTIN 157
Cdd:cd18554 46 TIIGIMFFIFLILRppveYYRQYFAQWIANKILYDIRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLM 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 158 QFFSSIFNVLLSIIAMMFVASFITLIvvplALFLFFISLIVIKkaqpYFVK--------VQNLFGDLNAFVEENLANTKV 229
Cdd:cd18554 126 NIWLDMITIIIAICIMLVLNPKLTFV----SLVIFPFYILAVK----YFFGrlrkltkeRSQALAEVQGFLHERIQGMSV 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 230 MNAFDQQDNIFNEFKK-----ITRGIKLTSFKADAIARssepwFGITSGIANLCVAVLAVSFYIykipvggigglgtnpD 304
Cdd:cd18554 198 IKSFALEKHEQKQFDKrnghfLTRALKHTRWNAKTFSA-----VNTITDLAPLLVIGFAAYLVI---------------E 257
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 502819783 305 GTATSGLIVTFISLNWNFMGPFQNLLNINFSFQMGLASSSRV 346
Cdd:cd18554 258 GNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDRV 299
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
507-590 |
1.81e-03 |
|
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: 41.54 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 507 GQN---LSQGQRQLIAIARAVLA---NKSILILDEATSNIdsSTEEIIQasLLKIMES-----KTSFVIAHRLSTIKTAD 575
Cdd:TIGR00630 824 GQPattLSGGEAQRIKLAKELSKrstGRTLYILDEPTTGL--HFDDIKK--LLEVLQRlvdkgNTVVVIEHNLDVIKTAD 899
|
90 100
....*....|....*....|.
gi 502819783 576 LIIV------VNNGEIIEIGT 590
Cdd:TIGR00630 900 YIIDlgpeggDGGGTVVASGT 920
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
22-350 |
2.16e-03 |
|
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; 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: 350044 [Multi-domain] Cd Length: 324 Bit Score: 40.56 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 22 SYLKHDSKKLYLGIFFSFCHSIF------YVIGSFLIGYIFQQYFANYIASSSKSDFNVKSFS----IWLVILGLV--FI 89
Cdd:cd18600 5 TYLRYITSHKSLIFVLILCLVIFaievaaSLVGLWLLRSQADRVNTTRPESSSNTYAVIVTFTssyyVFYIYVGVAdsLL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 90 AYGFFRyfdAYMYIKVSYQTSSRMRKEAMHKLIKMPISYYDKQKAGNLISTLINDINNVSNTMYNTINQFFSSIFNVLLS 169
Cdd:cd18600 85 AMGFFR---GLPLVHTLITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQLFLIVIGA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 170 IIAMMFVASFITLIVVPLAlflffISLIVIKKaqpYFVKVQNLFGDLN--------AFVEENLANTKVMNAFDQQDNIFN 241
Cdd:cd18600 162 ITVVSILQPYIFLATVPVI-----IAFIVLRA---YFLRTSQQLKQLEsearspifAHLVTSLKGLWTLRAFGRQPYFET 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 242 EFKKITRGIKLTSFkadaIARSSEPWFGITSGIAnlcvavlavsFYIYKIPVGGIgGLGTNPDGTATSGLIVTfisLNWN 321
Cdd:cd18600 234 LFHKALNLHTANWF----LYLSTLRWFQMRIEMI----------FVIFFTAVTFI-SIGTTGDGEGRVGIILT---LAMN 295
|
330 340
....*....|....*....|....*....
gi 502819783 322 FMGPFQNLLNINFSFQMGLASSSRVFKIL 350
Cdd:cd18600 296 IMSTLQWAVNTSIDVDSLMRSVSRIFKFI 324
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
84-188 |
2.46e-03 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 40.22 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 84 LGLVFIAYGFFRYFDAYMYIKVSYQTSSRMRKEAMHKLIKMPISYYDKQKAGNLISTLINDINNVSNTMYNTINQFFSSI 163
Cdd:cd18574 48 LLGLYLLQSLLTFAYISLLSVVGERVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVQEFKSSFKQCVSQGLRSV 127
|
90 100
....*....|....*....|....*...
gi 502819783 164 FNVLLSIIAMMFVA---SFITLIVVPLA 188
Cdd:cd18574 128 TQTVGCVVSLYLISpklTLLLLVIVPVV 155
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
509-580 |
4.66e-03 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 38.32 E-value: 4.66e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502819783 509 NLSQGQRQLIAIARAVLANKSILILDEATSNIDSSTEEIIQASLLKIME--SKTSFVIAHRLSTIK-TADLIIVV 580
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEegKKTALVVEHDLAVLDyLSDRIHVF 145
|
|
| VirB11-like_ATPase |
cd01130 |
Type IV secretory pathway component VirB11-like; Type IV secretory pathway component VirB11, ... |
399-438 |
5.89e-03 |
|
Type IV secretory pathway component VirB11-like; Type IV secretory pathway component VirB11, and related ATPases. The homohexamer, VirB11 is one of eleven Vir (virulence) proteins, which are required for T-pilus biogenesis and virulence in the transfer of T-DNA from the bacterial Ti (tumor-inducing)-plasmid into plant cells. The pilus is a fibrous cell surface organelle, which mediates adhesion between bacteria during conjugative transfer or between bacteria and host eukaryotic cells during infection. VirB11-related ATPases include Sulfolobus acidocaldarius FlaI, which plays key roles in archaellum (archaeal flagellum) assembly and motility functions, and the pilus assembly proteins CpaF/TadA and TrbB. This alignment contains the C-terminal domain, which is the ATPase.
Pssm-ID: 410874 [Multi-domain] Cd Length: 177 Bit Score: 38.29 E-value: 5.89e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 502819783 399 GQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKI-DGYELR 438
Cdd:cd01130 12 RKNILISGGTGSGKTTLLNALLSFIPPDERIVTIeDTRELQ 52
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
33-209 |
6.18e-03 |
|
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: 39.01 E-value: 6.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 33 LGIFFSFCHSIFYVIGSFLIGYIFqQYFANYIASSSKSDFnvksfsIWLVILGLVFIAYGFFryFDAYMYIkvSYQTSSR 112
Cdd:cd18579 1 LAGLLKLLEDLLSLAQPLLLGLLI-SYLSSYPDEPLSEGY------LLALALFLVSLLQSLL--LHQYFFL--SFRLGMR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 113 MRKEAM----HKLIKMPISYYDKQKAGNLISTLINDINNVSNTMYNtINQFFSSIFNVLLSIIAM---MFVASFITLIVV 185
Cdd:cd18579 70 VRSALSsliyRKALRLSSSARQETSTGEIVNLMSVDVQRIEDFFLF-LHYLWSAPLQIIVALYLLyrlLGWAALAGLGVL 148
|
170 180
....*....|....*....|....
gi 502819783 186 plaLFLFFISLIVIKKAQPYFVKV 209
Cdd:cd18579 149 ---LLLIPLQAFLAKLISKLRKKL 169
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
354-573 |
6.83e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 39.49 E-value: 6.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 354 TKKPHVEDITIDKIdgliefKNVSFKYDINSKKYQLYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYNSGSIKID 433
Cdd:PRK13545 11 TKKYKMYNKPFDKL------KDLFFRSKDGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 434 GYELRNIKTNNLREHMSVVlqdtfmfndtieNNIKLG------DKNATKEDVERAANLSNAIHFIKTLPNGFqtqienng 507
Cdd:PRK13545 85 GSAALIAISSGLNGQLTGI------------ENIELKglmmglTKEKIKEIIPEIIEFADIGKFIYQPVKTY-------- 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 508 qnlSQGQRQLIAIARAVLANKSILILDEATSNIDSSteeIIQASLLKIME----SKTSFVIAHRLSTIKT 573
Cdd:PRK13545 145 ---SSGMKSRLGFAISVHINPDILVIDEALSVGDQT---FTKKCLDKMNEfkeqGKTIFFISHSLSQVKS 208
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
389-438 |
7.64e-03 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 38.28 E-value: 7.64e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 502819783 389 LYNASFVAKPGQTVAIVGPTGAGKTTIINLLGKFYDYnSGSIKIDGYELR 438
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLNGRPLS 60
|
|
| ABC_6TM_PglK_like |
cd18553 |
Six-transmembrane helical domain of the ABC transporter PglK and similar proteins; This group ... |
35-250 |
8.00e-03 |
|
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: 38.68 E-value: 8.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 35 IFFSFCHSIFYVIGSFLI----------GYIFQQYFANYIAS----SSKSDFnVKSFSIWLVILglvFIAYGFFRYFDAY 100
Cdd:cd18553 1 LLFSIFVSLIETIGISAImpfisvasnfSLILSNKYYKFIYNffgfSSPVNF-VIFFGIILIGF---YIFRSLYNIFYTY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 101 MYIKVSYQTSSRMRKEAMHKLIKMPISYYDKQKAGNLISTLINDINNVSNtmyntinqffssIFNVLLSIIAMMFVASFI 180
Cdd:cd18553 77 LLNRFSFGRYHSIAYRLFKNYLKLNYQDFTNKNSSDLSKSIINEASNLSQ------------VIQSFLFILSEIFVILFI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 181 -----------TLIV-VPLALFLFFISLIVIKKAQPYFVKVQNLFGDLNAFVEENLANTKVMNAFDQQDNIFNEFKKITR 248
Cdd:cd18553 145 yslllyvnwkiTLVLtLFLGLNVFFITKIVSKKIKKQGKKREESQKKFYKILSETFGNFKIIKLKSNEKEILKNFSQASL 224
|
..
gi 502819783 249 GI 250
Cdd:cd18553 225 KF 226
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
403-555 |
8.90e-03 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 38.02 E-value: 8.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 403 AIVGPTGAGKTTIIN-----LLGKfydynsGSIKIDGYELRNIKTNNLREhMSVVLqdTFmfndtienniKLGDKnatKE 477
Cdd:cd03279 32 LICGPTGAGKSTILDaityaLYGK------TPRYGRQENLRSVFAPGEDT-AEVSF--TF----------QLGGK---KY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819783 478 DVERAANLsNAIHFIKT--LPNG-FQTQIENNGQNLSQGQRQLIAIARA-----VLANKS-----ILILDEATSNIDSST 544
Cdd:cd03279 90 RVERSRGL-DYDQFTRIvlLPQGeFDRFLARPVSTLSGGETFLASLSLAlalseVLQNRGgarleALFIDEGFGTLDPEA 168
|
170
....*....|.
gi 502819783 545 EEIIQASLLKI 555
Cdd:cd03279 169 LEAVATALELI 179
|
|
| |
